ID A0A0A2TCW4_9BACI Unreviewed; 442 AA.
AC A0A0A2TCW4;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=NADH dehydrogenase {ECO:0000313|EMBL:KGP71911.1};
GN ORFNames=N782_14840 {ECO:0000313|EMBL:KGP71911.1};
OS Pontibacillus yanchengensis Y32.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pontibacillus.
OX NCBI_TaxID=1385514 {ECO:0000313|EMBL:KGP71911.1, ECO:0000313|Proteomes:UP000030147};
RN [1] {ECO:0000313|EMBL:KGP71911.1, ECO:0000313|Proteomes:UP000030147}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y32 {ECO:0000313|EMBL:KGP71911.1,
RC ECO:0000313|Proteomes:UP000030147};
RX PubMed=26561516; DOI=10.1186/s40793-015-0085-y;
RA Huang J., Qiao Z.X., Tang J.W., Wang G.;
RT "High quality draft genome sequence of the moderately halophilic bacterium
RT Pontibacillus yanchengensis Y32(T) and comparison among Pontibacillus
RT genomes.";
RL Stand. Genomic Sci. 10:93-93(2015).
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:KGP71911.1}.
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DR EMBL; AVBF01000043; KGP71911.1; -; Genomic_DNA.
DR RefSeq; WP_036821511.1; NZ_AVBF01000043.1.
DR AlphaFoldDB; A0A0A2TCW4; -.
DR STRING; 1385514.N782_14840; -.
DR eggNOG; COG0446; Bacteria.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000030147; Unassembled WGS sequence.
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; 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; 2.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Reference proteome {ECO:0000313|Proteomes:UP000030147}.
FT DOMAIN 2..306
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 328..430
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 442 AA; 48812 MW; 15225D475D9FD5B8 CRC64;
MKFVIIGGDA AGMSAAMQIV RNSSGHEITT LEKGTIYSYG QCGLPYTFTN QVESTDDLIA
RTPERFKNKY GIDTRILHEV TRVDCEEKVV HGLNLTTNEP FQESYDRLLV ATGASPVLPP
WDGKDLDGIF TLKTIPDAQD IQSYLGKNIE NITIIGGGYI GLEMAESMAE IGKNVQIIER
GSQLAKIFDE EMAELIHDEA NHQNLTLTFG ESVEGFEGTT QVEKVITNKG EYHTDLVLVA
VGVAPNTTFM NDTGAYKTYN DALIVNHYME TNIKDIYAAG DCATQYHRIK EKDDYIPLGT
HANKQGQIAG VNMVDQPRTF KGVVGSSIIK FFSLTLGRTG LSEKEAKSLH FPYDTITIKS
THAAGYYSKD DKMTLKLVFN KETRVLLGGQ IIGGAGVDKR IDVLATALYH QMKIDDLQDL
DLSYAPPYNS VWDPIQQAAR KA
//
