ID   C11B1_MESAU             Reviewed;         499 AA.
AC   P97720;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   02-SEP-2026, entry version 109.
DE   RecName: Full=Cytochrome P450 11B1, mitochondrial;
DE   AltName: Full=CYPXIB1;
DE   AltName: Full=Cytochrome P450C11;
DE   AltName: Full=Steroid 11-beta-hydroxylase, CYP11B1 {ECO:0000250|UniProtKB:P15538};
DE            EC=1.14.15.4 {ECO:0000250|UniProtKB:P15538};
DE   Flags: Precursor;
GN   Name=CYP11B1;
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Syrian; TISSUE=Adrenal gland;
RX   PubMed=8645611; DOI=10.1016/0960-0760(95)00249-9;
RA   Veronneau S., Bernard H., Cloutier M., Courtemanche J., Ducharme L.,
RA   Lefebvre A., Mason J.I., Lehoux J.-G.;
RT   "The hamster adrenal cytochrome P450C11 has equipotent 11beta-hydroxylase
RT   and 19-hydroxylase activities, but no aldosterone synthase activity.";
RL   J. Steroid Biochem. Mol. Biol. 57:125-139(1996).
CC   -!- FUNCTION: A cytochrome P450 monooxygenase involved in the biosynthesis
CC       of adrenal corticoids (By similarity). Catalyzes a variety of reactions
CC       that are essential for many species, including detoxification, defense,
CC       and the formation of endogenous chemicals like steroid hormones (By
CC       similarity). Steroid 11beta, 18- and 19-hydroxylase with preferred
CC       regioselectivity at 11beta, then 18, and lastly 19. Catalyzes the
CC       hydroxylation of 11-deoxycortisol and 11-deoxycorticosterone (21-
CC       hydroxyprogesterone) at 11beta position, yielding cortisol or
CC       corticosterone, respectively, but cannot produce aldosterone (By
CC       similarity). Mechanistically, uses molecular oxygen inserting one
CC       oxygen atom into a substrate for hydroxylation and reducing the second
CC       into a water molecule. Two electrons are provided by NADPH via a two-
CC       protein mitochondrial transfer system comprising flavoprotein FDXR
CC       (adrenodoxin/ferredoxin reductase) and nonheme iron-sulfur protein FDX1
CC       or FDX2 (adrenodoxin/ferredoxin). Due to its lack of 18-oxidation
CC       activity, it is incapable of generating aldosterone. Besides its role
CC       in the biosynthesis of mineralocorticoids and glucocorticoids, it can
CC       also participate in the androgen metabolic pathway, converting androst-
CC       4-ene-3,17-dione to 11beta-hydroxyandrost-4-ene-3,17-dione, and
CC       testosterone (17beta-hydroxy-4-androsten-3-one) to 11beta,17beta-
CC       dihydroxyandrost-4-ene-3-one (By similarity).
CC       {ECO:0000250|UniProtKB:P15393, ECO:0000250|UniProtKB:P15538}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a steroid + 2 reduced [adrenodoxin] + O2 + 2 H(+) = an 11beta-
CC         hydroxysteroid + 2 oxidized [adrenodoxin] + H2O;
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         Evidence={ECO:0000250|UniProtKB:P15538};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15630;
CC         Evidence={ECO:0000250|UniProtKB:P15538};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=11-deoxycortisol + 2 reduced [adrenodoxin] + O2 + 2 H(+) =
CC         cortisol + 2 oxidized [adrenodoxin] + H2O; Xref=Rhea:RHEA:46100,
CC         Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17650,
CC         ChEBI:CHEBI:28324, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738;
CC         Evidence={ECO:0000250|UniProtKB:P15538};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46101;
CC         Evidence={ECO:0000250|UniProtKB:P15538};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=21-hydroxyprogesterone + 2 reduced [adrenodoxin] + O2 + 2 H(+)
CC         = corticosterone + 2 oxidized [adrenodoxin] + H2O;
CC         Xref=Rhea:RHEA:46104, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16827, ChEBI:CHEBI:16973, ChEBI:CHEBI:33737,
CC         ChEBI:CHEBI:33738; Evidence={ECO:0000250|UniProtKB:P15538};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46105;
CC         Evidence={ECO:0000250|UniProtKB:P15538};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=21-hydroxyprogesterone + 2 reduced [adrenodoxin] + O2 + 2 H(+)
CC         = 18-hydroxy-11-deoxycorticosterone + 2 oxidized [adrenodoxin] + H2O;
CC         Xref=Rhea:RHEA:76151, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16973, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC         ChEBI:CHEBI:195166; Evidence={ECO:0000250|UniProtKB:P15393};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76152;
CC         Evidence={ECO:0000250|UniProtKB:P15393};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=21-hydroxyprogesterone + 2 reduced [adrenodoxin] + O2 + 2 H(+)
CC         = 19-hydroxy-11-deoxycorticosterone + 2 oxidized [adrenodoxin] + H2O;
CC         Xref=Rhea:RHEA:76155, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16973, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC         ChEBI:CHEBI:195167; Evidence={ECO:0000250|UniProtKB:P15393};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76156;
CC         Evidence={ECO:0000250|UniProtKB:P15393};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cortisol + 2 reduced [adrenodoxin] + O2 + 2 H(+) = 18-
CC         hydroxycortisol + 2 oxidized [adrenodoxin] + H2O;
CC         Xref=Rhea:RHEA:76019, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:17650, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC         ChEBI:CHEBI:89455; Evidence={ECO:0000250|UniProtKB:P15393};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76020;
CC         Evidence={ECO:0000250|UniProtKB:P15393};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=11-deoxycortisol + 2 reduced [adrenodoxin] + O2 + 2 H(+) = 18-
CC         hydroxy-11-deoxycortisol + 2 oxidized [adrenodoxin] + H2O;
CC         Xref=Rhea:RHEA:76163, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:28324, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC         ChEBI:CHEBI:195179; Evidence={ECO:0000250|UniProtKB:P15393};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76164;
CC         Evidence={ECO:0000250|UniProtKB:P15393};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=androst-4-ene-3,17-dione + 2 reduced [adrenodoxin] + O2 + 2
CC         H(+) = 11beta-hydroxyandrost-4-ene-3,17-dione + 2 oxidized
CC         [adrenodoxin] + H2O; Xref=Rhea:RHEA:84071, Rhea:RHEA-COMP:9998,
CC         Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16422, ChEBI:CHEBI:27967,
CC         ChEBI:CHEBI:33737, ChEBI:CHEBI:33738;
CC         Evidence={ECO:0000250|UniProtKB:P15538};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:84072;
CC         Evidence={ECO:0000250|UniProtKB:P15538};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=testosterone + 2 reduced [adrenodoxin] + O2 + 2 H(+) =
CC         11beta,17beta-dihydroxyandrost-4-ene-3-one + 2 oxidized [adrenodoxin]
CC         + H2O; Xref=Rhea:RHEA:86455, Rhea:RHEA-COMP:9998, Rhea:RHEA-
CC         COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:17347, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC         ChEBI:CHEBI:81481; Evidence={ECO:0000250|UniProtKB:P15538};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:86456;
CC         Evidence={ECO:0000250|UniProtKB:P15538};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P19099};
CC   -!- PATHWAY: Steroid biosynthesis; glucocorticoid biosynthesis.
CC       {ECO:0000250|UniProtKB:P15538}.
CC   -!- PATHWAY: Steroid hormone biosynthesis. {ECO:0000250|UniProtKB:P15538}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P14137}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P14137}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; S82228; AAB47144.1; -; mRNA.
DR   AlphaFoldDB; P97720; -.
DR   SMR; P97720; -.
DR   STRING; 10036.ENSMAUP00000012066; -.
DR   eggNOG; KOG0159; Eukaryota.
DR   UniPathway; UPA00788; -.
DR   Proteomes; UP000886700; Unplaced.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0047783; F:corticosterone 18-monooxygenase activity; IEA:TreeGrafter.
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:0032342; P:aldosterone biosynthetic process; IEA:TreeGrafter.
DR   GO; GO:0071375; P:cellular response to peptide hormone stimulus; IEA:TreeGrafter.
DR   GO; GO:0008203; P:cholesterol metabolic process; IEA:TreeGrafter.
DR   GO; GO:0034650; P:cortisol metabolic process; IEA:TreeGrafter.
DR   GO; GO:0006704; P:glucocorticoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   InterPro; IPR050479; CYP11_CYP27_families.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002399; Cyt_P450_mitochondrial.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   PANTHER; PTHR24279; CYTOCHROME P450; 1.
DR   PANTHER; PTHR24279:SF116; STEROID 11BETA-MONOOXYGENASE; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00408; MITP450.
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;
KW   Mitochondrion inner membrane; Monooxygenase; Oxidoreductase;
KW   Reference proteome; Steroidogenesis; Transit peptide.
FT   TRANSIT         1..24
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           25..499
FT                   /note="Cytochrome P450 11B1, mitochondrial"
FT                   /id="PRO_0000003598"
FT   BINDING         446
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|UniProtKB:P19099"
SQ   SEQUENCE   499 AA;  56821 MW;  C798467266D741BD CRC64;
     MALRAKADVW LARPWQCLPR TRALGTTAAL APNTLRPFEA IPQYSRNRWL KMLQILREEG
     QEGLHLEMHE AFRELGPIFR YSMGRTQVVY VMLPEVAEKV FQADSTQPSR TLLEPWVAHR
     EHRGLSRGVF LLNGPEWRFN RLRINPHMLS PKAVQKFVPM VDMVARDFLE FLKKKVLANA
     HGSLSMNFYS SMFNYTIEAS HFVLFGERLG LLGDDLNSGS LKFVNALNSI MKTTPQLMLL
     PSGLTRWIST RVWKENFDSW DFVSEYVTKN VKNVYQEVQS GGPQSWSVIS QLVAEGALTM
     DAILANSLEL TAGSVDTTSV PLVMTLFELA RNPDVQQAVR QESLAAEASV AANPQRAMSD
     LPLLRAVLKE TLRLYPVAVF LERILSSDLV LQNYHVPAGT ILHMSLYSMG RNPAVFPRPE
     HYLPQRWLER NGSFQHLTFG FGVRQCLGKR LAQVEMLLLL HHVLKSFRVE TQEREDVRMV
     YRFVLAPSSS PLLTFRPVS
//