ID A0A093CFC2_TAUER Unreviewed; 451 AA.
AC A0A093CFC2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Glutamate decarboxylase-like 1 {ECO:0000313|EMBL:KFV11032.1};
DE Flags: Fragment;
GN ORFNames=N340_02696 {ECO:0000313|EMBL:KFV11032.1};
OS Tauraco erythrolophus (Red-crested turaco).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Musophagiformes; Musophagidae; Tauraco.
OX NCBI_TaxID=121530 {ECO:0000313|EMBL:KFV11032.1, ECO:0000313|Proteomes:UP000053661};
RN [1] {ECO:0000313|EMBL:KFV11032.1, ECO:0000313|Proteomes:UP000053661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N340 {ECO:0000313|EMBL:KFV11032.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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 -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
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DR EMBL; KL458564; KFV11032.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093CFC2; -.
DR Proteomes; UP000053661; Unassembled WGS sequence.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR CDD; cd06450; DOPA_deC_like; 1.
DR Gene3D; 3.90.1150.170; -; 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; IPR021115; Pyridoxal-P_BS.
DR PANTHER; PTHR45677:SF1; ACIDIC AMINO ACID DECARBOXYLASE GADL1; 1.
DR PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE 3: Inferred from homology;
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000053661}.
FT MOD_RES 263
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV11032.1"
FT NON_TER 451
FT /evidence="ECO:0000313|EMBL:KFV11032.1"
SQ SEQUENCE 451 AA; 51618 MW; DBAA40578AA9B10E CRC64;
VCEWRAPETL KQILDLEMRD TGESHQKLLQ LCQDVIQYSV KTSHPRFFNQ LYAGIDYYSL
VARFITEALN PSVYTYEVSP VFLLVEEAVI KKMIEFVGWE GGDGIFNPGG SVSNMYAMNL
ARYRFCPEIK EKGLSGLPRL VLFTSEECHY SMKKAASFLG IGTQNVYFIK TDERGKMIPE
ELEKQVQRAR KEGSAPFLVC ATAGTTVLGA FDPLDKIADI CEKHGLWLHV DASWGGSALI
SRKHCRLLHG IHRADSVAWN PHKMLLAGIQ CCALLVKDNS GLLKKCYSAK AAYLFQQDKF
YDVCYDTGDK SIQCSRRPDA FKFWLMWKAL GTTGLEERVN RALALARYLV EEIKKREGFR
LLLEPEYANV CFWYIPPSLR KMEDGPEFWQ KLHQVAPVIK ERMMKKGSMM LGYQPHQGKV
NFFRQVVISP RVSREDMDFL LDEIELLAKD L
//