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UniProtKB - Q4JIJ3 (METH_BOVIN)

Entry version 99 (02 Dec 2020)
Sequence version 1 (02 Aug 2005)
Previous versions | rss
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Protein

Methionine synthase

Gene

MTR

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score:

Annotation score:4 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 transcript 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 methylcob(III)alamin (MeCbl) to homocysteine, yielding enzyme-bound cob(I)alamin and methionine in the cytosol. MeCbl is an active form of cobalamin (vitamin B12) used as a cofactor for methionine biosynthesis. Cob(I)alamin form is regenerated to MeCbl by a transfer of a methyl group from 5-methyltetrahydrofolate. The processing of cobalamin in the cytosol occurs in a multiprotein complex composed of at least MMACHC, MMADHC, MTRR (methionine synthase reductase) and MTR which may contribute to shuttle safely and efficiently cobalamin towards MTR in order to produce methionine.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%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 '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%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 L-methionine from L-homocysteine (MetH route).
Proteins known to be involved in this subpathway in this organism are:
  1. Methionine synthase (MTR), Methionine synthase (MTR), Methionine synthase (MTR), Methionine synthase (MTR)
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%5Fsection">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 bindingi260ZincPROSITE-ProRule annotation1
Metal bindingi323ZincPROSITE-ProRule annotation1
Metal bindingi324ZincPROSITE-ProRule annotation1
<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 sitei449SubstrateBy similarity1
Binding sitei470SubstrateBy similarity1
Binding sitei537SubstrateBy similarity1
Binding sitei579SubstrateBy similarity1
Binding sitei585SubstrateBy similarity1
Binding sitei591SubstrateBy similarity1
Metal bindingi785Cobalt (cobalamin axial ligand)By similarity1
Binding sitei830CobalaminBy similarity1
Binding sitei974S-adenosyl-L-methionineBy similarity1
Binding sitei1172S-adenosyl-L-methionine; via carbonyl oxygenBy similarity1
Binding sitei1176Cobalamin; 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

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 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%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:
Methionine synthase (EC:2.1.1.13)
Short name:
MS
Alternative name(s):
5-methyltetrahydrofolate--homocysteine methyltransferase
Cobalamin-dependent methionine synthase
Vitamin-B12 dependent methionine synthase
<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:MTR
<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>OrganismiBos taurus (Bovine)
<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 identifieri9913 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Artiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos
<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
  • UP000009136 <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: Unplaced

<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 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_00002517341 – 1265Methionine synthaseAdd BLAST1265

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei1264PhosphothreonineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

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

More...PaxDbi		Q4JIJ3

PRoteomics IDEntifications database

More...PRIDEi		Q4JIJ3

<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

Monomer. Dimer.

Forms a multiprotein complex with MMACHC, MMADHC AND MTRR.

By similarity

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		9913.ENSBTAP00000016262

<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		Q4JIJ3

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%5Fand%5Fdomains%5Fsection">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>Domaini19 – 338Hcy-bindingPROSITE-ProRule annotationAdd BLAST320
Domaini371 – 632Pterin-bindingPROSITE-ProRule annotationAdd BLAST262
Domaini662 – 759B12-binding N-terminalPROSITE-ProRule annotationAdd BLAST98
Domaini772 – 907B12-bindingPROSITE-ProRule annotationAdd BLAST136
Domaini923 – 1265AdoMet activationPROSITE-ProRule annotationAdd BLAST343

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>Regioni382 – 384Substrate bindingBy similarity3
Regioni860 – 861Cobalamin-bindingBy similarity2
Regioni1227 – 1228S-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

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		KOG1579, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q4JIJ3

Database of Orthologous Groups

More...OrthoDBi		731388at2759

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%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.

Q4JIJ3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAPTLQDLTP SAGMKKTLQD EIEAILQERI MVLDGGMGTM IQRHKLSEED 
        60         70         80         90        100
FRGQEFKDHA RPLKGNNDIL SITQPNVIYQ IHKEYLLAGA DIIETNTFSS 
       110        120        130        140        150
TSIAQADYGL EHLAYRMNMC SAGVARKAAE DISLQTGIKR YVAGALGPTN 
       160        170        180        190        200
KTLSVSPSVE RPDYRNITFD ELVEAYKEQA KGLLDGGVDI LLIETIFDTA 
       210        220        230        240        250
NAKAALFAVQ KLFEEEYVPR PVFISGTIVD KSGRTLSGQT GEAFVISVSH 
       260        270        280        290        300
ADPLCIGLNC ALGAAEMRPF IETIGKCTTA YVLCYPNAGL PNTFGDYDET 
       310        320        330        340        350
PHVMAMHLKD FAVDGLVNIV GGCCGTTPDH IREIAEAVKN CKPRVPPATV 
       360        370        380        390        400
FEGHMLLSGL EPFRIGPYTN FVNIGERCNV AGSRRFAKLI MAGNYEEALS 
       410        420        430        440        450
VAKMQVEMGA QVLDINMDDG MLDGPSAMTR FCNFIASEPD IAKVPLCIDS 
       460        470        480        490        500
SNFAVIEAGL KCCQGKCIVN SISLKEGEDD FLEKARKIKK FGAAVVVMAF 
       510        520        530        540        550
DEEGQATETD PKIRVCTRAY HLLLKKLGFN PNDIIFDPNI LTIGTGMEEH 
       560        570        580        590        600
NLYAVNFINA TKVIKETLPG AKVSGGLSNL SFSFRGMEAI REAMHGVFLY 
       610        620        630        640        650
HAIKFGMDMG IVNAGSLPVY DDIHKELLQL CEDLIWNRDP EATEKLLHYA 
       660        670        680        690        700
QTQGKGGKKV IQTDEWRNGP LEERLEYALV KGIEKYIIED TEEARLNQEK 
       710        720        730        740        750
YPRPLNIIEG PLMNGMKIVG DLFGAGKMFL PQVIKSARVM KKAVGHLIPF 
       760        770        780        790        800
MEKEREETKV LTGKIEDEDP YQGTIVLATV KGDVHDIGKN IVGVVLGCNN 
       810        820        830        840        850
FRVIDLGVMT PCDKILKAAL DHKADIIGLS GLITPSLDEM IFVAKEMERL 
       860        870        880        890        900
AIKIPLLIGG ATTSRTHTAV KIAPRYSAPV IHVLDASKSV VVCSQLLDEN 
       910        920        930        940        950
LKDEYFEEIL EEYEDIRQDH YESLKERRYL TLRQARENGF HIDWLSEPPP 
       960        970        980        990       1000
VKPTFLGTRV FEDYDLQKLV DYIDWKPFFD VWQLRGKYPN RGFPKIFDDK 
      1010       1020       1030       1040       1050
TVGEEAKKVY DDAQNMLQAL ISQKKLQARG VVGFWPAQSI QDDIHLYAEG 
      1060       1070       1080       1090       1100
AVPQASEPIA TFYGLRQQAE KDSASSDPYL CLSDFIAPLH SGIPDYLGLF 
      1110       1120       1130       1140       1150
AVACFGVEEL SKAYEEECDD YSSIMVKALG DRLAEAFAEE LHERARRELW 
      1160       1170       1180       1190       1200
GYCSGEQLAV ADLRRLRYEG IRPAPGYPSQ PDHTEKLTVW RLADVEQRTG 
      1210       1220       1230       1240       1250
IRLTESLAMA PASAVSGLYF SNLKSKYFAV GKISKDQIED YASRKNMSVA 
      1260 
EVEKWLGPIL GYDTD
Length:1,265
Mass (Da):140,478
Last modified:August 2, 2005 - 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:i7E1E03AB95134529
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
DQ084519 mRNA Translation: AAY86762.1

NCBI Reference Sequences

More...RefSeqi		NP_001025469.1, NM_001030298.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		280869

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		bta:280869

<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
DQ084519 mRNA Translation: AAY86762.1
RefSeqiNP_001025469.1, NM_001030298.1

3D structure databases

SMRiQ4JIJ3
ModBaseiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000016262

Proteomic databases

PaxDbiQ4JIJ3
PRIDEiQ4JIJ3

Genome annotation databases

GeneIDi280869
KEGGibta:280869

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		4548

Phylogenomic databases

eggNOGiKOG1579, Eukaryota
InParanoidiQ4JIJ3
OrthoDBi731388at2759

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

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 nameiMETH_BOVIN
<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: Q4JIJ3
<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: October 3, 2006
Last sequence update: August 2, 2005
Last modified: December 2, 2020
This is version 99 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 programChordata 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

Reference proteome

Documents

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