ID   A0A1Q6CLK6_9GAMM        Unreviewed;       545 AA.
AC   A0A1Q6CLK6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Glutamate decarboxylase {ECO:0000313|EMBL:OKY27317.1};
GN   ORFNames=BI291_00360 {ECO:0000313|EMBL:OKY27317.1};
OS   Thalassotalea sp. PP2-459.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Thalassotalea.
OX   NCBI_TaxID=1742724 {ECO:0000313|EMBL:OKY27317.1, ECO:0000313|Proteomes:UP000186791};
RN   [1] {ECO:0000313|EMBL:OKY27317.1, ECO:0000313|Proteomes:UP000186791}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PP2-459 {ECO:0000313|EMBL:OKY27317.1,
RC   ECO:0000313|Proteomes:UP000186791};
RA   Barja J.L., Dubert J.;
RT   "Draft genome of the tyrosinase inhibitors producing Thalassotalea sp. PP2-
RT   459.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OKY27317.1}.
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DR   EMBL; MKQD01000019; OKY27317.1; -; Genomic_DNA.
DR   RefSeq; WP_074496429.1; NZ_MKQD01000019.1.
DR   AlphaFoldDB; A0A1Q6CLK6; -.
DR   STRING; 1742724.BI291_00360; -.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000186791; Unassembled WGS sequence.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProt.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR022517; Asp_decarboxylase_pyridox.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR03799; NOD_PanD_pyr; 1.
DR   PANTHER; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1.
DR   PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186791}.
FT   MOD_RES         338
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   545 AA;  60726 MW;  4A5C4AE2E757C558 CRC64;
     MTTNKRAANA TEESLLRIFT IPEAPDSTLG RIEQEISQNL AGFLGSHIAA KETALTEIEK
     DFDCSKIPEQ PAFVSDHMHH LLEKLVSQSV HTSSPSFIGH MTSALPYFIL PLSKLMVGLN
     QNLVKIETSK AFTPLERQVL GMMHRLVYQF EENFYQQWMH SANHSLGAFC SGGTVANITA
     LWVARNNLLR ADGSFKGVAR EGLFNALKHY QYDGLAILVS KRGHYSLKKS ADVLGIGQDS
     VVAIPTDEHN KMDPQKLREK CQELTAKNIR ILSIVGVAGT TETGNIDPLH ELADVANEYQ
     CHFHVDAAWG GATLLSSKHR GLLNGIERAD SVTIDAHKQM YVPMGAGLVV FRNPASVASI
     EHHAEYILRK GSKDLGAHTL EGSRPGMAML VYASLHIISR PGYEMLINQG IEKAKYFADI
     IDKHPDFELV TEPELCLLTY RYNPASVQQL LSKADENTLT NVNNLLDKLT KFIQKRQREN
     GKSFVSRTRI EVKKYHGRKT LVFRVVLANP LTSKEILKDV LEEQVELAQE SSHFLPKLVA
     LSQNL
//