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O33259

- METH_MYCTU

UniProt

O33259 - METH_MYCTU

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Protein

Methionine synthase

Gene

metH

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.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 – 2311ZincPROSITE-ProRule annotation
Metal bindingi297 – 2971ZincPROSITE-ProRule annotation
Metal bindingi298 – 2981ZincPROSITE-ProRule annotation
Metal bindingi742 – 7421Cobalt (cobalamin axial ligand)By similarity
Binding sitei787 – 7871CobalaminBy similarity
Binding sitei940 – 9401S-adenosyl-L-methionineBy similarity
Binding sitei1135 – 11351S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
Binding sitei1139 – 11391Cobalamin; 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

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 synthasePRO_0000204534Add
BLAST

Proteomic databases

PRIDEiO33259.

Interactioni

Protein-protein interaction databases

STRINGi83332.Rv2124c.

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 312312Hcy-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini343 – 601259Pterin-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini635 – 72894B12-binding N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini729 – 866138B12-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini893 – 1192300AdoMet activationPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni819 – 8202Cobalamin-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.
HOGENOMiHOG000251408.
InParanoidiO33259.
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

        10         20         30         40         50
MTAADKHLYD TDLLDVLSQR VMVGDGAMGT QLQAADLTLD DFRGLEGCNE
60 70 80 90 100
ILNETRPDVL ETIHRNYFEA GADAVETNTF GCNLSNLGDY DIADRIRDLS
110 120 130 140 150
QKGTAIARRV ADELGSPDRK RYVLGSMGPG TKLPTLGHTE YAVIRDAYTE
160 170 180 190 200
AALGMLDGGA DAILVETCQD LLQLKAAVLG SRRAMTRAGR HIPVFAHVTV
210 220 230 240 250
ETTGTMLLGS EIGAALTAVE PLGVDMIGLN CATGPAEMSE HLRHLSRHAR
260 270 280 290 300
IPVSVMPNAG LPVLGAKGAE YPLLPDELAE ALAGFIAEFG LSLVGGCCGT
310 320 330 340 350
TPAHIREVAA AVANIKRPER QVSYEPSVSS LYTAIPFAQD ASVLVIGERT
360 370 380 390 400
NANGSKGFRE AMIAEDYQKC LDIAKDQTRD GAHLLDLCVD YVGRDGVADM
410 420 430 440 450
KALASRLATS STLPIMLDST ETAVLQAGLE HLGGRCAINS VNYEDGDGPE
460 470 480 490 500
SRFAKTMALV AEHGAAVVAL TIDEEGQART AQKKVEIAER LINDITGNWG
510 520 530 540 550
VDESSILIDT LTFTIATGQE ESRRDGIETI EAIRELKKRH PDVQTTLGLS
560 570 580 590 600
NISFGLNPAA RQVLNSVFLH ECQEAGLDSA IVHASKILPM NRIPEEQRNV
610 620 630 640 650
ALDLVYDRRR EDYDPLQELM RLFEGVSAAS SKEDRLAELA GLPLFERLAQ
660 670 680 690 700
RIVDGERNGL DADLDEAMTQ KPPLQIINEH LLAGMKTVGE LFGSGQMQLP
710 720 730 740 750
FVLQSAEVMK AAVAYLEPHM ERSDDDSGKG RIVLATVKGD VHDIGKNLVD
760 770 780 790 800
IILSNNGYEV VNIGIKQPIA TILEVAEDKS ADVVGMSGLL VKSTVVMKEN
810 820 830 840 850
LEEMNTRGVA EKFPVLLGGA ALTRSYVEND LAEIYQGEVH YARDAFEGLK
860 870 880 890 900
LMDTIMSAKR GEAPDENSPE AIKAREKEAE RKARHQRSKR IAAQRKAAEE
910 920 930 940 950
PVEVPERSDV AADIEVPAPP FWGSRIVKGL AVADYTGLLD ERALFLGQWG
960 970 980 990 1000
LRGQRGGEGP SYEDLVETEG RPRLRYWLDR LSTDGILAHA AVVYGYFPAV
1010 1020 1030 1040 1050
SEGNDIVVLT EPKPDAPVRY RFHFPRQQRG RFLCIADFIR SRELAAERGE
1060 1070 1080 1090 1100
VDVLPFQLVT MGQPIADFAN ELFASNAYRD YLEVHGIGVQ LTEALAEYWH
1110 1120 1130 1140 1150
RRIREELKFS GDRAMAAEDP EAKEDYFKLG YRGARFAFGY GACPDLEDRA
1160 1170 1180 1190
KMMALLEPER IGVTLSEELQ LHPEQSTDAF VLHHPEAKYF NV
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...
MobiDBi 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.
InParanoidi O33259.
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: October 29, 2014
This is version 116 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