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B8D8J2 (B8D8J2_BUCA5) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 20. Feed History...

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

Protein namesRecommended name:
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase HAMAP MF_00172
EC=2.1.1.14 HAMAP MF_00172
Alternative name(s):
Cobalamin-independent methionine synthase HAMAP MF_00172
Methionine synthase, vitamin-B12 independent isozyme HAMAP MF_00172
Gene names
Name:metE HAMAP MF_00172 EMBL ACL30414.1
Ordered Locus Names:BUAP5A_029
OrganismBuchnera aphidicola subsp. Acyrthosiphon pisum (strain 5A) [Complete proteome] [HAMAP]
Taxonomic identifier563178 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length758 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 SAAS SAAS013215

Catalytic activity

5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = tetrahydropteroyltri-L-glutamate + L-methionine. HAMAP MF_00172 SAAS SAAS013215

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 SAAS SAAS013215

Sequence similarities

Belongs to the vitamin-B12 independent methionine synthase family. HAMAP MF_00172

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Metal binding6391Zinc By similarity HAMAP MF_00172
Metal binding6411Zinc By similarity HAMAP MF_00172
Metal binding7241Zinc By similarity HAMAP MF_00172

Sequences

Sequence LengthMass (Da)Tools
B8D8J2 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: 20F1C5160DF46D24

FASTA75887,916
        10         20         30         40         50         60 
MTILNHTLGF PRIGLNRELK KAQEQYWSGE LMIKDLLLVG SELRKKNWQK QKESGIDYIP 

        70         80         90        100        110        120 
VGDFAWYDHV LTTSMMLGNI PERHNNTVDS IDLDCLFRIA RGCPPDISAS EMTKWFNTNY 

       130        140        150        160        170        180 
HYIVPEFYKN KVLKYSWKQI LDEVDEALLL GHKVKPILLG PITYLWLGKV KGEYFDRLDI 

       190        200        210        220        230        240 
LKDIILIYKH VLKELSNRSI DFVQIDEPVL VLELPKKWKD AYHYAYKELS GITKLLLTTY 

       250        260        270        280        290        300 
FDSIEHNIEF IRDLPVQGIH IDLVHGKYNL KNFSSKIPSE WMLSLGVING RNIWRSDLLK 

       310        320        330        340        350        360 
WFKSIKSISN HHRKILIGSS CSLLHTPIDL VAEKHLDKEV KRWFSFAVQK CEELRLLSSA 

       370        380        390        400        410        420 
LNDNDIDSIK EWSLPIYERS VSKRVNKIEV ENRLSNVLID KHQRLSPYKT RSIEQNKKFN 

       430        440        450        460        470        480 
FPILPTTTIG SFPQTISIRK LRRDFKLGLV TEEEYTKIIK KNIKKVIKIQ EELDIDVLVH 

       490        500        510        520        530        540 
GEAERNDMVE YFGEHLDGFA FTDNGWVQSY GSRCVKPPII IGDISRPKPM TIEWSKYAQS 

       550        560        570        580        590        600 
LTKKPVKGML TGPVTILLWS FPREDVSLKK IATQIALALY DEVLDLEKEK IEIIQIDEPA 

       610        620        630        640        650        660 
LREGLPLRKS SWHEYLSWAV DVFRLSASGV KNTTQIHTHM CYCEFNDIMD SIALLDADVI 

       670        680        690        700        710        720 
TIEAARSDME LLESFKKFKY PNEVGPGAYD IHSSNIPSVQ SIISLLNKAM KYIPLKRIWV 

       730        740        750 
NPDCGLKTRN WNETILSLKN MVEATKILRE KMKDSECD

« Hide

References

[1]"The dynamics and time scale of ongoing genomic erosion in symbiotic bacteria."
Moran N.A., McLaughlin H.J., Sorek R.
Science 323:379-382(2009) [PubMed: 19150844] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 5A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001161 Genomic DNA. Translation: ACL30414.1.
RefSeqYP_002467801.1. NC_011833.1.

3D structure databases

ProteinModelPortalB8D8J2.
ModBaseSearch...

Protein-protein interaction databases

STRINGB8D8J2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBUCT00000000942; EBBUCP00000000897; EBBUCG00000000942.
GeneID7262375.
GenomeReviewsGene locus BUAP5A_029 in contig CP001161_GR.
KEGGbap:BUAP5A_029.
PATRIC21242279. VBIBucAph51993_0029.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000007816.
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 nameB8D8J2_BUCA5
AccessionPrimary (citable) accession number: B8D8J2
Entry history
Integrated into UniProtKB/TrEMBL: March 3, 2009
Last sequence update: March 3, 2009
Last modified: December 14, 2011
This is version 20 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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