ID A0A2G8LDC9_STIJA Unreviewed; 394 AA.
AC A0A2G8LDC9;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Putative cysteine sulfinic acid decarboxylase {ECO:0000313|EMBL:PIK58242.1};
GN ORFNames=BSL78_04829 {ECO:0000313|EMBL:PIK58242.1};
OS Stichopus japonicus (Sea cucumber).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Holothuroidea;
OC Aspidochirotacea; Aspidochirotida; Stichopodidae; Apostichopus.
OX NCBI_TaxID=307972 {ECO:0000313|EMBL:PIK58242.1, ECO:0000313|Proteomes:UP000230750};
RN [1] {ECO:0000313|EMBL:PIK58242.1, ECO:0000313|Proteomes:UP000230750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shaxun {ECO:0000313|EMBL:PIK58242.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PIK58242.1};
RX PubMed=29023486;
RA Zhang X., Sun L., Yuan J., Sun Y., Gao Y., Zhang L., Li S., Dai H.,
RA Hamel J.F., Liu C., Yu Y., Liu S., Lin W., Guo K., Jin S., Xu P.,
RA Storey K.B., Huan P., Zhang T., Zhou Y., Zhang J., Lin C., Li X., Xing L.,
RA Huo D., Sun M., Wang L., Mercier A., Li F., Yang H., Xiang J.;
RT "The sea cucumber genome provides insights into morphological evolution and
RT visceral regeneration.";
RL PLoS Biol. 15:E2003790-E2003790(2017).
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 -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {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:PIK58242.1}.
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DR EMBL; MRZV01000118; PIK58242.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G8LDC9; -.
DR STRING; 307972.A0A2G8LDC9; -.
DR Proteomes; UP000230750; Unassembled WGS sequence.
DR GO; GO:0016830; F:carbon-carbon lyase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
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 PANTHER; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
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:UP000230750}.
FT MOD_RES 299
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 394 AA; 44011 MW; 8D8F21E971F94DA6 CRC64;
MGFHTKIHTT IRRSFDVCSN LIVHDVLEDG KKEENKVIKF QYPKDLKKQL DLEIQDKSST
VDELMELCKS TIDNSVRTTH PFFNNQLWQG VDAVGLAGLY LAHALKTSVY TYEMAPVFLL
VENAILQKIR DLCGFSEGDG IFCPGGSMGN MYAINLARYQ INPEVKTKGV RGYQQSIIFT
SDVSHYSITK GASFMGIGSD NIQIVKSDDA GRMLPDELEK AIVSTKEKGD TPMIVVATSG
TTVQGAYDPL DKLADVCEKH GVWLHVDGAW GGSVLLSRQH KYKMKGVHRA DSFSWCLHKM
MGVPIQCSVL VLNKKGDLLK RCHGVSASYL FQSDKFYGAG YDTGDKSLQC SRLADAFKAW
FMWKAKGDLL LEREIDHKFD LAKVDIGNIY LYGM
//
