SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9KUW9

- METH_VIBCH

UniProt

Q9KUW9 - METH_VIBCH

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Methionine synthase

Gene
metH, VC_0390
Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Status
Reviewed - Annotation score: 4 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. cobalamin binding Source: UniProtKB-KW
  2. methionine synthase activity Source: TIGR
  3. S-adenosylmethionine-homocysteine S-methyltransferase activity Source: InterPro
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. methionine biosynthetic process Source: TIGR
  2. 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

BioCyciVCHO:VC0390-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:VC_0390
OrganismiVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Taxonomic identifieri243277 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
ProteomesiUP000000584: 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 synthasePRO_0000204538Add
BLAST

Proteomic databases

PRIDEiQ9KUW9.

Interactioni

Protein-protein interaction databases

STRINGi243277.VC0390.

Structurei

3D structure databases

ProteinModelPortaliQ9KUW9.
SMRiQ9KUW9. Positions 654-1224.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 326321Hcy-bindingAdd
BLAST
Domaini357 – 618262Pterin-bindingAdd
BLAST
Domaini651 – 74595B12-binding N-terminalAdd
BLAST
Domaini747 – 882136B12-bindingAdd
BLAST
Domaini898 – 1226329AdoMet activationAdd
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.
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.

Q9KUW9-1 [UniParc]FASTAAdd to Basket

« Hide

MGKEVRQQLE QQLKQRILLI DGGMGTMIQS YKLQEEDYRG ARFVDWHCDL     50
KGNNDLLVLT QPQIIKEIHS AYLEAGADIL ETNTFNSTTI AMADYDMQSL 100
SAEINFAAAK LAREVADEWT AKDPSRPRYV AGVLGPTNRT CSISPDVNDP 150
GFRNVTFDGL VEAYSESTRA LIKGGSDLIL IETIFDTLNA KACAFAVDSV 200
FEELGISLPV MISGTITDAS GRTLSGQTTE AFYNALRHVR PISFGLNCAL 250
GPDELRQYVE ELSRISECYV SAHPNAGLPN AFGEYDLSAE EMAEHIAEWA 300
QAGFLNLVGG CCGTTPEHIA AIAKAVEGVK PRALPDLKVE CRLSGLEPLN 350
IGPETLFVNV GERTNVTGSA RFKRLIKEEQ YDEALDVARE QVENGAQIID 400
INMDEGMLDA EACMVRFLNL CASEPEISKV PVMVDSSKWE VIEAGLKCIQ 450
GKGIVNSISL KEGKEKFIAQ AKLVRRYGAA VIVMAFDEVG QADTRERKLE 500
ICRRAYHILV DEVGFPPEDI IFDPNIFAVA TGIDEHNNYA LDFINAVADI 550
KRELPHAMIS GGVSNVSFSF RGNNYVREAI HAVFLYHCFK HGMDMGIVNA 600
GQLEIYDNVP LKLREAVEDV ILNRRSDGTE RLLEIAEAYR ENSVGKEEDA 650
SALEWRAWPV AKRLEHALVK GITEFIVQDT EEARQQASKP LEVIEGPLMD 700
GMNVVGDLFG EGKMFLPQVV KSARVMKQAV AYLEPFINAQ KSGSTSNGKI 750
LLATVKGDVH DIGKNIVGVV LQCNNFEIID LGVMVPCEQI LKVAREQNVD 800
IIGLSGLITP SLDEMVHVAK EMERQGFELP LLIGGATTSK AHTAVKIEQN 850
YHAPVVYVNN ASRAVGVCTS LLSDEQRPGF IERLDLDYER TRDQHARKTP 900
KSRPVTLEQA RANKAALDWA NYTPPAPAKP GVHVFENIAL ATLRPYIDWT 950
PFFMTWSLMG KYPAILEHEE VGEEAKRLFH DANALLDKVE REGLLKASGM 1000
CALFPAASVG DDIEVYSDES RTQVAHVLYN LRQQTEKPKG ANYCLSDYVA 1050
PKESGKRDWI GAFAVTGGIG ERALADAYKA QGDDYNAIMI QAVADRLAEA 1100
FAEYLHEKVR KEIWGYASDE NLSNDDLIRE RYQGIRPAPG YPACPEHTEK 1150
ATLWQMLNVE ETIGMSLTTS YAMWPGASVS GWYFSHPDSR YFAVAQIQPD 1200
QLHSYAERKG WRLEEAEKWL APNLDA 1226
Length:1,226
Mass (Da):135,793
Last modified:October 1, 2000 - v1
Checksum:i5CF4AB07A738D74F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE003852 Genomic DNA. Translation: AAF93563.1.
PIRiE82328.
RefSeqiNP_230044.1. NC_002505.1.

Genome annotation databases

EnsemblBacteriaiAAF93563; AAF93563; VC_0390.
GeneIDi2614987.
KEGGivch:VC0390.
PATRICi20079861. VBIVibCho83274_0365.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE003852 Genomic DNA. Translation: AAF93563.1 .
PIRi E82328.
RefSeqi NP_230044.1. NC_002505.1.

3D structure databases

ProteinModelPortali Q9KUW9.
SMRi Q9KUW9. Positions 654-1224.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243277.VC0390.

Proteomic databases

PRIDEi Q9KUW9.

Protocols and materials databases

DNASUi 2614987.
Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAF93563 ; AAF93563 ; VC_0390 .
GeneIDi 2614987.
KEGGi vch:VC0390.
PATRICi 20079861. VBIVibCho83274_0365.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00051 ; UER00081 .
BioCyci VCHO:VC0390-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: ATCC 39315 / El Tor Inaba N16961.

Entry informationi

Entry nameiMETH_VIBCH
AccessioniPrimary (citable) accession number: Q9KUW9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 87 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, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi