ID A0A1G9WRQ8_9ACTN Unreviewed; 367 AA.
AC A0A1G9WRQ8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=3-ketosteroid 9alpha-monooxygenase subunit B {ECO:0000313|EMBL:SDM86891.1};
GN ORFNames=SAMN05192576_1134 {ECO:0000313|EMBL:SDM86891.1};
OS Nocardioides szechwanensis.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1005944 {ECO:0000313|EMBL:SDM86891.1, ECO:0000313|Proteomes:UP000199004};
RN [1] {ECO:0000313|EMBL:SDM86891.1, ECO:0000313|Proteomes:UP000199004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.11147 {ECO:0000313|EMBL:SDM86891.1,
RC ECO:0000313|Proteomes:UP000199004};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; FNIC01000001; SDM86891.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9WRQ8; -.
DR STRING; 1005944.SAMN05192576_1134; -.
DR OrthoDB; 9796486at2; -.
DR Proteomes; UP000199004; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR CDD; cd06214; PA_degradation_oxidoreductase_like; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR47354:SF8; 1,2-PHENYLACETYL-COA EPOXIDASE, SUBUNIT E; 1.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR PRINTS; PR00410; PHEHYDRXLASE.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW Monooxygenase {ECO:0000313|EMBL:SDM86891.1};
KW Oxidoreductase {ECO:0000313|EMBL:SDM86891.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199004}.
FT DOMAIN 3..112
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 278..367
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT REGION 259..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 367 AA; 39532 MW; 2AC8635B0E6781A6 CRC64;
MDTETFELTV AEVVEETADA HSISFDVPDG QTDHFAYKPG QFLTVAVPSD QTGVAARCYS
LSSSPLTFAE SGRLTITVKR TADGYASNWI CDHLRQGDTM RVLPPSGIFT PASLNADLLL
FAGGSGITPI LSITRTALAQ GSGRVVLFYA NRDESSVIFA GELTALAAAH PERLQVIHWL
ESVQGLPSAE QMKAFAAGHS SYDAFVCGPA PFMKMTIGAL KELGFPRERR HQEKFVSLGG
NPFGDLHDVE VAESEIAAAE TDEQDAAEDL AGSSRGPSRL EVELDGEKHE FDDWQPGTKM
LDHLEAKGVK APFSCREGEC SACAVRLLEG DVKLLHNDVL DDEDLAEGIR LACQAVPVTD
TVRVTYS
//
