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Database: UniProt/TrEMBL
Entry: A8H6T3_SHEPA
LinkDB: A8H6T3_SHEPA
Original site: A8H6T3_SHEPA 
ID   A8H6T3_SHEPA            Unreviewed;       464 AA.
AC   A8H6T3;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   25-OCT-2017, entry version 66.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   OrderedLocusNames=Spea_2953 {ECO:0000313|EMBL:ABV88270.1};
OS   Shewanella pealeana (strain ATCC 700345 / ANG-SQ1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=398579 {ECO:0000313|EMBL:ABV88270.1, ECO:0000313|Proteomes:UP000002608};
RN   [1] {ECO:0000313|EMBL:ABV88270.1, ECO:0000313|Proteomes:UP000002608}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700345 / ANG-SQ1 {ECO:0000313|Proteomes:UP000002608};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S.Z., Manno D., Hawari J., Richardson P.;
RT   "Complete sequence of Shewanella pealeana ATCC 700345.";
RL   Submitted (OCT-2007) 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:RU361171};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU361171}.
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DR   EMBL; CP000851; ABV88270.1; -; Genomic_DNA.
DR   RefSeq; WP_012156174.1; NC_009901.1.
DR   ProteinModelPortal; A8H6T3; -.
DR   STRING; 398579.Spea_2953; -.
DR   EnsemblBacteria; ABV88270; ABV88270; Spea_2953.
DR   KEGG; spl:Spea_2953; -.
DR   eggNOG; ENOG4105CVK; Bacteria.
DR   eggNOG; COG0076; LUCA.
DR   HOGENOM; HOG000070228; -.
DR   KO; K01580; -.
DR   OMA; RPNLVMG; -.
DR   OrthoDB; POG091H06F5; -.
DR   BioCyc; SPEA398579:GHG5-3085-MONOMER; -.
DR   Proteomes; UP000002608; 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:UP000002608};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU361171};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU361171};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002608}.
FT   MOD_RES     274    274       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   464 AA;  52490 MW;  3FF2EA15D50C6F91 CRC64;
     MPLHSKDTVR DDLLDDIYSS SDLALSMPKY KMPEQENNPR HAYQIVHDEL MMDGNSRQNL
     ATFCQTWVED EVHQLMDECI DKNMIDKDEY PQTAELEARC VHMLADLWNS PDAENTLGCS
     TTGSSEAAML GGMALKWAWR KKMKALGKPT DKPNMVCGPV QVCWHKFARY WDIELREIPM
     EGDRLIMNAE EVIKRCDENT IGVVPTLGVT FTCQYEPVKA VHDALDKLQK ETGLDIPMHV
     DAASGGFLAP FCQPELEWDF KLPRVKSINA SGHKFGLSPL GVGWVIWRDA SALDEDLIFN
     VNYLGGNMPT FALNFSRPGG QIVAQYYNFL RLGKEGYRKI HQACYDTAQY LSSEIEKLGM
     FEIIYDGHDG IPAMSWSLKE GVDPGFNLFD LSDRIRSRGW QIAAYAMPPK REDLVIMRIL
     VRHGFSRDQA DLLVADLKHC VEFFAEHPIS HGSDAKESSG FNHG
//
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