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P37586

- METH_SALTY

UniProt

P37586 - METH_SALTY

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Protein
Methionine synthase
Gene
metH, STM4188
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
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 bindingi247 – 2471Zinc By similarity
Metal bindingi310 – 3101Zinc By similarity
Metal bindingi311 – 3111Zinc By similarity
Metal bindingi759 – 7591Cobalt (cobalamin axial ligand) By similarity
Binding sitei804 – 8041Cobalamin By similarity
Binding sitei946 – 9461S-adenosyl-L-methionine By similarity
Binding sitei1134 – 11341S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding sitei1138 – 11381Cobalamin; 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

BioCyciSENT99287:GCTI-4218-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:STM4188
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000001014: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. intracellular Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 12271226Methionine synthase
PRO_0000204536Add
BLAST

Proteomic databases

PaxDbiP37586.
PRIDEiP37586.

Interactioni

Protein-protein interaction databases

STRINGi99287.STM4188.S.

Structurei

3D structure databases

ProteinModelPortaliP37586.
SMRiP37586. Positions 651-1227.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 325324Hcy-binding
Add
BLAST
Domaini356 – 617262Pterin-binding
Add
BLAST
Domaini650 – 74495B12-binding N-terminal
Add
BLAST
Domaini746 – 881136B12-binding
Add
BLAST
Domaini897 – 1227331AdoMet activation
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni834 – 8352Cobalamin-binding By similarity
Regioni1189 – 11902S-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.
PhylomeDBiP37586.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P37586-1 [UniParc]FASTAAdd to Basket

« Hide

MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLHEEDFRGE RFADWPCDLK     50
GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYRMESLS 100
AEINYAAAKL ARACADEWTA RTPEKPRFVA GVLGPTNRTA SISPDVNDPA 150
FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKEEF 200
EALGVDLPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG 250
PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE 300
AGFLNIVGGC CGTTPEHIAA MSRAVAGLLP RQLPDIPVAC RLSGLEPLNI 350
GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VESGAQIIDI 400
NMDEGMLDAE AAMVRFLSLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG 450
KGIVNSISMK EGVEAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI 500
CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK 550
RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG 600
QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLDLAEKYRG SKTDEAANAQ 650
QAEWRSWDVK KRLEYSLVKG ITEFIEQDTE EARQQAARPI EVIEGPLMDG 700
MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EKGSSNGKMV 750
IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAREVNADL 800
IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY 850
SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHARKKPR 900
TPPVTLEAAR DNDLAFDWER YTPPVAHRLG VQEVEASIET LRNYIDWTPF 950
FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KLLNPRGVVG 1000
LFPANRVGDD IEIYRDETRT HVLTVSHHLR QQTEKVGFAN YCLADFVAPK 1050
LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA IADRLAEAFA 1100
EYLHERVRKV YWGYAPNESL SNDELIRENY QGIRPAPGYP ACPEHTEKGT 1150
IWQLLDVEKH TGMKLTESFA MWPGASVSGW YFSHPESKYF AVAQIQRDQV 1200
TDYAFRKGMS VEDVERWLAP NLGYDAD 1227
Length:1,227
Mass (Da):136,004
Last modified:January 23, 2007 - v3
Checksum:i11C8E21745FF5354
GO

Sequence cautioni

The sequence AAL23012.1 differs from that shown. Reason: Erroneous initiation.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti115 – 1151A → R1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE006468 Genomic DNA. Translation: AAL23012.1. Different initiation.
RefSeqiNP_463053.2. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL23012; AAL23012; STM4188.
GeneIDi1255714.
KEGGistm:STM4188.S.
PATRICi32387269. VBISalEnt20916_4402.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE006468 Genomic DNA. Translation: AAL23012.1 . Different initiation.
RefSeqi NP_463053.2. NC_003197.1.

3D structure databases

ProteinModelPortali P37586.
SMRi P37586. Positions 651-1227.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 99287.STM4188.S.

Proteomic databases

PaxDbi P37586.
PRIDEi P37586.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAL23012 ; AAL23012 ; STM4188 .
GeneIDi 1255714.
KEGGi stm:STM4188.S.
PATRICi 32387269. VBISalEnt20916_4402.

Phylogenomic databases

eggNOGi COG1410.
KOi K00548.
OMAi LTEHYAM.
OrthoDBi EOG6091CH.
PhylomeDBi P37586.

Enzyme and pathway databases

UniPathwayi UPA00051 ; UER00081 .
BioCyci SENT99287:GCTI-4218-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

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: LT2 / SGSC1412 / ATCC 700720.
  2. "The control region of the metH gene of Salmonella typhimurium LT2: an atypical met promoter."
    Urbanowski M.L., Stauffer G.V.
    Gene 73:193-200(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-371.
    Strain: LT2.

Entry informationi

Entry nameiMETH_SALTY
AccessioniPrimary (citable) accession number: P37586
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 115 of the entry and version 3 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