ID A0A1I4Z0L4_9FLAO Unreviewed; 479 AA.
AC A0A1I4Z0L4;
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=Pyridoxal-dependent decarboxylase conserved domain-containing protein {ECO:0000313|EMBL:SFN43593.1};
GN ORFNames=SAMN05660413_01066 {ECO:0000313|EMBL:SFN43593.1};
OS Salegentibacter flavus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Salegentibacter.
OX NCBI_TaxID=287099 {ECO:0000313|EMBL:SFN43593.1, ECO:0000313|Proteomes:UP000199153};
RN [1] {ECO:0000313|EMBL:SFN43593.1, ECO:0000313|Proteomes:UP000199153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17794 {ECO:0000313|EMBL:SFN43593.1,
RC ECO:0000313|Proteomes:UP000199153};
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|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
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DR EMBL; FOVL01000004; SFN43593.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4Z0L4; -.
DR STRING; 287099.SAMN05660413_01066; -.
DR OrthoDB; 9803665at2; -.
DR Proteomes; UP000199153; 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 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:SF165; DECARBOXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G04980)-RELATED; 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|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR602129-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000199153}.
FT MOD_RES 303
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 479 AA; 53152 MW; C3DA16DBF32D4100 CRC64;
MEDLKSRILA LQKISAGLEP TPSQRDNYFN EVNDYSNSFL NGLSTSGTYS PEKVRHEAFA
LGKEPKSLEK ILRIFEEEVA GKGIKPASGG YMGYIPGGGI YASALGDYLA DITNEYAGMS
FASPGAVAME HELLNWMKSL FGFPESAVGN LTSGGSIANL IALTSARDKH KIKGATIEKS
VVYLSPQLHH CNLKALRIIG LEDVIIRELK LDEGSRIVAS DLKQKLEEDK AAGLNPFLLI
ASAGTTDTGA MDPLNELGEI AEANKLWYHV DAAYGGFFIL SEKRKHLFKG IEKSDSLAVD
PHKGLFLPFG LGAVLVKDRE AVFHSHHRSA NYMQDAVEND SEINPADVSP ELTKHFRALR
LWLPLQLHGI KPFVACLEEK LLLTVYFRER LEEKGFALGP EPDLSVSYFW WPLSENETNF
NKKLLKEIHN DGTVFFSSTN IEGCFVIRMA LLAFRTKIEH VDRAVELLDK ARNRLLGRL
//