ID A0A401NQA1_SCYTO Unreviewed; 520 AA.
AC A0A401NQA1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Glutamate decarboxylase like 1 {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=scyTo_0013152 {ECO:0000313|EMBL:GCB63046.1};
OS Scyliorhinus torazame (Cloudy catshark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes; Scyliorhinidae;
OC Scyliorhinus.
OX NCBI_TaxID=75743 {ECO:0000313|EMBL:GCB63046.1, ECO:0000313|Proteomes:UP000288216};
RN [1] {ECO:0000313|EMBL:GCB63046.1, ECO:0000313|Proteomes:UP000288216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCB63046.1}.
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DR EMBL; BFAA01006605; GCB63046.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401NQA1; -.
DR STRING; 75743.A0A401NQA1; -.
DR OMA; NNHAYEG; -.
DR Proteomes; UP000288216; 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:UP000288216}.
FT MOD_RES 332
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:GCB63046.1"
SQ SEQUENCE 520 AA; 59074 MW; A31008C2DFB67F7D CRC64;
FCPVYQVPSP LSENEMITDH YLKKGAILVD GVVLNGPLLD AKAGERFVEE AFPIIMEDAI
KKATDVNEKV CEWQPPEELM KLLDLELRDT GESHHQLLQH CRDVIKYSVK TGHPRFYNQL
YGGMDHYSLV ARFITEALNP SIYTYEVAPV FVLMEEVVLR KMRALIGWTE GDGIFSPGGS
VSNMYAVNLA RYKCCPELKE LGLSGSPALA MFTSEECHYS VKKAAAFLGI GTRNVYMVKA
DKRGKMIPEE LEKEIQRAKK EGALPFIVIA TAGTTVLGAF DPLNEIADIC EAHGTWFHVD
ASWGGGALIS RKHRSLLNGI HRADSVAWNP HKMLMAGIQC CAFLLKDNTG LIDRCHCGQA
MYLFQQDKFY NVDYDKGDKS IQCSRRADAF KFWLTWKAIG SSGLEERVNR AFASARYLAD
EIKKKKEFRL ILEPEYTNVC FWYIPPSLRD VPEDQDFWKK LHMVAPVIKE RMMKKGSMMV
GYQPHRDKVN FFRQIIISPL VSREDMDFIL NEIDNLGKDL
//