ID A0A2C9SZ18_9MYCO Unreviewed; 357 AA.
AC A0A2C9SZ18;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=3-ketosteroid-9-alpha-hydroxylase reductase subunit {ECO:0000313|EMBL:GAY16804.1};
GN ORFNames=MSZK_35300 {ECO:0000313|EMBL:GAY16804.1};
OS Mycobacterium sp. shizuoka-1.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=2039281 {ECO:0000313|EMBL:GAY16804.1, ECO:0000313|Proteomes:UP000223528};
RN [1] {ECO:0000313|EMBL:GAY16804.1, ECO:0000313|Proteomes:UP000223528}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=shizuoka-1 {ECO:0000313|Proteomes:UP000223528};
RA Yoshida M., Izumiyama S., Fukano H., Sugiyama K., Suzuki M., Shibayama K.,
RA Hoshino Y.;
RT "Draft genome sequence of Mycobacterium sp. shizuoka-1.";
RL Submitted (OCT-2017) 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:GAY16804.1}.
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DR EMBL; BEWG01000061; GAY16804.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C9SZ18; -.
DR Proteomes; UP000223528; 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:UP000223528}.
FT DOMAIN 9..118
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 270..357
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 357 AA; 37829 MW; B48F76CAC3A6C460 CRC64;
MVDSGSEAIA PGRGVVVTVT DVIAEGADAR SFVFAIPDDH RDRFGYRPGQ FLTLRVPSEL
TGSVARCYSL ASSPHTDAAP KVTVKRTMGG YASNWLCDNL SSGASIEVLP PSGVFTPADL
DSDFLLWAAG SGITPVISIL KSVLAAGTGR VVLCYANRDE RSVIFAAELR ELAARYAGRL
TVLHWLESVQ GLPTRAQMRG FSQTVFAGSA ALQSFICGPA PFMAVVKAAL TEAGVPRERV
HLEVFESLTG HPFTDDVAAV QADPDGADGA SVLLDLDGHS HRLRWPRRAT LVDTMIAAGI
DVPYSCKEGR CGSCAATVVR GEVEMATCDI LEPEDRAAGL ILACQARPVS DDLHIAF
//
