ID   Q9KSV7_VIBCH            Unreviewed;       548 AA.
AC   Q9KSV7;
DT   01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 121.
DE   SubName: Full=Glutamate decarboxylase, putative {ECO:0000313|EMBL:AAF94308.1};
GN   OrderedLocusNames=VC_1149 {ECO:0000313|EMBL:AAF94308.1};
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277 {ECO:0000313|EMBL:AAF94308.1, ECO:0000313|Proteomes:UP000000584};
RN   [1] {ECO:0000313|EMBL:AAF94308.1, ECO:0000313|Proteomes:UP000000584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961
RC   {ECO:0000313|Proteomes:UP000000584};
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D., Ermolaeva M.D.,
RA   Vamathevan J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.,
RA   Utterback T., Fleishmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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}.
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DR   EMBL; AE003852; AAF94308.1; -; Genomic_DNA.
DR   PIR; H82234; H82234.
DR   RefSeq; NP_230794.1; NC_002505.1.
DR   RefSeq; WP_000253201.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KSV7; -.
DR   STRING; 243277.VC_1149; -.
DR   DNASU; 2614582; -.
DR   EnsemblBacteria; AAF94308; AAF94308; VC_1149.
DR   KEGG; vch:VC_1149; -.
DR   PATRIC; fig|243277.26.peg.1098; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_011856_0_4_6; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProt.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008117; F:sphinganine-1-phosphate aldolase activity; IBA:GO_Central.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   GO; GO:0030149; P:sphingolipid catabolic process; IBA:GO_Central.
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:UP000000584}.
FT   MOD_RES         338
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   548 AA;  61693 MW;  DCBFD48556AF50B2 CRC64;
     MVSEHKSAQV NFDSLLKIFT VPEGPDSTLT KIDEELSRNL NHFLRKHIVA EEKPLKEIEK
     DFSNAHIPEQ PQFVSDHTQY LLDTLVSHSV HTASPSFIGH MTSALPYFLM PLSKIMIALN
     QNLVKIETSK AFTPLERQVL GMIHRLIYGE TDHFYQQWMH SAEHSLGAFC SGGTIANITA
     LWVARNNALK AEGDFPGVEK AGLFKAMRHY GHEGLAILVS ERGHYSLKKA ADVLGIGQEG
     LVAVKTDAHN RICPHDLEQK ITELKANKIK VFAVVGVAGT TETGNIDPLR TIAQICQREQ
     IHFHIDAAWG GATLMSNRYR GLLDGVELAD SVTIDAHKQL YIPMGAGMVL FKDPNAMRSI
     EHHAQYILRQ GSKDLGSHTL EGSRSGMAML VYASMHIISR PGYQLLIDQS IEKARYFADL
     IDAQTDFELV SQPELCLLTY RYLPEHVRMA LEKSQGVQRA QLNELLNELT KFIQKKQRET
     GKSFVSRTQL NPHQWDKLAT IVFRVVLANP LTTKEILHNV LDEQREIAQQ APKLMRQIEH
     LTQCILNQ
//