GenomeNet

Database: UniProt
Entry: A0A0W8JGA0_9VIBR
LinkDB: A0A0W8JGA0_9VIBR
Original site: A0A0W8JGA0_9VIBR 
ID   A0A0W8JGA0_9VIBR        Unreviewed;       550 AA.
AC   A0A0W8JGA0;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Glutamate decarboxylase eukaryotic type {ECO:0000313|EMBL:KUI99285.1};
GN   ORFNames=VRK_13690 {ECO:0000313|EMBL:KUI99285.1};
OS   Vibrio sp. MEBiC08052.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1761910 {ECO:0000313|EMBL:KUI99285.1, ECO:0000313|Proteomes:UP000054473};
RN   [1] {ECO:0000313|EMBL:KUI99285.1, ECO:0000313|Proteomes:UP000054473}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MEBiC08052 {ECO:0000313|EMBL:KUI99285.1,
RC   ECO:0000313|Proteomes:UP000054473};
RA   Kim Y.J., Lee J.-H., Kwon K.K.;
RT   "Genome sequence of Vibrio sp. MEBiC08052.";
RL   Submitted (DEC-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:KUI99285.1}.
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DR   EMBL; LQIY01000009; KUI99285.1; -; Genomic_DNA.
DR   RefSeq; WP_059120610.1; NZ_KQ947475.1.
DR   AlphaFoldDB; A0A0W8JGA0; -.
DR   STRING; 1761910.VRK_13690; -.
DR   PATRIC; fig|1761910.3.peg.1381; -.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000054473; 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}.
FT   MOD_RES         338
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   550 AA;  61380 MW;  30D951822499FE63 CRC64;
     MVLKSKTAEA NFDSLLRIFT IPEGPGSTLT QIEEEISQNL NQFLREHIVS EEKPLKAIEQ
     DFLSSQIPEQ PVFVSEHTQH LLDKVVAQSV HTSAPSFIGH MTSALPYFLM PLSKIMIALN
     QNLVKIETSK AFTPLERQVI GMLHRLIYTG SEDFYTQWMH SANHSLGAFC SGGTIANITA
     LWVARNNALK AQGAFQGVEK EGLFRAMKHY GYEGLAILVS ERGHYSLKKA ADLLGIGQQG
     LVVIPTDEHN KIKPDALQTT IRQLKQQQIL PFAVVGVAGT TETGNIDPLA EMAAICQQEQ
     CHFHVDAAWG GATLMSHQYR HLLNGIEQAD SVTIDAHKQL YLPMGAGMVL FKSPTSSHAI
     EHHAQYILRE GSKDLGSRTL EGSRSGMAML VYACMHIISR AGYELLINES IQKAAYFADL
     IRQQDDFELV SEPELCLLTY RYVPEQARLA LQHSTGDTLA QLNQQLNELT KFIQKKQRES
     GKSFVSRTQL TPKRWQYLNT IVFRAVLANP LTTKDILHAV LEEQRHIAAL APTLLRQIQR
     SAERILSGNI
//
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