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B2TBS1 (METE_BURPP) 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:Bphyt_5364
OrganismBurkholderia phytofirmans (strain DSM 17436 / PsJN) [Complete proteome] [HAMAP]
Taxonomic identifier398527 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia

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_1000097821

Sites

Metal binding6411Zinc By similarity
Metal binding6431Zinc By similarity
Metal binding7261Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
B2TBS1 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: 046279E5437DD89A

FASTA76485,321
        10         20         30         40         50         60 
MARTHIPGFP RIGAQRELKF AQESFWRGES DEQYLLGVAR ELRARHWQLQ QDAKLDFVTV 

        70         80         90        100        110        120 
GDFAYYDQML NLSALLGALP QRFGFDAKTL SLARYYELAR GNAAQPAMEM TKWFDTNYHY 

       130        140        150        160        170        180 
LVPELGPQTT FDGGVEWLFD EIDEALALNL PVKPVLIGPI TYLWLSKSHV AGFDRLSLLP 

       190        200        210        220        230        240 
KLVIRYSRLL EKLKQRGIEW VQLDEPALCV DLPVEWLDAF SAAYDVLGTS GVKVLLATYF 

       250        260        270        280        290        300 
ESAAEHAPRV AVLPVAGVHL DLVRAPQQLD AWRAALPKHA VLSAGVIDGR NIWRADLGEI 

       310        320        330        340        350        360 
FESLQALHAE FGERLWVSSS CSLLHVPVSL DAEQKLDADL KSWLAFATEK LGEVATLALA 

       370        380        390        400        410        420 
LRDPAAAEAT LAAADRALDA RRHSSTVVNA LVQKRVAAVS SAMADRQSPF AERNRLQREA 

       430        440        450        460        470        480 
LGLPLLPTTT IGSFPQTPAI RQARAAYKRG ELRALDYLQR MRAEIEIAVR KQEELGLDVL 

       490        500        510        520        530        540 
VHGEAERNDM VEYFGEQLWG YAFTENGWVQ SYGSRCVKPP IIYGDVYRPE PMTVETTRYA 

       550        560        570        580        590        600 
QSLTQRLMKG MLTGPVTMLQ WSFVRDDQPR STTALQLALA IRDEVVDLEK AGIRIIQIDE 

       610        620        630        640        650        660 
PAFREGLPLR RGDWAAYLEW ATRVFRISAA GVADQTQIHT HMCYSEFNDI LPSIAAMDAD 

       670        680        690        700        710        720 
VITIETSRSA MELLDGFGAF AYPNEIGPGV YDIHSPRVPD AQAMQRLLER ACEVIPAERL 

       730        740        750        760 
WVNPDCGLKT RGWPETEAAL TNMVRAAKAL RAKLAAKQPD EVTA 

« Hide

References

[1]"Complete sequence of chromosome 2 of Burkholderia phytofirmans PsJN."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Nowak J., Sessitsch A., Lazarovits G., Compant S., Barka E., Tiedje J.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17436 / PsJN.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001053 Genomic DNA. Translation: ACD19723.1.
RefSeqYP_001889093.1. NC_010676.1.

3D structure databases

ProteinModelPortalB2TBS1.
SMRB2TBS1. Positions 3-753.
ModBaseSearch...

Protein-protein interaction databases

STRINGB2TBS1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6280325.
GenomeReviewsGene locus Bphyt_5364 in contig CP001053_GR.
KEGGbpy:Bphyt_5364.
PATRIC19205419. VBIBurPhy117947_1512.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG287495.
OMALWLSKSH.
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_BURPP
AccessionPrimary (citable) accession number: B2TBS1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 1, 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