ID   C11B1_PIG               Reviewed;         503 AA.
AC   Q29552;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   24-JAN-2024, entry version 96.
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:P15150};
DE            EC=1.14.15.4 {ECO:0000250|UniProtKB:P15150};
DE            EC=1.14.15.5 {ECO:0000250|UniProtKB:P15150};
DE   Flags: Precursor;
GN   Name=CYP11B1;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Adrenal gland;
RX   PubMed=7696143; DOI=10.1016/0960-0760(94)00167-k;
RA   Sun T., Zhao Y., Nonaka Y., Okamoto M.;
RT   "Cloning and expression of cytochrome P450(11 beta) of porcine adrenal
RT   cortex.";
RL   J. Steroid Biochem. Mol. Biol. 52:227-232(1995).
CC   -!- FUNCTION: A cytochrome P450 monooxygenase that catalyzes the
CC       biosynthesis of aldosterone and other adrenal corticoids. Differing
CC       from other species (such as human, rat and mice), it is able to
CC       catalyze three sequential oxidative reactions of 11-deoxycorticosterone
CC       (21-hydroxyprogesterone), namely 11-beta hydroxylation, followed by two
CC       successive oxidations at C18 yielding 18-hydroxy and then 18-oxo
CC       intermediates, and ending with the formation of aldosterone. Steroid
CC       11beta, 18- and 19-hydroxylase. Mechanistically, uses molecular oxygen
CC       inserting one oxygen atom into a substrate and reducing the second into
CC       a water molecule. Two electrons are provided by NADPH via a two-protein
CC       mitochondrial transfer system comprising flavoprotein FDXR
CC       (adrenodoxin/ferredoxin reductase) and nonheme iron-sulfur protein FDX1
CC       or FDX2 (adrenodoxin/ferredoxin). {ECO:0000250|UniProtKB:P15150}.
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         Evidence={ECO:0000250|UniProtKB:P15150};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15630;
CC         Evidence={ECO:0000250|UniProtKB:P15150};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=11-deoxycortisol + 2 H(+) + O2 + 2 reduced [adrenodoxin] =
CC         cortisol + H2O + 2 oxidized [adrenodoxin]; 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 H(+) + O2 + 2 reduced [adrenodoxin]
CC         = corticosterone + H2O + 2 oxidized [adrenodoxin];
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:P15150};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46105;
CC         Evidence={ECO:0000250|UniProtKB:P15150};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=corticosterone + 2 H(+) + O2 + 2 reduced [adrenodoxin] = 18-
CC         hydroxycorticosterone + H2O + 2 oxidized [adrenodoxin];
CC         Xref=Rhea:RHEA:11872, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16485, ChEBI:CHEBI:16827, ChEBI:CHEBI:33737,
CC         ChEBI:CHEBI:33738; EC=1.14.15.5;
CC         Evidence={ECO:0000250|UniProtKB:P15150};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11873;
CC         Evidence={ECO:0000250|UniProtKB:P15150};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=18-hydroxycorticosterone + 2 H(+) + O2 + 2 reduced
CC         [adrenodoxin] = aldosterone + 2 H2O + 2 oxidized [adrenodoxin];
CC         Xref=Rhea:RHEA:50792, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16485, ChEBI:CHEBI:27584, ChEBI:CHEBI:33737,
CC         ChEBI:CHEBI:33738; Evidence={ECO:0000250|UniProtKB:P15150};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50793;
CC         Evidence={ECO:0000250|UniProtKB:P15150};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=21-hydroxyprogesterone + 2 H(+) + O2 + 2 reduced [adrenodoxin]
CC         = 19-hydroxy-11-deoxycorticosterone + H2O + 2 oxidized [adrenodoxin];
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:P15150};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76156;
CC         Evidence={ECO:0000250|UniProtKB:P15150};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=19-hydroxy-11-deoxycorticosterone + 2 H(+) + O2 + 2 reduced
CC         [adrenodoxin] = 19-oxo-11-deoxycorticosterone + 2 H2O + 2 oxidized
CC         [adrenodoxin]; Xref=Rhea:RHEA:76439, Rhea:RHEA-COMP:9998, Rhea:RHEA-
CC         COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:174650,
CC         ChEBI:CHEBI:195167; Evidence={ECO:0000250|UniProtKB:P15150};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76440;
CC         Evidence={ECO:0000250|UniProtKB:P15150};
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; D38590; BAA07600.1; -; mRNA.
DR   AlphaFoldDB; Q29552; -.
DR   SMR; Q29552; -.
DR   STRING; 9823.ENSSSCP00000043770; -.
DR   InParanoid; Q29552; -.
DR   UniPathway; UPA00788; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Proteomes; UP000694570; Unplaced.
DR   Proteomes; UP000694571; Unplaced.
DR   Proteomes; UP000694720; Unplaced.
DR   Proteomes; UP000694722; Unplaced.
DR   Proteomes; UP000694723; Unplaced.
DR   Proteomes; UP000694724; Unplaced.
DR   Proteomes; UP000694725; Unplaced.
DR   Proteomes; UP000694726; Unplaced.
DR   Proteomes; UP000694727; Unplaced.
DR   Proteomes; UP000694728; Unplaced.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR   GO; GO:0047783; F:corticosterone 18-monooxygenase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0032342; P:aldosterone biosynthetic process; IBA:GO_Central.
DR   GO; GO:0071375; P:cellular response to peptide hormone stimulus; IBA:GO_Central.
DR   GO; GO:0008203; P:cholesterol metabolic process; IBA:GO_Central.
DR   GO; GO:0034650; P:cortisol metabolic process; IBA:GO_Central.
DR   GO; GO:0006704; P:glucocorticoid biosynthetic process; IBA:GO_Central.
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;
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..503
FT                   /note="Cytochrome P450 11B1, mitochondrial"
FT                   /id="PRO_0000003602"
FT   BINDING         450
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   503 AA;  57340 MW;  4C40B1EEAAC49B05 CRC64;
     MAIWAKAEAW LAGPWLALNR ARTLGTRAVL APKGVLPFEA IPQFPGKKWM RVLQLWREQG
     FENNHLEMHQ TFQELGPIFR FDVGGRNMVL VMLPEDVERC QKVEGLHPQR DVPGPWLAYR
     HLRGHKCGVF LLNGPTWRLD RLQLNPGVLS LQAMQKFTPL VDGVARDFSQ ALRARVMQNA
     RGSLTLDIKP SIFRYTIEAS NLVLFGERLG LLAHQPNPES LDFIHALEVM FKSTVQLMFM
     PRSLSRWTST GTWKEHFEAW DCIFQYANKA IQRLYQELTL GHPWHYSGVV AELLTHANMT
     VDAIKANSID LTAGSVDTTA YPLLMTLFEL ARNPEVQQAL RQESLAAAAR ISENPQKAIT
     ELPLLRAALK ETLRLYPVGI FLDRCVTSDL VLQNYHIPAG TLVKVLLYSL GRNPAVFARP
     ERYHPQRWLD NQGSGTRFPH LAFGFGMRQC LGRRLAQVEM LLLLHHVLKN FLVETLVQED
     IKMIYRFIMT PSTLPLLTFR AIS
//