C11B1_CAVPO
ID C11B1_CAVPO Reviewed; 500 AA.
AC Q64408;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Cytochrome P450 11B1, mitochondrial;
DE AltName: Full=Aldosterone synthase;
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 Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Dunkin-Hartley; TISSUE=Adrenal gland;
RX PubMed=8619851; DOI=10.1006/bbrc.1996.0591;
RA Buelow H.E., Mobius K., Bahr V., Bernhardt R.;
RT "Molecular cloning and functional expression of the cytochrome P450 11B-
RT hydroxylase of the guinea pig.";
RL Biochem. Biophys. Res. Commun. 221:304-312(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; Z69785; CAA93633.1; -; mRNA.
DR PIR; JC4709; JC4709.
DR RefSeq; NP_001166410.1; NM_001172939.1.
DR AlphaFoldDB; Q64408; -.
DR SMR; Q64408; -.
DR STRING; 10141.ENSCPOP00000012206; -.
DR PRIDE; Q64408; -.
DR GeneID; 111755182; -.
DR CTD; 1584; -.
DR eggNOG; KOG0159; Eukaryota.
DR HOGENOM; CLU_001570_28_4_1; -.
DR InParanoid; Q64408; -.
DR UniPathway; UPA00788; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
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 2: Evidence at transcript level;
KW Heme; Iron; Lipid metabolism; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Monooxygenase; Oxidoreductase;
KW Reference proteome; Steroid metabolism; Steroidogenesis; Transit peptide.
FT TRANSIT 1..24
FT /note="Mitochondrion"
FT CHAIN 25..500
FT /note="Cytochrome P450 11B1, mitochondrial"
FT /id="PRO_0000003595"
FT BINDING 447
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 500 AA; 57820 MW; C4B5AB6041CD4AF2 CRC64;
MAFRLKSDVR LAGSWLCLRG ARALGTRAVT ASKASVLPFE VIPQHQGNKR QRVLQFWKEQ
NHDDLHLEMH QTFQELGPIF RCDVGSTRIV AVMLPEDCAR LHQAESPYPH RMHLEPWMAY
REHRRQNLGV FLLNGPEWLS NRRWLNPNVL SPKAVQNLLP MVDTVARDFS EALKQKVLQS
AQGSLTMDMQ PDIHKYTVEV SNFALFGERL GLFGCNPSSQ SLKFIHALEA VFKTTTQLMF
LPRSLSRWMR SQAWKEHFEA WDYISEYAEN RIQKKYEELA RGCSQYNSIV ANLMLQGNLP
LRAMKANIMD LVAGSVDTTA LPLMMTLFEL ARNPTVQQAL RQESMATEPN IYENPQRLRM
ELPLLWAAIK ETLRMYPVGL FLERFLTSPL VLQNYHIPAG TLVHLNLYSM GRNPEVFLSP
EHYNPQRWLE NKETYKHLAF GFGVRQCIGR RLAEVEMLLF LHHVLKSFCV ETAFQEDVKF
AYRFVMMPTS APLLTFRPVS
