ID C9YXB7_STRSW Unreviewed; 387 AA.
AC C9YXB7;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Ferredoxin reductase {ECO:0000313|EMBL:CBG67897.1};
GN OrderedLocusNames=SCAB_7061 {ECO:0000313|EMBL:CBG67897.1};
OS Streptomyces scabiei (strain 87.22).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG67897.1, ECO:0000313|Proteomes:UP000001444};
RN [1] {ECO:0000313|EMBL:CBG67897.1, ECO:0000313|Proteomes:UP000001444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=87.22 {ECO:0000313|EMBL:CBG67897.1,
RC ECO:0000313|Proteomes:UP000001444};
RX PubMed=20064060; DOI=10.1094/MPMI-23-2-0161;
RA Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., Parry R.J.,
RA Loria R.;
RT "Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic
RT cluster that contributes to plant-microbe interactions.";
RL Mol. Plant Microbe Interact. 23:161-175(2010).
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; FN554889; CBG67897.1; -; Genomic_DNA.
DR RefSeq; WP_012998633.1; NC_013929.1.
DR AlphaFoldDB; C9YXB7; -.
DR STRING; 680198.SCAB_7061; -.
DR GeneID; 24306768; -.
DR KEGG; scb:SCAB_7061; -.
DR eggNOG; COG0446; Bacteria.
DR HOGENOM; CLU_003291_4_0_11; -.
DR Proteomes; UP000001444; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR028202; Reductase_C.
DR PANTHER; PTHR43557; APOPTOSIS-INDUCING FACTOR 1; 1.
DR PANTHER; PTHR43557:SF2; RIESKE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF14759; Reductase_C; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001444}.
FT DOMAIN 3..294
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 319..386
FT /note="Reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14759"
SQ SEQUENCE 387 AA; 40053 MW; 7A2C25D3BB524B17 CRC64;
MRTVAVVGAS LAGLSAARSL RKQGFDGRLV VIGDELHRPY DRPPLSKEFL SGTLGEAELA
LEAEGEDLAA EWLLGTRATG LDHTARTVRL ADGREVRADG FVIATGAVAR TLPGSAGLAG
VHTLRTLDDA RALRDELASG GRLVVIGGGF IGAEVASTAR ALGLEVTVVE AAPTPLAGPL
GATMGAVVSG LHADHGVRLL CGVGVKGLSG EHRVDAVLLE DGRSLPADIV VVGVGAHPCV
EWLEGSGIAL DNGVKCGADG RTSLAGVVAV GDCANWYDPR AGHHRRVEHW TGARERPEAA
VATLLAGGAV EPGVPRPPYF WSDQYGVRIQ FAGHAAEADS ITVEAGTADG RDVLAVYRRD
GRPVAVLGMN QPRLFMRARK QLAAATS
//
