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A1S8X3 (A1S8X3_SHEAM) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 42. 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
Ordered Locus Names:Sama_2627
OrganismShewanella amazonensis (strain ATCC BAA-1098 / SB2B) [Complete proteome] [HAMAP] EMBL ABM00830.1
Taxonomic identifier326297 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length756 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. HAMAP MF_00172

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Metal binding6421Zinc By similarity HAMAP MF_00172
Metal binding6441Zinc By similarity HAMAP MF_00172
Metal binding7271Zinc By similarity HAMAP MF_00172

Sequences

Sequence LengthMass (Da)Tools
A1S8X3 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 3D58220D81F4FCBE

FASTA75685,006
        10         20         30         40         50         60 
MQLNSLGFPR IGRRRELKFA LEQYWRGELS RNELVAQAKA LRQTHWQWQA DAGVERLPVG 

        70         80         90        100        110        120 
DFAYYDQVLT LAATLNVIPE RHRDGDKVDL DTLFRVARGR APSGKAAAAA EMTKYFNTNY 

       130        140        150        160        170        180 
HYIVPELHPN QTFSIAWTQL FDEVEEVKAL GYDPKPCILG PVSFLYLSKA YGSEFDKLSL 

       190        200        210        220        230        240 
LPQLLVTYAE LLARFAAQGV SWVQIEEPVL ALDLDESWQA AFATAYQAFT CVSVKLLLTT 

       250        260        270        280        290        300 
YYGSVAHHAD IIQTLPVAGL HLDLVSAPEQ LEVFLPRLGQ QQVLSLGLIN GRNVWAEDLD 

       310        320        330        340        350        360 
LIAERIAPVA RELGDRLWLA TSCSLLHTPV DLDVETALKP ELKRQLAFAR QKLLELRSLN 

       370        380        390        400        410        420 
TLLTVPNGAD AAAIAAECVA RRTARAQAAD AAVAARLDAL TKADFERQSA FPERQQQQQQ 

       430        440        450        460        470        480 
RLKLPLLPTT TIGSFPQTPA IRGLRNRFRK GEISALEYDN QLRQVCRNTI DRQLKLGIDV 

       490        500        510        520        530        540 
LVHGEAERND MVEYFGEQLE GVGFTKHGWV QSYGSRCVKP PLIYGDVSRP KPMTLDWAEY 

       550        560        570        580        590        600 
AQSLTDKPVK GMLTGPVTIL HWSFAREDIS RDTLCKQIAL AIRDEVADLE RVGIAIIQID 

       610        620        630        640        650        660 
EPAFREGLPL RRCDWKAYLD WAVDSFKLSA ACVRDNTQIH THMCYSEFND TIAAIAAMDA 

       670        680        690        700        710        720 
DVITIETSRS AMELLRAFED FEYPAEIGPG VYDIHSPNTP DVGAMVTLME RAARRIPLRQ 

       730        740        750 
LWVNPDCGLK TRTWDEVEPA LRNMVDATRE LRRRLG 

« Hide

References

[1]"Complete sequence of Shewanella amazonensis SB2B."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Fredrickson J., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1098 / SB2B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000507 Genomic DNA. Translation: ABM00830.1.
RefSeqYP_928499.1. NC_008700.1.

3D structure databases

ProteinModelPortalA1S8X3.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1S8X3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4604874.
GenomeReviewsGene locus Sama_2627 in contig CP000507_GR.
KEGGsaz:Sama_2627.
NMPDRfig|326297.7.peg.2462.
PATRIC23454101. VBISheAma74963_2702.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0620.
HOGENOMHBG287495.
OMARNIWRAN.
PhylomeDBA1S8X3.
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 nameA1S8X3_SHEAM
AccessionPrimary (citable) accession number: A1S8X3
Entry history
Integrated into UniProtKB/TrEMBL: February 6, 2007
Last sequence update: February 6, 2007
Last modified: December 14, 2011
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)