ID A0A1R0UD00_9MYCO Unreviewed; 360 AA.
AC A0A1R0UD00;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=3-ketosteroid-9-alpha-hydroxylase {ECO:0000313|EMBL:OMC16779.1};
GN ORFNames=A5736_17495 {ECO:0000313|EMBL:OMC16779.1};
OS Mycobacterium sp. SP-6446.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834162 {ECO:0000313|EMBL:OMC16779.1, ECO:0000313|Proteomes:UP000187139};
RN [1] {ECO:0000313|Proteomes:UP000187139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP-6446 {ECO:0000313|Proteomes:UP000187139};
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:OMC16779.1}.
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DR EMBL; MBEM01000106; OMC16779.1; -; Genomic_DNA.
DR RefSeq; WP_076128556.1; NZ_MBEM01000106.1.
DR AlphaFoldDB; A0A1R0UD00; -.
DR Proteomes; UP000187139; 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:0016491; F:oxidoreductase activity; IEA:InterPro.
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}.
FT DOMAIN 12..124
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 271..360
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 360 AA; 38672 MW; A2DD22B84CBEADE6 CRC64;
MTEAIPDEPL GDHVLELQIA EVVAETDDAR SLVFAVPDAA GDPAIPPERL RYAPGQFLTL
RVPSDRTGSV ARCYSLCSSP FTDDALTVTV KRTADGYASN WLCDHAHKGM RIHVLAPSGN
FVPKTLDADF LLMAAGSGIT PIMSICKSAL AEGSGQVTLL YANRDDRSVI FADALRELSA
KYPDRLTVLH WLESLQGLPS ATALAKLAAP YTDRPVYICG PGPFMDASRE ALEALKVPAP
QVHIEVFKSL DSDPFAAVKI EDTAEGDEPP ATAVVELDGE THTVSWPRNA KLLDVLLAKG
LDAPFSCREG HCGACACTLR SGKVNMEVND VLEQQDLDEG LILACQSHPE SDSVEVTYDD
//
