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Q49775

- METH_MYCLE

UniProt

Q49775 - METH_MYCLE

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Protein

Methionine synthase

Gene

metH

Organism
Mycobacterium leprae (strain TN)
Status
Reviewed - Annotation score: 3 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

Methylcobalamin (MeCBL).By similarity
Binds 1 zinc ion per subunit.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi233 – 2331ZincPROSITE-ProRule annotation
Metal bindingi299 – 2991ZincPROSITE-ProRule annotation
Metal bindingi300 – 3001ZincPROSITE-ProRule annotation
Metal bindingi753 – 7531Cobalt (cobalamin axial ligand)By similarity
Binding sitei798 – 7981CobalaminBy similarity
Binding sitei954 – 9541S-adenosyl-L-methionineBy similarity
Binding sitei1149 – 11491S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
Binding sitei1153 – 11531Cobalamin; 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

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 synthasePRO_0000204533Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi272631.ML1307.

Structurei

3D structure databases

ProteinModelPortaliQ49775.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 314314Hcy-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini350 – 609260Pterin-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini642 – 73594B12-binding N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini740 – 877138B12-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini907 – 1206300AdoMet activationPROSITE-ProRule annotationAdd
BLAST

Region

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

        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 AAA17182.1 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...
MobiDBi 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: October 1, 2014
This is version 110 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