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Q87L95

- METH_VIBPA

UniProt

Q87L95 - METH_VIBPA

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Protein
Methionine synthase
Gene
metH, VP2717
Organism
Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

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.

Catalytic activityi

5-methyltetrahydrofolate + L-homocysteine = tetrahydrofolate + L-methionine.

Cofactori

Methylcobalamin (MeCBL) By similarity.
Binds 1 zinc ion per subunit By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi248 – 2481Zinc By similarity
Metal bindingi311 – 3111Zinc By similarity
Metal bindingi312 – 3121Zinc By similarity
Metal bindingi760 – 7601Cobalt (cobalamin axial ligand) By similarity
Binding sitei805 – 8051Cobalamin By similarity
Binding sitei948 – 9481S-adenosyl-L-methionine By similarity
Binding sitei1136 – 11361S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding sitei1140 – 11401Cobalamin; via carbonyl oxygen By similarity

GO - Molecular functioni

  1. S-adenosylmethionine-homocysteine S-methyltransferase activity Source: InterPro
  2. cobalamin binding Source: UniProtKB-KW
  3. methionine synthase activity Source: UniProtKB-EC
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. pteridine-containing compound metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Methionine biosynthesis

Keywords - Ligandi

Cobalamin, Cobalt, Metal-binding, S-adenosyl-L-methionine, Zinc

Enzyme and pathway databases

BioCyciVPAR223926:GHK4-2806-MONOMER.
UniPathwayiUPA00051; UER00081.

Names & Taxonomyi

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
Gene namesi
Name:metH
Ordered Locus Names:VP2717
OrganismiVibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
Taxonomic identifieri223926 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
ProteomesiUP000002493: Chromosome 1

Subcellular locationi

GO - Cellular componenti

  1. intracellular Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12261226Methionine synthase
PRO_0000204541Add
BLAST

Proteomic databases

PRIDEiQ87L95.

Interactioni

Protein-protein interaction databases

STRINGi223926.VP2717.

Structurei

3D structure databases

ProteinModelPortaliQ87L95.
SMRiQ87L95. Positions 654-1224.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 326321Hcy-binding
Add
BLAST
Domaini357 – 618262Pterin-binding
Add
BLAST
Domaini651 – 74595B12-binding N-terminal
Add
BLAST
Domaini747 – 882136B12-binding
Add
BLAST
Domaini898 – 1226329AdoMet activation
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni835 – 8362Cobalamin-binding By similarity
Regioni1191 – 11922S-adenosyl-L-methionine binding By similarity

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.

Sequence similaritiesi

Contains 1 B12-binding domain.
Contains 1 Hcy-binding domain.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG1410.
HOGENOMiHOG000251409.
KOiK00548.
OMAiLTEHYAM.
OrthoDBiEOG6091CH.

Family and domain databases

Gene3Di1.10.1240.10. 1 hit.
3.10.196.10. 1 hit.
3.20.20.20. 1 hit.
3.20.20.330. 1 hit.
3.40.50.280. 1 hit.
InterProiIPR003759. Cbl-bd_cap.
IPR006158. Cobalamin-bd.
IPR011005. Dihydropteroate_synth-like.
IPR011822. MetH.
IPR000489. Pterin-binding.
IPR003726. S_MeTrfase.
IPR004223. VitB12-dep_Met_synth_activ_dom.
[Graphical view]
PfamiPF02310. 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.
[Graphical view]
PIRSFiPIRSF000381. MetH. 1 hit.
SMARTiSM01018. B12-binding_2. 1 hit.
[Graphical view]
SUPFAMiSSF47644. SSF47644. 1 hit.
SSF51717. SSF51717. 1 hit.
SSF52242. SSF52242. 1 hit.
SSF56507. SSF56507. 1 hit.
SSF82282. SSF82282. 1 hit.
TIGRFAMsiTIGR02082. metH. 1 hit.
PROSITEiPS50974. ADOMET_ACTIVATION. 1 hit.
PS51332. B12_BINDING. 1 hit.
PS51337. B12_BINDING_NTER. 1 hit.
PS50970. HCY. 1 hit.
PS50972. PTERIN_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q87L95-1 [UniParc]FASTAAdd to Basket

« Hide

MGSKVRQQIE AQLKQRILLI DGGMGTMIQG YKLEEQDYRG ERFANWHCDL     50
KGNNDLLVLS QPQLIKEIHS AYLEAGADIL ETNTFNATTI AMADYEMESL 100
SEEINFAAAK LAREVADEWT AKTPDKPRYV AGVLGPTNRT CSISPDVNDP 150
GYRNVSFDEL VEAYSESTRA LIRGGADLIL IETIFDTLNA KACAFAVDSV 200
FEELGVALPV MISGTITDAS GRTLSGQTTE AFYNSLRHVR PLSFGLNCAL 250
GPDELRPYVE ELSRISESFV SAHPNAGLPN AFGEYDLSPE DMAEHVKEWA 300
SSGFLNLIGG CCGTTPEHIR QMAQAVEGVT PRALPDLPVA CRLSGLEPLT 350
IEKETLFINV GERTNVTGSA RFKRLIKEEQ YDEALEVARQ QVENGAQIID 400
INMDEGMLDA QACMVRFLNL CASEPEISKV PIMVDSSKWE VIEAGLKCIQ 450
GKGIVNSISL KEGKEKFVEQ AKLIRRYGAA VIVMAFDEVG QAETRTRKLE 500
ICTNAYRILV DEVGFPPEDI IFDPNIFAVA TGIDEHNNYA VDFIEAVADI 550
KRDLPHAMIS GGVSNVSFSF RGNNYVREAI HAVFLYHCFK NGMDMGIVNA 600
GQLEIYDNVP EKLREAVEDV VLNRRDDATE RLLDIAAEYA DKGVGKEEDA 650
SALEWRTWPV AKRLEHALVK GITEFIVADT EEARVNAVKP LEVIEGPLMD 700
GMNVVGDLFG EGKMFLPQVV KSARVMKQAV AHLEPFINAE KQSGSSNGKI 750
LLATVKGDVH DIGKNIVGVV LQCNNYEIID LGVMVPCEKI LKVAIEENVD 800
IIGLSGLITP SLDEMVHVAK EMERLNFDLP LLIGGATTSK AHTAVKIEQN 850
YKNPVVYVNN ASRAVGVCSS LLSDERRPAF IEKLDADYER VRDQHNRKKP 900
RTKPVTLEQA RANKVAIDWD AYTPPVPAKP GLHIFDDFDV ATLRKYIDWT 950
PFFMTWSLVG KYPTIFKHEE VGEEAQRLFH DANELLDRVE REGLLKARGI 1000
CGLFPAASVG DDIEVYTDES RTEVAKVLRN LRQQTEKPKG FNYCLSDYIA 1050
PKESGKQDWV GAFAVTGGIG ERELADEYKA QGDDYNAIMI QAVADRLAEA 1100
FAEYLHERVR KEIWGYAADE NLSNDELIRE KYQGIRPAPG YPACPEHTEK 1150
GPLWELLNVE ENIGMSLTTS YAMYPGASVS GWYFSHPDSR YFAIAQIQDD 1200
QLESYADRKG WDRIEAEKWL GPNING 1226
Length:1,226
Mass (Da):136,218
Last modified:June 1, 2003 - v1
Checksum:i2F7A3269FB7C20A9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000031 Genomic DNA. Translation: BAC60980.1.
RefSeqiNP_799096.1. NC_004603.1.

Genome annotation databases

EnsemblBacteriaiBAC60980; BAC60980; BAC60980.
GeneIDi1190262.
KEGGivpa:VP2717.
PATRICi20143630. VBIVibPar50997_2612.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000031 Genomic DNA. Translation: BAC60980.1 .
RefSeqi NP_799096.1. NC_004603.1.

3D structure databases

ProteinModelPortali Q87L95.
SMRi Q87L95. Positions 654-1224.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 223926.VP2717.

Proteomic databases

PRIDEi Q87L95.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAC60980 ; BAC60980 ; BAC60980 .
GeneIDi 1190262.
KEGGi vpa:VP2717.
PATRICi 20143630. VBIVibPar50997_2612.

Phylogenomic databases

eggNOGi COG1410.
HOGENOMi HOG000251409.
KOi K00548.
OMAi LTEHYAM.
OrthoDBi EOG6091CH.

Enzyme and pathway databases

UniPathwayi UPA00051 ; UER00081 .
BioCyci VPAR223926:GHK4-2806-MONOMER.

Family and domain databases

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.
3.40.50.280. 1 hit.
InterProi IPR003759. Cbl-bd_cap.
IPR006158. Cobalamin-bd.
IPR011005. Dihydropteroate_synth-like.
IPR011822. MetH.
IPR000489. Pterin-binding.
IPR003726. S_MeTrfase.
IPR004223. VitB12-dep_Met_synth_activ_dom.
[Graphical view ]
Pfami 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.
[Graphical view ]
PIRSFi PIRSF000381. MetH. 1 hit.
SMARTi SM01018. B12-binding_2. 1 hit.
[Graphical view ]
SUPFAMi SSF47644. SSF47644. 1 hit.
SSF51717. SSF51717. 1 hit.
SSF52242. SSF52242. 1 hit.
SSF56507. SSF56507. 1 hit.
SSF82282. SSF82282. 1 hit.
TIGRFAMsi TIGR02082. metH. 1 hit.
PROSITEi 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.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae."
    Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.
    Lancet 361:743-749(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: RIMD 2210633.

Entry informationi

Entry nameiMETH_VIBPA
AccessioniPrimary (citable) accession number: Q87L95
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: June 1, 2003
Last modified: July 9, 2014
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome

Documents

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

External Data

Dasty 3

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