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B1K5S8 (METE_BURCC) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase

EC=2.1.1.14
Alternative name(s):
Cobalamin-independent methionine synthase
Methionine synthase, vitamin-B12 independent isozyme
Gene names
Name:metE
Ordered Locus Names:Bcenmc03_4982
OrganismBurkholderia cenocepacia (strain MC0-3) [Complete proteome] [HAMAP]
Taxonomic identifier406425 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length764 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation By similarity. HAMAP MF_00172

Catalytic activity

5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = tetrahydropteroyltri-L-glutamate + L-methionine. HAMAP MF_00172

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP MF_00172

Pathway

Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetE route): step 1/1. HAMAP MF_00172

Sequence similarities

Belongs to the vitamin-B12 independent methionine synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 7647645-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase HAMAP MF_00172
PRO_1000097818

Sites

Metal binding6501Zinc By similarity
Metal binding6521Zinc By similarity
Metal binding7351Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
B1K5S8 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: 5323BF8E96F77AC2

FASTA76485,630
        10         20         30         40         50         60 
MVTTHNLGFP RIGAKRELKF GLERYWKGES SRDELKALGA ELRRRHWHDQ RDLDLAPIGD 

        70         80         90        100        110        120 
FAFYDQVLDM SFTLGNLPKR VQDFHGDALD NYFRVARGRS AQSAEEHAAC CGGVAAGEMT 

       130        140        150        160        170        180 
KWFDTNYHYI VPEFHADTNF SLDPSRLLQQ LAEANAQGVN AKPVILGPVT YLWLGKAKDD 

       190        200        210        220        230        240 
SDRLALLPKL LPVYGALLDT LTAQGVEWVQ IDEPILVTEL DAEWRQAFRI AYAALETRRI 

       250        260        270        280        290        300 
KLLLATYFGQ LQDNLTLAAS LPVDGLHIDA INARDEVDAL VRELPAERVL SVGAINGRNI 

       310        320        330        340        350        360 
WKTDLNAALD WLEPLAKQLG DRLWLAPSCS LLHVPVDLAS EEKLDAEIRS WLAFALQKLD 

       370        380        390        400        410        420 
ELKVLATALN EGRDKVADAL AANAAAIDSR RRSPRVNNPA VKAAIARIDA RLGNRTSPYT 

       430        440        450        460        470        480 
QRASKQSARL NLPAFPTTTI GSFPQTAEIR QARSRFKAGA LDEAGYRKAM QAEIERSVRE 

       490        500        510        520        530        540 
QESLELDVLV HGEAERNDMV EYFGEQLDGY AFSQFGWVQS YGSRCVKPPI LFGDISRPKA 

       550        560        570        580        590        600 
MTVEWIAYAQ SLTRKPMKGM LTGPVTILNW SFVRDDQPRA VSCYQLALAI REEVLDLEKA 

       610        620        630        640        650        660 
GVRVIQIDEA ALREGLPLRR AQWSEYLKWA VESFRITANG VQDDTQIHTH MCYSEFNDII 

       670        680        690        700        710        720 
ASIADMDADV ITIETSRSDM ELLDAFDTFK YPNEIGPGVY DIHSPNIPTQ DHIVGLMRKA 

       730        740        750        760 
AERIPAERLW VNPDCGLKTR QWAEVIPALT NMVAAAKMLR NQVQ 

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References

[1]"Complete sequence of chromosome 2 of Burkholderia cenocepacia MC0-3."
Copeland A., Lucas S., Lapidus A., Barry K., Bruce D., Goodwin L., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Mikhailova N., Tiedje J., Richardson P.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MC0-3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000959 Genomic DNA. Translation: ACA94112.1.
RefSeqYP_001778602.1. NC_010515.1.

3D structure databases

ProteinModelPortalB1K5S8.
SMRB1K5S8. Positions 3-762.
ModBaseSearch...

Protein-protein interaction databases

STRINGB1K5S8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6127794.
GenomeReviewsGene locus Bcenmc03_4982 in contig CP000959_GR.
KEGGbcm:Bcenmc03_4982.
PATRIC19099642. VBIBurCen61509_6282.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG287495.
OMARNIWRAN.
ProtClustDBPRK05222.

Family and domain databases

HAMAPMF_00172. Meth_synth.
[Tree]
InterProIPR013215. Cbl-indep_Met_Synth_N.
IPR006276. Cobalamin-indep_Met_synthase.
IPR002629. Methionine_synth.
[Graphical view]
KOK00549.
PfamPF08267. Meth_synt_1. 1 hit.
PF01717. Meth_synt_2. 1 hit.
[Graphical view]
PIRSFPIRSF000382. MeTrfase_B12_ind. 1 hit.
TIGRFAMsTIGR01371. Met_syn_B12ind. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMETE_BURCC
AccessionPrimary (citable) accession number: B1K5S8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 29, 2008
Last modified: January 25, 2012
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families