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Entry version 89 (10 Feb 2021)
Sequence version 1 (01 Jun 2001)
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Protein

Methionine synthase

Gene

metH

Organism
Aliivibrio fischeri (Vibrio fischeri)
Status
Reviewed-Annotation score:

Annotation score:3 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>
-Protein inferred from homologyi <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 (By similarity).

By similarity

Miscellaneous

L-homocysteine is bound via the zinc atom.By similarity

<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). 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 <a href="http://www.uniprot.org/help/function_section">Function</a> 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 bindingi249ZincPROSITE-ProRule annotation1
Metal bindingi312ZincPROSITE-ProRule annotation1
Metal bindingi313ZincPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei696Methylcob(III)alaminBy similarity1
Metal bindingi761Cobalt (methylcob(III)alamin axial ligand)By similarity1
Binding sitei806Methylcob(III)alaminBy similarity1
Binding sitei810Methylcob(III)alaminBy similarity1
Binding sitei862Methylcob(III)alamin; via amide nitrogenBy similarity1
Binding sitei949S-adenosyl-L-methionineBy similarity1
Binding sitei1137S-adenosyl-L-methionine; via carbonyl oxygenBy similarity1

<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

GO - Biological processi

<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

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
<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>OrganismiAliivibrio fischeri (Vibrio fischeri)
<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 identifieri668 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeAliivibrio

<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 '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_00002045401 – 1226Methionine synthaseAdd BLAST1226

<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

3D structure databases

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

More...
SMRi
Q9AJQ8

Database of comparative protein structure models

More...
ModBasei
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

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>Domaini7 – 327Hcy-bindingPROSITE-ProRule annotationAdd BLAST321
Domaini358 – 619Pterin-bindingPROSITE-ProRule annotationAdd BLAST262
Domaini652 – 746B12-binding N-terminalPROSITE-ProRule annotationAdd BLAST95
Domaini748 – 883B12-bindingPROSITE-ProRule annotationAdd BLAST136
Domaini899 – 1226AdoMet activationPROSITE-ProRule annotationAdd BLAST328

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>Regioni758 – 762Methylcob(III)alamin bindingBy similarity5
Regioni1192 – 1193S-adenosyl-L-methionine bindingBy similarity2

<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 (By similarity).By similarity

<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

Keywords - Domaini

Repeat

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>. 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_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.

Q9AJQ8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAGSNIKVQI EKQLSERILL IDGGMGTMIQ GYKFEEKDYR GGRFNQWHCD
60 70 80 90 100
LKGNNDLLVL SQPQIIRDIH EAYLEAGADI LETNTFNATT IAMADYDMES
110 120 130 140 150
LSEEINFEAA KLAREVADKW TEKTPNKPRY VAGVLGPTNR TCSISPDVND
160 170 180 190 200
PGFRNVSFDE LVEAYSESTR ALIRGGSDLI LIETIFDTLN AKACSFAVES
210 220 230 240 250
VFEELGITLP VMISGTITDA SGRTLSGQTT EAFYNALRHV KPISFGLNCA
260 270 280 290 300
LGPDELREYV SELSRISECY VSAHPNAGLP NAFGEYDLSP EDMAEHVAEW
310 320 330 340 350
ASSGFLNLIG GCCGTTPEHI RQMALVVEGV KPRQLPELPV ACRLSGLEPL
360 370 380 390 400
TIEKDSLFIN VGERTNVTGS ARFKRLIKEE LYDEALSVAQ EQVENGAQII
410 420 430 440 450
DINMDEGMLD AEACMVRFLN LCASEPEISK VPVMVDSSKW EVIEAGLKCI
460 470 480 490 500
QGKGIVNSIS LKEGKEKFVH QAKLIRRYGA AVIVMAFDEV GQADTRERKI
510 520 530 540 550
EICTNAYNIL VDEVGFPPED IIFDPNIFAV ATGIDEHNNY AVDFIEAVGD
560 570 580 590 600
IKRTLPHAMI SGGVSNVSFS FRGNNYVREA IHAVFLYHCF KNGMDMGIVN
610 620 630 640 650
AGQLEIYDNV PEDLREAVED VVLNRRDDST ERLLDIATEY LERAVGKVED
660 670 680 690 700
KSALEWRDWP VEKRLEHSLV KGITEFIVED TEEARINAER PIEVIEGPLM
710 720 730 740 750
DGMNVVGDLF GEGKMFLPQV VKSARVMKQA VAHLEPFINA SKEVGATNGK
760 770 780 790 800
ILLATVKGDV HDIGKNIVGV VLQCNNYEII DLGVMVSCET ILKVAKEENV
810 820 830 840 850
DIIGLSGLIT PSLDEMVHVA KEMERQGFDL PLLIGGATTS KAHTAVKIEQ
860 870 880 890 900
NYSQPVVYVN NASRAVGVCT SLLSNELKPS FVEKLDIDYE RVREQHSRKQ
910 920 930 940 950
PRTKPVTLEV ARANKVAIDW ASYTPPVPLK PGVHIFDNFD VSTLRNYIDW
960 970 980 990 1000
TPFFMTWSLV GKYPKILEHE EVGEEAKRLF KDANDLLDRV EKEGLLKARG
1010 1020 1030 1040 1050
MCALFPASSV GDDIEVYTDE SRTTVAKVLH NLRQQTEKPK GFNYCLSDYI
1060 1070 1080 1090 1100
APKESGKNDW IGGFAVTGGI GERELADEYK ANGDDYNAIM IQAVADRLAE
1110 1120 1130 1140 1150
AFAEYLHEKV RKEIWGYSPN ETLSNDDLIR EKYQGIRPAP GYPACPEHTE
1160 1170 1180 1190 1200
KGALWELMNV EESIGMSLTS SYAMWPGASV SGMYFSHPDS RYFAIAQIQQ
1210 1220
DQAESYADRK GWNMLEAEKW LGPNLN
Length:1,226
Mass (Da):136,266
Last modified:June 1, 2001 - 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:iAF210E43E119E50C
GO

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
AB039955 Genomic DNA Translation: BAB39355.1

<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
AB039955 Genomic DNA Translation: BAB39355.1

3D structure databases

SMRiQ9AJQ8
ModBaseiSearch...

Enzyme and pathway databases

UniPathwayiUPA00051;UER00081

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

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 nameiMETH_ALIFS
<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: Q9AJQ8
<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: November 22, 2005
Last sequence update: June 1, 2001
Last modified: February 10, 2021
This is version 89 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 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
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