C11B1_PAPHU
ID C11B1_PAPHU Reviewed; 503 AA.
AC Q29527;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 83.
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 Papio hamadryas ursinus (Chacma baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=36229;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Blood;
RX PubMed=8969902; DOI=10.1080/07435809609043737;
RA Hampf M., Swart A.C., Swart P.;
RT "Sequence of the 11 beta-hydroxylase gene from the Cape baboon (Papio
RT ursinus).";
RL Endocr. Res. 22:495-499(1996).
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 -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; U52085; AAA96967.1; -; Genomic_DNA.
DR EMBL; U52081; AAA96967.1; JOINED; Genomic_DNA.
DR EMBL; U52082; AAA96967.1; JOINED; Genomic_DNA.
DR EMBL; U52083; AAA96967.1; JOINED; Genomic_DNA.
DR EMBL; U52084; AAA96967.1; JOINED; Genomic_DNA.
DR AlphaFoldDB; Q29527; -.
DR SMR; Q29527; -.
DR UniPathway; UPA00788; -.
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; IPR002399; Cyt_P450_mitochondrial.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00408; MITP450.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Heme; Iron; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Monooxygenase; Oxidoreductase;
KW 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_0000003601"
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; 57644 MW; 413E7EFC3A578B86 CRC64;
MALRAKAEVC MAAPWLSLQR ARALGTRATR VPRTVLPFEA MPRRPGNRWL RLLQIWREQG
YEHLHLEVHQ TFQELGPIFR YDLGGAGMVC VMLPEDVEKL QQVDSLNPRR MSLEPWVAYR
QHRGHKCGVF LLNGPEWRFN RLRLNPDVLS PKAVQRFLPM VDAVARDFSQ ALRKKVVQNA
RESVTLDIQP SIFHYTIEAS NLALFGERLG LVGHSPSSAS LSFLHALEVM FKSTVQLMFM
PRSLSRWTSP KVWKEHFEAW DCIFQYGDNC IQKIYQELAL SRPQQYTSIV AELLLNAELS
PDAIKANSME LTAGSVDTTV FPLLMTLFEL ARNPNVQQAL RQESLAAAAS ISEHPQKATT
ELPLLRAALK ETLRLYPVGL FLERVVSSDL VLQNYHIPAG TLVRVFLYSL GRNPALFPRP
ERYNPQRWLD IRGSGRNFYH VPFGFGMRQC LGRRLAEAEM LLLLHHVLKH LQVETLTQED
IKMVYSFILR PSTFPLLTFR AIN
