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Protein

Methionine synthase

Gene

metH

Organism
Mycobacterium leprae (strain TN)
Status
Reviewed-Annotation score: -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

Miscellaneous

L-homocysteine is bound via the zinc atom.By similarity

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:

Pathwayi: L-methionine biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes L-methionine from L-homocysteine (MetH route).
Proteins known to be involved in this subpathway in this organism are:
  1. Methionine synthase (metH)
This subpathway is part of the pathway L-methionine biosynthesis via de novo pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-methionine from L-homocysteine (MetH route), the pathway L-methionine biosynthesis via de novo pathway and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi233ZincPROSITE-ProRule annotation1
Metal bindingi299ZincPROSITE-ProRule annotation1
Metal bindingi300ZincPROSITE-ProRule annotation1
Metal bindingi753Cobalt (cobalamin axial ligand)By similarity1
Binding sitei798CobalaminBy similarity1
Binding sitei954S-adenosyl-L-methionineBy similarity1
Binding sitei1149S-adenosyl-L-methionine; via carbonyl oxygenBy similarity1
Binding sitei1153Cobalamin; via carbonyl oxygenBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionMethyltransferase, Transferase
Biological processAmino-acid biosynthesis, Methionine biosynthesis
LigandCobalamin, Cobalt, Metal-binding, S-adenosyl-L-methionine, Zinc

Enzyme and pathway databases

BioCyciMLEP272631:G1GT5-1430-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:ML1307
ORF Names:B2126_C1_157, MLCB2533.04
OrganismiMycobacterium leprae (strain TN)
Taxonomic identifieri272631 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
Proteomesi
  • UP000000806 Componenti: Chromosome

Organism-specific databases

LepromaiML1307

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002045331 – 1206Methionine synthaseAdd BLAST1206

Proteomic databases

PRIDEiQ49775

Interactioni

Protein-protein interaction databases

STRINGi272631.ML1307

Structurei

3D structure databases

ProteinModelPortaliQ49775
SMRiQ49775
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 314Hcy-bindingPROSITE-ProRule annotationAdd BLAST314
Domaini350 – 609Pterin-bindingPROSITE-ProRule annotationAdd BLAST260
Domaini642 – 735B12-binding N-terminalPROSITE-ProRule annotationAdd BLAST94
Domaini740 – 877B12-bindingPROSITE-ProRule annotationAdd BLAST138
Domaini907 – 1206AdoMet activationPROSITE-ProRule annotationAdd BLAST300

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni830 – 831Cobalamin-bindingBy similarity2
Regioni1203 – 1204S-adenosyl-L-methionine bindingBy similarity2

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4105C3R Bacteria
COG0646 LUCA
COG1410 LUCA
HOGENOMiHOG000251408
KOiK00548
OMAiKYPRPLN
OrthoDBiPOG091H030I

Family and domain databases

CDDicd02069 methionine_synthase_B12_BD, 1 hit
Gene3Di1.10.1240.10, 1 hit
3.10.196.10, 2 hits
3.20.20.20, 1 hit
3.20.20.330, 1 hit
InterProiView protein in InterPro
IPR003759 Cbl-bd_cap
IPR006158 Cobalamin-bd
IPR036724 Cobalamin-bd_sf
IPR011005 Dihydropteroate_synth-like
IPR003726 HCY_dom
IPR036589 HCY_dom_sf
IPR033706 Met_synthase_B12-bd
IPR011822 MetH
IPR036594 Meth_synthase_dom
IPR000489 Pterin-binding_dom
IPR004223 VitB12-dep_Met_synth_activ_dom
IPR037010 VitB12-dep_Met_synth_activ_sf
PfamiView protein in Pfam
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
PIRSFiPIRSF000381 MetH, 1 hit
SMARTiView protein in SMART
SM01018 B12-binding_2, 1 hit
SUPFAMiSSF47644 SSF47644, 1 hit
SSF51717 SSF51717, 1 hit
SSF52242 SSF52242, 1 hit
SSF56507 SSF56507, 1 hit
SSF82282 SSF82282, 1 hit
TIGRFAMsiTIGR02082 metH, 1 hit
PROSITEiView protein in PROSITE
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

Sequencei

Sequence statusi: Complete.

Q49775-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRVTAANQHQ YDTDLLETLA QRVMVGDGAM GTQLQDAELT LDDFRGLEGC
60 70 80 90 100
NEILNETRPD VLETIHRRYF EAGADLVETN TFGCNLSNLG DYDIADKIRD
110 120 130 140 150
LSQRGTVIAR RVADELTTPD HKRYVLGSMG PGTKLPTLGH TEYRVVRDAY
160 170 180 190 200
TESALGMLDG GADAVLVETC QDLLQLKAAV LGSRRAMTQA GRHIPVFVHV
210 220 230 240 250
TVETTGTMLL GSEIGAALAA VEPLGVDMIG LNCATGPAEM SEHLRHLSKH
260 270 280 290 300
ARIPVSVMPN AGLPVLGAKG AEYPLQPDEL AEALAGFIAE FGLSLVGGCC
310 320 330 340 350
GTTPDHIREV AAAVARCNDG TVPRGERHVT YEPSVSSLYT AIPFAQKPSV
360 370 380 390 400
LMIGERTNAN GSKVFREAMI AEDYQKCLDI AKDQTRGGAH LLDLCVDYVG
410 420 430 440 450
RNGVADMKAL AGRLATVSTL PIMLDSTEIP VLQAGLEHLG GRCVINSVNY
460 470 480 490 500
EDGDGPESRF VKTMELVAEH GAAVVALTID EQGQARTVEK KVEVAERLIN
510 520 530 540 550
DITSNWGVDK SAILIDCLTF TIATGQEESR KDGIETIDAI RELKKRHPAV
560 570 580 590 600
QTTLGLSNIS FGLNPSARQV LNSVFLHECQ EAGLDSAIVH ASKILPINRI
610 620 630 640 650
PEEQRQAALD LVYDRRREGY DPLQKLMWLF KGVSSPSSKE TREAELAKLP
660 670 680 690 700
LFDRLAQRIV DGERNGLDVD LDEAMTQKPP LAIINENLLD GMKTVGELFG
710 720 730 740 750
SGQMQLPFVL QSAEVMKAAV AYLEPHMEKS DCDFGKGLAK GRIVLATVKG
760 770 780 790 800
DVHDIGKNLV DIILSNNGYE VVNLGIKQPI TNILEVAEDK SADVVGMSGL
810 820 830 840 850
LVKSTVIMKE NLEEMNTRGV AEKFPVLLGG AALTRSYVEN DLAEVYEGEV
860 870 880 890 900
HYARDAFEGL KLMDTIMSAK RGEALAPGSP ESLAAEADRN KETERKARHE
910 920 930 940 950
RSKRIAVQRK AAEEPVEVPE RSDVPSDVEV PAPPFWGSRI IKGLAVADYT
960 970 980 990 1000
GFLDERALFL GQWGLRGVRG GAGPSYEDLV QTEGRPRLRY WLDRLSTYGV
1010 1020 1030 1040 1050
LAYAAVVYGY FPAVSEDNDI VVLAEPRPDA EQRYRFTFPR QQRGRFLCIA
1060 1070 1080 1090 1100
DFIRSRDLAT ERSEVDVLPF QLVTMGQPIA DFVGELFVSN SYRDYLEVHG
1110 1120 1130 1140 1150
IGVQLTEALA EYWHRRIREE LKFSGNRTMS ADDPEAVEDY FKLGYRGARF
1160 1170 1180 1190 1200
AFGYGACPDL EDRIKMMELL QPERIGVTIS EELQLHPEQS TDAFVLHHPA

AKYFNV
Length:1,206
Mass (Da):132,392
Last modified:April 27, 2001 - v3
Checksum:i7786CE5307D7CA86
GO

Sequence cautioni

The sequence AAA17182 differs from that shown. Reason: Frameshift at position 873.Curated
The sequence CAA22918 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00017 Genomic DNA Translation: AAA17182.1 Frameshift.
AL035310 Genomic DNA Translation: CAA22918.1 Different initiation.
AL583921 Genomic DNA Translation: CAC31688.1
PIRiE87072
S72842
RefSeqiNP_301940.1, NC_002677.1
WP_010908261.1, NC_002677.1

Genome annotation databases

EnsemblBacteriaiCAC31688; CAC31688; CAC31688
GeneIDi910429
KEGGimle:ML1307
PATRICifig|272631.5.peg.2411

Similar proteinsi

Entry informationi

Entry nameiMETH_MYCLE
AccessioniPrimary (citable) accession number: Q49775
Secondary accession number(s): Q9CC37, Q9S378
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: April 27, 2001
Last modified: May 23, 2018
This is version 128 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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