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Q7MHB1

- METH_VIBVY

UniProt

Q7MHB1 - METH_VIBVY

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Protein
Methionine synthase
Gene
metH, VV2960
Organism
Vibrio vulnificus (strain YJ016)
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

BioCyciVVUL196600:GJ9W-3052-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:VV2960
OrganismiVibrio vulnificus (strain YJ016)
Taxonomic identifieri196600 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
ProteomesiUP000002675: Chromosome I

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_0000204543Add
BLAST

Proteomic databases

PRIDEiQ7MHB1.

Interactioni

Protein-protein interaction databases

STRINGi196600.VV2960.

Structurei

3D structure databases

ProteinModelPortaliQ7MHB1.
SMRiQ7MHB1. 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.

Q7MHB1-1 [UniParc]FASTAAdd to Basket

« Hide

MGSNIRAQIE AQLKQRILLI DGGMGTMIQG YKLQEQDYRG ERFADWHSDL     50
KGNNDLLVLT QPQLIKEIHH AYLEAGADIL ETNTFNATTI AMADYDMESL 100
SEEINFAAAK LAREAADEWT AKNPAKPRYV AGVLGPTNRT CSISPDVNDP 150
GYRNVSFDEL VEAYSESTRA LIRGGSDLIL IETIFDTLNA KACAFAVESV 200
FEELGFALPV MISGTITDAS GRTLSGQTTE AFYNSLRHVR PISFGLNCAL 250
GPDELRPYVE ELSRISETFV STHPNAGLPN AFGEYDLSPE EMAEHVKEWA 300
QSGFLNLIGG CCGTTPEHIR HMAMAVEGES PRVLPEIPVA CRLSGLEPLT 350
IAKDTLFVNV GERTNVTGSA RFKRLIKEEL YDEALDVARE QVENGAQIID 400
INMDEGMLDA EACMVRFLNL CASEPEISKV PIMVDSSKWE VIEAGLKCIQ 450
GKGIVNSISL KEGKEKFVEQ AKLIRRYGAA VIVMAFDEVG QADTRERKLE 500
ICTKAYRILV DEVGFPPEDV IFDPNIFAVA TGIDEHNNYA VDFIEAVADI 550
KRDLPHAMIS GGVSNVSFSF RGNNYVREAI HAVFLYHCFK NGMDMGIVNA 600
GQLEIYDNVP EKLREAVEDV VLNRRDDATE RLLEIAEEYR ENAVGKQEDA 650
SALEWRTWSV EKRLEHALVK GITEFIVEDT EEARLNASKP LEVIEGPLMD 700
GMNVVGDLFG EGKMFLPQVV KSARVMKQAV AHLEPFINAS KQVGSSNGKI 750
LLATVKGDVH DIGKNIVGVV LQCNNYEIID LGVMVPCEQI LKVAKEQQVD 800
IIGLSGLITP SLDEMVHVAK EMERLGFDLP LLIGGATTSK AHTAVKIEQN 850
YSHPVVYVNN ASRAVGVCTS LLSDELRPAF VERLQADYEL VRDQHNRKKP 900
RTKPVTLEAA RANKVAIDWQ SYTPPAPSQP GVHVFDDFDV ATLRQYIDWT 950
PFFLTWSLVG KYPTIFEHEE VGEEAKRLFE DANEWLDRIE QEGLLKARGM 1000
CGLFPAASVG DDIEVYTDES RTQVAKVLHN LRQQTEKPKG ANYCLSDYVA 1050
PKESGKKDWI GAFAVTGGVN ERELADQFKA QGDDYNAIMI QAVADRLAEA 1100
FAEYLHERVR KEIWGYAADE NLSNEELIRE KYQGIRPAPG YPACPEHTEK 1150
GPLWELLNVE ETIGMSLTSS YAMWPGASVS GWYFSHPDSR YFAIAQIQQD 1200
QVESYAKRKG WDLLEAEKWL GPNING 1226
Length:1,226
Mass (Da):136,333
Last modified:December 15, 2003 - v1
Checksum:i299B647CC6D24028
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000037 Genomic DNA. Translation: BAC95724.1.
RefSeqiNP_935753.1. NC_005139.1.
WP_011151258.1. NC_005139.1.

Genome annotation databases

EnsemblBacteriaiBAC95724; BAC95724; BAC95724.
GeneIDi2625802.
KEGGivvy:VV2960.
PATRICi20172780. VBIVibVul40472_2940.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000037 Genomic DNA. Translation: BAC95724.1 .
RefSeqi NP_935753.1. NC_005139.1.
WP_011151258.1. NC_005139.1.

3D structure databases

ProteinModelPortali Q7MHB1.
SMRi Q7MHB1. Positions 654-1224.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 196600.VV2960.

Proteomic databases

PRIDEi Q7MHB1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAC95724 ; BAC95724 ; BAC95724 .
GeneIDi 2625802.
KEGGi vvy:VV2960.
PATRICi 20172780. VBIVibVul40472_2940.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00051 ; UER00081 .
BioCyci VVUL196600:GJ9W-3052-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: YJ016.

Entry informationi

Entry nameiMETH_VIBVY
AccessioniPrimary (citable) accession number: Q7MHB1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: December 15, 2003
Last modified: September 3, 2014
This is version 79 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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