CP11B_LITCT
ID CP11B_LITCT Reviewed; 517 AA.
AC Q92104;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Cytochrome P450 11B, mitochondrial;
DE AltName: Full=CYPXIB;
DE AltName: Full=Cytochrome P450C11;
DE AltName: Full=P-450(11 beta,aldo);
DE AltName: Full=Steroid 11-beta-hydroxylase;
DE EC=1.14.15.4;
DE Flags: Precursor;
GN Name=CYP11B;
OS Lithobates catesbeianus (American bullfrog) (Rana catesbeiana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX NCBI_TaxID=8400;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Adrenal gland;
RX PubMed=7744036; DOI=10.1111/j.1432-1033.1995.tb20462.x;
RA Nonaka Y., Takemori H., Halder S.K., Sun T., Ohta M., Hatano O.,
RA Takakusu A., Okamoto M.;
RT "Frog cytochrome P-450 (11 beta,aldo), a single enzyme involved in the
RT final steps of glucocorticoid and mineralocorticoid biosynthesis.";
RL Eur. J. Biochem. 229:249-256(1995).
CC -!- FUNCTION: Has 11 beta-hydroxylation, 18-hydroxylation activities and
CC aldosterone synthetic activity. Catalyzes the final steps of
CC glucocorticoid and mineralocorticoid biosynthesis.
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 -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P19099};
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; D10984; BAA01756.1; -; mRNA.
DR PIR; S69347; S69347.
DR AlphaFoldDB; Q92104; -.
DR SMR; Q92104; -.
DR GO; GO:0031966; C:mitochondrial 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:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW.
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; Membrane; Metal-binding; Mitochondrion; Monooxygenase;
KW Oxidoreductase; Steroidogenesis; Transit peptide.
FT TRANSIT 1..45
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 46..517
FT /note="Cytochrome P450 11B, mitochondrial"
FT /id="PRO_0000003607"
FT BINDING 465
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"
SQ SEQUENCE 517 AA; 59539 MW; 8F94DCD66BA6370B CRC64;
MLEKTAARQI GSCLMRCRTL DTTSPLWTGF SRLSTAPLIH EAREDGSLAS QTLPYEAIPT
TGRSAWFNLF QFWRKNSFQH MHLAMEENFQ NLGPIYREKL GTHNSVNIML PQDVARLFQS
EGIFPRRMTM EAWSKHRELR NHKQGVFLLN GEAWRSDRII LNKEVLSLAG VKKFLPFLDE
AAADFVTFMK KRMSKNTRGS LTVDLYADLF RFTLEASSYV LYGQRLGLLE EHPNADTLRF
ISAVETVLKT TLPLLYYPHQ ILQLFQTRLW NEHMHAWDVI FEQADRCIQN IYQEYCLGQE
RGYSGIMAEL LLQAELPLDS IKANITELMA GGVDTTAMPL LFTLFELARN PSVQRELREE
IRKAEAQNPN DLNQLLNSLP LLKGAIKETL RLYPVGITVQ RHLIKDIVLH NYHIPAGTLV
QVGLYPMGRS PLLFQDALRY DPARWLKRED TNFKALAFGF GSRQCIGRRI AETEITLFLM
HMLKNFQIDT VSKDDIKTVF GFILMPEKPP LLTFRPI
