ID Q9KJ93_STRCL Unreviewed; 407 AA.
AC Q9KJ93;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=Cytochrome P-450 {ECO:0000313|EMBL:AAF85938.1};
DE SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:AAK56488.1};
GN Name=cyp {ECO:0000313|EMBL:AAF85938.1};
OS Streptomyces clavuligerus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1901 {ECO:0000313|EMBL:AAF85938.1};
RN [1] {ECO:0000313|EMBL:AAF85938.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC27064 {ECO:0000313|EMBL:AAF85938.1};
RX PubMed=10869089; DOI=10.1128/JB.182.14.4087-4095.2000;
RA Li R., Khaleeli N., Townsend C.A.;
RT "Expansion of the clavulanic acid gene cluster: identification and in vivo
RT functional analysis of three new genes required for biosynthesis of
RT clavulanic acid by Streptomyces clavuligerus.";
RL J. Bacteriol. 182:4087-4095(2000).
RN [2] {ECO:0000313|EMBL:AAK56488.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=11988517;
RA Mellado E., Lorenzana L.M., Rodriguez-Saiz M., Diez B., Liras P.,
RA Barredo J.L.;
RT "The clavulanic acid biosynthetic cluster of Streptomyces clavuligerus:
RT genetic organization of the region upstream of the car gene.";
RL Microbiology 148:1427-1438(2002).
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR EMBL; AF200819; AAF85938.1; -; Genomic_DNA.
DR EMBL; AY034175; AAK56488.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9KJ93; -.
DR SMR; Q9KJ93; -.
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 CDD; cd11030; CYP105-like; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002397; Cyt_P450_B.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR46696; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR PANTHER; PTHR46696:SF1; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00359; BP450.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|RuleBase:RU000461}; Iron {ECO:0000256|RuleBase:RU000461};
KW Metal-binding {ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461}.
SQ SEQUENCE 407 AA; 44906 MW; AC97CAB3EC30F5C3 CRC64;
MNEAAPQSDQ VAPAYPMHRV CPVDPPPQLA GLRSQKAASR VTLWDGSQVW LVTSHAGARA
VLGDRRFTAV TSAPGFPMLT RTSQLVRANP ESASFIRMDD PQHSRLRSML TRDFLARRAE
ALRPAVRELL DEILGGLVKG ERPVDLVAGL TIPVPSRVIT LLFGAGDDRR EFIEDRSAVL
IDRGYTPEQV AKARDELDGY LRELVEERIE NPGTDLISRL VIDQVRPGHL RVEEMVPMCR
LLLVAGHGTT TSQASLSLLS LLTDPELAGR LTEDPALLPK AVEELLRFHS IVQNGLARAA
VEDVQLDDVL IRAGEGVVLS LSAGNRDETV FPDPDRVDVD RDARRHLAFG HGMHQCLGQW
LARVELEEIL AAVLRWMPGA RLAVPFEELD FRHEVSSYGL GALPVTW
//
