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Database: UniProt
Entry: J9S3M8_9ACTN
LinkDB: J9S3M8_9ACTN
Original site: J9S3M8_9ACTN 
ID   J9S3M8_9ACTN            Unreviewed;       238 AA.
AC   J9S3M8;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   SubName: Full=Flavodoxin reductases (Ferredoxin-NADPH reductases) family 1 {ECO:0000313|EMBL:AFR49126.1};
GN   ORFNames=KTR9_2489 {ECO:0000313|EMBL:AFR49126.1};
OS   Gordonia sp. KTR9.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=337191 {ECO:0000313|EMBL:AFR49126.1, ECO:0000313|Proteomes:UP000003281};
RN   [1] {ECO:0000313|EMBL:AFR49126.1, ECO:0000313|Proteomes:UP000003281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KTR9 {ECO:0000313|EMBL:AFR49126.1,
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};
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DR   EMBL; CP002907; AFR49126.1; -; Genomic_DNA.
DR   RefSeq; WP_014926843.1; NC_018581.1.
DR   AlphaFoldDB; J9S3M8; -.
DR   STRING; 337191.KTR9_2489; -.
DR   KEGG; gor:KTR9_2489; -.
DR   PATRIC; fig|337191.3.peg.2805; -.
DR   eggNOG; COG1018; Bacteria.
DR   HOGENOM; CLU_003827_7_3_11; -.
DR   Proteomes; UP000003281; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd06217; FNR_iron_sulfur_binding_3; 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; 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:SF5; PROTEIN RFBI; 1.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00371; FPNCR.
DR   PRINTS; PR00410; PHEHYDRXLASE.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   4: Predicted;
FT   DOMAIN          2..103
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   238 AA;  26668 MW;  21DDBB35281B55F5 CRC64;
     MTTWHLTTVT SVVDITPTAR TLRLALPEAI HALPGQHVDI RLTAEDGYST ARAYSLSDVR
     ETRSVEVTVE RLHDGEVSPY LVDVVEPGDP LEISDPHGFW FTWPSGDDRP VQLIGGGSGI
     APLMSMIRSR EVEAPQTPFS LVYSVRSPDR VYYRDEFRQL IDHRRMDVHL IHTRVGPENA
     TRPPGRLTAD ELAGLTLDPA TSPTVFICGP NRFVENCAQW MVDAGHDRTR IRTERFGE
//
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