ID H9F6G5_MACMU Unreviewed; 476 AA.
AC H9F6G5;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Cysteine sulfinic acid decarboxylase isoform 1 {ECO:0000313|EMBL:AFE70224.1};
DE Flags: Fragment;
GN Name=CSAD {ECO:0000313|EMBL:AFE70224.1};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|EMBL:AFE70224.1};
RN [1] {ECO:0000313|EMBL:AFE70224.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Caudate {ECO:0000313|EMBL:AFE70224.1};
RX PubMed=25319552; DOI=10.1186/1745-6150-9-20;
RA Zimin A.V., Cornish A.S., Maudhoo M.D., Gibbs R.M., Zhang X., Pandey S.,
RA Meehan D.T., Wipfler K., Bosinger S.E., Johnson Z.P., Tharp G.K.,
RA Marcais G., Roberts M., Ferguson B., Fox H.S., Treangen T., Salzberg S.L.,
RA Yorke J.A., Norgren R.B.Jr.;
RT "A new rhesus macaque assembly and annotation for next-generation
RT sequencing analyses.";
RL Biol. Direct 9:20-20(2014).
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|RuleBase:RU000382}.
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DR EMBL; JU326466; AFE70222.1; -; mRNA.
DR EMBL; JU326467; AFE70223.1; -; mRNA.
DR EMBL; JU326468; AFE70224.1; -; mRNA.
DR EMBL; JU326469; AFE70225.1; -; mRNA.
DR EMBL; JU326470; AFE70226.1; -; mRNA.
DR EMBL; JU326471; AFE70227.1; -; mRNA.
DR EMBL; JU326472; AFE70228.1; -; mRNA.
DR EMBL; JU326473; AFE70229.1; -; mRNA.
DR AlphaFoldDB; H9F6G5; -.
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 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 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 2: Evidence at transcript level;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382}.
FT MOD_RES 288
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFE70224.1"
SQ SEQUENCE 476 AA; 53317 MW; C346A5637CEEA54B CRC64;
EALLRAVFGV VVDEAIQKGT SASQKVCEWK EPEELKQLLD LELRSQGESQ EQILERCRTV
IRYSVKTGHP RFFNQLFSGL DPHALAGRII TESLNTSQYT YEIAPVFVLM EEEVLRKLRA
LVGWSSGDGI FCPGGSISNM YAVNLARYQR YPDCKQRGLR TLPPLALFTS KECHYSIQKG
AAFLGLGTDS VRVVKADERG KMVPEDLERQ IGMAEAEGAV PFLVSATSGT TVLGAFDPLE
AIADVCQRHG LWLHVDAAWG GSVLLSQTHR HLLDGIQRAD SVAWNPHKLL AAGLQCSALL
LQDTSNLLKR CHGSQASYLF QQDKFYDVAL DTGDKVVQCG RRVDCLKLWL MWKAQGDQGL
ERRIDQAFAL ARYLVEEIKK REGLELVMEP EFVNVCFWFV PPSLRGKQDS PDYHERLSKV
APVLKERMVK EGSMMIGYQP HGTRGNFFRV VVANPALTCA DMDFLLNELE RLGQDL
//
