ID   CP11B_AQUCT             Reviewed;         517 AA.
AC   Q92104;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   24-JAN-2024, entry version 95.
DE   RecName: Full=Cytochrome P450 11B, mitochondrial;
DE   AltName: Full=CYPXIB;
DE   AltName: Full=Cytochrome P450C11;
DE   AltName: Full=P-450(11 beta,aldo);
DE   AltName: Full=Steroid 11-beta-hydroxylase;
DE            EC=1.14.15.4;
DE   Flags: Precursor;
GN   Name=CYP11B;
OS   Aquarana catesbeiana (American bullfrog) (Rana catesbeiana).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Rana; Aquarana.
OX   NCBI_TaxID=8400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Adrenal gland;
RX   PubMed=7744036; DOI=10.1111/j.1432-1033.1995.tb20462.x;
RA   Nonaka Y., Takemori H., Halder S.K., Sun T., Ohta M., Hatano O.,
RA   Takakusu A., Okamoto M.;
RT   "Frog cytochrome P-450 (11 beta,aldo), a single enzyme involved in the
RT   final steps of glucocorticoid and mineralocorticoid biosynthesis.";
RL   Eur. J. Biochem. 229:249-256(1995).
CC   -!- FUNCTION: Has 11 beta-hydroxylation, 18-hydroxylation activities and
CC       aldosterone synthetic activity. Catalyzes the final steps of
CC       glucocorticoid and mineralocorticoid biosynthesis.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a steroid + 2 H(+) + O2 + 2 reduced [adrenodoxin] = an 11beta-
CC         hydroxysteroid + H2O + 2 oxidized [adrenodoxin];
CC         Xref=Rhea:RHEA:15629, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:35341,
CC         ChEBI:CHEBI:35346; EC=1.14.15.4;
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P19099};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; D10984; BAA01756.1; -; mRNA.
DR   PIR; S69347; S69347.
DR   AlphaFoldDB; Q92104; -.
DR   SMR; Q92104; -.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004507; F:steroid 11-beta-monooxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd20644; CYP11B; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 1.
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; PTHR24279; -; 1.
DR   PANTHER; PTHR24279:SF1; CYTOCHROME P450 11B2, MITOCHONDRIAL; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   2: Evidence at transcript level;
KW   Heme; Iron; Membrane; Metal-binding; Mitochondrion; Monooxygenase;
KW   Oxidoreductase; Steroidogenesis; Transit peptide.
FT   TRANSIT         1..45
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           46..517
FT                   /note="Cytochrome P450 11B, mitochondrial"
FT                   /id="PRO_0000003607"
FT   BINDING         465
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   517 AA;  59539 MW;  8F94DCD66BA6370B CRC64;
     MLEKTAARQI GSCLMRCRTL DTTSPLWTGF SRLSTAPLIH EAREDGSLAS QTLPYEAIPT
     TGRSAWFNLF QFWRKNSFQH MHLAMEENFQ NLGPIYREKL GTHNSVNIML PQDVARLFQS
     EGIFPRRMTM EAWSKHRELR NHKQGVFLLN GEAWRSDRII LNKEVLSLAG VKKFLPFLDE
     AAADFVTFMK KRMSKNTRGS LTVDLYADLF RFTLEASSYV LYGQRLGLLE EHPNADTLRF
     ISAVETVLKT TLPLLYYPHQ ILQLFQTRLW NEHMHAWDVI FEQADRCIQN IYQEYCLGQE
     RGYSGIMAEL LLQAELPLDS IKANITELMA GGVDTTAMPL LFTLFELARN PSVQRELREE
     IRKAEAQNPN DLNQLLNSLP LLKGAIKETL RLYPVGITVQ RHLIKDIVLH NYHIPAGTLV
     QVGLYPMGRS PLLFQDALRY DPARWLKRED TNFKALAFGF GSRQCIGRRI AETEITLFLM
     HMLKNFQIDT VSKDDIKTVF GFILMPEKPP LLTFRPI
//