ID   A0A0Q8DSD2_9ACTN        Unreviewed;       362 AA.
AC   A0A0Q8DSD2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=3-ketosteroid-9-alpha-hydroxylase {ECO:0000313|EMBL:KRA32890.1};
GN   ORFNames=ASD81_14850 {ECO:0000313|EMBL:KRA32890.1};
OS   Nocardioides sp. Root614.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=1736571 {ECO:0000313|EMBL:KRA32890.1, ECO:0000313|Proteomes:UP000051699};
RN   [1] {ECO:0000313|EMBL:KRA32890.1, ECO:0000313|Proteomes:UP000051699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root614 {ECO:0000313|EMBL:KRA32890.1,
RC   ECO:0000313|Proteomes:UP000051699};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRA32890.1, ECO:0000313|Proteomes:UP000051699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root614 {ECO:0000313|EMBL:KRA32890.1,
RC   ECO:0000313|Proteomes:UP000051699};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KRA32890.1}.
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DR   EMBL; LMGV01000006; KRA32890.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q8DSD2; -.
DR   Proteomes; UP000051699; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051699}.
FT   DOMAIN          1..107
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   DOMAIN          273..362
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
SQ   SEQUENCE   362 AA;  39003 MW;  93994023FD478ECF CRC64;
     MESFVLDVVG VVEETADAKS ISFAVPAGAE EKFVYKPGQF LTVAVPSDQT GIAARCYSLS
     SSPHDGGPLT VTVKRTAGGF ASNWICDNLS VGDTLRALPP SGIFTPSSID NDLLLFGGGS
     GVTPIMSITR TALAEGTGKI VVFYANRDEK SVIFAEEFAR LAAENPERLQ VIHWLESVQG
     LPTPEQMKAF CSGYLDREAF VCGPAPFMKM VTTVLKELEV PRSQRHQEKF VSLGGNPFGD
     IEEMRQQAAA EIALADGNDD GADDFADAPT GPVKVEVELD GEEFTFDDWN PRTTLLDFLE
     SKGVKAPYSC REGECSACAI RLLAGDVRML HNDVLDKDDL DDGIRLGCQS VPVTDTVKVT
     YS
//