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Protein

Methionine synthase

Gene

metH

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: 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).By similarity

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi247 – 2471ZincPROSITE-ProRule annotation
Metal bindingi310 – 3101ZincPROSITE-ProRule annotation
Metal bindingi311 – 3111ZincPROSITE-ProRule annotation
Metal bindingi759 – 7591Cobalt (cobalamin axial ligand)By similarity
Binding sitei804 – 8041CobalaminBy similarity
Binding sitei946 – 9461S-adenosyl-L-methionineBy similarity
Binding sitei1134 – 11341S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
Binding sitei1138 – 11381Cobalamin; via carbonyl oxygenBy similarity

GO - Molecular functioni

  1. cobalamin binding Source: UniProtKB-KW
  2. methionine synthase activity Source: UniProtKB-EC
  3. S-adenosylmethionine-homocysteine S-methyltransferase activity Source: InterPro
  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 Componenti: 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 – 11RemovedBy similarity
Chaini2 – 12271226Methionine synthasePRO_0000204536Add
BLAST

Proteomic databases

PaxDbiP37586.
PRIDEiP37586.

Interactioni

Protein-protein interaction databases

STRINGi99287.STM4188.S.

Structurei

3D structure databases

ProteinModelPortaliP37586.
SMRiP37586. Positions 651-1227.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 325324Hcy-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini356 – 617262Pterin-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini650 – 74495B12-binding N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini746 – 881136B12-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini897 – 1227331AdoMet activationPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni834 – 8352Cobalamin-bindingBy similarity
Regioni1189 – 11902S-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.
OMAiDYNSIMV.
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

        10         20         30         40         50
MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLHEEDFRGE RFADWPCDLK
60 70 80 90 100
GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYRMESLS
110 120 130 140 150
AEINYAAAKL ARACADEWTA RTPEKPRFVA GVLGPTNRTA SISPDVNDPA
160 170 180 190 200
FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKEEF
210 220 230 240 250
EALGVDLPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG
260 270 280 290 300
PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE
310 320 330 340 350
AGFLNIVGGC CGTTPEHIAA MSRAVAGLLP RQLPDIPVAC RLSGLEPLNI
360 370 380 390 400
GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VESGAQIIDI
410 420 430 440 450
NMDEGMLDAE AAMVRFLSLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG
460 470 480 490 500
KGIVNSISMK EGVEAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI
510 520 530 540 550
CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK
560 570 580 590 600
RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG
610 620 630 640 650
QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLDLAEKYRG SKTDEAANAQ
660 670 680 690 700
QAEWRSWDVK KRLEYSLVKG ITEFIEQDTE EARQQAARPI EVIEGPLMDG
710 720 730 740 750
MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EKGSSNGKMV
760 770 780 790 800
IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAREVNADL
810 820 830 840 850
IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY
860 870 880 890 900
SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHARKKPR
910 920 930 940 950
TPPVTLEAAR DNDLAFDWER YTPPVAHRLG VQEVEASIET LRNYIDWTPF
960 970 980 990 1000
FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KLLNPRGVVG
1010 1020 1030 1040 1050
LFPANRVGDD IEIYRDETRT HVLTVSHHLR QQTEKVGFAN YCLADFVAPK
1060 1070 1080 1090 1100
LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA IADRLAEAFA
1110 1120 1130 1140 1150
EYLHERVRKV YWGYAPNESL SNDELIRENY QGIRPAPGYP ACPEHTEKGT
1160 1170 1180 1190 1200
IWQLLDVEKH TGMKLTESFA MWPGASVSGW YFSHPESKYF AVAQIQRDQV
1210 1220
TDYAFRKGMS VEDVERWLAP NLGYDAD
Length:1,227
Mass (Da):136,004
Last modified:January 22, 2007 - v3
Checksum:i11C8E21745FF5354
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti115 – 1151A → R (PubMed:3072256).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AE006468 Genomic DNA. Translation: AAL23012.1. Different initiation.
RefSeqiNP_463053.2. NC_003197.1.

3D structure databases

ProteinModelPortaliP37586.
SMRiP37586. Positions 651-1227.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi99287.STM4188.S.

Proteomic databases

PaxDbiP37586.
PRIDEiP37586.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiCOG1410.
KOiK00548.
OMAiDYNSIMV.
OrthoDBiEOG6091CH.
PhylomeDBiP37586.

Enzyme and pathway databases

UniPathwayiUPA00051; UER00081.
BioCyciSENT99287:GCTI-4218-MONOMER.

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]
ProtoNetiSearch...

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(1987) [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: September 30, 1994
Last sequence update: January 22, 2007
Last modified: January 6, 2015
This is version 118 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.