ID A0A0R1M9R8_9LACO Unreviewed; 404 AA.
AC A0A0R1M9R8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Putidaredoxin reductase {ECO:0000313|EMBL:KRL05085.1};
GN ORFNames=FD46_GL001029 {ECO:0000313|EMBL:KRL05085.1};
OS Liquorilactobacillus oeni DSM 19972.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Liquorilactobacillus.
OX NCBI_TaxID=1423777 {ECO:0000313|EMBL:KRL05085.1, ECO:0000313|Proteomes:UP000051686};
RN [1] {ECO:0000313|EMBL:KRL05085.1, ECO:0000313|Proteomes:UP000051686}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19972 {ECO:0000313|EMBL:KRL05085.1,
RC ECO:0000313|Proteomes:UP000051686};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRL05085.1}.
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DR EMBL; AZEH01000034; KRL05085.1; -; Genomic_DNA.
DR RefSeq; WP_057895931.1; NZ_AZEH01000034.1.
DR AlphaFoldDB; A0A0R1M9R8; -.
DR STRING; 1423777.FD46_GL001029; -.
DR PATRIC; fig|1423777.3.peg.1064; -.
DR OrthoDB; 9792592at2; -.
DR Proteomes; UP000051686; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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 PANTHER; PTHR43557; APOPTOSIS-INDUCING FACTOR 1; 1.
DR PANTHER; PTHR43557:SF4; APOPTOSIS-INDUCING FACTOR 1, MITOCHONDRIAL; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000051686};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 9..302
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 404 AA; 44450 MW; 14FE80919D5F8514 CRC64;
MTQENNHFNY LLIGGGMAAD KAATGIRKTD SKGTIAIISA DNDAPYARPA LSKKLWVDEE
FKEKDTDLKT AEKNNVKIFL SKKVTALDPT AHSVVTTNGE HFRYDKLLLA TGSQAQRIPG
PESDLVVALR SKADYRKIKA LSGKQKHIIV VGSGYVGSEI AAGLIQNETK VSLIISGQKI
YDERFPDYLS SQYQQKYLDE GINILVNKHA QKYEVDGQTV KLYFSDGQIL EGDGLVLGIG
ANTDHSLGEN AGLSSDKFGI IVDEHLHTSA PDIWAAGDII SYPDKILGRQ SSAHVNHAVK
SGLIAGRAMA GEEVVYDYTP SFYSWVFDIS WDAIGHLSSK MQMYSEKLPG AAEKSIVYYF
DDSGIIQGIL SWNSKVNLNH LRNILKMKPT LSQLQQVLPL EKVE
//
