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Database: UniProt
Entry: M0QL69_9ACTN
LinkDB: M0QL69_9ACTN
Original site: M0QL69_9ACTN 
ID   M0QL69_9ACTN            Unreviewed;       370 AA.
AC   M0QL69;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Putative NADPH oxidoreductase {ECO:0000313|EMBL:GAC69179.1};
GN   ORFNames=GS4_22_00110 {ECO:0000313|EMBL:GAC69179.1};
OS   Gordonia soli NBRC 108243.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=1223545 {ECO:0000313|EMBL:GAC69179.1, ECO:0000313|Proteomes:UP000011666};
RN   [1] {ECO:0000313|EMBL:GAC69179.1, ECO:0000313|Proteomes:UP000011666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 108243 {ECO:0000313|EMBL:GAC69179.1,
RC   ECO:0000313|Proteomes:UP000011666};
RA   Isaki-Nakamura S., Hosoyama A., Tsuchikane K., Ando Y., Baba S., Ohji S.,
RA   Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT   "Whole genome shotgun sequence of Gordonia soli NBRC 108243.";
RL   Submitted (JAN-2013) 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:GAC69179.1}.
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DR   EMBL; BANX01000022; GAC69179.1; -; Genomic_DNA.
DR   RefSeq; WP_007621974.1; NZ_BANX01000022.1.
DR   AlphaFoldDB; M0QL69; -.
DR   STRING; 1223545.GS4_22_00110; -.
DR   eggNOG; COG1018; Bacteria.
DR   OrthoDB; 9796486at2; -.
DR   Proteomes; UP000011666; 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; cd06216; FNR_iron_sulfur_binding_2; 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; 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; NADH OXIDOREDUCTASE HCR; 1.
DR   PANTHER; PTHR47354:SF6; 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; 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:UP000011666}.
FT   DOMAIN          50..154
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   DOMAIN          289..370
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
SQ   SEQUENCE   370 AA;  40758 MW;  F4B74D9319586819 CRC64;
     MNLLKWSKRP AAGVEAKNPE VNILRGLVAR ATTPLLPDDY LHLINPLWSA RELRGQIVDV
     VKETEDTATV TIRTGWGFPD SYKPGQYVGI GIQIGGRWHW RSYSLTSIGA TQDKVITITV
     KANPDGFLST HLVDGLEPGT IIRLQSPKGD FHLPEPVPGK ILFVTAGSGI TPVMAMLRQL
     SSHGQTPDVV HIHSAPTRDD VIFLDELEAL SGEENQYDLN LQLTQEMGKF DIARIDEWAP
     DWRERECWAC GPVALLDSME NHYEDGGLRD RLHIERFTIA RTDHGGEGGT VTFSISDKTA
     EIDGATTLLE AGEELGVQMP FGCRMGICQT CVVPLAGGYV RDLRTGEERR EGERIQTCIS
     SVSGECTIDL
//
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