ID C11B1_SHEEP Reviewed; 503 AA.
AC P51663; O19181;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 08-NOV-2023, entry version 103.
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 Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Merino; TISSUE=Adrenal cortex;
RX PubMed=7999785; DOI=10.1016/0167-4781(94)00190-e;
RA Boon W.C., Roche P.J., Hammond V.E., Jeyaseelan K., Crawford R.J.,
RA Coghlan J.P.;
RT "Cloning and expression analysis of a cytochrome P-450(11 beta) cDNA in
RT sheep.";
RL Biochim. Biophys. Acta 1260:109-112(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Adrenal gland, and Liver;
RX PubMed=10728821; DOI=10.3109/10425179809020897;
RA Anwar A., Coghlan J.P., Jeyaseelan K.;
RT "Structure of an ovine CYP11B1 gene.";
RL DNA Seq. 8:357-374(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-77.
RX PubMed=7804143;
RA Anwar A., Jeyaseelan K., Coghlan J.P.;
RT "Molecular cloning and characterization of the ovine CYP11B1 promoter.";
RL Biochem. Mol. Biol. Int. 33:1169-1178(1994).
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; L34337; AAA62308.1; -; mRNA.
DR EMBL; L47569; AAA81576.1; -; Genomic_DNA.
DR EMBL; U78478; AAB64249.1; -; Genomic_DNA.
DR EMBL; U78477; AAB64248.1; -; mRNA.
DR EMBL; L28716; AAA83384.1; -; Genomic_DNA.
DR PIR; S52085; S52085.
DR RefSeq; NP_001068568.1; NM_001075100.2.
DR AlphaFoldDB; P51663; -.
DR SMR; P51663; -.
DR STRING; 9940.ENSOARP00000000890; -.
DR PaxDb; 9940-ENSOARP00000000890; -.
DR Ensembl; ENSOART00020020700; ENSOARP00020017139; ENSOARG00020013254.
DR GeneID; 767576; -.
DR KEGG; oas:767576; -.
DR CTD; 1584; -.
DR eggNOG; KOG0159; Eukaryota.
DR OrthoDB; 2658719at2759; -.
DR UniPathway; UPA00788; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0047783; F:corticosterone 18-monooxygenase activity; IEA:RHEA.
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:0006704; P:glucocorticoid biosynthetic process; IEA:UniProtKB-UniPathway.
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 CHAIN 25..503
FT /note="Cytochrome P450 11B1, mitochondrial"
FT /id="PRO_0000003606"
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"
FT CONFLICT 99
FT /note="R -> S (in Ref. 2; AAB64248/AAB64249)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="A -> G (in Ref. 1; AAA62308)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="P -> R (in Ref. 1; AAA62308)"
FT /evidence="ECO:0000305"
FT CONFLICT 500
FT /note="R -> G (in Ref. 2; AAB64248/AAB64249)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 503 AA; 57784 MW; 968F2DF6EE7D595B CRC64;
MALWAKARVW MAGPWLSLHR ARPLGTRASA APKAVLPFEA MPRCPGNKWM RVLQIWKEQG
SENMHLDMHQ TFQELGPIFR YDVGGRHMVF VMLPEDVERL QQAESLHPQR MLLEPWLAYR
QARGHKCGVF LLNGPQWRLD RLRLNPDVLS LPALQKYTPL VDGVARDFSQ TLKARVLQNA
RGSLTLDIAP SVFRYTIEAS TLVLYGERLG LLTQQPNPDS LNFIHALEAM FKSTVQLMFV
PRRLSRWTSS SMWREHFEAW DYIFQYANRA IQRIYQELAL GHPWHYSGIV AELLMRADMT
LDTIKANTID LTAGSVDTTA FPLLMTLFEL ARNPEVQQAL RQESLVAEAR ISENPQRATT
ELPLLRAALK ETLRLYPVGI TLERQVSSDL VLQNYHIPAG TLVKVLLYSL GRNPAVFARP
ESYHPQRWLD RQGSGSRFPH LAFGFGMRQC LGRRVAEVEM LLLLHHVLKN FLVETLAQED
IKMVYRFILM PSTLPLFTFR AIQ
//
