ID A0A3N6FF75_9ACTN Unreviewed; 408 AA.
AC A0A3N6FF75;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Pentalenic acid synthase {ECO:0000313|EMBL:RPK56936.1};
DE EC=1.14.15.11 {ECO:0000313|EMBL:RPK56936.1};
GN ORFNames=EES43_22840 {ECO:0000313|EMBL:RPK56936.1};
OS Streptomyces sp. ADI96-02.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1522760 {ECO:0000313|EMBL:RPK56936.1, ECO:0000313|Proteomes:UP000273170};
RN [1] {ECO:0000313|EMBL:RPK56936.1, ECO:0000313|Proteomes:UP000273170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ADI96-02 {ECO:0000313|EMBL:RPK56936.1,
RC ECO:0000313|Proteomes:UP000273170};
RA Guerrero-Garzon J.F., Zehl M., Urban E., Schneider O., Ruckert C.,
RA Busche T., Kalinowski J., Zotchev S.B.;
RT "Streptomyces spp. from the marine sponge Antho dichothoma: analyses of
RT secondary metabolite biosynthesis gene clusters and some of their
RT products.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RPK56936.1}.
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DR EMBL; RPGW01000151; RPK56936.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N6FF75; -.
DR OrthoDB; 3664945at2; -.
DR Proteomes; UP000273170; Unassembled WGS sequence.
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,
KW ECO:0000313|EMBL:RPK56936.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000273170}.
SQ SEQUENCE 408 AA; 45595 MW; A77A0B874FD575BE CRC64;
MSNAAPELPT EEHETFPYVR PCPFSQPAAY EAMAEEDVSQ VTLTGSGLRI WTVTGYTTIR
TLLTDPRVSA SRKHADFPFY FIAPPEFRTE TSFIGYDGEE HTRTRRKAAL TFTHRQVQRL
RPRIEEIVDD YLDRMLAMGP PVDMHRVFSL AVPMTVICEL LGIPQDQHDF FIRHGTALLG
GHSSPEERQA AIVEVNAYVS ELIQRKRKEP GDDLLSRAMA DYEESGEDYT DRDLFNMVRL
LMNGGHETTA SQISLGTACL LENPDQLAQL LADPSLIRPA VEELVRIATI GDTAVPRVAL
EDIEIGGRTI RAGDGILCLG LAGNRDPEVF PEPEKLIISR GSRKHLGFGH GVHHCIGADL
ARLELEIVWS RLFQRVPGLR LARPLADLPR KEGAVIYGLW ELPVTWDA
//
