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Q9KUW9

- METH_VIBCH

UniProt

Q9KUW9 - METH_VIBCH

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Protein

Methionine synthase

Gene

metH

Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
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).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 – 2481ZincPROSITE-ProRule annotation
Metal bindingi311 – 3111ZincPROSITE-ProRule annotation
Metal bindingi312 – 3121ZincPROSITE-ProRule annotation
Metal bindingi760 – 7601Cobalt (cobalamin axial ligand)By similarity
Binding sitei805 – 8051CobalaminBy similarity
Binding sitei948 – 9481S-adenosyl-L-methionineBy similarity
Binding sitei1136 – 11361S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
Binding sitei1140 – 11401Cobalamin; via carbonyl oxygenBy 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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 326321Hcy-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini357 – 618262Pterin-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini651 – 74595B12-binding N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini747 – 882136B12-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini898 – 1226329AdoMet activationPROSITE-ProRule annotationAdd
BLAST

Region

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

Sequence similaritiesi

Contains 1 AdoMet activation domain.PROSITE-ProRule annotation
Contains 1 B12-binding domain.PROSITE-ProRule annotation
Contains 1 Hcy-binding domain.PROSITE-ProRule annotation
Contains 1 pterin-binding domain.PROSITE-ProRule annotation

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

        10         20         30         40         50
MGKEVRQQLE QQLKQRILLI DGGMGTMIQS YKLQEEDYRG ARFVDWHCDL
60 70 80 90 100
KGNNDLLVLT QPQIIKEIHS AYLEAGADIL ETNTFNSTTI AMADYDMQSL
110 120 130 140 150
SAEINFAAAK LAREVADEWT AKDPSRPRYV AGVLGPTNRT CSISPDVNDP
160 170 180 190 200
GFRNVTFDGL VEAYSESTRA LIKGGSDLIL IETIFDTLNA KACAFAVDSV
210 220 230 240 250
FEELGISLPV MISGTITDAS GRTLSGQTTE AFYNALRHVR PISFGLNCAL
260 270 280 290 300
GPDELRQYVE ELSRISECYV SAHPNAGLPN AFGEYDLSAE EMAEHIAEWA
310 320 330 340 350
QAGFLNLVGG CCGTTPEHIA AIAKAVEGVK PRALPDLKVE CRLSGLEPLN
360 370 380 390 400
IGPETLFVNV GERTNVTGSA RFKRLIKEEQ YDEALDVARE QVENGAQIID
410 420 430 440 450
INMDEGMLDA EACMVRFLNL CASEPEISKV PVMVDSSKWE VIEAGLKCIQ
460 470 480 490 500
GKGIVNSISL KEGKEKFIAQ AKLVRRYGAA VIVMAFDEVG QADTRERKLE
510 520 530 540 550
ICRRAYHILV DEVGFPPEDI IFDPNIFAVA TGIDEHNNYA LDFINAVADI
560 570 580 590 600
KRELPHAMIS GGVSNVSFSF RGNNYVREAI HAVFLYHCFK HGMDMGIVNA
610 620 630 640 650
GQLEIYDNVP LKLREAVEDV ILNRRSDGTE RLLEIAEAYR ENSVGKEEDA
660 670 680 690 700
SALEWRAWPV AKRLEHALVK GITEFIVQDT EEARQQASKP LEVIEGPLMD
710 720 730 740 750
GMNVVGDLFG EGKMFLPQVV KSARVMKQAV AYLEPFINAQ KSGSTSNGKI
760 770 780 790 800
LLATVKGDVH DIGKNIVGVV LQCNNFEIID LGVMVPCEQI LKVAREQNVD
810 820 830 840 850
IIGLSGLITP SLDEMVHVAK EMERQGFELP LLIGGATTSK AHTAVKIEQN
860 870 880 890 900
YHAPVVYVNN ASRAVGVCTS LLSDEQRPGF IERLDLDYER TRDQHARKTP
910 920 930 940 950
KSRPVTLEQA RANKAALDWA NYTPPAPAKP GVHVFENIAL ATLRPYIDWT
960 970 980 990 1000
PFFMTWSLMG KYPAILEHEE VGEEAKRLFH DANALLDKVE REGLLKASGM
1010 1020 1030 1040 1050
CALFPAASVG DDIEVYSDES RTQVAHVLYN LRQQTEKPKG ANYCLSDYVA
1060 1070 1080 1090 1100
PKESGKRDWI GAFAVTGGIG ERALADAYKA QGDDYNAIMI QAVADRLAEA
1110 1120 1130 1140 1150
FAEYLHEKVR KEIWGYASDE NLSNDDLIRE RYQGIRPAPG YPACPEHTEK
1160 1170 1180 1190 1200
ATLWQMLNVE ETIGMSLTTS YAMWPGASVS GWYFSHPDSR YFAVAQIQPD
1210 1220
QLHSYAERKG WRLEEAEKWL APNLDA
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: October 1, 2014
This is version 88 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