ID Q73BP6_BACC1 Unreviewed; 444 AA.
AC Q73BP6;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 114.
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase, class I {ECO:0000313|EMBL:AAS40301.1};
GN OrderedLocusNames=BCE_1372 {ECO:0000313|EMBL:AAS40301.1};
OS Bacillus cereus (strain ATCC 10987 / NRS 248).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=222523 {ECO:0000313|EMBL:AAS40301.1, ECO:0000313|Proteomes:UP000002527};
RN [1] {ECO:0000313|EMBL:AAS40301.1, ECO:0000313|Proteomes:UP000002527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10987 / NRS 248 {ECO:0000313|Proteomes:UP000002527};
RX PubMed=14960714; DOI=10.1093/nar/gkh258;
RA Rasko D.A., Ravel J., Okstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.,
RA Nelson W.C., Kolsto A.-B., Fraser C.M., Read T.D.;
RT "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL Nucleic Acids Res. 32:977-988(2004).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00009130}.
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DR EMBL; AE017194; AAS40301.1; -; Genomic_DNA.
DR AlphaFoldDB; Q73BP6; -.
DR KEGG; bca:BCE_1372; -.
DR HOGENOM; CLU_003291_1_2_9; -.
DR Proteomes; UP000002527; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
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; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR PANTHER; PTHR43429:SF1; COENZYME A DISULFIDE REDUCTASE; 1.
DR PANTHER; PTHR43429; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 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 3: Inferred from homology;
KW NADP {ECO:0000256|ARBA:ARBA00022857}.
FT DOMAIN 2..294
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 330..430
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 444 AA; 49405 MW; 2C348D25E45FCD46 CRC64;
MNYVIIGGDA AGMSAAMQIV RNDENANVVT LEKGEIYSYA QCGLPYVISG AIASTEKLIA
RNVKTFRDKY GIDAKVRHEV TKVDTEKKIV YAEHTKTKDV FEFSYDRLLI ATGVRPVMPE
WEGRDLQGVH LLKTIPDAEC ILKTLETNKV EDVTIIGGGA IGLEMAETFV ELGKKVRMIE
RNDHIGTIYD GDMAEYIHKE ADKHHIEILT NENVKAFKGN ERVEAVETDK GTYKADLVLV
SVGVKPNTDF LEGTNIRTNH KGAIEVNAYM QTNVQDVYAA GDCATHYHVI KEIHDHIPIG
TTANKQGRLA GLNMLDKRRA FKGTLGTGII KFMDLTLART GLNEKEAKGL HIPYKTVKVD
STNMAGYYPN AKPLYLKLLY RSDTKQLLGG QVIGEEGVDK RIDVIAMALF NKMSIHDLED
VDLSYAPPYN SVWDPIQQAA RRAE
//
