ID   A0A1I0RND2_9BACT        Unreviewed;       491 AA.
AC   A0A1I0RND2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Glutamate decarboxylase {ECO:0000313|EMBL:SEW42728.1};
GN   ORFNames=SAMN05428988_5392 {ECO:0000313|EMBL:SEW42728.1};
OS   Chitinophaga sp. YR573.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=1881040 {ECO:0000313|EMBL:SEW42728.1, ECO:0000313|Proteomes:UP000198758};
RN   [1] {ECO:0000313|EMBL:SEW42728.1, ECO:0000313|Proteomes:UP000198758}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YR573 {ECO:0000313|EMBL:SEW42728.1,
RC   ECO:0000313|Proteomes:UP000198758};
RA   de Groot N.N.;
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}.
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DR   EMBL; FOJF01000003; SEW42728.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0RND2; -.
DR   STRING; 1881040.SAMN05428988_5392; -.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000198758; 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; 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   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         296
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   491 AA;  55123 MW;  822D33D3861FC3FA CRC64;
     MTIVRDVNNI VPESQYVCPE AFKEPFVLKQ KTIAEYKDFL KYELRSSLVD VSSPKFIGHM
     TGPVPPFIHE LQQWIGQLNQ NMVKFETSGA GTFIERQVLG CFHRLFYNET AAFYDSYIQE
     PAVSLGNVTS GGTLSNLTAL SYALSKKLND AGAMFKEDGL AKSLQDTGYK RAVIMGSSHC
     HYSLQKVMRL LGLGTNAFIS LDTHELQSNN GRQMLDAEIR KLKADGVLII ALVGVAGTTE
     AGKIDPLEMM AEIAAENQIH FHVDAAFGGA FSFSDRLSAR LNGISSADSI TLCGHKQLYL
     PMGTSLCLFK SPGLVKQVEI NSYYQARKGS VDLGKYTIEG SRPFSALIFH GALQVVGKEG
     YTEILESNYD RALLFTGMIR SDSNFQLYME PDLNIVLYRY VPDALREKAV NNTLTDEERN
     SLNKLNVYLQ QEQFRRKISF VSYTELPDPS GKRHVWLRSV FMNPDTTHQH LEEILEEQRN
     IVSSYKNKNH E
//