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O33259

- METH_MYCTU

UniProt

O33259 - METH_MYCTU

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Protein
Methionine synthase
Gene
metH, Rv2124c, MTCY261.20c
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

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 bindingi231 – 2311Zinc By similarity
Metal bindingi297 – 2971Zinc By similarity
Metal bindingi298 – 2981Zinc By similarity
Metal bindingi742 – 7421Cobalt (cobalamin axial ligand) By similarity
Binding sitei787 – 7871Cobalamin By similarity
Binding sitei940 – 9401S-adenosyl-L-methionine By similarity
Binding sitei1135 – 11351S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding sitei1139 – 11391Cobalamin; 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
Complete GO annotation...

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

BioCyciMTBRV:RV2124C-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:Rv2124c
ORF Names:MTCY261.20c
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
ProteomesiUP000001584: Chromosome

Organism-specific databases

TubercuListiRv2124c.

Subcellular locationi

GO - Cellular componenti

  1. cell wall Source: MTBBASE
  2. cytosol Source: MTBBASE
  3. plasma membrane Source: MTBBASE
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11921192Methionine synthase
PRO_0000204534Add
BLAST

Proteomic databases

PRIDEiO33259.

Interactioni

Protein-protein interaction databases

STRINGi83332.Rv2124c.

Structurei

3D structure databases

ProteinModelPortaliO33259.
SMRiO33259. Positions 16-621, 637-1192.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 312312Hcy-binding
Add
BLAST
Domaini343 – 601259Pterin-binding
Add
BLAST
Domaini635 – 72894B12-binding N-terminal
Add
BLAST
Domaini729 – 866138B12-binding
Add
BLAST
Domaini893 – 1192300AdoMet activation
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni819 – 8202Cobalamin-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.
HOGENOMiHOG000251408.
KOiK00548.
OMAiLTEHYAM.
OrthoDBiEOG6091CH.
PhylomeDBiO33259.

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.

O33259-1 [UniParc]FASTAAdd to Basket

« Hide

MTAADKHLYD TDLLDVLSQR VMVGDGAMGT QLQAADLTLD DFRGLEGCNE     50
ILNETRPDVL ETIHRNYFEA GADAVETNTF GCNLSNLGDY DIADRIRDLS 100
QKGTAIARRV ADELGSPDRK RYVLGSMGPG TKLPTLGHTE YAVIRDAYTE 150
AALGMLDGGA DAILVETCQD LLQLKAAVLG SRRAMTRAGR HIPVFAHVTV 200
ETTGTMLLGS EIGAALTAVE PLGVDMIGLN CATGPAEMSE HLRHLSRHAR 250
IPVSVMPNAG LPVLGAKGAE YPLLPDELAE ALAGFIAEFG LSLVGGCCGT 300
TPAHIREVAA AVANIKRPER QVSYEPSVSS LYTAIPFAQD ASVLVIGERT 350
NANGSKGFRE AMIAEDYQKC LDIAKDQTRD GAHLLDLCVD YVGRDGVADM 400
KALASRLATS STLPIMLDST ETAVLQAGLE HLGGRCAINS VNYEDGDGPE 450
SRFAKTMALV AEHGAAVVAL TIDEEGQART AQKKVEIAER LINDITGNWG 500
VDESSILIDT LTFTIATGQE ESRRDGIETI EAIRELKKRH PDVQTTLGLS 550
NISFGLNPAA RQVLNSVFLH ECQEAGLDSA IVHASKILPM NRIPEEQRNV 600
ALDLVYDRRR EDYDPLQELM RLFEGVSAAS SKEDRLAELA GLPLFERLAQ 650
RIVDGERNGL DADLDEAMTQ KPPLQIINEH LLAGMKTVGE LFGSGQMQLP 700
FVLQSAEVMK AAVAYLEPHM ERSDDDSGKG RIVLATVKGD VHDIGKNLVD 750
IILSNNGYEV VNIGIKQPIA TILEVAEDKS ADVVGMSGLL VKSTVVMKEN 800
LEEMNTRGVA EKFPVLLGGA ALTRSYVEND LAEIYQGEVH YARDAFEGLK 850
LMDTIMSAKR GEAPDENSPE AIKAREKEAE RKARHQRSKR IAAQRKAAEE 900
PVEVPERSDV AADIEVPAPP FWGSRIVKGL AVADYTGLLD ERALFLGQWG 950
LRGQRGGEGP SYEDLVETEG RPRLRYWLDR LSTDGILAHA AVVYGYFPAV 1000
SEGNDIVVLT EPKPDAPVRY RFHFPRQQRG RFLCIADFIR SRELAAERGE 1050
VDVLPFQLVT MGQPIADFAN ELFASNAYRD YLEVHGIGVQ LTEALAEYWH 1100
RRIREELKFS GDRAMAAEDP EAKEDYFKLG YRGARFAFGY GACPDLEDRA 1150
KMMALLEPER IGVTLSEELQ LHPEQSTDAF VLHHPEAKYF NV 1192
Length:1,192
Mass (Da):130,323
Last modified:January 1, 1998 - v1
Checksum:i820450DCE77BE15B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL123456 Genomic DNA. Translation: CCP44899.1.
PIRiG70513.
RefSeqiNP_216640.1. NC_000962.3.
YP_006515540.1. NC_018143.2.

Genome annotation databases

EnsemblBacteriaiCCP44899; CCP44899; Rv2124c.
GeneIDi13316931.
888711.
KEGGimtu:Rv2124c.
mtv:RVBD_2124c.
PATRICi18153284. VBIMycTub87468_2371.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL123456 Genomic DNA. Translation: CCP44899.1 .
PIRi G70513.
RefSeqi NP_216640.1. NC_000962.3.
YP_006515540.1. NC_018143.2.

3D structure databases

ProteinModelPortali O33259.
SMRi O33259. Positions 16-621, 637-1192.
ModBasei Search...

Protein-protein interaction databases

STRINGi 83332.Rv2124c.

Proteomic databases

PRIDEi O33259.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CCP44899 ; CCP44899 ; Rv2124c .
GeneIDi 13316931.
888711.
KEGGi mtu:Rv2124c.
mtv:RVBD_2124c.
PATRICi 18153284. VBIMycTub87468_2371.

Organism-specific databases

TubercuListi Rv2124c.

Phylogenomic databases

eggNOGi COG1410.
HOGENOMi HOG000251408.
KOi K00548.
OMAi LTEHYAM.
OrthoDBi EOG6091CH.
PhylomeDBi O33259.

Enzyme and pathway databases

UniPathwayi UPA00051 ; UER00081 .
BioCyci MTBRV:RV2124C-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 25618 / H37Rv.
  2. "targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis."
    Raman K., Yeturu K., Chandra N.
    BMC Syst. Biol. 2:109-109(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ATCC 25618 / H37Rv.

Entry informationi

Entry nameiMETH_MYCTU
AccessioniPrimary (citable) accession number: O33259
Secondary accession number(s): L0T8Q3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: September 3, 2014
This is version 114 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.
Was identified as a high-confidence drug target.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi