ID S5V2B6_STRC3 Unreviewed; 421 AA.
AC S5V2B6;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Ferredoxin reductase {ECO:0000313|EMBL:AGS69364.1};
GN ORFNames=B446_12720 {ECO:0000313|EMBL:AGS69364.1};
OS Streptomyces collinus (strain DSM 40733 / Tue 365).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1214242 {ECO:0000313|EMBL:AGS69364.1, ECO:0000313|Proteomes:UP000015423};
RN [1] {ECO:0000313|Proteomes:UP000015423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40733 / Tue 365 {ECO:0000313|Proteomes:UP000015423};
RA Ruckert C., Szczepanowski R., Goesmann A., Pross E.K., Musiol E.M.,
RA Blin K., Wohlleben W., Puhler A., Weber T., Kalinowski J.;
RT "The complete genome sequence of Streptomyces collinus Tu 365.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AGS69364.1, ECO:0000313|Proteomes:UP000015423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40733 / Tue 365 {ECO:0000313|Proteomes:UP000015423};
RX PubMed=24140291; DOI=10.1016/j.jbiotec.2013.10.004;
RA Ruckert C., Szczepanowski R., Albersmeier A., Goesmann A., Iftime D.,
RA Musiol E.M., Blin K., Wohlleben W., Puhler A., Kalinowski J., Weber T.;
RT "Complete genome sequence of the kirromycin producer Streptomyces collinus
RT Tu 365 consisting of a linear chromosome and two linear plasmids.";
RL J. Biotechnol. 168:739-740(2013).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP006259; AGS69364.1; -; Genomic_DNA.
DR RefSeq; WP_020939838.1; NC_021985.1.
DR AlphaFoldDB; S5V2B6; -.
DR STRING; 1214242.B446_12720; -.
DR KEGG; sci:B446_12720; -.
DR PATRIC; fig|1214242.5.peg.2611; -.
DR eggNOG; COG0446; Bacteria.
DR HOGENOM; CLU_003291_4_0_11; -.
DR Proteomes; UP000015423; 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; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000015423}.
FT DOMAIN 8..314
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 334..419
FT /note="Reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14759"
SQ SEQUENCE 421 AA; 45341 MW; DEAE5629ABFB9319 CRC64;
MVDADQTFVI VGGGLAGAKA AETLRAEGFT GRVILICDER DHPYERPPLS KGYLLGKEER
DSVFVHEPAW YARNDVELHL GQTVDRIDRT ARTVRLGDAG TLVHYDKLLL ATGAEPRRLD
IPGTDLAGVH HLRRLAHAER LKGVLTSLGR DNGHLVIAGA GWIGLEVAAA AREYGAEVTV
IEPAQTPLHG VLGPELGNVF AEVHRAHGVR FHFGARLTEI VGQDGVVLAA RTDDGEEHPA
HAVLAAIGAA PRTALAEAAG LELADRAHGG GVLVDERLRT SDPDIHAAGD VAAFPHPLSD
TRIRVEHWAN ALNGGPVAAR AMLGQDVTYD RVPYFFTDQY DLGMEYSGWA PPGSYDQVVI
RGDAGKREFI AFWVREGRVL AGMNVNVWDV TDPIQRLIRS RAAVDTEALA DPHVPLDGLA
S
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