ID A0A3Q3BEH1_KRYMA Unreviewed; 494 AA.
AC A0A3Q3BEH1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Cysteine sulfinic acid decarboxylase {ECO:0000313|Ensembl:ENSKMAP00000028050.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000028050.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000028050.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; A0A3Q3BEH1; -.
DR STRING; 37003.ENSKMAP00000028050; -.
DR Ensembl; ENSKMAT00000028403.1; ENSKMAP00000028050.1; ENSKMAG00000020806.1.
DR GeneTree; ENSGT00940000158240; -.
DR OMA; CVDLHKW; -.
DR Proteomes; UP000264800; Unplaced.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0004782; F:sulfinoalanine decarboxylase activity; IEA:Ensembl.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0042412; P:taurine biosynthetic process; IEA:Ensembl.
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: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.
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:UP000264800}.
FT MOD_RES 306
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 494 AA; 55905 MW; 33CE680AB0F2623F CRC64;
MEPALCDLKD PLINHAEGQL FLNEAFKIIV EEVLCKGTDV QQKVCEWREP DELARLLDLE
LRDAGEQQDR LLQRVRDVAK YSVKTSHPRF FNQQFAGVDY HSLAGRFLTE ALNTNLFTYE
VAPVFVLMET EVLRSLRQLV GWTEGDGIFC PGGSTSTVYA MNLARYRLFP EVKSQGLWAL
PRLAIFTSPE SHYSVRKGAA FLGFGTDNVI LVKVDERGHM IPEDLDEKIE LSKSQGAVPF
LVSCTAGTTV QGAFDPLDGI ADVCDKHKLW LHVDAAWGGS VLFSKQHRHL MKGVDRANSV
AWNLHKMLAA GLQCSALLLK DTTDLLKRCH SSNASYLFQQ DKFYDVNLDI GDKSVQCGRK
VDCLKLWLMW KAVGSSGLEQ RVDKAFLLVR YLVDQMKKRD GFHLLSEPEF VNVCFWFIPP
SLRGKEGNAD YQNKLAKVAP TIKERMMKRG TLMVGYQPLG DKVNFFRVTV FSHLVSHKDM
DFFLDEIERL GSDL
//