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B6J6H8 (METE_COXB1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 24. 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:CbuK_2095
OrganismCoxiella burnetii (strain CbuK_Q154) (Coxiella burnetii (strain Q154)) [Complete proteome] [HAMAP]
Taxonomic identifier434924 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella

Protein attributes

Sequence length775 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 – 7757755-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase HAMAP MF_00172
PRO_1000097822

Sites

Metal binding6451Zinc By similarity
Metal binding6471Zinc By similarity
Metal binding7301Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
B6J6H8 [UniParc].

Last modified December 16, 2008. Version 1.
Checksum: 5FBC2B4A170D13DE

FASTA77588,391
        10         20         30         40         50         60 
MVYAHNLGFP RIGIKREMKK TVEAYWRGEI SQQQLQQQAI ELQLTNWKIQ AEAGVDLIPV 

        70         80         90        100        110        120 
GDFSWYDHVL DMAVRVGAIP SRFKALNSNI TDTMFCMARG QAPNGIETSA CEMTKWFDTN 

       130        140        150        160        170        180 
YHYIVPEFTT NQSFELHHDD LFKSTKLALE NNYRAKPVIL GPLSFLWLGK CKGESFNKLL 

       190        200        210        220        230        240 
LLEKLLPVYA EIFEQLSSLG VEWVQVDEPI LVLDLPPEWQ QAFLTTYQQL NFFNLKCLLA 

       250        260        270        280        290        300 
TYFGSLDDNL SLTCQLPVDG LHIDYCRAPD QLDSVLSQLP AEKILSVGII DGRNIWCNDL 

       310        320        330        340        350        360 
NRSLTLLENI QSSLGDRLWV APSCSLLHVP IDLDQENKLD VELKSWFAFA KQKVAEAAFL 

       370        380        390        400        410        420 
TRGLREGRES IGAELKKNEE VIISRKTSKR IHNPNVEKKA ASVTERLMRR QHEHSIRKNK 

       430        440        450        460        470        480 
QTAQLNLPLF PTTTIGSFPQ TSQIRCLRRD YKQGKIDDAL YEEKIRQEIA EVIGIQVKLG 

       490        500        510        520        530        540 
LDVLVHGEPE RNDMVEYFGE LLDGIAITSN GWVQSYGSRC VKPPIIFGDV SRERPMTLRW 

       550        560        570        580        590        600 
IEYAQSLTTK SVKGMLTGPV TILAWSFVRD DQPRSQTAKQ IALALRDEVQ DLERSGVRVI 

       610        620        630        640        650        660 
QIDEPAFREC LPLRKAAWQD YLEWAVKCFR LASCGVKDET QIHTHMCYSE FNDIIEAIAA 

       670        680        690        700        710        720 
LDADVITIES SRSETEILKS FEKFAYPNDI GPGIYDIHSP RIPRVAEIEE LAVRALQYIP 

       730        740        750        760        770 
IERLWINPDC GLKTRNWEET KEALSRMVDA AKHLRKAFSS EKTPTIDLEL QPAST 

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References

[1]"Comparative genomics reveal extensive transposon-mediated genomic plasticity and diversity among potential effector proteins within the genus Coxiella."
Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D., Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., Samuel J.E., Heinzen R.A.
Infect. Immun. 77:642-656(2009) [PubMed: 19047403] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CbuK_Q154.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001020 Genomic DNA. Translation: ACJ21188.1.
RefSeqYP_002306333.1. NC_011528.1.

3D structure databases

ProteinModelPortalB6J6H8.
ModBaseSearch...

Protein-protein interaction databases

STRINGB6J6H8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7016608.
GenomeReviewsGene locus CbuK_2095 in contig CP001020_GR.
KEGGcbc:CbuK_2095.
PATRIC17919652. VBICoxBur77120_2101.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG287495.
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_COXB1
AccessionPrimary (citable) accession number: B6J6H8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: December 16, 2008
Last modified: January 25, 2012
This is version 24 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