ID H2QM83_PANTR Unreviewed; 516 AA.
AC H2QM83;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 24-JAN-2024, entry version 58.
DE SubName: Full=Glutamate decarboxylase like 1 {ECO:0000313|Ensembl:ENSPTRP00000025376.5};
GN Name=GADL1 {ECO:0000313|Ensembl:ENSPTRP00000025376.5,
GN ECO:0000313|VGNC:VGNC:1823};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000025376.5, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000025376.5, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000025376.5}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-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 EMBL; AACZ04000207; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H2QM83; -.
DR Ensembl; ENSPTRT00000027517.5; ENSPTRP00000025376.5; ENSPTRG00000014712.5.
DR VGNC; VGNC:1823; GADL1.
DR eggNOG; KOG0629; Eukaryota.
DR GeneTree; ENSGT00940000158391; -.
DR HOGENOM; CLU_011856_0_0_1; -.
DR OMA; LDKPECT; -.
DR TreeFam; TF314688; -.
DR Proteomes; UP000002277; Chromosome 3.
DR Bgee; ENSPTRG00000014712; Expressed in skeletal muscle tissue and 6 other cell types or tissues.
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:UP000002277}.
FT MOD_RES 328
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 516 AA; 58763 MW; B566423AA779BDCD CRC64;
GDIDQQEMIP SKKNAVLVDG VVLNGPTTDA KAGEKFVEEA CRLIMEEVVL KATDVNEKVC
EWRPPEQLKQ LLDLEMRDSG EPPHKLLELC RDVIHYSVKT NHPRFFNQLY AGLDYYSLVA
RFMTEALNPS VYTYEVSPVF LLVEEAVLKK MIEFIGWKEG DGIFNPGGSV SNMYAMNLAR
YKYCPDIKEK GLSGLPRLIL FTSAECHYSM KKAASFLGIG TENVCFVETD GRGKMIPEEL
EKQVWQARKE KARGRENGAA PFLVCATSGT TVLGAFDPLD EIADICERHS LWLHVDASWG
GSALMSRKHR KLLHGIHRAD SVAWNPHKML MAGIQCCALL VKDKSDLLKK CYSAKASYLF
QQDKFYDVSY DTGDKSIQCS RRPDAFKFWM TWKALGTLGL EERVNRALAL SRYLVDEIKK
REGFKLLMEP EYANICFWYI PPSLREMEEG PEFWAKLNLV APAIKERMMK KGSLMLGYQP
HRGKVNFFRQ VVISPQVSRE DMDFLLDEID LLGKDM
//