UniProtKB - Q5YXQ1 (MAIA_NOCFA)
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>sp|Q5YXQ1|MAIA_NOCFA Maleate isomerase OS=Nocardia farcinica (strain IFM 10152) OX=247156 GN=maiA PE=1 SV=1 MGIRRIGLVVPSSNVTVETEMPALLSRHPGAEFSFHSTRMRMHTVSPEGLAAMNAQRERC VLEIADAAPEVILYACLVAVMVGGPGEHHRVESAVAEQLATGGSQALVRSSAGALVEGLR ALDAQRVALVTPYMRPLAEKVVAYLEAEGFTISDWRALEVADNTEVGCIPGEQVMAAARS LDLSEVDALVISCCVQMPSLPLVETAEREFGIPVLSAATAGAYSILRSLDLPVAVPGAGR LLRQDSAVTASCommunity curation ()Add a publicationFeedback
Protein
Maleate isomerase
Gene
maiA
Organism
Nocardia farcinica (strain IFM 10152)
Status
Reviewed-Annotation score:
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<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
Catalyzes cis-trans isomerization of the C2-C3 double bond in maleate to yield fumarate. Shows a strict specificity for maleate, with no activity detected toward structurally related substrates including citraconate, mesaconate, dimethylmaleate, and maleamide.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"A covalent succinylcysteine-like intermediate in the enzyme-catalyzed transformation of maleate to fumarate by maleate isomerase."
Fisch F., Fleites C.M., Delenne M., Baudendistel N., Hauer B., Turkenburg J.P., Hart S., Bruce N.C., Grogan G.
J. Am. Chem. Soc. 132:11455-11457(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF WILD-TYPE AND MUTANT ALA-194 WITH A COVALENTLY BOUND SUCCINYLCYSTEINE INTERMEDIATE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT, REACTION MECHANISM, ACTIVE SITE, SUCCINATION AT CYS-76, MUTAGENESIS OF CYS-76; TYR-133 AND CYS-194.
Miscellaneous
Reaction is initiated by nucleophilic attack of cysteine at the double bond, yielding a covalent succinylcysteine-like intermediate.1 Publication
Manual assertion based on experiment ini
- Ref.2"A covalent succinylcysteine-like intermediate in the enzyme-catalyzed transformation of maleate to fumarate by maleate isomerase."
Fisch F., Fleites C.M., Delenne M., Baudendistel N., Hauer B., Turkenburg J.P., Hart S., Bruce N.C., Grogan G.
J. Am. Chem. Soc. 132:11455-11457(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF WILD-TYPE AND MUTANT ALA-194 WITH A COVALENTLY BOUND SUCCINYLCYSTEINE INTERMEDIATE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT, REACTION MECHANISM, ACTIVE SITE, SUCCINATION AT CYS-76, MUTAGENESIS OF CYS-76; TYR-133 AND CYS-194.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
- maleateEC:5.2.1.1
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.2"A covalent succinylcysteine-like intermediate in the enzyme-catalyzed transformation of maleate to fumarate by maleate isomerase."
Fisch F., Fleites C.M., Delenne M., Baudendistel N., Hauer B., Turkenburg J.P., Hart S., Bruce N.C., Grogan G.
J. Am. Chem. Soc. 132:11455-11457(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF WILD-TYPE AND MUTANT ALA-194 WITH A COVALENTLY BOUND SUCCINYLCYSTEINE INTERMEDIATE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT, REACTION MECHANISM, ACTIVE SITE, SUCCINATION AT CYS-76, MUTAGENESIS OF CYS-76; TYR-133 AND CYS-194.
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
Manual assertion based on experiment ini
- Ref.2"A covalent succinylcysteine-like intermediate in the enzyme-catalyzed transformation of maleate to fumarate by maleate isomerase."
Fisch F., Fleites C.M., Delenne M., Baudendistel N., Hauer B., Turkenburg J.P., Hart S., Bruce N.C., Grogan G.
J. Am. Chem. Soc. 132:11455-11457(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF WILD-TYPE AND MUTANT ALA-194 WITH A COVALENTLY BOUND SUCCINYLCYSTEINE INTERMEDIATE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT, REACTION MECHANISM, ACTIVE SITE, SUCCINATION AT CYS-76, MUTAGENESIS OF CYS-76; TYR-133 AND CYS-194.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
maleate- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
zoom
=fumarate- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
zoom
<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
kcat is 2.8 sec(-1).1 Publication
Manual assertion based on experiment ini
- Ref.2"A covalent succinylcysteine-like intermediate in the enzyme-catalyzed transformation of maleate to fumarate by maleate isomerase."
Fisch F., Fleites C.M., Delenne M., Baudendistel N., Hauer B., Turkenburg J.P., Hart S., Bruce N.C., Grogan G.
J. Am. Chem. Soc. 132:11455-11457(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF WILD-TYPE AND MUTANT ALA-194 WITH A COVALENTLY BOUND SUCCINYLCYSTEINE INTERMEDIATE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT, REACTION MECHANISM, ACTIVE SITE, SUCCINATION AT CYS-76, MUTAGENESIS OF CYS-76; TYR-133 AND CYS-194.
- KM=4.6 µM for maleate (at pH 7.5)1 Publication
Manual assertion based on experiment ini
- Ref.2"A covalent succinylcysteine-like intermediate in the enzyme-catalyzed transformation of maleate to fumarate by maleate isomerase."
Fisch F., Fleites C.M., Delenne M., Baudendistel N., Hauer B., Turkenburg J.P., Hart S., Bruce N.C., Grogan G.
J. Am. Chem. Soc. 132:11455-11457(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF WILD-TYPE AND MUTANT ALA-194 WITH A COVALENTLY BOUND SUCCINYLCYSTEINE INTERMEDIATE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT, REACTION MECHANISM, ACTIVE SITE, SUCCINATION AT CYS-76, MUTAGENESIS OF CYS-76; TYR-133 AND CYS-194.
pH dependencei
Optimum pH is 7.5.1 Publication
Manual assertion based on experiment ini
- Ref.2"A covalent succinylcysteine-like intermediate in the enzyme-catalyzed transformation of maleate to fumarate by maleate isomerase."
Fisch F., Fleites C.M., Delenne M., Baudendistel N., Hauer B., Turkenburg J.P., Hart S., Bruce N.C., Grogan G.
J. Am. Chem. Soc. 132:11455-11457(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF WILD-TYPE AND MUTANT ALA-194 WITH A COVALENTLY BOUND SUCCINYLCYSTEINE INTERMEDIATE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT, REACTION MECHANISM, ACTIVE SITE, SUCCINATION AT CYS-76, MUTAGENESIS OF CYS-76; TYR-133 AND CYS-194.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 | 14 | Substrate1 Publication Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 | 76 | Nucleophile1 Publication Manual assertion based on experiment ini
| 1 | |
| Binding sitei | 133 | Substrate1 Publication Manual assertion based on experiment ini
| 1 | |
| Binding sitei | 163 | Substrate1 Publication Manual assertion based on experiment ini
| 1 | |
| Active sitei | 194 | Proton donor1 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
- maleate isomerase activity Source: UniProtKB-UniRule
<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 | Isomerase |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | NFAR247156:NFA_RS11020-MONOMER |
<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%5Fand%5Ftaxonomy%5Fsection">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: Maleate isomerase1 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 (EC:5.2.1.1
Manual assertion according to rulesi 1 PublicationManual assertion based on experiment ini
Short name: MI1 Publication Manual assertion based on opinion ini
Alternative name(s): Maleate cis-trans isomeraseUniRule annotation Manual assertion according to rulesi |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:maiAUniRule annotation Manual assertion according to rulesi Ordered Locus Names:NFA_21930Imported <p>Manually validated information which has been imported from another database.</p> <p><a href="/manual/evidences#ECO:0000312">More...</a></p> Manual assertion inferred from database entriesi |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 | Nocardia farcinica (strain IFM 10152) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI 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 | 247156 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 › Terrabacteria group › Actinobacteria › Actinobacteria › Corynebacteriales › Nocardiaceae › Nocardia › Nocardia farcinica |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 |
|
<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%5Fand%5Fbiotech%5Fsection">'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 | 76 | C → S: Reduces catalytic activity by more than 1000-fold. No change in substrate affinity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 133 | Y → F: No change in catalytic efficiency. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 194 | C → A: Loss of catalytic activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 194 | C → S: Reduces catalytic activity by more than 1000-fold. No change in substrate affinity. 1 Publication 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 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000448066 | 1 – 251 | Maleate isomeraseAdd BLAST | 251 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 76 | S-(2-succinyl)cysteineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0007744">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 |
<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Homodimer.
1 PublicationManual assertion based on experiment ini
- Ref.2"A covalent succinylcysteine-like intermediate in the enzyme-catalyzed transformation of maleate to fumarate by maleate isomerase."
Fisch F., Fleites C.M., Delenne M., Baudendistel N., Hauer B., Turkenburg J.P., Hart S., Bruce N.C., Grogan G.
J. Am. Chem. Soc. 132:11455-11457(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF WILD-TYPE AND MUTANT ALA-194 WITH A COVALENTLY BOUND SUCCINYLCYSTEINE INTERMEDIATE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT, REACTION MECHANISM, ACTIVE SITE, SUCCINATION AT CYS-76, MUTAGENESIS OF CYS-76; TYR-133 AND CYS-194.
Protein-protein interaction databases
STRING: functional protein association networks More...STRINGi | 247156.NFA_21930 |
<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
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> 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 | 2 – 11 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> 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 | 17 – 25 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| Beta strandi | 33 – 40 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| Helixi | 47 – 54 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| Helixi | 57 – 65 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| Beta strandi | 70 – 74 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 77 – 81 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 87 – 101 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 15 | |
| Beta strandi | 107 – 110 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 111 – 121 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| Beta strandi | 126 – 131 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Helixi | 135 – 147 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| Beta strandi | 151 – 157 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| Helixi | 163 – 167 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 171 – 180 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| Beta strandi | 187 – 197 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| Helixi | 202 – 210 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| Beta strandi | 214 – 216 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 217 – 228 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| Beta strandi | 236 – 238 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 240 – 243 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code 'T'.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 244 – 247 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 |
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q5YXQ1 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q5YXQ1 |
<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
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 76 – 78 | Substrate binding1 Publication Manual assertion based on experiment ini
| 3 | |
| Regioni | 195 – 196 | Substrate binding1 Publication Manual assertion based on experiment ini
| 2 |
<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
Belongs to the maleate isomerase family.UniRule annotation
Manual assertion according to rulesi
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | COG3473, Bacteria |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | CLU_068086_0_0_11 |
Identification of Orthologs from Complete Genome Data More...OMAi | AIMSMGK |
Family and domain databases
HAMAP database of protein families More...HAMAPi | MF_00943, Maleate_isomerase, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR026286, MaiA/AMDase IPR028615, Maleate_isomerase |
The PANTHER Classification System More...PANTHERi | PTHR40267, PTHR40267, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF17645, Amdase, 1 hit |
PIRSF; a whole-protein classification database More...PIRSFi | PIRSF015736, MI, 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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.
Q5YXQ1-1 [UniParc]FASTAAdd to basketAdded to basket
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MGIRRIGLVV PSSNVTVETE MPALLSRHPG AEFSFHSTRM RMHTVSPEGL
60 70 80 90 100
AAMNAQRERC VLEIADAAPE VILYACLVAV MVGGPGEHHR VESAVAEQLA
110 120 130 140 150
TGGSQALVRS SAGALVEGLR ALDAQRVALV TPYMRPLAEK VVAYLEAEGF
160 170 180 190 200
TISDWRALEV ADNTEVGCIP GEQVMAAARS LDLSEVDALV ISCCVQMPSL
210 220 230 240 250
PLVETAEREF GIPVLSAATA GAYSILRSLD LPVAVPGAGR LLRQDSAVTA
S
Length:251
Mass (Da):26,457
Last modified:November 23, 2004 - v1
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i4381DC35CDC54FFB
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 | AP006618 Genomic DNA Translation: BAD57040.1 |
NCBI Reference Sequences More...RefSeqi | WP_011208725.1, NC_006361.1 |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | BAD57040; BAD57040; NFA_21930 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | nfa:NFA_21930 |
<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 | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| Q5YXQ1 | Maleate isomerase | 251 | UniRef90_Q5YXQ1 | |||
| Maleate isomerase | 251 | |||||
| +6 | ||||||
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| Q5YXQ1 | Maleate isomerase | 251 | UniRef50_Q5YXQ1 | |||
| Maleate isomerase | 251 | |||||
| Maleate isomerase | 250 | |||||
| Maleate isomerase | 265 | |||||
| Maleate isomerase | 254 | |||||
| +239 | ||||||
<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: EMBLi GenBanki DDBJi Links Updated | AP006618 Genomic DNA Translation: BAD57040.1 |
| RefSeqi | WP_011208725.1, NC_006361.1 |
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 |
| 2XEC | X-ray | 2.20 | A/B/C/D | 1-251 | [»] | |
| 2XED | X-ray | 1.95 | A/B/C/D | 1-251 | [»] | |
| SMRi | Q5YXQ1 | |||||
| ModBasei | Search... | |||||
| PDBe-KBi | Search... | |||||
Protein-protein interaction databases
| STRINGi | 247156.NFA_21930 |
Genome annotation databases
| EnsemblBacteriai | BAD57040; BAD57040; NFA_21930 |
| KEGGi | nfa:NFA_21930 |
Phylogenomic databases
| eggNOGi | COG3473, Bacteria |
| HOGENOMi | CLU_068086_0_0_11 |
| OMAi | AIMSMGK |
Enzyme and pathway databases
| BioCyci | NFAR247156:NFA_RS11020-MONOMER |
Miscellaneous databases
| EvolutionaryTracei | Q5YXQ1 |
Family and domain databases
| HAMAPi | MF_00943, Maleate_isomerase, 1 hit |
| InterProi | View protein in InterPro IPR026286, MaiA/AMDase IPR028615, Maleate_isomerase |
| PANTHERi | PTHR40267, PTHR40267, 1 hit |
| Pfami | View protein in Pfam PF17645, Amdase, 1 hit |
| PIRSFi | PIRSF015736, MI, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | 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 | MAIA_NOCFA | |
| <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 | Q5YXQ1Primary (citable) accession number: Q5YXQ1 | |
| <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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 16, 2019 |
| Last sequence update: | November 23, 2004 | |
| Last modified: | April 7, 2021 | |
| This is version 94 of the entry and version 1 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 | |
<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
