ID   C5K7K6_PERM5            Unreviewed;       833 AA.
AC   C5K7K6;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 63.
DE   RecName: Full=cysteine dioxygenase {ECO:0000256|ARBA:ARBA00013133};
DE            EC=1.13.11.20 {ECO:0000256|ARBA:ARBA00013133};
GN   ORFNames=Pmar_PMAR012522 {ECO:0000313|EMBL:EER19541.1};
OS   Perkinsus marinus (strain ATCC 50983 / TXsc).
OC   Eukaryota; Sar; Alveolata; Perkinsozoa; Perkinsea; Perkinsida; Perkinsidae;
OC   Perkinsus.
OX   NCBI_TaxID=423536 {ECO:0000313|Proteomes:UP000007800};
RN   [1] {ECO:0000313|EMBL:EER19541.1, ECO:0000313|Proteomes:UP000007800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50983 / TXsc {ECO:0000313|Proteomes:UP000007800};
RA   El-Sayed N., Caler E., Inman J., Amedeo P., Hass B., Wortman J.;
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR602129-50};
CC   -!- SIMILARITY: Belongs to the cysteine dioxygenase family.
CC       {ECO:0000256|ARBA:ARBA00006622}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|ARBA:ARBA00009533}.
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DR   EMBL; GG671079; EER19541.1; -; Genomic_DNA.
DR   RefSeq; XP_002787745.1; XM_002787699.1.
DR   AlphaFoldDB; C5K7K6; -.
DR   EnsemblProtists; EER19541; EER19541; Pmar_PMAR012522.
DR   GeneID; 9039802; -.
DR   InParanoid; C5K7K6; -.
DR   OMA; WRIPNIN; -.
DR   OrthoDB; 275912at2759; -.
DR   Proteomes; UP000007800; Unassembled WGS sequence.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR   GO; GO:0017172; F:cysteine dioxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005506; F:iron ion binding; 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; cd10548; cupin_CDO; 1.
DR   Gene3D; 3.90.1150.170; -; 2.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR010300; CDO_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   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   PANTHER; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1.
DR   PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR   Pfam; PF05995; CDO_I; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   SUPFAM; SSF51182; RmlC-like cupins; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|PIRSR:PIRSR610300-51};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR610300-51};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007800};
KW   Thioether bond {ECO:0000256|PIRSR:PIRSR610300-50}.
FT   BINDING         131
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610300-51"
FT   BINDING         133
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610300-51"
FT   BINDING         187
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610300-51"
FT   MOD_RES         541
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
FT   CROSSLNK        138..203
FT                   /note="3'-(S-cysteinyl)-tyrosine (Cys-Tyr)"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610300-50"
SQ   SEQUENCE   833 AA;  93175 MW;  E5709099913284CB CRC64;
     MPVNSPAAGR NLTAEIAAPE FQKVIPNGVN GSEQQIPTRV DPDCTPPIVC LEVLENELTR
     VLHNRTDPSR LEKAKKVLER YKGNDWIIHQ SCPSQHGFHV CGYSRVKVRH RTDLFQLLVL
     TWSPRSRSPI HNHPCERCFL MPLQGELYEE RYKVDEEGPK EARQELIART LIPIRTAAWI
     DNSLGWHAIE NSGDGLGVSL HCYIPAYNQC KIIDTMSKEI RSVACLPKDV CMQPLHEAVM
     ERTRKYIAAQ EDCCSDDNPP IPVVSARGKQ DIESAFASVS CPIAFEEECP PMDDDCLKRA
     VDFTCDLSVN TGHLFFFNQL FARPDPLAVA AEGLTAALNV NMYTFEMAPV MLLMEHRLLQ
     HMASFLGWYE HMLQFDGMLL PGASHCNITA LHVARQQLFP DTINEGLMGA GHPRGRLMVF
     TSANSHCSME RGCMMLGLGR KSLVYVKCDP ETCQMIPSEL ENCINDEIEK GNTPFFVNAT
     AGSTVAGAFD DCSALAGIAK KYGCWLHVDG ALGASFLLAR GEEPYDSGMD QADSISWNLH
     KLLGVPLQCS ALLCRHSGCL KAAHEEQHAS EVVLTRRMRV RFHAQAFPCL SPLDTVYCSS
     MSGRKADAFK AWILWKKMGD CGMANRVRLV YTHTQEFAAM LTSFPVRKQF DEAQLKYEEP
     IIEKMPNDVE GANDNAFHLA FQPTSACTCF WWVPYDLRDR FMKEGPSALS KELFTVACRM
     RAALLSEGSL MISFYSTEEK PAFWRIPNIN PEISHEHMWA ILKIVNRVGH FCFPPGTKKW
     ESDPCLPGDC SMPSRPATPA STSWLVPPEF DELKKTRSAA QLLGGIEATG EFI
//