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UniProtKB - P07623 (METAS_ECOLI)

Entry version 174 (23 Feb 2022)
Sequence version 4 (23 Jan 2007)
Previous versions | rss
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Protein

Homoserine O-succinyltransferase

Gene

metAS

Organism
Escherichia coli (strain K12)
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>

<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

Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine (PubMed:10572016, PubMed:17442255, PubMed:17302437, PubMed:28581482).

Utilizes a ping-pong kinetic mechanism in which the succinyl group of succinyl-CoA is initially transferred to the enzyme to form a succinyl-enzyme intermediate before subsequent transfer to homoserine to form the final product, O-succinylhomoserine (PubMed:10572016, PubMed:17442255, PubMed:17302437).

Cannot use acetyl-CoA (PubMed:10572016).

4 Publications

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by iodoacetamide in a pH-dependent manner.1 Publication

<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 24 sec(-1) with succinyl-CoA as substrate. kcat is 24 sec(-1) with L-homoserine as substrate. kcat is 5.23 sec(-1) with CoA as substrate. kcat is 5.23 sec(-1) with O-succinylhomoserine as substrate.1 Publication
  1. KM=0.17 mM for succinyl-CoA1 Publication
  2. KM=0.13 mM for succinyl-CoA1 Publication
  3. KM=0.28 mM for succinyl-CoA1 Publication
  4. KM=1.6 mM for L-homoserine1 Publication
  5. KM=0.72 mM for L-homoserine1 Publication
  6. KM=0.38 mM for L-homoserine1 Publication
  7. KM=0.64 mM for CoA1 Publication
  8. KM=3.5 mM for O-succinylhomoserine1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'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-succinyl-L-homoserine from L-homoserine.UniRule annotation1 Publication This subpathway is part of the pathway L-methionine biosynthesis via de novo pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes O-succinyl-L-homoserine from L-homoserine, the pathway L-methionine biosynthesis via de novo pathway and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei111Important for acyl-CoA specificityUniRule annotation1
<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 sitei142Acyl-thioester intermediateUniRule annotation3 Publications1
<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 sitei163SubstrateUniRule annotation1
Binding sitei192SubstrateUniRule annotation1
Sitei192Important for substrate specificityUniRule annotation1
Active sitei235Proton acceptorUniRule annotation2 Publications1
Active sitei237UniRule annotation2 Publications1
Binding sitei249SubstrateUniRule annotation1

<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-UniRule
  • homoserine O-succinyltransferase activity Source: EcoCyc
Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionAcyltransferase, Transferase
Biological processAmino-acid biosynthesis, Methionine biosynthesis

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:HOMSUCTRAN-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.3.1.46, 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P07623

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi		UPA00051;UER00075

<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:
Homoserine O-succinyltransferase1 PublicationUniRule annotation (EC:2.3.1.464 Publications)
Short name:
HST1 PublicationUniRule annotation
Alternative name(s):
Homoserine transsuccinylase1 PublicationUniRule annotation
Short name:
HTS1 PublicationUniRule annotation
<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:metAS1 PublicationUniRule annotation
Synonyms:metA1 Publication
Ordered Locus Names:b4013, JW3973
<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>OrganismiEscherichia coli (strain K12)
<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 identifieri83333 [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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<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
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

<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

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 keyPosition(s)DescriptionActionsGraphical viewLength
<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>Mutagenesisi46 – 47KK → AA: Lack of activity. 3 Publications2
Mutagenesisi46K → A: 16-fold decrease in Km for L-homoserine. 32-fold decrease in catalytic activity. 1 Publication1
Mutagenesisi46K → L: 6-fold increase in Km for L-homoserine and in Km for succinyl-CoA. Slight increase in catalytic activity. 1 Publication1
Mutagenesisi46K → R: Slight decrease in catalytic activity. 1 Publication1
Mutagenesisi47K → A: 22-fold decrease in Km for L-homoserine. Almost loss of catalytic activity. 1 Publication1
Mutagenesisi47K → L: 8-fold decrease in Km for L-homoserine and 10-fold increase in Km for succinyl-CoA. 20-fold decrease in catalytic activity. 1 Publication1
Mutagenesisi47K → R: 14-fold decrease in Km for L-homoserine. 72-fold decrease in catalytic activity. 1 Publication1
Mutagenesisi90C → A or S: No change in activity. 1 Publication1
Mutagenesisi142C → A or S: Lack of activity. 2 Publications1
Mutagenesisi157K → L: Lack of activity. 1 Publication1
Mutagenesisi193R → A: 3-fold increase in Km for L-homoserine. 8-fold decrease in catalytic activity. 1 Publication1
Mutagenesisi193R → K: 8-fold decrease in catalytic activity. 1 Publication1
Mutagenesisi235H → A or N: Lack of activity. 2 Publications1
Mutagenesisi237E → A: 32-fold decrease in catalytic activity. 1 Publication1
Mutagenesisi237E → D: 3-fold decrease in catalytic activity. 1 Publication1
Mutagenesisi238Y → F: 5-fold increase in Km for L-homoserine. 1 Publication1
Mutagenesisi246E → A: 150-fold increase in Km for L-homoserine. 1 Publication1
Mutagenesisi246E → D: 24-fold increase in Km for L-homoserine. 1 Publication1
Mutagenesisi249R → K: 4-fold increase in Km for L-homoserine. 1 Publication1

<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 keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / 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 methionineiRemoved1 Publication
<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_00001997482 – 309Homoserine O-succinyltransferaseAdd BLAST308

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P07623

PRoteomics IDEntifications database

More...PRIDEi		P07623

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Contains two transcription starting points, P1 and P2, which are 74 bp apart. P1 is under negative control by methionine, whereas P2 is independent of the intracellular methionine concentration.1 Publication

<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.

UniRule annotation1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		4259289, 20 interactors

Protein interaction database and analysis system

More...IntActi		P07623, 2 interactors

Molecular INTeraction database

More...MINTi		P07623

STRING: functional protein association networks

More...STRINGi		511145.b4013

<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

1309
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P07623

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

<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

<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 MetA family.UniRule annotationCurated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG1897, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_057851_0_1_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P07623

Database for complete collections of gene phylogenies

More...PhylomeDBi		P07623

Family and domain databases

Conserved Domains Database

More...CDDi		cd03131, GATase1_HTS, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.50.880, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_00295, MetA_acyltransf, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR029062, Class_I_gatase-like
IPR005697, HST_MetA
IPR033752, MetA_family

The PANTHER Classification System

More...PANTHERi		PTHR20919, PTHR20919, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF04204, HTS, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF000450, H_ser_succinyltr, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF52317, SSF52317, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR01001, metA, 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.

<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 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.

P07623-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPIRVPDELP AVNFLREENV FVMTTSRASG QEIRPLKVLI LNLMPKKIET 
        60         70         80         90        100
ENQFLRLLSN SPLQVDIQLL RIDSRESRNT PAEHLNNFYC NFEDIQDQNF 
       110        120        130        140        150
DGLIVTGAPL GLVEFNDVAY WPQIKQVLEW SKDHVTSTLF VCWAVQAALN 
       160        170        180        190        200
ILYGIPKQTR TEKLSGVYEH HILHPHALLT RGFDDSFLAP HSRYADFPAA 
       210        220        230        240        250
LIRDYTDLEI LAETEEGDAY LFASKDKRIA FVTGHPEYDA QTLAQEFFRD 
       260        270        280        290        300
VEAGLDPDVP YNYFPHNDPQ NTPRASWRSH GNLLFTNWLN YYVYQITPYD 

LRHMNPTLD
Length:309
Mass (Da):35,727
Last modified:January 23, 2007 - v4
<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:iA2C395A9A9CFE2C0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti67I → V (PubMed:2654885).Curated1
Sequence conflicti67I → V (PubMed:6094503).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
X14501 Genomic DNA Translation: CAA32654.1
U00006 Genomic DNA Translation: AAC43107.1
U00096 Genomic DNA Translation: AAC76983.1
AP009048 Genomic DNA Translation: BAE78015.1
M10210 Genomic DNA Translation: AAA24157.1
X12431 Genomic DNA No translation available.

Protein sequence database of the Protein Information Resource

More...PIRi		D65208, XYECM

NCBI Reference Sequences

More...RefSeqi		NP_418437.1, NC_000913.3
WP_001122779.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC76983; AAC76983; b4013
BAE78015; BAE78015; BAE78015

Database of genes from NCBI RefSeq genomes

More...GeneIDi		948513

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW3973
eco:b4013

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.2700

<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

<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
X14501 Genomic DNA Translation: CAA32654.1
U00006 Genomic DNA Translation: AAC43107.1
U00096 Genomic DNA Translation: AAC76983.1
AP009048 Genomic DNA Translation: BAE78015.1
M10210 Genomic DNA Translation: AAA24157.1
X12431 Genomic DNA No translation available.
PIRiD65208, XYECM
RefSeqiNP_418437.1, NC_000913.3
WP_001122779.1, NZ_LN832404.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
6MTGX-ray1.85A/B1-296[»]
7CBEX-ray1.70A/B1-309[»]
SMRiP07623
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4259289, 20 interactors
IntActiP07623, 2 interactors
MINTiP07623
STRINGi511145.b4013

Proteomic databases

PaxDbiP07623
PRIDEiP07623

Genome annotation databases

EnsemblBacteriaiAAC76983; AAC76983; b4013
BAE78015; BAE78015; BAE78015
GeneIDi948513
KEGGiecj:JW3973
eco:b4013
PATRICifig|1411691.4.peg.2700

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...EchoBASEi		EB0576

Phylogenomic databases

eggNOGiCOG1897, Bacteria
HOGENOMiCLU_057851_0_1_6
InParanoidiP07623
PhylomeDBiP07623

Enzyme and pathway databases

UniPathwayiUPA00051;UER00075
BioCyciEcoCyc:HOMSUCTRAN-MONOMER
BRENDAi2.3.1.46, 2026
SABIO-RKiP07623

Miscellaneous databases

Protein Ontology

More...PROi		PR:P07623

Family and domain databases

CDDicd03131, GATase1_HTS, 1 hit
Gene3Di3.40.50.880, 1 hit
HAMAPiMF_00295, MetA_acyltransf, 1 hit
InterProiView protein in InterPro
IPR029062, Class_I_gatase-like
IPR005697, HST_MetA
IPR033752, MetA_family
PANTHERiPTHR20919, PTHR20919, 1 hit
PfamiView protein in Pfam
PF04204, HTS, 1 hit
PIRSFiPIRSF000450, H_ser_succinyltr, 1 hit
SUPFAMiSSF52317, SSF52317, 1 hit
TIGRFAMsiTIGR01001, metA, 1 hit

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 nameiMETAS_ECOLI
<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>AccessioniPrimary (citable) accession number: P07623
Secondary accession number(s): Q2M6U1
<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 historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: February 23, 2022
This is version 174 of the entry and version 4 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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic 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, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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