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Database: UniProt
Entry: A0A067L5H8_JATCU
LinkDB: A0A067L5H8_JATCU
Original site: A0A067L5H8_JATCU 
ID   A0A067L5H8_JATCU        Unreviewed;       394 AA.
AC   A0A067L5H8;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Cytochrome P450 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=JCGZ_00295 {ECO:0000313|EMBL:KDP42498.1};
OS   Jatropha curcas (Barbados nut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Jatropheae;
OC   Jatropha.
OX   NCBI_TaxID=180498 {ECO:0000313|EMBL:KDP42498.1, ECO:0000313|Proteomes:UP000027138};
RN   [1] {ECO:0000313|EMBL:KDP42498.1, ECO:0000313|Proteomes:UP000027138}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. GZQX0401 {ECO:0000313|Proteomes:UP000027138};
RC   TISSUE=Young leaves {ECO:0000313|EMBL:KDP42498.1};
RX   PubMed=24837971; DOI=10.1371/journal.pone.0097878;
RA   Zhang L., Zhang C., Wu P., Chen Y., Li M., Jiang H., Wu G.;
RT   "Global Analysis of Gene Expression Profiles in Physic Nut (Jatropha curcas
RT   L.) Seedlings Exposed to Salt Stress.";
RL   PLoS ONE 9:E97878-E97878(2014).
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971};
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR   EMBL; KK914298; KDP42498.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A067L5H8; -.
DR   Proteomes; UP000027138; Unassembled WGS sequence.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 2.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   PANTHER; PTHR24298:SF800; CYTOCHROME P450 89A2-RELATED; 1.
DR   PANTHER; PTHR24298; FLAVONOID 3'-MONOOXYGENASE-RELATED; 1.
DR   Pfam; PF00067; p450; 2.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|RuleBase:RU000461}; Iron {ECO:0000256|RuleBase:RU000461};
KW   Metal-binding {ECO:0000256|RuleBase:RU000461};
KW   Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027138}.
SQ   SEQUENCE   394 AA;  45295 MW;  B7CB53759D5F364F CRC64;
     MEIWFVIVIS LSIAALLKPF LNLFFISKNS TISLPPRPLS FVGSILWLKK TSFWEFESTI
     RSFHAKFGSM VALPIGTKLH FYVADGRLAH QALIQNGVSF ASRPPPTNTY RIISCNQHNI
     GMAFYGPTWR LLRRNLVSEM LHPSVVKSYS EARKWALQIL IERLESQSKE LPDMKRKLNE
     EEIVTLCDEF FNGGTESTST ALQWIMANLV KYPHIQEKLF MEMKMVVGNE EEEHIKEEDL
     HKMKYLKAVI LEGLRRHPPS HMLLPHAVSD DVVLGNYLVP KNGIINFMVA DIGLDPKVWE
     DPMEFKPERF NGDEAFDIKG SREIKMMPFG AGRRICPGYS LGLFHLEYFV ANLVWKFEWK
     AVDGNDIDLS EKTEVIVVMK NPLKAHLSPR FKKI
//
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