ID   A0A135I668_9GAMM        Unreviewed;       548 AA.
AC   A0A135I668;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Glutamate decarboxylase {ECO:0000313|EMBL:KXF80950.1};
GN   ORFNames=ATN88_18025 {ECO:0000313|EMBL:KXF80950.1};
OS   Enterovibrio coralii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Enterovibrio.
OX   NCBI_TaxID=294935 {ECO:0000313|EMBL:KXF80950.1, ECO:0000313|Proteomes:UP000070529};
RN   [1] {ECO:0000313|EMBL:KXF80950.1, ECO:0000313|Proteomes:UP000070529}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CAIM 912 {ECO:0000313|EMBL:KXF80950.1,
RC   ECO:0000313|Proteomes:UP000070529};
RA   Gomez-Gil B., Enciso-Ibarra J.;
RT   "Genomic Taxonomy of the Vibrionaceae.";
RL   Submitted (NOV-2015) 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:KXF80950.1}.
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DR   EMBL; LNTY01000043; KXF80950.1; -; Genomic_DNA.
DR   RefSeq; WP_067418420.1; NZ_LNTY01000043.1.
DR   AlphaFoldDB; A0A135I668; -.
DR   STRING; 294935.ATN88_18025; -.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000070529; 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:UP000070529}.
FT   MOD_RES         338
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   548 AA;  60623 MW;  DE001C8384D75861 CRC64;
     MVRDTKKAEA SLESLQRIFT VPEAPNSTLG SIEQAISQNL NRFLQDHIAA TDRSLTDIEK
     DFSNPAIPEQ PTFVSDHTEF LLDKLVSQSV HTSSPRFIGH MTSALPYFLM PLSKIMIGLN
     QNTVKIETSK AFTPLERQVL GMLHKLIYSQ PETFYESCMH SAHHSLGAFC SGGTIANITA
     LWVARNSALK PDDNFKGVAE EGLFRAMKYY GYDDLAILVS ERGHYSLKKS ADVLGIGRES
     LVAVPTDANN RIRLDKLEET IAELKARNVK PFALVGVAGT TETGNIDPLD AMADIAEREG
     MHFHVDAAWG GASLMSNNQR PKLKGIERAD SVTIDAHKQL YVPMGAGMVI FKDPSQVSAI
     EHHADYILRK GSKDLGSHTL EGSRSGMAML LFACLNIIGR EGYELLIDQS VEKASYFSNL
     VANRNDFELV TEPELCLLTY RYAPDAVQKA LAQATPEDVE QLNALLNDLT IFIQKRQREA
     GNTFVSRTTL KPEKYGRQAT SVFRVVLANP LTTQEILQEV LDEQRAIAET STIALPQLLA
     KAEEILTR
//