ID   A0A091UCT8_PHALP        Unreviewed;       453 AA.
AC   A0A091UCT8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Glutamate decarboxylase-like 1 {ECO:0000313|EMBL:KFQ71818.1};
DE   Flags: Fragment;
GN   ORFNames=N335_11044 {ECO:0000313|EMBL:KFQ71818.1};
OS   Phaethon lepturus (White-tailed tropicbird).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Eurypygimorphae; Phaethontiformes;
OC   Phaethontidae; Phaethon.
OX   NCBI_TaxID=97097 {ECO:0000313|EMBL:KFQ71818.1, ECO:0000313|Proteomes:UP000053638};
RN   [1] {ECO:0000313|EMBL:KFQ71818.1, ECO:0000313|Proteomes:UP000053638}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N335 {ECO:0000313|EMBL:KFQ71818.1};
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KK446583; KFQ71818.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091UCT8; -.
DR   PhylomeDB; A0A091UCT8; -.
DR   Proteomes; UP000053638; 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:UP000053638}.
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:KFQ71818.1"
FT   NON_TER         453
FT                   /evidence="ECO:0000313|EMBL:KFQ71818.1"
SQ   SEQUENCE   453 AA;  51861 MW;  38CCA633156E88EA CRC64;
     VCEWRAPETL KQILDLEMRD TGESHQKLLQ LCRDVIQYSV KTSHPRFFNQ LYAGIDYYSL
     VGRFITEALN PSVYTYEVSP VFLLVEEAVI KKMIEFIGWE EGDGIFNPGG SISNMYAMNL
     ARYRFCPEIK EKGLSGLPRL VLFTSEECHY SMKKAASFLG IGTENVYFIK TDEKGKMMPE
     ELEKQVQRTR KEGSAPFLVC ATAGTTVLGA FDPLDKIADI CEKHGLWLHV DASWGGSALV
     SRKHCRLLHG IHRADSVAWN PHKMLLAGIQ CCALLVKDNS GLLKKCYSAK AAYLFQQDKF
     YDVSYDTGDK SIQCSRHPDA FKFWLMWKAL GTTGLEERVN RALALARYLV EEIKKREGFK
     LLLEPEYANV CFWYIPPTLR KMEDGPEFWQ KLHQASVAPI IKERMMKKGS MMLGYQPHRG
     KVNFFRQVVI SPQVSRKDMD FLLDEIELLA KDL
//