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B2JNZ4 (METE_BURP8) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 27. 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:Bphy_5470
OrganismBurkholderia phymatum (strain DSM 17167 / STM815) [Complete proteome] [HAMAP]
Taxonomic identifier391038 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia

Protein attributes

Sequence length763 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 – 7637635-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase HAMAP MF_00172
PRO_1000097820

Sites

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

Sequences

Sequence LengthMass (Da)Tools
B2JNZ4 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: 9B468EECD01C8A5E

FASTA76384,900
        10         20         30         40         50         60 
MVTTHNLGFP RIGAHRELKF ALEKYWKGES SRAELKAVGA QLRARHWQDQ ARLDFSPVGD 

        70         80         90        100        110        120 
FAFYDQVLDM SFTLGNLPER VRGFHGDALD NAFRVARGRS AHGADDHSAC CGGVAAGEMT 

       130        140        150        160        170        180 
KWFDTNYHYI VPEFDTNTQF SLDPSRLLEQ IKEAHAQGVK AKPVIIGPVT YLWLGKAKDG 

       190        200        210        220        230        240 
SDKLTLLPRL LPVYAALLDY FTAQGIDWVQ IDEPVLVTEL DARWRDAFVP AYDALAARRV 

       250        260        270        280        290        300 
RVLLATYFGQ LKENLELACQ LPVDGLHIDA IHARDEVAQV AAQVPETAVL SVGVINGRNV 

       310        320        330        340        350        360 
WKTDLNAALA WLEPLHATLG DRLWIAPSCS LLHSPVDLNS ERKLDADIRS WLAFALQKLD 

       370        380        390        400        410        420 
ELTLLASALN NGRACVEAEL LANAKAIESR RASPRVHNAA VKAALARIDA SLGQRANAYP 

       430        440        450        460        470        480 
ARAAKQAAAL ALPAFPTTTI GSFPQTADIR RARSQFKAGE LDYAGYKLAM EREITRAVKE 

       490        500        510        520        530        540 
QETLGLDVLV HGEAERNDMV EYFGEQLDGY VFSQFGWVQS YGSRCVKPPI LFGDISRPKA 

       550        560        570        580        590        600 
MTVEWICYAQ AQTAKPMKGM LTGPVTILNW SFVRDDQPRS VSCRQLALAI REEVLDLEKA 

       610        620        630        640        650        660 
GVRVIQIDEA ALREGLPLRR SQWNEYLQWA VESFRIAANG VQDETQIHTH MCYSEFNDII 

       670        680        690        700        710        720 
ASIAEMDADV ITIETSRSDM ELLDAFDDFH YPNQIGPGVY DIHSPNIPDQ AHVVDLMKKA 

       730        740        750        760 
AERIPAERLW VNPDCGLKTR AWEEVIPALK NMVAAARTLR QAV 

« Hide

References

[1]"Complete sequence of chromosome 2 of Burkholderia phymatum STM815."
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Bruce D., Goodwin L., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Mikhailova N., Bacher J., Blanchard J., Cohan F., James E., Lawrence J., Lizotte-Waniewski M., Moulin L., Rainey P., Riley M., Souza V., Wertz J., Young P.
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17167 / STM815.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001044 Genomic DNA. Translation: ACC74547.1.
RefSeqYP_001861593.1. NC_010623.1.

3D structure databases

ProteinModelPortalB2JNZ4.
SMRB2JNZ4. Positions 3-761.
ModBaseSearch...

Protein-protein interaction databases

STRINGB2JNZ4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6246954.
GenomeReviewsGene locus Bphy_5470 in contig CP001044_GR.
KEGGbph:Bphy_5470.
PATRIC19197752. VBIBurPhy25146_5757.

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_BURP8
AccessionPrimary (citable) accession number: B2JNZ4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: June 10, 2008
Last modified: January 25, 2012
This is version 27 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