ID   A0A1M5KU22_9FLAO        Unreviewed;       479 AA.
AC   A0A1M5KU22;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Glutamate or tyrosine decarboxylase {ECO:0000313|EMBL:SHG56019.1};
GN   ORFNames=SAMN05444148_0428 {ECO:0000313|EMBL:SHG56019.1};
OS   Winogradskyella jejuensis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Winogradskyella.
OX   NCBI_TaxID=1089305 {ECO:0000313|EMBL:SHG56019.1, ECO:0000313|Proteomes:UP000184522};
RN   [1] {ECO:0000313|EMBL:SHG56019.1, ECO:0000313|Proteomes:UP000184522}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25330 {ECO:0000313|EMBL:SHG56019.1,
RC   ECO:0000313|Proteomes:UP000184522};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; FQWS01000001; SHG56019.1; -; Genomic_DNA.
DR   RefSeq; WP_073082395.1; NZ_FQWS01000001.1.
DR   AlphaFoldDB; A0A1M5KU22; -.
DR   STRING; 1089305.SAMN05444148_0428; -.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000184522; Unassembled WGS sequence.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   CDD; cd06450; DOPA_deC_like; 1.
DR   Gene3D; 3.90.1150.170; -; 1.
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; IPR010977; Aromatic_deC.
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; PTHR11999:SF70; AROMATIC-L-AMINO-ACID DECARBOXYLASE; 1.
DR   PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   PRINTS; PR00800; YHDCRBOXLASE.
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         293
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   479 AA;  53741 MW;  6818EA71B16086E5 CRC64;
     MVKDLNLTET EMRDLGYRVV DTLVTHFNEL PQKKPVALGT RKEMDFLFLE EAPQGATQVN
     DVLDFVVKNV FTNTNLVTHP KSYAFVPGPS NYVSVMADTL ATGFNTFSGG WNASPAASEL
     EIVTINWLLK MFGLPPKKGG GLFTSGGSVA NLTALVTARN KMCGEDFSKA RIYLSDQAHS
     SNVKAIRIMG LKKEQIRIIP TDSEYRFSVN KLKNAIARDR LEGYVPFCVI ASAGTTNTGT
     VDPLQEIAII CKEEKIWFHI DAAYGGAAIL SQQGKKLLKG IQKADSITVD PHKWFYQPYE
     MGCLLVRDHS WLKNTFIEKP EYLRDIEGNE SEINFYDMGM QLTRRFRALK LFMSIKTFGL
     DAFAKAITYN IELAEIVERL LRESSRWEVI SSASLAIINF RYNPISLELS EKEIDELNQH
     IASKVTESRE AILATTILNG QVVLRMCLIN PRTTIDDVKE TLLQCESFAS LKLENVFSV
//