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Q9KUW9 (METH_VIBCH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methionine synthase

EC=2.1.1.13
Alternative name(s):
5-methyltetrahydrofolate--homocysteine methyltransferase
Methionine synthase, vitamin-B12 dependent
Short name=MS
Gene names
Name:metH
Ordered Locus Names:VC_0390
OrganismVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) [Reference proteome] [HAMAP]
Taxonomic identifier243277 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length1226 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 activity

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

Cofactor

Methylcobalamin (MeCBL) By similarity.

Binds 1 zinc ion per subunit By similarity.

Pathway

Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetH route): step 1/1.

Domain

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.

Miscellaneous

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

Sequence similarities

Belongs to the vitamin-B12 dependent methionine synthase family.

Contains 1 AdoMet activation domain.

Contains 1 B12-binding domain.

Contains 1 B12-binding N-terminal domain.

Contains 1 Hcy-binding domain.

Contains 1 pterin-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12261226Methionine synthase
PRO_0000204538

Regions

Domain6 – 326321Hcy-binding
Domain357 – 618262Pterin-binding
Domain651 – 74595B12-binding N-terminal
Domain747 – 882136B12-binding
Domain898 – 1226329AdoMet activation
Region835 – 8362Cobalamin-binding By similarity
Region1191 – 11922S-adenosyl-L-methionine binding By similarity

Sites

Metal binding2481Zinc By similarity
Metal binding3111Zinc By similarity
Metal binding3121Zinc By similarity
Metal binding7601Cobalt (cobalamin axial ligand) By similarity
Binding site8051Cobalamin By similarity
Binding site9481S-adenosyl-L-methionine By similarity
Binding site11361S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site11401Cobalamin; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9KUW9 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 5CF4AB07A738D74F

FASTA1,226135,793
        10         20         30         40         50         60 
MGKEVRQQLE QQLKQRILLI DGGMGTMIQS YKLQEEDYRG ARFVDWHCDL KGNNDLLVLT 

        70         80         90        100        110        120 
QPQIIKEIHS AYLEAGADIL ETNTFNSTTI AMADYDMQSL SAEINFAAAK LAREVADEWT 

       130        140        150        160        170        180 
AKDPSRPRYV AGVLGPTNRT CSISPDVNDP GFRNVTFDGL VEAYSESTRA LIKGGSDLIL 

       190        200        210        220        230        240 
IETIFDTLNA KACAFAVDSV FEELGISLPV MISGTITDAS GRTLSGQTTE AFYNALRHVR 

       250        260        270        280        290        300 
PISFGLNCAL GPDELRQYVE ELSRISECYV SAHPNAGLPN AFGEYDLSAE EMAEHIAEWA 

       310        320        330        340        350        360 
QAGFLNLVGG CCGTTPEHIA AIAKAVEGVK PRALPDLKVE CRLSGLEPLN IGPETLFVNV 

       370        380        390        400        410        420 
GERTNVTGSA RFKRLIKEEQ YDEALDVARE QVENGAQIID INMDEGMLDA EACMVRFLNL 

       430        440        450        460        470        480 
CASEPEISKV PVMVDSSKWE VIEAGLKCIQ GKGIVNSISL KEGKEKFIAQ AKLVRRYGAA 

       490        500        510        520        530        540 
VIVMAFDEVG QADTRERKLE ICRRAYHILV DEVGFPPEDI IFDPNIFAVA TGIDEHNNYA 

       550        560        570        580        590        600 
LDFINAVADI KRELPHAMIS GGVSNVSFSF RGNNYVREAI HAVFLYHCFK HGMDMGIVNA 

       610        620        630        640        650        660 
GQLEIYDNVP LKLREAVEDV ILNRRSDGTE RLLEIAEAYR ENSVGKEEDA SALEWRAWPV 

       670        680        690        700        710        720 
AKRLEHALVK GITEFIVQDT EEARQQASKP LEVIEGPLMD GMNVVGDLFG EGKMFLPQVV 

       730        740        750        760        770        780 
KSARVMKQAV AYLEPFINAQ KSGSTSNGKI LLATVKGDVH DIGKNIVGVV LQCNNFEIID 

       790        800        810        820        830        840 
LGVMVPCEQI LKVAREQNVD IIGLSGLITP SLDEMVHVAK EMERQGFELP LLIGGATTSK 

       850        860        870        880        890        900 
AHTAVKIEQN YHAPVVYVNN ASRAVGVCTS LLSDEQRPGF IERLDLDYER TRDQHARKTP 

       910        920        930        940        950        960 
KSRPVTLEQA RANKAALDWA NYTPPAPAKP GVHVFENIAL ATLRPYIDWT PFFMTWSLMG 

       970        980        990       1000       1010       1020 
KYPAILEHEE VGEEAKRLFH DANALLDKVE REGLLKASGM CALFPAASVG DDIEVYSDES 

      1030       1040       1050       1060       1070       1080 
RTQVAHVLYN LRQQTEKPKG ANYCLSDYVA PKESGKRDWI GAFAVTGGIG ERALADAYKA 

      1090       1100       1110       1120       1130       1140 
QGDDYNAIMI QAVADRLAEA FAEYLHEKVR KEIWGYASDE NLSNDDLIRE RYQGIRPAPG 

      1150       1160       1170       1180       1190       1200 
YPACPEHTEK ATLWQMLNVE ETIGMSLTTS YAMWPGASVS GWYFSHPDSR YFAVAQIQPD 

      1210       1220 
QLHSYAERKG WRLEEAEKWL APNLDA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE003852 Genomic DNA. Translation: AAF93563.1.
PIRE82328.
RefSeqNP_230044.1. NC_002505.1.

3D structure databases

ProteinModelPortalQ9KUW9.
SMRQ9KUW9. Positions 654-1224.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243277.VC0390.

Proteomic databases

PRIDEQ9KUW9.

Protocols and materials databases

DNASU2614987.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF93563; AAF93563; VC_0390.
GeneID2614987.
KEGGvch:VC0390.
PATRIC20079861. VBIVibCho83274_0365.

Phylogenomic databases

eggNOGCOG1410.
KOK00548.
OMALTEHYAM.
OrthoDBEOG6091CH.

Enzyme and pathway databases

BioCycVCHO:VC0390-MONOMER.
UniPathwayUPA00051; UER00081.

Family and domain databases

Gene3D1.10.1240.10. 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.
InterProIPR003759. 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]
PfamPF02310. 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]
PIRSFPIRSF000381. MetH. 1 hit.
SMARTSM01018. B12-binding_2. 1 hit.
[Graphical view]
SUPFAMSSF47644. SSF47644. 1 hit.
SSF51717. SSF51717. 1 hit.
SSF52242. SSF52242. 1 hit.
SSF56507. SSF56507. 1 hit.
SSF82282. SSF82282. 1 hit.
TIGRFAMsTIGR02082. metH. 1 hit.
PROSITEPS50974. 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]
ProtoNetSearch...

Entry information

Entry nameMETH_VIBCH
AccessionPrimary (citable) accession number: Q9KUW9
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways