ID   CP17A_RANDY             Reviewed;         519 AA.
AC   O57525;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Steroid 17-alpha-hydroxylase/17,20 lyase;
DE            EC=1.14.14.19 {ECO:0000250|UniProtKB:P05093};
DE            EC=1.14.14.32 {ECO:0000250|UniProtKB:P05093};
DE   AltName: Full=17-alpha-hydroxyprogesterone aldolase;
DE   AltName: Full=CYPXVII;
DE   AltName: Full=Cytochrome P450 17A1;
DE   AltName: Full=Cytochrome P450-C17;
DE            Short=Cytochrome P450c17;
GN   Name=CYP17A1; Synonyms=CYP17;
OS   Rana dybowskii (Dybovsky's frog) (Korean brown frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Rana; Rana.
OX   NCBI_TaxID=71582;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Choi H.H., Kang H.M., Choi H.S., Kwon H.B.;
RT   "Cloning and characterization of cDNA encoding 17-alpha-hydroxylase/17,20
RT   lyase (P450c17) in amphibia (Rana dybowskii).";
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Conversion of pregnenolone and progesterone to their 17-
CC       alpha-hydroxylated products and subsequently to dehydroepiandrosterone
CC       (DHEA) and androstenedione. Catalyzes both the 17-alpha-hydroxylation
CC       and the 17,20-lyase reaction.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a C21-steroid + O2 + reduced [NADPH--hemoprotein reductase] =
CC         a 17alpha-hydroxy-C21-steroid + H(+) + H2O + oxidized [NADPH--
CC         hemoprotein reductase]; Xref=Rhea:RHEA:65760, Rhea:RHEA-COMP:11964,
CC         Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:61313, ChEBI:CHEBI:138141; EC=1.14.14.19;
CC         Evidence={ECO:0000250|UniProtKB:P05093};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=17alpha-hydroxyprogesterone + O2 + reduced [NADPH--hemoprotein
CC         reductase] = acetate + androst-4-ene-3,17-dione + 2 H(+) + H2O +
CC         oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:14753,
CC         Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16422,
CC         ChEBI:CHEBI:17252, ChEBI:CHEBI:30089, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210; EC=1.14.14.32;
CC         Evidence={ECO:0000250|UniProtKB:P05093};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=17alpha-hydroxypregnenolone + O2 + reduced [NADPH--hemoprotein
CC         reductase] = 3beta-hydroxyandrost-5-en-17-one + acetate + 2 H(+) +
CC         H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:50244,
CC         Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:28689,
CC         ChEBI:CHEBI:28750, ChEBI:CHEBI:30089, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210; EC=1.14.14.32;
CC         Evidence={ECO:0000250|UniProtKB:P05093};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- PATHWAY: Lipid metabolism; steroid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AF042278; AAB97686.1; -; mRNA.
DR   AlphaFoldDB; O57525; -.
DR   SMR; O57525; -.
DR   UniPathway; UPA00062; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0047442; F:17-alpha-hydroxyprogesterone aldolase activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004508; F:steroid 17-alpha-monooxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0007548; P:sex differentiation; IEA:InterPro.
DR   GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR033282; CYP17A1.
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; PTHR24289:SF7; PTHR24289:SF7; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   2: Evidence at transcript level;
KW   Heme; Iron; Lipid metabolism; Lyase; Membrane; Metal-binding;
KW   Monooxygenase; Oxidoreductase; Steroidogenesis.
FT   CHAIN           1..519
FT                   /note="Steroid 17-alpha-hydroxylase/17,20 lyase"
FT                   /id="PRO_0000051948"
FT   BINDING         455
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   519 AA;  58948 MW;  FDF866CF15593A2E CRC64;
     MKLCFFLLIF IRSFLLFKIK LVRTSEKKWR MGSRSHGDVK HPKSLPSLPV IGSLLHLGKK
     LPPHILFCNL QKKYGSLYSF MMGSHYVVVV NNHEDAREVL LKKGKTFGGR PRTVTTDILT
     RDGKDIAFAD YSPTWKFHRK MVHSALCMFG EGTVAIEQII SREAASLCQT LTSFQRIPLD
     MAPELIRAVT NVVCSLCFNT RYKRGDAEFE TMLKYSKGIV DTVAKDSLVD IFPWLQIFPN
     KDLDILRQSV AARDQLLQKK INEHKDAFCG ETVKDLVDAL LKAKLNMENN NSNVSQDVGL
     TEDHILMTVG DIFGAGVETT STVLKWAVAY LLHYPEVQKK IQEELDVKVG FGRYPLLSDR
     KILHYTEAAI SEVLRIRPVS PLLIPHVALK ESSIGEYTIP KEARVVINLW SLHHDEKEWV
     NPHLFSPDRF LDENGNRVYS PSPSFLPFGA GIRVCLGEAL AKMEVFLFLS WILQRFTLEV
     PEGDPLPDLE GKFGVVIQVK PFKVIAKLRE VWKNIEIVT