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Database: UniProt
Entry: A0A093CFC2_TAUER
LinkDB: A0A093CFC2_TAUER
Original site: A0A093CFC2_TAUER 
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
//
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