ID A0A150L037_9BACI Unreviewed; 442 AA.
AC A0A150L037;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:KYD05449.1};
DE EC=1.6.99.3 {ECO:0000313|EMBL:KYD05449.1};
GN ORFNames=B4102_3173 {ECO:0000313|EMBL:KYD05449.1};
OS Heyndrickxia sporothermodurans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Heyndrickxia.
OX NCBI_TaxID=46224 {ECO:0000313|EMBL:KYD05449.1, ECO:0000313|Proteomes:UP000075666};
RN [1] {ECO:0000313|EMBL:KYD05449.1, ECO:0000313|Proteomes:UP000075666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4102 {ECO:0000313|EMBL:KYD05449.1,
RC ECO:0000313|Proteomes:UP000075666};
RA Berendsen E.M., Wells-Bennik M.H., Krawcyk A.O., De Jong A., Holsappel S.,
RA Eijlander R.T., Kuipers O.P.;
RT "Genome Sequences of Twelve Sporeforming Bacillus Species Isolated from
RT Foods.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:KYD05449.1}.
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DR EMBL; LQYN01000056; KYD05449.1; -; Genomic_DNA.
DR RefSeq; WP_066231723.1; NZ_LQYN01000056.1.
DR AlphaFoldDB; A0A150L037; -.
DR STRING; 46224.B4102_3173; -.
DR PATRIC; fig|46224.3.peg.3147; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000075666; 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; 3.50.50.60; 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; 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};
KW Oxidoreductase {ECO:0000313|EMBL:KYD05449.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000075666}.
FT DOMAIN 1..306
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 328..429
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 442 AA; 48627 MW; 9E0353461E099B0E CRC64;
MKYVIIGGDA AGMSAAMQIV RNAEDAEIVT LEKGGIYSYG QCGLPYVISG TVSSTDEVIA
RSVETFRQKY GIDAHLYCEV KSIDSGEKKV YGVHTKTGEA FCQSYDKLLI ATGASPNLPE
WEGVELEHVH VLKTIPDTHR ILDSLKEEIN DVTIVGGGYI GLEMAENFHK LGKHVRIIQR
GKQLASIFDE DMAVHIHKEA QDKGIEVILE EDVKRIVGET TVEAIVTDKR RYETDLVLIS
IGVHPNTTFL KGTDIRLSTN GAIEVNRYME TNVKDIYAAG DCAVQYHRIK EQDDYIPLGT
TANKQGRIAG LNMAGNGVAF GGIVGSSIIK FMDLTLGKTG LSEKEASALQ FPFQTISLEV
KDHADYYPGA SPLSIKLMYR KDNDLLLGGQ IIGKDGVDKR IDVLATALFN KMSITELTDL
DLSYAPPYNS PWDPIQQVAR RH
//
