ID A0A0R1VSI9_9LACO Unreviewed; 400 AA.
AC A0A0R1VSI9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Putidaredoxin reductase {ECO:0000313|EMBL:KRM04540.1};
GN ORFNames=FC89_GL002226 {ECO:0000313|EMBL:KRM04540.1};
OS Liquorilactobacillus ghanensis DSM 18630.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Liquorilactobacillus.
OX NCBI_TaxID=1423750 {ECO:0000313|EMBL:KRM04540.1, ECO:0000313|Proteomes:UP000051451};
RN [1] {ECO:0000313|EMBL:KRM04540.1, ECO:0000313|Proteomes:UP000051451}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18630 {ECO:0000313|EMBL:KRM04540.1,
RC ECO:0000313|Proteomes:UP000051451};
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:KRM04540.1}.
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DR EMBL; AZGB01000027; KRM04540.1; -; Genomic_DNA.
DR RefSeq; WP_057872585.1; NZ_AZGB01000027.1.
DR AlphaFoldDB; A0A0R1VSI9; -.
DR STRING; 1423750.FC89_GL002226; -.
DR PATRIC; fig|1423750.3.peg.2266; -.
DR OrthoDB; 9792592at2; -.
DR Proteomes; UP000051451; 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 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:UP000051451};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 8..301
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 400 AA; 43693 MW; 25DB3B5A7947CEA2 CRC64;
MTAIQHFKYL LVGGGMAADQ AAAGIRAVDA QGSIGILSAD VDGPYARPAL SKKLWVDENF
HDEDIDFKTA EKQQAQLFLR TVVTQIDPAA HQVKTSTGQA FSYDKLLLAT GAKARTLAGT
ASQRVVALRS KADYLKIRAF SGQQQTVIVV GDGFIGSEIA AGLAQSNTQV IYVIAGSQLF
ERKLPTALCQ ELEQKYTAAG VKFYYQEKAA TYQLKGEQVE LTLEDGTRLL GDGLVLGLGA
EIDYQLAKQA GLHLDKNGVV VDQYLQTSAA DVWAAGDIIS YPDVILGQTK SEHVKHAIQS
GYIAGKNMAG QAAAYTYTPY FYSWVFDISW EALGTVDTSL QLYQEKLTSG QLVYYFDDQG
QLQGILSWNA AVDLDHLRNL FRQHPDLKTL QQVLPLKPIK
//
