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Database: UniProt/TrEMBL
Entry: B0TPE4_SHEHH
LinkDB: B0TPE4_SHEHH
Original site: B0TPE4_SHEHH 
ID   B0TPE4_SHEHH            Unreviewed;       464 AA.
AC   B0TPE4;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   25-OCT-2017, entry version 64.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   OrderedLocusNames=Shal_3043 {ECO:0000313|EMBL:ABZ77591.1};
OS   Shewanella halifaxensis (strain HAW-EB4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=458817 {ECO:0000313|EMBL:ABZ77591.1, ECO:0000313|Proteomes:UP000001317};
RN   [1] {ECO:0000313|EMBL:ABZ77591.1, ECO:0000313|Proteomes:UP000001317}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB4 {ECO:0000313|EMBL:ABZ77591.1,
RC   ECO:0000313|Proteomes:UP000001317};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella halifaxensis HAW-EB4.";
RL   Submitted (JAN-2008) 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; CP000931; ABZ77591.1; -; Genomic_DNA.
DR   RefSeq; WP_012278117.1; NC_010334.1.
DR   ProteinModelPortal; B0TPE4; -.
DR   STRING; 458817.Shal_3043; -.
DR   EnsemblBacteria; ABZ77591; ABZ77591; Shal_3043.
DR   KEGG; shl:Shal_3043; -.
DR   eggNOG; ENOG4105CVK; Bacteria.
DR   eggNOG; COG0076; LUCA.
DR   HOGENOM; HOG000070228; -.
DR   KO; K01580; -.
DR   OMA; RPNLVMG; -.
DR   OrthoDB; POG091H06F5; -.
DR   Proteomes; UP000001317; 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:UP000001317};
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}.
FT   MOD_RES     274    274       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   464 AA;  52394 MW;  36E4102AEFD4FC78 CRC64;
     MPLHSKDTVR DDLLDDIYSS TDLALSMPKY KMPEQENNSR HAYQIVHDEL MMDGNSRQNL
     ATFCQTWVED EVHQLMDECI DKNMIDKDEY PQTAELEARC VHMLADLWNS PDAENTLGCS
     TTGSSEAAML GGMALKWAWR KKMKALGKPT DKPNMICGPV QVCWHKFARY WDIELREIPM
     EGDRLIMNAE EVIKRCDENT IGVVPTLGVT FTCQYEPVKA VHDALDQLQK DTGLDIPMHV
     DAASGGFLAP FCQPDLEWDF KLPRVKSINA SGHKFGLSPL GVGWVIWRDA SVLDEDLIFN
     VNYLGGNMPT FALNFSRPGG QIVAQYYNFL RLGKEGYRKI HQACYDTAQY LSSEIEKLGM
     FEIIYDGHGG IPAMSWSLKE GVDPGFNLFD LSDRIRSRGW QIAAYAMPPK REDLVIMRIL
     VRHGFSRDQA DLLVADLKHC VDFFASHPIS HGSDAKESSG FNHG
//
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