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Q87L95 (METH_VIBPA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:VP2717
OrganismVibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633) [Complete proteome] [HAMAP]
Taxonomic identifier223926 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio ›

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

Cobalamin 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_0000204541

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
Q87L95 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 2F7A3269FB7C20A9

FASTA1,226136,218
        10         20         30         40         50         60 
MGSKVRQQIE AQLKQRILLI DGGMGTMIQG YKLEEQDYRG ERFANWHCDL KGNNDLLVLS 

        70         80         90        100        110        120 
QPQLIKEIHS AYLEAGADIL ETNTFNATTI AMADYEMESL SEEINFAAAK LAREVADEWT 

       130        140        150        160        170        180 
AKTPDKPRYV AGVLGPTNRT CSISPDVNDP GYRNVSFDEL VEAYSESTRA LIRGGADLIL 

       190        200        210        220        230        240 
IETIFDTLNA KACAFAVDSV FEELGVALPV MISGTITDAS GRTLSGQTTE AFYNSLRHVR 

       250        260        270        280        290        300 
PLSFGLNCAL GPDELRPYVE ELSRISESFV SAHPNAGLPN AFGEYDLSPE DMAEHVKEWA 

       310        320        330        340        350        360 
SSGFLNLIGG CCGTTPEHIR QMAQAVEGVT PRALPDLPVA CRLSGLEPLT IEKETLFINV 

       370        380        390        400        410        420 
GERTNVTGSA RFKRLIKEEQ YDEALEVARQ QVENGAQIID INMDEGMLDA QACMVRFLNL 

       430        440        450        460        470        480 
CASEPEISKV PIMVDSSKWE VIEAGLKCIQ GKGIVNSISL KEGKEKFVEQ AKLIRRYGAA 

       490        500        510        520        530        540 
VIVMAFDEVG QAETRTRKLE ICTNAYRILV DEVGFPPEDI IFDPNIFAVA TGIDEHNNYA 

       550        560        570        580        590        600 
VDFIEAVADI KRDLPHAMIS GGVSNVSFSF RGNNYVREAI HAVFLYHCFK NGMDMGIVNA 

       610        620        630        640        650        660 
GQLEIYDNVP EKLREAVEDV VLNRRDDATE RLLDIAAEYA DKGVGKEEDA SALEWRTWPV 

       670        680        690        700        710        720 
AKRLEHALVK GITEFIVADT EEARVNAVKP LEVIEGPLMD GMNVVGDLFG EGKMFLPQVV 

       730        740        750        760        770        780 
KSARVMKQAV AHLEPFINAE KQSGSSNGKI LLATVKGDVH DIGKNIVGVV LQCNNYEIID 

       790        800        810        820        830        840 
LGVMVPCEKI LKVAIEENVD IIGLSGLITP SLDEMVHVAK EMERLNFDLP LLIGGATTSK 

       850        860        870        880        890        900 
AHTAVKIEQN YKNPVVYVNN ASRAVGVCSS LLSDERRPAF IEKLDADYER VRDQHNRKKP 

       910        920        930        940        950        960 
RTKPVTLEQA RANKVAIDWD AYTPPVPAKP GLHIFDDFDV ATLRKYIDWT PFFMTWSLVG 

       970        980        990       1000       1010       1020 
KYPTIFKHEE VGEEAQRLFH DANELLDRVE REGLLKARGI CGLFPAASVG DDIEVYTDES 

      1030       1040       1050       1060       1070       1080 
RTEVAKVLRN LRQQTEKPKG FNYCLSDYIA PKESGKQDWV GAFAVTGGIG ERELADEYKA 

      1090       1100       1110       1120       1130       1140 
QGDDYNAIMI QAVADRLAEA FAEYLHERVR KEIWGYAADE NLSNDELIRE KYQGIRPAPG 

      1150       1160       1170       1180       1190       1200 
YPACPEHTEK GPLWELLNVE ENIGMSLTTS YAMYPGASVS GWYFSHPDSR YFAIAQIQDD 

      1210       1220 
QLESYADRKG WDRIEAEKWL GPNING

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000031 Genomic DNA. Translation: BAC60980.1.
RefSeqNP_799096.1. NC_004603.1.

3D structure databases

ProteinModelPortalQ87L95.
SMRQ87L95. Positions 654-1224.
ModBaseSearch...

Protein-protein interaction databases

STRING223926.VP2717.

Proteomic databases

PRIDEQ87L95.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC60980; BAC60980; BAC60980.
GeneID1190262.
KEGGvpa:VP2717.
PATRIC20143630. VBIVibPar50997_2612.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1410.
HOGENOMHOG000251409.
KOK00548.
OMAVRKEFWG.
ProtClustDBPRK09490.

Enzyme and pathway databases

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]
PANTHERPTHR21091:SF9. PTHR21091:SF9. 1 hit.
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]
SUPFAMSSF52242. Cbl-bd. 1 hit.
SSF51717. DHP_synth_like. 1 hit.
SSF56507. Met_synth_B12. 1 hit.
SSF47644. Met_synth_Cbl-bd. 1 hit.
SSF82282. S_methyl_trans. 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_VIBPA
AccessionPrimary (citable) accession number: Q87L95
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: June 1, 2003
Last modified: May 1, 2013
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents