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};
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; 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
//