ID A0A2W7HX32_9FLAO Unreviewed; 462 AA.
AC A0A2W7HX32;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Glutamate/tyrosine decarboxylase-like PLP-dependent enzyme {ECO:0000313|EMBL:PZW39146.1};
GN ORFNames=LX95_02287 {ECO:0000313|EMBL:PZW39146.1};
OS Mesonia algae.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Mesonia.
OX NCBI_TaxID=213248 {ECO:0000313|EMBL:PZW39146.1, ECO:0000313|Proteomes:UP000249542};
RN [1] {ECO:0000313|EMBL:PZW39146.1, ECO:0000313|Proteomes:UP000249542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15361 {ECO:0000313|EMBL:PZW39146.1,
RC ECO:0000313|Proteomes:UP000249542};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (JUN-2018) 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}.
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:PZW39146.1}.
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DR EMBL; QKYV01000006; PZW39146.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W7HX32; -.
DR Proteomes; UP000249542; 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 InterPro; IPR021115; Pyridoxal-P_BS.
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.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 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:UP000249542}.
FT MOD_RES 292
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 462 AA; 51118 MW; 540C3C60D893A367 CRC64;
MKSMHSIDME TVEMTLDIMK YAINRISNTN PELGSPVREE ELLNRVGETV TKEGIGGEKA
FQMFKDVLVK TAVPADHPRH LAFVPAAPTR AATLFDLVTS ASSMHGAYWM TGGGGIFCEN
QAMKWLVSLT GLPEGAFGVF TSGGTSANLS AMIAAREAWR DRNEDNRAYK ALLITSNGAH
SSVKSMAKVI DADIILVDDD EDDRLTGKWL QKAIDDLSEL DRKRLFAVVA TGGTTNAGII
DELDTVADVC EKENLWYHVD AAYGGGALAA PSVRHLFTGI ERADSITIDP HKWMFSPYDC
GAVIYKDLEL AKNAHSQKGS YLDIFKDPGA QGFNPSDYQI QLTRRLRGLP LWFSLAMHGT
DKYTEAIERG LELAQNAAQQ IEAAPHLELV RDPSLSCVLF RRVGWNPDNY RDWTYDNHKA
GFALVTPTKW TKNGKTETIS RFCFINPDTT EKDIEEILAS MK
//