UniProtKB - P45131 (METXA_HAEIN)
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- BLAST>sp|P45131|METXA_HAEIN Homoserine O-acetyltransferase OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=metXA PE=1 SV=3 MSVQNVVLFDTQPLTLMLGGKLSHINVAYQTYGTLNAEKNNAVLICHALTGDAEPYFDDG RDGWWQNFMGAGLALDTDRYFFISSNVLGGCKGTTGPSSINPQTGKPYGSQFPNIVVQDI VKVQKALLDHLGISHLKAIIGGSFGGMQANQWAIDYPDFMDNIVNLCSSIYFSAEAIGFN HVMRQAVINDPNFNGGDYYEGTPPDQGLSIARMLGMLTYRTDLQLAKAFGRATKSDGSFW GDYFQVESYLSYQGKKFLERFDANSYLHLLRALDMYDPSLGYDNVKEALSRIKARYTLVS VTTDQLFKPIDLYKSKQLLEQSGVDLHFYEFPSDYGHDAFLVDYDQFEKRIRDGLAGN
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Homoserine O-acetyltransferase
metXA
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.2"Enzyme-catalyzed acylation of homoserine: mechanistic characterization of the Haemophilus influenzae met2-encoded homoserine transacetylase."
Born T.L., Franklin M., Blanchard J.S.
Biochemistry 39:8556-8564(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES, REACTION MECHANISM, SUBUNIT. - Ref.3"Parallel evolution of non-homologous isofunctional enzymes in methionine biosynthesis."
Bastard K., Perret A., Mariage A., Bessonnet T., Pinet-Turpault A., Petit J.L., Darii E., Bazire P., Vergne-Vaxelaire C., Brewee C., Debard A., Pellouin V., Besnard-Gonnet M., Artiguenave F., Medigue C., Vallenet D., Danchin A., Zaparucha A. , Weissenbach J., Salanoubat M., de Berardinis V.
Nat. Chem. Biol. 13:858-866(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF LEU-306, 3D-STRUCTURE MODELING.
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi
2 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.2"Enzyme-catalyzed acylation of homoserine: mechanistic characterization of the Haemophilus influenzae met2-encoded homoserine transacetylase."
Born T.L., Franklin M., Blanchard J.S.
Biochemistry 39:8556-8564(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES, REACTION MECHANISM, SUBUNIT. - Ref.3"Parallel evolution of non-homologous isofunctional enzymes in methionine biosynthesis."
Bastard K., Perret A., Mariage A., Bessonnet T., Pinet-Turpault A., Petit J.L., Darii E., Bazire P., Vergne-Vaxelaire C., Brewee C., Debard A., Pellouin V., Besnard-Gonnet M., Artiguenave F., Medigue C., Vallenet D., Danchin A., Zaparucha A. , Weissenbach J., Salanoubat M., de Berardinis V.
Nat. Chem. Biol. 13:858-866(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF LEU-306, 3D-STRUCTURE MODELING.
<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.2"Enzyme-catalyzed acylation of homoserine: mechanistic characterization of the Haemophilus influenzae met2-encoded homoserine transacetylase."
Born T.L., Franklin M., Blanchard J.S.
Biochemistry 39:8556-8564(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES, REACTION MECHANISM, SUBUNIT. - Ref.3"Parallel evolution of non-homologous isofunctional enzymes in methionine biosynthesis."
Bastard K., Perret A., Mariage A., Bessonnet T., Pinet-Turpault A., Petit J.L., Darii E., Bazire P., Vergne-Vaxelaire C., Brewee C., Debard A., Pellouin V., Besnard-Gonnet M., Artiguenave F., Medigue C., Vallenet D., Danchin A., Zaparucha A. , Weissenbach J., Salanoubat M., de Berardinis V.
Nat. Chem. Biol. 13:858-866(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF LEU-306, 3D-STRUCTURE MODELING.
- KM=130 µM for L-homoserine (at 25 degrees Celsius and pH 7.5)1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.2"Enzyme-catalyzed acylation of homoserine: mechanistic characterization of the Haemophilus influenzae met2-encoded homoserine transacetylase."
Born T.L., Franklin M., Blanchard J.S.
Biochemistry 39:8556-8564(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES, REACTION MECHANISM, SUBUNIT.
- KM=570 µM for L-homoserine1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.3"Parallel evolution of non-homologous isofunctional enzymes in methionine biosynthesis."
Bastard K., Perret A., Mariage A., Bessonnet T., Pinet-Turpault A., Petit J.L., Darii E., Bazire P., Vergne-Vaxelaire C., Brewee C., Debard A., Pellouin V., Besnard-Gonnet M., Artiguenave F., Medigue C., Vallenet D., Danchin A., Zaparucha A. , Weissenbach J., Salanoubat M., de Berardinis V.
Nat. Chem. Biol. 13:858-866(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF LEU-306, 3D-STRUCTURE MODELING.
- KM=140 µM for acetyl-CoA (at 25 degrees Celsius and pH 7.5)1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.2"Enzyme-catalyzed acylation of homoserine: mechanistic characterization of the Haemophilus influenzae met2-encoded homoserine transacetylase."
Born T.L., Franklin M., Blanchard J.S.
Biochemistry 39:8556-8564(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES, REACTION MECHANISM, SUBUNIT.
- KM=586 µM for acetyl-CoA1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.3"Parallel evolution of non-homologous isofunctional enzymes in methionine biosynthesis."
Bastard K., Perret A., Mariage A., Bessonnet T., Pinet-Turpault A., Petit J.L., Darii E., Bazire P., Vergne-Vaxelaire C., Brewee C., Debard A., Pellouin V., Besnard-Gonnet M., Artiguenave F., Medigue C., Vallenet D., Danchin A., Zaparucha A. , Weissenbach J., Salanoubat M., de Berardinis V.
Nat. Chem. Biol. 13:858-866(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF LEU-306, 3D-STRUCTURE MODELING.
- KM=90 µM for propionyl-CoA (at 25 degrees Celsius and pH 7.5)1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.2"Enzyme-catalyzed acylation of homoserine: mechanistic characterization of the Haemophilus influenzae met2-encoded homoserine transacetylase."
Born T.L., Franklin M., Blanchard J.S.
Biochemistry 39:8556-8564(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES, REACTION MECHANISM, SUBUNIT.
- KM=130 µM for crotonyl-CoA (at 25 degrees Celsius and pH 7.5)1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.2"Enzyme-catalyzed acylation of homoserine: mechanistic characterization of the Haemophilus influenzae met2-encoded homoserine transacetylase."
Born T.L., Franklin M., Blanchard J.S.
Biochemistry 39:8556-8564(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES, REACTION MECHANISM, SUBUNIT.
- KM=210 µM for butyryl-CoA (at 25 degrees Celsius and pH 7.5)1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.2"Enzyme-catalyzed acylation of homoserine: mechanistic characterization of the Haemophilus influenzae met2-encoded homoserine transacetylase."
Born T.L., Franklin M., Blanchard J.S.
Biochemistry 39:8556-8564(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES, REACTION MECHANISM, SUBUNIT.
- KM=280 µM for glutaryl-CoA (at 25 degrees Celsius and pH 7.5)1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.2"Enzyme-catalyzed acylation of homoserine: mechanistic characterization of the Haemophilus influenzae met2-encoded homoserine transacetylase."
Born T.L., Franklin M., Blanchard J.S.
Biochemistry 39:8556-8564(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES, REACTION MECHANISM, SUBUNIT.
- KM=360 µM for succinyl-CoA (at 25 degrees Celsius and pH 7.5)1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.2"Enzyme-catalyzed acylation of homoserine: mechanistic characterization of the Haemophilus influenzae met2-encoded homoserine transacetylase."
Born T.L., Franklin M., Blanchard J.S.
Biochemistry 39:8556-8564(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES, REACTION MECHANISM, SUBUNIT.
- KM=1400 µM for 4-nitrophenyl acetate (at 25 degrees Celsius and pH 7.5)1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.2"Enzyme-catalyzed acylation of homoserine: mechanistic characterization of the Haemophilus influenzae met2-encoded homoserine transacetylase."
Born T.L., Franklin M., Blanchard J.S.
Biochemistry 39:8556-8564(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES, REACTION MECHANISM, SUBUNIT.
- KM=4700 µM for D-homoserine (at 25 degrees Celsius and pH 7.5)1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.2"Enzyme-catalyzed acylation of homoserine: mechanistic characterization of the Haemophilus influenzae met2-encoded homoserine transacetylase."
Born T.L., Franklin M., Blanchard J.S.
Biochemistry 39:8556-8564(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES, REACTION MECHANISM, SUBUNIT.
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">‘Function’</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-methionine biosynthesis via de novo pathway
This protein is involved in step 1 of the subpathway that synthesizes O-acetyl-L-homoserine from L-homoserine.UniRule annotation<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi
Proteins known to be involved in this subpathway in this organism are:
- Homoserine O-acetyltransferase (metXA)
View all proteins of this organism that are known to be involved in the subpathway that synthesizes O-acetyl-L-homoserine from L-homoserine, the pathway L-methionine biosynthesis via de novo pathway and in Amino-acid biosynthesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 143 | NucleophileUniRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi 1 Publication<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More…</a></p> Manual assertion inferred by curator fromi
| 1 | |
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 212 | SubstrateUniRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi 1 Publication<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More…</a></p> Manual assertion inferred by curator fromi
| 1 | |
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 304 | UniRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi 1 Publication<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More…</a></p> Manual assertion inferred by curator fromi
| 1 | |
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 337 | UniRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi 1 Publication<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More…</a></p> Manual assertion inferred by curator fromi
| 1 | |
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 338 | SubstrateUniRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi 1 Publication<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More…</a></p> Manual assertion inferred by curator fromi
| 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- homoserine O-acetyltransferase activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- homoserine metabolic process Source: GO_Central
- methionine biosynthetic process Source: GO_Central
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
Molecular function | Acyltransferase, Transferase |
Biological process | Amino-acid biosynthesis, Methionine biosynthesis |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | HINF71421:G1GJ1-1291-MONOMER. |
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 2.3.1.31. 2529. |
UniPathway: a resource for the exploration and annotation of metabolic pathways More...UniPathwayi | UPA00051; UER00074. |
Protein family/group databases
ESTHER database of the Alpha/Beta-hydrolase fold superfamily of proteins More...ESTHERi | haein-metx. Homoserine_transacetylase. |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Homoserine O-acetyltransferaseUniRule annotation<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi Curated (EC:2.3.1.31UniRule annotation<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi 2 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
Short name: HAT1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini
<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi Alternative name(s): Homoserine O-trans-acetylaseCurated Homoserine transacetylase1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini
<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi Short name: HTAUniRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi Curated |
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:metXA1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini
<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi Synonyms:met2 Ordered Locus Names:HI_1263 |
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) |
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the <span class="caps">NCBI</span> to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 71421 [NCBI] |
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus › Haemophilus influenzae |
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
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<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
- Cytoplasm UniRule annotation
<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti
- cytoplasm Source: UniProtKB-SubCell
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
Cytoplasm<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 306 | L → R: Can no longer use acetyl-CoA as acyl donor, but can use succinyl-CoA. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span> / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methioninei | Removed1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| |||
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000155719 | 2 – 358 | Homoserine O-acetyltransferaseAdd BLAST | 357 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">‘Interaction’</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">‘Function’</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi
2 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.2"Enzyme-catalyzed acylation of homoserine: mechanistic characterization of the Haemophilus influenzae met2-encoded homoserine transacetylase."
Born T.L., Franklin M., Blanchard J.S.
Biochemistry 39:8556-8564(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES, REACTION MECHANISM, SUBUNIT. - Ref.4"Crystal structure of homoserine transacetylase from Haemophilus influenzae reveals a new family of alpha/beta-hydrolases."
Mirza I.A., Nazi I., Korczynska M., Wright G.D., Berghuis A.M.
Biochemistry 44:15768-15773(2005) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS), ACTIVE SITE, SUBUNIT.
Protein-protein interaction databases
STRING: functional protein association networks More...STRINGi | 71421.HI1263. |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 4 – 12 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 24 – 33 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 42 – 46 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 58 – 60 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 66 – 68 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 73 – 76 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the <span class="caps">DSSP</span> secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 77 – 79 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 81 – 85 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 91 – 95 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the <span class="caps">DSSP</span> secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 102 – 104 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 105 – 107 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 109 – 111 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 117 – 130 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 136 – 142 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 144 – 155 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 159 – 167 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 174 – 188 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 15 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 194 – 196 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 205 – 219 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 15 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 222 – 228 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the <span class="caps">DSSP</span> secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 229 – 231 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 245 – 258 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 263 – 275 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the <span class="caps">DSSP</span> secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 278 – 281 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 285 – 289 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 294 – 301 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 305 – 307 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 309 – 321 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 325 – 331 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 336 – 338 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 339 – 342 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 344 – 356 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 |
3D structure databases
Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2B61 | X-ray | 1.65 | A | 1-358 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P45131. | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P45131. | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P45131. |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 41 – 343 | AB hydrolase-1UniRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi Add BLAST | 303 |
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG4105DWV. Bacteria. COG2021. LUCA. |
KEGG Orthology (KO) More...KOi | K00641. |
Identification of Orthologs from Complete Genome Data More...OMAi | CQGTTGP. |
Database for complete collections of gene phylogenies More...PhylomeDBi | P45131. |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.40.50.1820. 2 hits. |
HAMAP database of protein families More...HAMAPi | MF_00296. MetX_acyltransf. 1 hit. |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR029058. AB_hydrolase. IPR000073. AB_hydrolase_1. IPR008220. HAT_MetX-like. |
The PANTHER Classification System More...PANTHERi | PTHR32268. PTHR32268. 1 hit. |
Pfam protein domain database More...Pfami | View protein in Pfam PF00561. Abhydrolase_1. 1 hit. |
PIRSF; a whole-protein classification database More...PIRSFi | PIRSF000443. Homoser_Ac_trans. 1 hit. |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF53474. SSF53474. 1 hit. |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR01392. homoserO_Ac_trn. 1 hit. |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
10 20 30 40 50
MSVQNVVLFD TQPLTLMLGG KLSHINVAYQ TYGTLNAEKN NAVLICHALT
60 70 80 90 100
GDAEPYFDDG RDGWWQNFMG AGLALDTDRY FFISSNVLGG CKGTTGPSSI
110 120 130 140 150
NPQTGKPYGS QFPNIVVQDI VKVQKALLDH LGISHLKAII GGSFGGMQAN
160 170 180 190 200
QWAIDYPDFM DNIVNLCSSI YFSAEAIGFN HVMRQAVIND PNFNGGDYYE
210 220 230 240 250
GTPPDQGLSI ARMLGMLTYR TDLQLAKAFG RATKSDGSFW GDYFQVESYL
260 270 280 290 300
SYQGKKFLER FDANSYLHLL RALDMYDPSL GYDNVKEALS RIKARYTLVS
310 320 330 340 350
VTTDQLFKPI DLYKSKQLLE QSGVDLHFYE FPSDYGHDAF LVDYDQFEKR
IRDGLAGN
<p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.2"Enzyme-catalyzed acylation of homoserine: mechanistic characterization of the Haemophilus influenzae met2-encoded homoserine transacetylase."
Born T.L., Franklin M., Blanchard J.S.
Biochemistry 39:8556-8564(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES, REACTION MECHANISM, SUBUNIT.
Sequence databases
Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | L42023 Genomic DNA. Translation: AAC22916.1. |
Protein sequence database of the Protein Information Resource More...PIRi | D64113. |
NCBI Reference Sequences More...RefSeqi | NP_439418.1. NC_000907.1. WP_005694320.1. NC_000907.1. |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | AAC22916; AAC22916; HI_1263. |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 950208. |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hin:HI1263. |
Pathosystems Resource Integration Center (PATRIC) More...PATRICi | fig|71421.8.peg.1315. |
<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
Protein | Similar proteins | Organisms | Length | Cluster ID | Cluster name | Size | |
---|---|---|---|---|---|---|---|
P45131 | UPI00006836BC UPI0008029614 UPI0001F36972 UPI00093AAF04 A4MZP1 H1LM93 F9GUD4 UPI0005895700 A0A0Y0AG77 E1X782 +38 | Haemophilus influenzae Haemophilus influenzae 22.1-21 Haemophilus sp. oral taxon 851 str. F0397 Haemophilus haemolyticus M21127 Streptococcus pneumoniae Haemophilus influenzae (strain 10810) Haemophilus haemolyticus M21621 Haemophilus influenzae (strain NTHi 3655) Haemophilus influenzae (strain 86-028NP) Haemophilus haemolyticus And more | 358 | UniRef90_P45131 | Cluster: Homoserine O-acetyltransferase | 49 |
Protein | Similar proteins | Organisms | Length | Cluster ID | Cluster name | Size | |
---|---|---|---|---|---|---|---|
P45131 | UPI00006836BC UPI0008029614 A0A0Y7IBJ5 UPI0008DBAC86 F9GYD9 UPI00062D1814 E7A443 UPI0005895700 UPI0006813100 A0A1V2BLS8 +43 | Haemophilus influenzae Haemophilus haemolyticus M21621 Haemophilus haemolyticus Haemophilus influenzae F3031 Streptococcus pneumoniae Haemophilus influenzae (strain 10810) Haemophilus sp. oral taxon 851 str. F0397 Haemophilus sp. CCUG 66565 Haemophilus haemolyticus M19501 Haemophilus influenzae 22.1-21 And more | 358 | UniRef50_P45131 | Cluster: Homoserine O-acetyltransferase | 54 |
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | L42023 Genomic DNA. Translation: AAC22916.1. |
Protein sequence database of the Protein Information Resource More...PIRi | D64113. |
NCBI Reference Sequences More...RefSeqi | NP_439418.1. NC_000907.1. WP_005694320.1. NC_000907.1. |
3D structure databases
Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2B61 | X-ray | 1.65 | A | 1-358 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P45131. | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P45131. | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Protein-protein interaction databases
STRING: functional protein association networks More...STRINGi | 71421.HI1263. |
Protein family/group databases
ESTHER database of the Alpha/Beta-hydrolase fold superfamily of proteins More...ESTHERi | haein-metx. Homoserine_transacetylase. |
Protocols and materials databases
Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | AAC22916; AAC22916; HI_1263. |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 950208. |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hin:HI1263. |
Pathosystems Resource Integration Center (PATRIC) More...PATRICi | fig|71421.8.peg.1315. |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG4105DWV. Bacteria. COG2021. LUCA. |
KEGG Orthology (KO) More...KOi | K00641. |
Identification of Orthologs from Complete Genome Data More...OMAi | CQGTTGP. |
Database for complete collections of gene phylogenies More...PhylomeDBi | P45131. |
Enzyme and pathway databases
UniPathway: a resource for the exploration and annotation of metabolic pathways More...UniPathwayi | UPA00051; UER00074. |
BioCyc Collection of Pathway/Genome Databases More...BioCyci | HINF71421:G1GJ1-1291-MONOMER. |
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 2.3.1.31. 2529. |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P45131. |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.40.50.1820. 2 hits. |
HAMAP database of protein families More...HAMAPi | MF_00296. MetX_acyltransf. 1 hit. |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR029058. AB_hydrolase. IPR000073. AB_hydrolase_1. IPR008220. HAT_MetX-like. |
The PANTHER Classification System More...PANTHERi | PTHR32268. PTHR32268. 1 hit. |
Pfam protein domain database More...Pfami | View protein in Pfam PF00561. Abhydrolase_1. 1 hit. |
PIRSF; a whole-protein classification database More...PIRSFi | PIRSF000443. Homoser_Ac_trans. 1 hit. |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF53474. SSF53474. 1 hit. |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR01392. homoserO_Ac_trn. 1 hit. |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | METXA_HAEIN | |
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | P45131Primary (citable) accession number: P45131 | |
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1995 |
Last sequence update: | January 23, 2007 | |
Last modified: | February 28, 2018 | |
This is version 134 of the entry and version 3 of the sequence. See complete history. | ||
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |