C11B1_BOVIN
ID C11B1_BOVIN Reviewed; 503 AA.
AC P15150; Q29457;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 2.
DT 03-AUG-2022, entry version 143.
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:0000303|PubMed:3499608};
DE EC=1.14.15.4 {ECO:0000250|UniProtKB:P15538};
DE Flags: Precursor;
GN Name=CYP11B1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOZYME-2), AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=3429448; DOI=10.1093/oxfordjournals.jbchem.a122089;
RA Morohashi K., Yoshioka H., Gotoh O., Okada Y., Yamamoto K., Miyata T.,
RA Sogawa K., Fujii-Kuriyama Y., Omura T.;
RT "Molecular cloning and nucleotide sequence of DNA of mitochondrial
RT cytochrome P-450(11 beta) of bovine adrenal cortex.";
RL J. Biochem. 102:559-568(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOZYME-3).
RC TISSUE=Adrenal cortex;
RX PubMed=3266212; DOI=10.1093/oxfordjournals.jbchem.a122533;
RA Kirita S., Morohashi K., Hashimoto T., Yoshioka H., Fujii-Kuriyama Y.,
RA Omura T.;
RT "Expression of two kinds of cytochrome P-450(11 beta) mRNA in bovine
RT adrenal cortex.";
RL J. Biochem. 104:683-686(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3499608; DOI=10.1073/pnas.84.20.7193;
RA Chua S.C., Szabo P., Vitek A., Grzeschik K.H., John M., White P.C.;
RT "Cloning of cDNA encoding steroid 11 beta-hydroxylase (P450c11).";
RL Proc. Natl. Acad. Sci. U.S.A. 84:7193-7197(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2753866; DOI=10.1093/oxfordjournals.jbchem.a122725;
RA Hashimoto T., Morohashi K., Omura T.;
RT "Cloning and characterization of bovine cytochrome P-450(11 beta) genes.";
RL J. Biochem. 105:676-679(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1965187; DOI=10.1093/oxfordjournals.jbchem.a123302;
RA Kirita S., Hashimoto T., Kitajima M., Honda S., Morohashi K., Omura T.;
RT "Structural analysis of multiple bovine P-450(11 beta) genes and their
RT promoter activities.";
RL J. Biochem. 108:1030-1041(1990).
CC -!- FUNCTION: A cytochrome P450 monooxygenase involved in the biosynthesis
CC of adrenal corticoids. Catalyzes the hydroxylation of carbon hydrogen
CC bond at 11-beta position of 11-deoxycortisol and 11-
CC deoxycorticosterone/21-hydroxyprogesterone yielding cortisol or
CC corticosterone, respectively. 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:P15538}.
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:P15538};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15630;
CC Evidence={ECO:0000250|UniProtKB:P15538};
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:P15538};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46105;
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 -!- MISCELLANEOUS: The sequence shown is that of isozyme 11-beta-2.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA00127.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D00185; BAA00127.1; ALT_FRAME; mRNA.
DR EMBL; D00361; BAA00268.1; -; mRNA.
DR EMBL; M17843; AAA83383.1; -; mRNA.
DR EMBL; D00455; BAA00347.1; -; Genomic_DNA.
DR PIR; A28415; A28415.
DR PIR; JX0071; JX0071.
DR PIR; JX0151; JX0151.
DR RefSeq; NP_777063.2; NM_174638.3.
DR AlphaFoldDB; P15150; -.
DR SMR; P15150; -.
DR BindingDB; P15150; -.
DR ChEMBL; CHEMBL2927; -.
DR DrugCentral; P15150; -.
DR PaxDb; P15150; -.
DR GeneID; 282422; -.
DR KEGG; bta:282422; -.
DR CTD; 1584; -.
DR eggNOG; KOG0159; Eukaryota.
DR InParanoid; P15150; -.
DR UniPathway; UPA00788; -.
DR PRO; PR:P15150; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005743; C:mitochondrial inner 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:0006704; P:glucocorticoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.630.10; -; 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 Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Heme; Iron; Lipid metabolism; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion inner membrane; Monooxygenase;
KW Oxidoreductase; Reference proteome; Steroid metabolism; Steroidogenesis;
KW Transit peptide.
FT TRANSIT 1..24
FT /note="Mitochondrion"
FT CHAIN 25..503
FT /note="Cytochrome P450 11B1, mitochondrial"
FT /id="PRO_0000003594"
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 VARIANT 30
FT /note="A -> V (in 11-beta-3)"
FT VARIANT 60
FT /note="S -> G (in 11-beta-3)"
FT VARIANT 106
FT /note="H -> R (in 11-beta-3)"
FT CONFLICT 191..192
FT /note="SV -> RL (in Ref. 3; AAA83383)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="Q -> T (in Ref. 4; BAA00347 and 5; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="A -> P (in Ref. 3; AAA83383)"
FT /evidence="ECO:0000305"
FT CONFLICT 502
FT /note="I -> Y (in Ref. 4; BAA00347)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 503 AA; 57847 MW; 9FBEEC132975FD72 CRC64;
MALWAKARVR MAGPWLSLHE ARLLGTRGAA APKAVLPFEA MPRCPGNKWM RMLQIWKEQS
SENMHLDMHQ TFQELGPIFR YDVGGRHMVF VMLPEDVERL QQADSHHPQR MILEPWLAYR
QARGHKCGVF LLNGPQWRLD RLRLNPDVLS LPALQKYTPL VDGVARDFSQ TLKARVLQNA
RGSLTLDIAP SVFRYTIEAS TLVLYGERLG LLTQQPNPDS LNFIHALEAM LKSTVQLMFV
PRRLSRWMST NMWREHFEAW DYIFQYANRA IQRIYQELAL GHPWHYSGIV AELLMRADMT
LDTIKANTID LTAGSVDTTA FPLLMTLFEL ARNPEVQQAV RQESLVAEAR ISENPQRAIT
ELPLLRAALK ETLRLYPVGI TLEREVSSDL VLQNYHIPAG TLVKVLLYSL GRNPAVFARP
ESYHPQRWLD RQGSGSRFPH LAFGFGVRQC LGRRVAEVEM LLLLHHVLKN FLVETLEQED
IKMVYRFILM PSTLPLFTFR AIQ
