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UniProtKB - P13009 (METH_ECOLI)

Protein

Methionine synthase

Gene

metH

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

Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate.

Miscellaneous

L-homocysteine is bound via the zinc atom.

<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. 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 ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<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 L-methionine from L-homocysteine (MetH route).
Proteins known to be involved in this subpathway in this organism are:
  1. Methionine synthase (metH)
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 L-methionine from L-homocysteine (MetH route), the pathway L-methionine biosynthesis via de novo pathway and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi247Zinc1
Metal bindingi310Zinc1
Metal bindingi311Zinc1
Metal bindingi759Cobalt (cobalamin axial ligand)1 Publication1
<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 sitei804Cobalamin2 Publications1
Binding sitei946S-adenosyl-L-methionine1 Publication1
Binding sitei1134S-adenosyl-L-methionine; via carbonyl oxygen1 Publication1
Binding sitei1138Cobalamin; via carbonyl oxygen2 Publications1

<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

  • cobalamin binding Source: BHF-UCL
  • methionine synthase activity Source: BHF-UCL
  • protein methyltransferase activity Source: BHF-UCL
  • zinc ion binding Source: EcoCyc
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the 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 functionMethyltransferase, Transferase
Biological processAmino-acid biosynthesis, Methionine biosynthesis
LigandCobalamin, Cobalt, Metal-binding, S-adenosyl-L-methionine, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:HOMOCYSMETB12-MONOMER
MetaCyc:HOMOCYSMETB12-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.1.1.13 2026

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

More...UniPathwayi
UPA00051;UER00081

<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:
Methionine synthase (EC:2.1.1.13)
Alternative name(s):
5-methyltetrahydrofolate--homocysteine methyltransferase
Methionine synthase, vitamin-B12-dependent
Short name:
MS
<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:metH
Ordered Locus Names:b4019, JW3979
<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>OrganismiEscherichia coli (strain K12)
<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 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_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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<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
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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

Organism-specific databases

Escherichia coli strain K12 genome database

More...EcoGenei		EG10587 metH

<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

GO - Cellular componenti

View the complete GO annotation on QuickGO ...

<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_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>Mutagenesisi310C → A or S: Loss of zinc binding. Loss of catalytic activity. 1 Publication1
Mutagenesisi311C → A or S: Loss of zinc binding. Loss of catalytic activity. 1 Publication1
Mutagenesisi757D → E: Decreases activity by about 70%. 1 Publication1
Mutagenesisi757D → N: Decreases activity by about 45%. 1 Publication1
Mutagenesisi759H → G: Loss of catalytic activity. 1 Publication1
Mutagenesisi810S → A: Decreases activity by about 40%. 1 Publication1

Chemistry databases

Drug and drug target database

More...DrugBanki		DB03614 Methylcobalamin

<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_processing_section">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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002045322 – 1227Methionine synthaseAdd BLAST1226

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P13009

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

More...PaxDbi		P13009

PRoteomics IDEntifications database

More...PRIDEi		P13009

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...SWISS-2DPAGEi		P13009

<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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		4263452, 39 interactors

Protein interaction database and analysis system

More...IntActi		P13009, 13 interactors

STRING: functional protein association networks

More...STRINGi		316385.ECDH10B_4208

<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

11227
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P13009

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

More...SMRi		P13009

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		P13009

<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 keyPosition(s)DescriptionActionsGraphical viewLength
<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>Domaini2 – 325Hcy-bindingPROSITE-ProRule annotationAdd BLAST324
Domaini356 – 617Pterin-bindingPROSITE-ProRule annotationAdd BLAST262
Domaini650 – 744B12-binding N-terminalPROSITE-ProRule annotationAdd BLAST95
Domaini746 – 881B12-bindingPROSITE-ProRule annotationAdd BLAST136
Domaini897 – 1227AdoMet activationPROSITE-ProRule annotationAdd BLAST331

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Regioni834 – 835Cobalamin-binding2
Regioni1189 – 1190S-adenosyl-L-methionine binding2

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Modular enzyme with four functionally distinct domains. The isolated Hcy-binding domain catalyzes methyl transfer from free methylcobalamin to homocysteine. The Hcy-binding domain in association with the pterin-binding domain catalyzes the methylation of cob(I)alamin by methyltetrahydrofolate and the methylation of homocysteine. The B12-binding domain binds the cofactor. The AdoMet activation domain binds S-adenosyl-L-methionine. Under aerobic conditions cob(I)alamin can be converted to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L-methionine and flavodoxin regenerates methylcobalamin.1 Publication

<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 vitamin-B12 dependent methionine synthase family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG4105C3R Bacteria
COG0646 LUCA
COG1410 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000251409

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P13009

KEGG Orthology (KO)

More...KOi		K00548

Database for complete collections of gene phylogenies

More...PhylomeDBi		P13009

Family and domain databases

Conserved Domains Database

More...CDDi		cd02069 methionine_synthase_B12_BD, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.1240.10, 1 hit
3.10.196.10, 1 hit
3.20.20.20, 1 hit
3.20.20.330, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR003759 Cbl-bd_cap
IPR006158 Cobalamin-bd
IPR036724 Cobalamin-bd_sf
IPR011005 Dihydropteroate_synth-like
IPR003726 HCY_dom
IPR036589 HCY_dom_sf
IPR033706 Met_synthase_B12-bd
IPR011822 MetH
IPR036594 Meth_synthase_dom
IPR000489 Pterin-binding_dom
IPR004223 VitB12-dep_Met_synth_activ_dom
IPR037010 VitB12-dep_Met_synth_activ_sf

Pfam protein domain database

More...Pfami		View protein in Pfam
PF02310 B12-binding, 1 hit
PF02607 B12-binding_2, 1 hit
PF02965 Met_synt_B12, 1 hit
PF00809 Pterin_bind, 1 hit
PF02574 S-methyl_trans, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF000381 MetH, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM01018 B12-binding_2, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF47644 SSF47644, 1 hit
SSF51717 SSF51717, 1 hit
SSF52242 SSF52242, 1 hit
SSF56507 SSF56507, 1 hit
SSF82282 SSF82282, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR02082 metH, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50974 ADOMET_ACTIVATION, 1 hit
PS51332 B12_BINDING, 1 hit
PS51337 B12_BINDING_NTER, 1 hit
PS50970 HCY, 1 hit
PS50972 PTERIN_BINDING, 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.

P13009-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK 
        60         70         80         90        100
GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS 
       110        120        130        140        150
AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA 
       160        170        180        190        200
FRNITFDGLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF 
       210        220        230        240        250
EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG 
       260        270        280        290        300
PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ 
       310        320        330        340        350
AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI 
       360        370        380        390        400
GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI 
       410        420        430        440        450
NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG 
       460        470        480        490        500
KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI 
       510        520        530        540        550
CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK 
       560        570        580        590        600
RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG 
       610        620        630        640        650
QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ 
       660        670        680        690        700
QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG 
       710        720        730        740        750
MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV 
       760        770        780        790        800
IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL 
       810        820        830        840        850
IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY 
       860        870        880        890        900
SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR 
       910        920        930        940        950
TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF 
       960        970        980        990       1000
FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG 
      1010       1020       1030       1040       1050
LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK 
      1060       1070       1080       1090       1100
LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA 
      1110       1120       1130       1140       1150
EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT 
      1160       1170       1180       1190       1200
IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV 
      1210       1220 
EDYARRKGMS VTEVERWLAP NLGYDAD
Length:1,227
Mass (Da):135,997
Last modified:January 23, 2007 - v5
<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:i91F0CAA1E9127D9A
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 conflicti113A → R (PubMed:2185137).Curated1
Sequence conflicti113A → R (PubMed:2668277).Curated1
Sequence conflicti641S → T (PubMed:2185137).Curated1
Sequence conflicti641S → T (PubMed:2668277).Curated1
Sequence conflicti1079 – 1080QH → HD in CAA34601 (PubMed:2185137).Curated2
Sequence conflicti1195 – 1227IQRDQ…GYDAD → TSARSG in CAA34601 (PubMed:2185137).CuratedAdd BLAST33

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
X16584 Genomic DNA Translation: CAA34601.1
J04975 Unassigned DNA Translation: AAA02995.1
U00006 Genomic DNA Translation: AAC43113.1
U00096 Genomic DNA Translation: AAC76989.1
AP009048 Genomic DNA Translation: BAE78021.1

Protein sequence database of the Protein Information Resource

More...PIRi		B65209 XYECMH

NCBI Reference Sequences

More...RefSeqi		NP_418443.1, NC_000913.3
WP_000096011.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC76989; AAC76989; b4019
BAE78021; BAE78021; BAE78021

Database of genes from NCBI RefSeq genomes

More...GeneIDi		948522

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW3979
eco:b4019

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|511145.12.peg.4132

<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
X16584 Genomic DNA Translation: CAA34601.1
J04975 Unassigned DNA Translation: AAA02995.1
U00006 Genomic DNA Translation: AAC43113.1
U00096 Genomic DNA Translation: AAC76989.1
AP009048 Genomic DNA Translation: BAE78021.1
PIRiB65209 XYECMH
RefSeqiNP_418443.1, NC_000913.3
WP_000096011.1, 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
1BMTX-ray3.00A/B651-896[»]
1K7YX-ray3.00A651-1227[»]
1K98X-ray3.75A651-1227[»]
1MSKX-ray1.80A897-1227[»]
3BULX-ray2.30A649-1227[»]
3IV9X-ray3.25A649-1227[»]
3IVAX-ray2.70A649-1227[»]
6BDYX-ray1.51A897-1227[»]
6BM5X-ray1.50A897-1227[»]
6BM6X-ray1.50A897-1227[»]
ProteinModelPortaliP13009
SMRiP13009
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263452, 39 interactors
IntActiP13009, 13 interactors
STRINGi316385.ECDH10B_4208

Chemistry databases

DrugBankiDB03614 Methylcobalamin

2D gel databases

SWISS-2DPAGEiP13009

Proteomic databases

EPDiP13009
PaxDbiP13009
PRIDEiP13009

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76989; AAC76989; b4019
BAE78021; BAE78021; BAE78021
GeneIDi948522
KEGGiecj:JW3979
eco:b4019
PATRICifig|511145.12.peg.4132

Organism-specific databases

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

More...EchoBASEi		EB0582
EcoGeneiEG10587 metH

Phylogenomic databases

eggNOGiENOG4105C3R Bacteria
COG0646 LUCA
COG1410 LUCA
HOGENOMiHOG000251409
InParanoidiP13009
KOiK00548
PhylomeDBiP13009

Enzyme and pathway databases

UniPathwayi
UPA00051;UER00081

BioCyciEcoCyc:HOMOCYSMETB12-MONOMER
MetaCyc:HOMOCYSMETB12-MONOMER
BRENDAi2.1.1.13 2026

Miscellaneous databases

EvolutionaryTraceiP13009

Protein Ontology

More...PROi		PR:P13009

Family and domain databases

CDDicd02069 methionine_synthase_B12_BD, 1 hit
Gene3Di1.10.1240.10, 1 hit
3.10.196.10, 1 hit
3.20.20.20, 1 hit
3.20.20.330, 1 hit
InterProiView protein in InterPro
IPR003759 Cbl-bd_cap
IPR006158 Cobalamin-bd
IPR036724 Cobalamin-bd_sf
IPR011005 Dihydropteroate_synth-like
IPR003726 HCY_dom
IPR036589 HCY_dom_sf
IPR033706 Met_synthase_B12-bd
IPR011822 MetH
IPR036594 Meth_synthase_dom
IPR000489 Pterin-binding_dom
IPR004223 VitB12-dep_Met_synth_activ_dom
IPR037010 VitB12-dep_Met_synth_activ_sf
PfamiView protein in Pfam
PF02310 B12-binding, 1 hit
PF02607 B12-binding_2, 1 hit
PF02965 Met_synt_B12, 1 hit
PF00809 Pterin_bind, 1 hit
PF02574 S-methyl_trans, 1 hit
PIRSFiPIRSF000381 MetH, 1 hit
SMARTiView protein in SMART
SM01018 B12-binding_2, 1 hit
SUPFAMiSSF47644 SSF47644, 1 hit
SSF51717 SSF51717, 1 hit
SSF52242 SSF52242, 1 hit
SSF56507 SSF56507, 1 hit
SSF82282 SSF82282, 1 hit
TIGRFAMsiTIGR02082 metH, 1 hit
PROSITEiView protein in PROSITE
PS50974 ADOMET_ACTIVATION, 1 hit
PS51332 B12_BINDING, 1 hit
PS51337 B12_BINDING_NTER, 1 hit
PS50970 HCY, 1 hit
PS50972 PTERIN_BINDING, 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 nameiMETH_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: P13009
Secondary accession number(s): Q2M6T5
<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 historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: December 5, 2018
This is version 187 of the entry and version 5 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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