ID A0A0D0LE49_9NOCA Unreviewed; 342 AA.
AC A0A0D0LE49;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KIQ15189.1};
GN ORFNames=RU01_16315 {ECO:0000313|EMBL:KIQ15189.1};
OS Rhodococcus sp. MEB064.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1587522 {ECO:0000313|EMBL:KIQ15189.1, ECO:0000313|Proteomes:UP000032087};
RN [1] {ECO:0000313|EMBL:KIQ15189.1, ECO:0000313|Proteomes:UP000032087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MEB064 {ECO:0000313|EMBL:KIQ15189.1,
RC ECO:0000313|Proteomes:UP000032087};
RA Perisin M.A., Vetter M., Gilbert J.A., Bergelson J.;
RT "16Stimator: statistical estimation of ribosomal gene copy numbers from
RT draft genome assemblies.";
RL Submitted (DEC-2014) 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:KIQ15189.1}.
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DR EMBL; JXQS01000036; KIQ15189.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0LE49; -.
DR Proteomes; UP000032087; 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 8..108
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 254..342
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 342 AA; 36891 MW; 7CCE17C73908A4C0 CRC64;
MDSVDVAVHT VRLQVDEVIR ETADAVTLVF STPLDYRPGQ FLTLEIPSPD GEPAARCYSL
SSSPATRERA AISVKRTAGG FASNWICDTA AAGMTLTSLH PAGTFVPTRW DRPLVLVAAG
SGITPIMSIL KTALTSHGER VVLLYANRSR DSVMFADTLD ELLRRFPTRL TVAHWYEAES
GLPTDAGLRD LLDTSVENAD AYLCGPEPFM EVARRSLVTS GVSQENIHRE VFASLTSNPF
RAVAPTPTGS GIGTPVEAEV EGETHSFHCP PDTVLLDAML SEGIDAPFVC REGNCGACAF
TLLSGEVHMH VNDTLDDYEL KKGVRLACQS VPVSDSLRLE IE
//
