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Q49775 (METH_MYCLE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methionine synthase

EC=2.1.1.13
Alternative name(s):
5-methyltetrahydrofolate--homocysteine methyltransferase
Methionine synthase, vitamin-B12 dependent
Short name=MS
Gene names
Name:metH
Ordered Locus Names:ML1307
ORF Names:B2126_C1_157, MLCB2533.04
OrganismMycobacterium leprae (strain TN) [Complete proteome] [HAMAP]
Taxonomic identifier272631 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length1206 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 activity

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

Cofactor

Methylcobalamin (MeCBL) By similarity.

Binds 1 zinc ion per subunit By similarity.

Pathway

Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetH route): step 1/1.

Domain

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.

Miscellaneous

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

Sequence similarities

Belongs to the vitamin-B12 dependent methionine synthase family.

Contains 1 AdoMet activation domain.

Contains 1 B12-binding domain.

Contains 1 B12-binding N-terminal domain.

Contains 1 Hcy-binding domain.

Contains 1 pterin-binding domain.

Sequence caution

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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12061206Methionine synthase
PRO_0000204533

Regions

Domain1 – 314314Hcy-binding
Domain350 – 609260Pterin-binding
Domain642 – 73594B12-binding N-terminal
Domain740 – 877138B12-binding
Domain907 – 1206300AdoMet activation
Region830 – 8312Cobalamin-binding By similarity
Region1203 – 12042S-adenosyl-L-methionine binding By similarity

Sites

Metal binding2331Zinc By similarity
Metal binding2991Zinc By similarity
Metal binding3001Zinc By similarity
Metal binding7531Cobalt (cobalamin axial ligand) By similarity
Binding site7981Cobalamin By similarity
Binding site9541S-adenosyl-L-methionine By similarity
Binding site11491S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site11531Cobalamin; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q49775 [UniParc].

Last modified April 27, 2001. Version 3.
Checksum: 7786CE5307D7CA86

FASTA1,206132,392
        10         20         30         40         50         60 
MRVTAANQHQ YDTDLLETLA QRVMVGDGAM GTQLQDAELT LDDFRGLEGC NEILNETRPD 

        70         80         90        100        110        120 
VLETIHRRYF EAGADLVETN TFGCNLSNLG DYDIADKIRD LSQRGTVIAR RVADELTTPD 

       130        140        150        160        170        180 
HKRYVLGSMG PGTKLPTLGH TEYRVVRDAY TESALGMLDG GADAVLVETC QDLLQLKAAV 

       190        200        210        220        230        240 
LGSRRAMTQA GRHIPVFVHV TVETTGTMLL GSEIGAALAA VEPLGVDMIG LNCATGPAEM 

       250        260        270        280        290        300 
SEHLRHLSKH ARIPVSVMPN AGLPVLGAKG AEYPLQPDEL AEALAGFIAE FGLSLVGGCC 

       310        320        330        340        350        360 
GTTPDHIREV AAAVARCNDG TVPRGERHVT YEPSVSSLYT AIPFAQKPSV LMIGERTNAN 

       370        380        390        400        410        420 
GSKVFREAMI AEDYQKCLDI AKDQTRGGAH LLDLCVDYVG RNGVADMKAL AGRLATVSTL 

       430        440        450        460        470        480 
PIMLDSTEIP VLQAGLEHLG GRCVINSVNY EDGDGPESRF VKTMELVAEH GAAVVALTID 

       490        500        510        520        530        540 
EQGQARTVEK KVEVAERLIN DITSNWGVDK SAILIDCLTF TIATGQEESR KDGIETIDAI 

       550        560        570        580        590        600 
RELKKRHPAV QTTLGLSNIS FGLNPSARQV LNSVFLHECQ EAGLDSAIVH ASKILPINRI 

       610        620        630        640        650        660 
PEEQRQAALD LVYDRRREGY DPLQKLMWLF KGVSSPSSKE TREAELAKLP LFDRLAQRIV 

       670        680        690        700        710        720 
DGERNGLDVD LDEAMTQKPP LAIINENLLD GMKTVGELFG SGQMQLPFVL QSAEVMKAAV 

       730        740        750        760        770        780 
AYLEPHMEKS DCDFGKGLAK GRIVLATVKG DVHDIGKNLV DIILSNNGYE VVNLGIKQPI 

       790        800        810        820        830        840 
TNILEVAEDK SADVVGMSGL LVKSTVIMKE NLEEMNTRGV AEKFPVLLGG AALTRSYVEN 

       850        860        870        880        890        900 
DLAEVYEGEV HYARDAFEGL KLMDTIMSAK RGEALAPGSP ESLAAEADRN KETERKARHE 

       910        920        930        940        950        960 
RSKRIAVQRK AAEEPVEVPE RSDVPSDVEV PAPPFWGSRI IKGLAVADYT GFLDERALFL 

       970        980        990       1000       1010       1020 
GQWGLRGVRG GAGPSYEDLV QTEGRPRLRY WLDRLSTYGV LAYAAVVYGY FPAVSEDNDI 

      1030       1040       1050       1060       1070       1080 
VVLAEPRPDA EQRYRFTFPR QQRGRFLCIA DFIRSRDLAT ERSEVDVLPF QLVTMGQPIA 

      1090       1100       1110       1120       1130       1140 
DFVGELFVSN SYRDYLEVHG IGVQLTEALA EYWHRRIREE LKFSGNRTMS ADDPEAVEDY 

      1150       1160       1170       1180       1190       1200 
FKLGYRGARF AFGYGACPDL EDRIKMMELL QPERIGVTIS EELQLHPEQS TDAFVLHHPA 


AKYFNV 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00017 Genomic DNA. Translation: AAA17182.1. Frameshift.
AL035310 Genomic DNA. Translation: CAA22918.1. Different initiation.
AL583921 Genomic DNA. Translation: CAC31688.1.
PIRE87072.
S72842.
RefSeqNP_301940.1. NC_002677.1.

3D structure databases

ProteinModelPortalQ49775.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272631.ML1307.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC31688; CAC31688; CAC31688.
GeneID910429.
KEGGmle:ML1307.
PATRIC18054948. VBIMycLep78757_2411.

Organism-specific databases

LepromaML1307.
CMRSearch...

Phylogenomic databases

eggNOGCOG1410.
HOGENOMHOG000251408.
KOK00548.
OMALTEHYAM.
OrthoDBEOG6091CH.

Enzyme and pathway databases

UniPathwayUPA00051; UER00081.

Family and domain databases

Gene3D1.10.1240.10. 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.
InterProIPR003759. 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]
PfamPF02310. 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]
PIRSFPIRSF000381. MetH. 1 hit.
SMARTSM01018. B12-binding_2. 1 hit.
[Graphical view]
SUPFAMSSF47644. SSF47644. 1 hit.
SSF51717. SSF51717. 1 hit.
SSF52242. SSF52242. 1 hit.
SSF56507. SSF56507. 1 hit.
SSF82282. SSF82282. 1 hit.
TIGRFAMsTIGR02082. metH. 1 hit.
PROSITEPS50974. 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]
ProtoNetSearch...

Entry information

Entry nameMETH_MYCLE
AccessionPrimary (citable) accession number: Q49775
Secondary accession number(s): Q9CC37, Q9S378
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: April 27, 2001
Last modified: July 9, 2014
This is version 108 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways