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Q49775

- METH_MYCLE

UniProt

Q49775 - METH_MYCLE

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Protein
Methionine synthase
Gene
metH, ML1307, B2126_C1_157, MLCB2533.04
Organism
Mycobacterium leprae (strain TN)
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 bindingi233 – 2331Zinc By similarity
Metal bindingi299 – 2991Zinc By similarity
Metal bindingi300 – 3001Zinc By similarity
Metal bindingi753 – 7531Cobalt (cobalamin axial ligand) By similarity
Binding sitei798 – 7981Cobalamin By similarity
Binding sitei954 – 9541S-adenosyl-L-methionine By similarity
Binding sitei1149 – 11491S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding sitei1153 – 11531Cobalamin; 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

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 lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
ProteomesiUP000000806: Chromosome

Organism-specific databases

LepromaiML1307.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12061206Methionine synthase
PRO_0000204533Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi272631.ML1307.

Structurei

3D structure databases

ProteinModelPortaliQ49775.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 314314Hcy-binding
Add
BLAST
Domaini350 – 609260Pterin-binding
Add
BLAST
Domaini642 – 73594B12-binding N-terminal
Add
BLAST
Domaini740 – 877138B12-binding
Add
BLAST
Domaini907 – 1206300AdoMet activation
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni830 – 8312Cobalamin-binding By similarity
Regioni1203 – 12042S-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.

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.

Q49775-1 [UniParc]FASTAAdd to Basket

« Hide

MRVTAANQHQ YDTDLLETLA QRVMVGDGAM GTQLQDAELT LDDFRGLEGC     50
NEILNETRPD VLETIHRRYF EAGADLVETN TFGCNLSNLG DYDIADKIRD 100
LSQRGTVIAR RVADELTTPD HKRYVLGSMG PGTKLPTLGH TEYRVVRDAY 150
TESALGMLDG GADAVLVETC QDLLQLKAAV LGSRRAMTQA GRHIPVFVHV 200
TVETTGTMLL GSEIGAALAA VEPLGVDMIG LNCATGPAEM SEHLRHLSKH 250
ARIPVSVMPN AGLPVLGAKG AEYPLQPDEL AEALAGFIAE FGLSLVGGCC 300
GTTPDHIREV AAAVARCNDG TVPRGERHVT YEPSVSSLYT AIPFAQKPSV 350
LMIGERTNAN GSKVFREAMI AEDYQKCLDI AKDQTRGGAH LLDLCVDYVG 400
RNGVADMKAL AGRLATVSTL PIMLDSTEIP VLQAGLEHLG GRCVINSVNY 450
EDGDGPESRF VKTMELVAEH GAAVVALTID EQGQARTVEK KVEVAERLIN 500
DITSNWGVDK SAILIDCLTF TIATGQEESR KDGIETIDAI RELKKRHPAV 550
QTTLGLSNIS FGLNPSARQV LNSVFLHECQ EAGLDSAIVH ASKILPINRI 600
PEEQRQAALD LVYDRRREGY DPLQKLMWLF KGVSSPSSKE TREAELAKLP 650
LFDRLAQRIV DGERNGLDVD LDEAMTQKPP LAIINENLLD GMKTVGELFG 700
SGQMQLPFVL QSAEVMKAAV AYLEPHMEKS DCDFGKGLAK GRIVLATVKG 750
DVHDIGKNLV DIILSNNGYE VVNLGIKQPI TNILEVAEDK SADVVGMSGL 800
LVKSTVIMKE NLEEMNTRGV AEKFPVLLGG AALTRSYVEN DLAEVYEGEV 850
HYARDAFEGL KLMDTIMSAK RGEALAPGSP ESLAAEADRN KETERKARHE 900
RSKRIAVQRK AAEEPVEVPE RSDVPSDVEV PAPPFWGSRI IKGLAVADYT 950
GFLDERALFL GQWGLRGVRG GAGPSYEDLV QTEGRPRLRY WLDRLSTYGV 1000
LAYAAVVYGY FPAVSEDNDI VVLAEPRPDA EQRYRFTFPR QQRGRFLCIA 1050
DFIRSRDLAT ERSEVDVLPF QLVTMGQPIA DFVGELFVSN SYRDYLEVHG 1100
IGVQLTEALA EYWHRRIREE LKFSGNRTMS ADDPEAVEDY FKLGYRGARF 1150
AFGYGACPDL EDRIKMMELL QPERIGVTIS EELQLHPEQS TDAFVLHHPA 1200
AKYFNV 1206
Length:1,206
Mass (Da):132,392
Last modified:April 27, 2001 - v3
Checksum:i7786CE5307D7CA86
GO

Sequence cautioni

The sequence AAA17182.1 differs from that shown. Reason: Frameshift at position 873.
The sequence CAA22918.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
PATRICi18054948. VBIMycLep78757_2411.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U00017 Genomic DNA. Translation: AAA17182.1 . Frameshift.
AL035310 Genomic DNA. Translation: CAA22918.1 . Different initiation.
AL583921 Genomic DNA. Translation: CAC31688.1 .
PIRi E87072.
S72842.
RefSeqi NP_301940.1. NC_002677.1.
WP_010908261.1. NC_002677.1.

3D structure databases

ProteinModelPortali Q49775.
ModBasei Search...

Protein-protein interaction databases

STRINGi 272631.ML1307.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAC31688 ; CAC31688 ; CAC31688 .
GeneIDi 910429.
KEGGi mle:ML1307.
PATRICi 18054948. VBIMycLep78757_2411.

Organism-specific databases

Lepromai ML1307.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00051 ; UER00081 .

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. Smith D.R., Robison K.
    Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: TN.

Entry informationi

Entry nameiMETH_MYCLE
AccessioniPrimary (citable) accession number: Q49775
Secondary accession number(s): Q9CC37, Q9S378
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: April 27, 2001
Last modified: September 3, 2014
This is version 109 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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