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Q2JXU5 (Q2JXU5_SYNJA) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 48. 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 1 HAMAP MF_00172
EC=2.1.1.14 HAMAP MF_00172
Alternative name(s):
Cobalamin-independent methionine synthase 1 HAMAP MF_00172
Methionine synthase, vitamin-B12 independent isozyme 1 HAMAP MF_00172
Gene names
Name:metE-1 EMBL ABC98377.1
Synonyms:metE1 HAMAP MF_00172
Ordered Locus Names:CYA_0148
OrganismSynechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone A-Prime) [Complete proteome] [HAMAP]
Taxonomic identifier321327 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Chroococcales › Synechococcus

Protein attributes

Sequence length754 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 binding6311Zinc By similarity HAMAP MF_00172
Metal binding6331Zinc By similarity HAMAP MF_00172
Metal binding7161Zinc By similarity HAMAP MF_00172

Sequences

Sequence LengthMass (Da)Tools
Q2JXU5 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: 883695787C41F834

FASTA75484,835
        10         20         30         40         50         60 
MTAQTMTLGY ARMGKRRELK KALEGFWSGA LGSEALLATF WDLETQAWQT QLQAGIDHIA 

        70         80         90        100        110        120 
VGDQTLYDHV LDWATWLGLI PSRFRGLSGL DRYFAMARGR EGLPALEMTK WFDTNYHYLV 

       130        140        150        160        170        180 
PEIEPEADPS PNFGDFLERV RRAQGILGER TSPVVLSPVT LLCLSQRSGD LRADLEKLLP 

       190        200        210        220        230        240 
LYRDLLQELK QLGIPEVQIH DPILVTSQGS GLREAVEMSY RQLATAGIRV HLVTYFDDLG 

       250        260        270        280        290        300 
ETYPWVVQLP VAGISLDFTR GHTLDLVRTY GFPADQILGA GVVDARNVWK VQPETVLASL 

       310        320        330        340        350        360 
RELQGVAPNL RVQPSASLQF VPHDAALEAQ LPEPLRNVLS FAEQKLAEVA LLARALNGED 

       370        380        390        400        410        420 
TAAQQAEIQQ QWQSFAQFSP PNPQVRQALA NLKLQDFERF LPYEQRLSRQ VQLPPLPTTT 

       430        440        450        460        470        480 
IGSFPQTPEV RQWRAKYKRG EVSQAEYEAA IDAEIAKCIR IQEEIGLDVL VHGEFERTDM 

       490        500        510        520        530        540 
VEYFAQKLEG FAFTEHGWVQ SYGSRCVRPP ILYGDVVRPQ PMTVREFQVA QSHTQKPVKG 

       550        560        570        580        590        600 
MLTGPVTMLN WSFPRVDIPR REQALQIALA LRAEVADLEA AGAVMVQVDE PALREGLPLK 

       610        620        630        640        650        660 
KERWPEYLSW AVDAFRLATG GAKPETQIHT HMCYSEFGDI IEHIERLDAD VLSIENSRSN 

       670        680        690        700        710        720 
NKTLLQIAQA GYRHQVGNGV YDVHSPAVPS VEQILQQLRT GLAHLPVEQT WVNPDCGLKT 

       730        740        750 
RRWEEVIPAL KNMVAAAHQL REELLETQPE GLRE

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References

[1]"Population level functional diversity in a microbial community revealed by comparative genomic and metagenomic analyses."
Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N., Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.
ISME J. 1:703-713(2007) [PubMed: 18059494] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JA-3-3Ab.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000239 Genomic DNA. Translation: ABC98377.1.
RefSeqYP_473640.1. NC_007775.1.

3D structure databases

ProteinModelPortalQ2JXU5.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2JXU5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3897814.
GenomeReviewsGene locus CYA_0148 in contig CP000239_GR.
KEGGcya:CYA_0148.
PATRIC23808559. VBISynSp90045_0148.
TIGRCYA_0148.

Phylogenomic databases

eggNOGCOG0620.
HOGENOMHBG287495.
OMANIWANDF.
PhylomeDBQ2JXU5.
ProtClustDBPRK05222.

Enzyme and pathway databases

BioCycSSP321327:CYA_0148-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 nameQ2JXU5_SYNJA
AccessionPrimary (citable) accession number: Q2JXU5
Entry history
Integrated into UniProtKB/TrEMBL: March 7, 2006
Last sequence update: March 7, 2006
Last modified: January 25, 2012
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info