ID A0A3P8P6J2_ASTCA Unreviewed; 524 AA.
AC A0A3P8P6J2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Glutamate decarboxylase like 1 {ECO:0008006|Google:ProtNLM};
OS Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000012631.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000012631.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000012631.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 AlphaFoldDB; A0A3P8P6J2; -.
DR STRING; 8154.ENSACLP00000012631; -.
DR Ensembl; ENSACLT00000012938.1; ENSACLP00000012631.1; ENSACLG00000008579.1.
DR GeneTree; ENSGT00940000158391; -.
DR OMA; RCNSAEA; -.
DR Proteomes; UP000265100; Chromosome 11.
DR Bgee; ENSACLG00000008579; Expressed in liver and 1 other cell type or tissue.
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}.
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 336
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 524 AA; 59270 MW; 19340102BE3CB422 CRC64;
ISSNMERHIN GKTFSSCESQ APVTQPEKCS PAGSFDVSSS TADEQIAESF IRQAMEIIVD
EAVKKATNVQ EKVCEWHSPE QLKKLLDLEL RDRGEPESEI LQRCRDAIRY SVKTSHPRFF
NQLYAGMEPY SMVASFIAEA VKTNLYTYEV APVFTLMEDA VLRKMIKVIG WEEGGDGIFN
PGGSLSNIYA VNLARYRYCP DFKEVGMFSA PRLVILTSQE CHYSISKGAA LMGIGTKNVY
TVPTDERGRM IPSALEEKIK LAKSEGAVPF MVNATAGTTV LGAFDPIDEI ADICEKHNLW
LHVDACWGGA AIMSKKHKHL LKGIHRVDSV AWNPHKMLMA SLQCSAFLVR DKTSLLQRCH
SARASYLFQQ DKFYDVSYDT GDKSVQCSRK PDAFKFWLMW KALGSRELEQ RVDRALAMAR
YLAEEIKKRE GFRLVLEPEF ANVCFWYLPP SLRNLPESPE LWKKLHTVAP VVKQRMMKTG
SMMTGYQPLG EKANFFRMVV ISPQVSRQDL DFVLDEIHNL GKDL
//