ID W7YHB9_9BACL Unreviewed; 453 AA.
AC W7YHB9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=NADH dehydrogenase {ECO:0000313|EMBL:GAF07857.1};
GN ORFNames=JCM16418_1889 {ECO:0000313|EMBL:GAF07857.1};
OS Paenibacillus pini JCM 16418.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1236976 {ECO:0000313|EMBL:GAF07857.1, ECO:0000313|Proteomes:UP000019364};
RN [1] {ECO:0000313|EMBL:GAF07857.1, ECO:0000313|Proteomes:UP000019364}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 16418 {ECO:0000313|EMBL:GAF07857.1,
RC ECO:0000313|Proteomes:UP000019364};
RA Yuki M., Oshima K., Suda W., Oshida Y., Kitamura K., Iida Y., Hattori M.,
RA Ohkuma M.;
RT "Draft Genome Sequence of Paenibacillus pini JCM 16418T, Isolated from the
RT Rhizosphere of Pine Tree.";
RL Genome Announc. 2:e00210-14(2014).
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:GAF07857.1}.
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DR EMBL; BAVZ01000004; GAF07857.1; -; Genomic_DNA.
DR RefSeq; WP_036647645.1; NZ_BAZT01000004.1.
DR AlphaFoldDB; W7YHB9; -.
DR STRING; 1236976.JCM16418_1889; -.
DR eggNOG; COG0446; Bacteria.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000019364; 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; 3.30.390.30; -; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000019364}.
FT DOMAIN 1..305
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 330..428
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 453 AA; 49606 MW; 46F3A22C34A79B52 CRC64;
MKIAVIGCTH AGTAAVVNAA KLYPEAEITV YERNDNISFL SCGIALYVGG VVKDPDGLFY
SSPQQLADLG VTTHMRHEVM SVDTHAKTLQ IRNLASGEVF HDSFDKLIVT TGSWPIIPKL
DGMDLGNILL CKNYDHSNTI IEKAQHAHHI TVVGAGYIGV ELVEAFQQSG KQVTLIDSED
RILNRYLDAE FSSQIEEFFR SKGIELALGQ TVQSFDGQDG MVSKVITSKG EIQTDLVILC
IGFRPNTELL RGQVDMLPNG AIIVDSYMQT SQKDVFAAGD SCAVRYNPTG KAAYIPLATN
AVRMGMLVAR NLMGNTTKYL GTQGTSGLKI YELNLASTGL TEGASADENL NVDTVTIQEA
YRPEFMPTAE TVTLKVVFDK ESRRLLGAQI MSKVDLTQAM NTLSVCIQNN MTVDELAFVD
FFFQPHYNKP WNFLNSAAIA ALPEIKTQQL QHS
//
