ID E0I7W3_9BACL Unreviewed; 442 AA.
AC E0I7W3;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=FAD-dependent pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:EFM11268.1};
GN ORFNames=PaecuDRAFT_1714 {ECO:0000313|EMBL:EFM11268.1};
OS Paenibacillus curdlanolyticus YK9.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=717606 {ECO:0000313|EMBL:EFM11268.1, ECO:0000313|Proteomes:UP000005387};
RN [1] {ECO:0000313|EMBL:EFM11268.1, ECO:0000313|Proteomes:UP000005387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YK9 {ECO:0000313|EMBL:EFM11268.1,
RC ECO:0000313|Proteomes:UP000005387};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Land M.L., Hauser L., Chang Y.-J., Jeffries C., Anderson I.J.,
RA Johnson E., Loganathan U., Mulhopadhyay B., Kyrpides N., Woyke T.J.;
RT "The draft genome of Paenibacillus curdlanolyticus YK9.";
RL Submitted (JUL-2010) 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}.
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DR EMBL; AEDD01000004; EFM11268.1; -; Genomic_DNA.
DR RefSeq; WP_006037725.1; NZ_AEDD01000004.1.
DR AlphaFoldDB; E0I7W3; -.
DR STRING; 717606.PaecuDRAFT_1714; -.
DR eggNOG; COG0446; Bacteria.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000005387; 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:UP000005387}.
FT DOMAIN 1..305
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 328..428
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 442 AA; 48960 MW; 203CD7A0C430C70B CRC64;
MKIAVIGCTH AGTAAVTQMA QLYPEAQISV YERNDNVSFL SCGIALHVGG VVQDVQKLFY
ASPQQLTDLG VQMNMRHDVL EVNADAHMIR VRNLETGITR VETYDKLVVT TGSWPIIPKL
GGMELDNILL CKNYGHAQTI IDKARHAERV TVIGAGYIGI ELVEAFEELG KQVTLIDNMD
RILFKYLDRT FTDGIENELE ARHIRLQLGQ TVTGFEGENG KVNKVITTAG EYETDLVVLC
IGFRPNTELL KDQVEMLLNG AIIVDEYMRT SHPDVLAAGD SCAVMYNPTH KHAYIPLATN
AVRMGTLVAR NLLKPTVRYL GTQGTSGIKI YDLNIASTGM TEQAAIDAGM IVKNVTIEEN
YRPEFMPTYE KALLKVVYEA DTGRIVGAQV MSKADLTQAI NTMSVCIQNG MTMDELSFVD
FFFQPHYNKP WNLLNQAGLQ AM
//
