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Database: UniProt/TrEMBL
Entry: A0A126V2N0_9RHOB
LinkDB: A0A126V2N0_9RHOB
Original site: A0A126V2N0_9RHOB 
ID   A0A126V2N0_9RHOB        Unreviewed;       464 AA.
AC   A0A126V2N0;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   05-JUL-2017, entry version 11.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=RC74_13750 {ECO:0000313|EMBL:AML52195.1};
OS   Halocynthiibacter arcticus.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Halocynthiibacter.
OX   NCBI_TaxID=1579316 {ECO:0000313|EMBL:AML52195.1, ECO:0000313|Proteomes:UP000070371};
RN   [1] {ECO:0000313|EMBL:AML52195.1, ECO:0000313|Proteomes:UP000070371}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC 20958 {ECO:0000313|EMBL:AML52195.1};
RA   Lee Y.M., Baek K., Lee H.K., Shin S.C.;
RT   "Complete genome sequence of Halocynthiibacter arcticus PAMC 20958t
RT   from arctic marine sediment.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: L-glutamate = 4-aminobutanoate + CO(2).
CC       {ECO:0000256|RuleBase:RU361171}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC         ECO:0000256|RuleBase:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; CP014327; AML52195.1; -; Genomic_DNA.
DR   RefSeq; WP_039000394.1; NZ_CP014327.1.
DR   EnsemblBacteria; AML52195; AML52195; RC74_13750.
DR   KEGG; hat:RC74_13750; -.
DR   KO; K01580; -.
DR   Proteomes; UP000070371; Chromosome.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006536; P:glutamate metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR010107; Glutamate_decarboxylase.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   PANTHER; PTHR43321; PTHR43321; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01788; Glu-decarb-GAD; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000070371};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070371}.
FT   MOD_RES     273    273       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   464 AA;  51538 MW;  4DAC060BA956B74E CRC64;
     MVDTTKTPAP SNHFDEIYGS DEMSVPLSES IFPGSESDPR NVYASIRDEL MLDGNSRQNL
     ATFCQTWEEP EIHQLMDDCI DKNMVDKDEY PQTAEIEQRC VRMLADLWNA PSGAATGCST
     TGSSEAAMLG GLAMKRRWEA RRKAEGKPID KPNLITGPVQ VCWHKFTRYW DVEHREIPME
     NGRLLMTPEE VLSLCDENTI GVVPTLGVTF TGQYEPVEAV SAALDKYEAE TGLDIPIHVD
     GASGGFLAPF CAPELMWDFR LPRVKSINAS GHKFGLAPLG VGWIVWRSAD DLPENLVFWV
     NYLGGNMRDI GLNFSRPGGP ITCQYYNFQR LGREGYTKIH KACYATAQYL AAEIGALGPF
     DIVYDGDMTS GIPALCWTLK PDVDLGFTLF DLADRLRIYG WQVPAYTLPA NCQTQAIQRI
     LVRNGVSRDL ATLLMRDIRK ALAHLTKHPA ETPLGENAAG GFHH
//
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