ID A0A1U8BKG4_MESAU Unreviewed; 493 AA.
AC A0A1U8BKG4;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Cysteine sulfinic acid decarboxylase isoform X1 {ECO:0000313|RefSeq:XP_005067354.1};
GN Name=Csad {ECO:0000313|RefSeq:XP_005067354.1,
GN ECO:0000313|RefSeq:XP_012966649.1, ECO:0000313|RefSeq:XP_012966650.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_012966650.1};
RN [1] {ECO:0000313|RefSeq:XP_005067354.1, ECO:0000313|RefSeq:XP_012966649.1}
RP IDENTIFICATION.
RG RefSeq;
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 RefSeq; XP_005067354.1; XM_005067297.3.
DR RefSeq; XP_012966649.1; XM_013111195.2.
DR RefSeq; XP_012966650.1; XM_013111196.2.
DR STRING; 10036.ENSMAUP00000018668; -.
DR GeneID; 101839535; -.
DR KEGG; maua:101839535; -.
DR CTD; 51380; -.
DR eggNOG; KOG0629; Eukaryota.
DR OrthoDB; 888358at2759; -.
DR Proteomes; UP000189706; Unplaced.
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: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:UP000189706}.
FT MOD_RES 305
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 493 AA; 55140 MW; 5123CE38DE32EB81 CRC64;
MAASKPLTAL DGDPMAVETL LRDVFGIVVD EAIRKGTSAS EKVCEWKEPE ELKRLLDLEL
QSQGESQERI LERCRDVIHY SVKTGHPRFF NQLFSGLDPH ALAGRIITES LNTSQYTYEI
APVFVLMEEE VLKKLRALVG WTSGDGVFCP GGSISNMYAM NLARYQRYPD CKQRGLRALP
PLALFTSKEC HYSISKGAAF LGLGTDSVRV IKADERGKMI PEDLERQISL AEAEGSVPFL
VSATSGTTVL GAFDPLDAIA DVCQRHGLWL HVDAAWGGSV LLSRTHRHLL HGIQRADSVA
WNPHKLLGAG LQCSALLLRD TSNLLKRCHG SQASYLFQQD KFYDVALDTG DKVVQCGRRV
DCLKLWLMWK AQGGQGLERR IDQAFALTRY LVEEIKKREG FELVMEPEFV NVCFWFVPPS
LRGKKESPDY SKRLSQVAPV LKERMVKKGS MMIGYQPHGT RANFFRMVVA NPTLTQADVD
FLLCELECLG QDL
//
