ID   Q16316_HUMAN            Unreviewed;       228 AA.
AC   Q16316;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 98.
DE   SubName: Full=Steroid 18-hydroxylase {ECO:0000313|EMBL:AAB34643.1};
DE   Flags: Fragment;
GN   Name=CYP11B2 {ECO:0000313|EMBL:AAB34643.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:AAB34643.1};
RN   [1] {ECO:0000313|EMBL:AAB34643.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=7792802; DOI=10.1016/0039-128X(94)00023-6;
RA   Shizuta Y., Kawamoto T., Mitsuuchi Y., Miyahara K., Rosler A., Ulick S.,
RA   Imura H.;
RT   "Inborn errors of aldosterone biosynthesis in humans.";
RL   Steroids 60:15-21(1995).
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:0000256|ARBA:ARBA00035574};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46105;
CC         Evidence={ECO:0000256|ARBA:ARBA00035574};
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:0000256|ARBA:ARBA00035575};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15630;
CC         Evidence={ECO:0000256|ARBA:ARBA00035575};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971};
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|ARBA:ARBA00010617}.
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DR   EMBL; AH004767; AAB34643.1; -; Genomic_DNA.
DR   EMBL; S77398; AAB34643.1; JOINED; Genomic_DNA.
DR   EMBL; S77401; AAB34643.1; JOINED; Genomic_DNA.
DR   EMBL; S77403; AAB34643.1; JOINED; Genomic_DNA.
DR   AlphaFoldDB; Q16316; -.
DR   SMR; Q16316; -.
DR   PeptideAtlas; Q16316; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProt.
DR   GO; GO:1901615; P:organic hydroxy compound metabolic process; IEA:UniProt.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   InterPro; IPR001128; Cyt_P450.
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   SUPFAM; SSF48264; Cytochrome P450; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAB34643.1"
FT   NON_TER         228
FT                   /evidence="ECO:0000313|EMBL:AAB34643.1"
SQ   SEQUENCE   228 AA;  25584 MW;  2094951268AEF1F6 CRC64;
     KKKVLQNAWG SLTLDVQPSI FHYTIEASNL ALFGERLGLV GHSPSSASLN FLHALEVMFK
     STVQLMFMPR SLSRWISPKV WKEHFEAWDC IFQYGDNCIQ KIYQELAFNR PQHYTGIVAE
     LLLKAELSLE AIKANSMELT AGSVDTTAFP LLMTLFELAR NPDVQQILRQ ESLAAAASIS
     EHPQKATTEL PLLRAALKET LRLYPVGLFL ERVASSDLVL QNYHIPAG
//