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Q0I3P2 (METE_HAES1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 47. 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:HS_0824
OrganismHaemophilus somnus (strain 129Pt) (Histophilus somni (strain 129Pt)) [Complete proteome] [HAMAP]
Taxonomic identifier205914 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHistophilus

Protein attributes

Sequence length757 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 – 7577575-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase HAMAP MF_00172
PRO_1000017247

Sites

Metal binding6431Zinc By similarity
Metal binding6451Zinc By similarity
Metal binding7281Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0I3P2 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: 7DB7AADB2887E374

FASTA75785,725
        10         20         30         40         50         60 
MTTFHVLGFP RVGAKRELKF AQERYWRKEL AEQDLLDLAK ALREKNWKHQ ADANADFVAV 

        70         80         90        100        110        120 
GDFTFYDHIL DLQVATGAIP ARFGFDSKNL TLDQYFQLAR GNKDQFAIEM TKWFDTNYHY 

       130        140        150        160        170        180 
LVPEFHKDTQ FKANPTHYVN QIREAKVAGH QVKPVIVGPL TFLWLGKEKG ESFNRFELLA 

       190        200        210        220        230        240 
QLVPVYVEIL NALVAEGAEW IQIDEPALAV DLPKEWGNAY KDVYATLSEK VNAKLLLATY 

       250        260        270        280        290        300 
FGSVTEHATL LKELSVDGLH LDLVRAPEQL VAFEDYNKVL SAGVIDGRNI WRANLNTVLD 

       310        320        330        340        350        360 
VLEPLKEKLG ERLWIAPSCS LLHTPFDLNV ETQLQENNPA LYSWLAFTLQ KVQELSVLKT 

       370        380        390        400        410        420 
ALEKGRTAVN VELDASQVAA DARANSKEIH RPEVAERLAN LPKNADQRKS PFGERIKLQN 

       430        440        450        460        470        480 
AWLNLPLLPT TSIGSFPQTT DIRRARAAFK KGDLSLEEYE NSMKKEIELV VREQEKLDLD 

       490        500        510        520        530        540 
VLVHGEPERN DMVEYFGELL DGFAFTKFGW VQSYGSRCVK PPVIYGDVVR PKAMTVRWSK 

       550        560        570        580        590        600 
YAQSLTKKVM KGMLTGPVTI LQWSFVRNDI PRSTVCKQIG VALSDEVLDL EKAGIKVIQI 

       610        620        630        640        650        660 
DEPAIREGLP LKRADWDTYL QWAGEAFRLS SMGVADDTQI HTHMCYSEFN DILPAIAALD 

       670        680        690        700        710        720 
ADVITIETSR SDMELLTAFG DFKYPNDIGP GVYDIHSPRV PTAEEIEHLL RKALNVVPKE 

       730        740        750 
RLWVNPDCGL KTRGWSETIA QLEVMMSVTK KLRAELA 

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References

[1]"Complete genome sequence of Haemophilus somnus (Histophilus somni) strain 129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus influenzae Rd."
Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O., Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N., Xie G., Inzana T.J.
J. Bacteriol. 189:1890-1898(2007) [PubMed: 17172329] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 129Pt.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000436 Genomic DNA. Translation: ABI25099.1.
RefSeqYP_719034.1. NC_008309.1.

3D structure databases

ProteinModelPortalQ0I3P2.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0I3P2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4240316.
GenomeReviewsGene locus HS_0824 in contig CP000436_GR.
KEGGhso:HS_0824.
NMPDRfig|205914.1.peg.295.
PATRIC20281657. VBIHaeSom53361_0865.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0620.
HOGENOMHBG287495.
OMARNIWRAN.
PhylomeDBQ0I3P2.
ProtClustDBPRK05222.

Enzyme and pathway databases

BioCycHSOM205914:HS_0824-MONOMER.

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_HAES1
AccessionPrimary (citable) accession number: Q0I3P2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 3, 2006
Last modified: January 25, 2012
This is version 47 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