ID A0A087CM93_9BIFI Unreviewed; 511 AA.
AC A0A087CM93;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:KFI84393.1};
GN ORFNames=BREU_1162 {ECO:0000313|EMBL:KFI84393.1};
OS Bifidobacterium reuteri DSM 23975.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1437610 {ECO:0000313|EMBL:KFI84393.1, ECO:0000313|Proteomes:UP000028984};
RN [1] {ECO:0000313|EMBL:KFI84393.1, ECO:0000313|Proteomes:UP000028984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23975 {ECO:0000313|EMBL:KFI84393.1,
RC ECO:0000313|Proteomes:UP000028984};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:KFI84393.1}.
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DR EMBL; JGZK01000017; KFI84393.1; -; Genomic_DNA.
DR RefSeq; WP_044089871.1; NZ_JGZK01000017.1.
DR AlphaFoldDB; A0A087CM93; -.
DR STRING; 1437610.BREU_1162; -.
DR eggNOG; COG4097; Bacteria.
DR OrthoDB; 9801223at2; -.
DR Proteomes; UP000028984; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd00322; FNR_like; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR47354:SF8; 1,2-PHENYLACETYL-COA EPOXIDASE, SUBUNIT E; 1.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
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;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000028984};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 72..91
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 111..133
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 154..173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 206..366
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 237..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 511 AA; 55202 MW; DA99F6DC7B73F2D0 CRC64;
MKHISSHIAL AWAVVLFIIP LPFLATLVAG FPALYSSSMF GAELGVIAYV WMLAAVYLAC
RPRWVDRTVG LPHMYMIHGV LAILAIVLAF VHQSLLPGAG ELIGLTGHLG LYLFMAVAVW
SLVFMAGWLT ARVPVLARIK RALEQVFRHE MSVWLHRLNL VAIALIVIHV HVIDYIASIK
PFIFLLDATT IIVFAYYIWS SVNREAFALR GRVVSVRPLA DRVTELTVAI EDANGSRGVS
RPRNAADAGS NARGTGLGGG TIRWNPGDFA FIAFPGKRGM GEFHPFSLTN SYPAPGAVSF
AVGAAASNTA VSTTSADGTT ITMPHPDAPT MAFAIRADGD FTAGIAALRP GDAVRIVPPY
GRYAEFIDEH DRRATTKADQ AAVQQGRTAG GTGTQQRTPL ALIGGGIGIT PLLGVLTAYA
DGERQVDFLY TVRSERDFIY RDQLEQFGRT TPATRVRLQA GRADEATIAP MIRPGAVYLI
AGPQPMMEAV RAILFKHGVA ADDIYYEPFA M
//
