ID B2A6P4_NATTJ Unreviewed; 503 AA.
AC B2A6P4;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Pyridine nucleotide-disulphide oxidoreductase dimerisation region {ECO:0000313|EMBL:ACB84177.1};
GN OrderedLocusNames=Nther_0582 {ECO:0000313|EMBL:ACB84177.1};
OS Natranaerobius thermophilus (strain ATCC BAA-1301 / DSM 18059 /
OS JW/NM-WN-LF).
OC Bacteria; Bacillota; Clostridia; Natranaerobiales; Natranaerobiaceae;
OC Natranaerobius.
OX NCBI_TaxID=457570 {ECO:0000313|EMBL:ACB84177.1, ECO:0000313|Proteomes:UP000001683};
RN [1] {ECO:0000313|EMBL:ACB84177.1, ECO:0000313|Proteomes:UP000001683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF
RC {ECO:0000313|Proteomes:UP000001683};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Mesbah N.M., Wiegel J.;
RT "Complete sequence of chromosome of Natranaerobius thermophilus JW/NM-WN-
RT LF.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACB84177.1, ECO:0000313|Proteomes:UP000001683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF
RC {ECO:0000313|Proteomes:UP000001683};
RX PubMed=21642468; DOI=10.1128/JB.05157-11;
RA Zhao B., Mesbah N.M., Dalin E., Goodwin L., Nolan M., Pitluck S.,
RA Chertkov O., Brettin T.S., Han J., Larimer F.W., Land M.L., Hauser L.,
RA Kyrpides N., Wiegel J.;
RT "Complete genome sequence of the anaerobic, halophilic alkalithermophile
RT Natranaerobius thermophilus JW/NM-WN-LF.";
RL J. Bacteriol. 193:4023-4024(2011).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532}.
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DR EMBL; CP001034; ACB84177.1; -; Genomic_DNA.
DR RefSeq; WP_012447063.1; NC_010718.1.
DR AlphaFoldDB; B2A6P4; -.
DR STRING; 457570.Nther_0582; -.
DR KEGG; nth:Nther_0582; -.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_0_3_9; -.
DR InParanoid; B2A6P4; -.
DR OrthoDB; 1705205at2; -.
DR Proteomes; UP000001683; Chromosome.
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; PTHR22912:SF217; DIHYDROLIPOYL DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR22912; DISULFIDE OXIDOREDUCTASE; 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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000001683}.
FT DOMAIN 20..362
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 383..490
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 503 AA; 54987 MW; 8ACC57E3011203A9 CRC64;
MLFFQGGKNI KKQNKFSNQY DLVVIGGGPG GTACALKAAR LGLTTALIEK DFPGGGSVAR
GYFPVKALIE AAKLKENKLA PNEECLAKAN ERVNKARAQW DSSLTKRFEQ LYLIPGEGEL
LSSTSEFYQI KIHSSKYQGE IQDPNIIDGD RYISAKSIVM ATGTAPGSPI PELTIDGKNV
ITHEHLLDMH YNNINSIAII GADVEGCEFA GLFNRLGIQV HLLEMEDNIL PNCDQEISNS
LSTEYKKQGI KIKTNTQVTG VQNLEGEALK LTYNSNTPQA HGDYYSSKTE NESDKSLEVD
KILVTGKRIP QLPKGYANLP LKITQEGLVE VNSQLESSAP EVYVIGDLAG GVPSANAAIH
EGKLVSQNLT EPRKNKHINY SFTPYVFFTD PQTSGIGVTE DYLRNKKIPY KKGIAYFKEN
LRTLSLGHDN GFVKVLLGKN ESLLGVHMIG HDISELISVI TVAMQSKIPA SKIVDLPLPH
PSMGELMIEA IEEAINTRIT TTG
//
