ID J9STZ3_9ACTN Unreviewed; 352 AA.
AC J9STZ3;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=3-Ketosteroid-9-alpha-hydroxylase, reductase component {ECO:0000313|EMBL:AFR51383.1};
GN Name=kshB {ECO:0000313|EMBL:AFR51383.1};
GN ORFNames=KTR9_3740 {ECO:0000313|EMBL:AFR51383.1};
OS Gordonia sp. KTR9.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=337191 {ECO:0000313|EMBL:AFR51383.1, ECO:0000313|Proteomes:UP000003281};
RN [1] {ECO:0000313|EMBL:AFR51383.1, ECO:0000313|Proteomes:UP000003281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KTR9 {ECO:0000313|EMBL:AFR51383.1,
RC ECO:0000313|Proteomes:UP000003281};
RX PubMed=22923396; DOI=10.1128/AEM.02120-12;
RA Chen H.P., Zhu S.H., Casabon I., Hallam S.J., Crocker F.H., Mohn W.W.,
RA Indest K.J., Eltis L.D.;
RT "Genomic and transcriptomic studies of an RDX (hexahydro-1,3,5-
RT trinitro-1,3,5-triazine)-degrading actinobacterium.";
RL Appl. Environ. Microbiol. 78:7798-7800(2012).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002907; AFR51383.1; -; Genomic_DNA.
DR RefSeq; WP_014928750.1; NC_018581.1.
DR AlphaFoldDB; J9STZ3; -.
DR STRING; 337191.KTR9_3740; -.
DR KEGG; gor:KTR9_3740; -.
DR PATRIC; fig|337191.3.peg.4115; -.
DR eggNOG; COG1018; Bacteria.
DR HOGENOM; CLU_003827_14_1_11; -.
DR Proteomes; UP000003281; Chromosome.
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 9..116
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 265..352
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 352 AA; 37463 MW; B55910EA60621674 CRC64;
MSDLTPHGSR SVILTVSEVI DETAEAKSIA FEVPEASAKA FTDYKPGQFL TLRIPSEQTG
SVARCYSLAS SPFTDPQPKV TVKRTADGYG SNWVCDHLSP GTQVEVLPPS GVFTPRSYDD
PLLLIAAGSG VTPVMSILKA ALAKGDAPIV FFYANRDVAD VIFAAELREL LTAHPGRLTV
IHWLESLQGL PSAAALSTAF APYAASHVAY MCGPGPFMDA VHKGLADADF PHHNVHTEVY
NSLSGDPFAD VELDEVTDEE QAAAATVEVE LDGETHTLTW PRSRTLIDIM LAAGLDAPYS
CQEGECGSCA CTLTEGSVDM DNAGALDPED IEDGYILGCQ AHPTSDTLKI EF
//
