ID D3P8V0_DEFDS Unreviewed; 440 AA.
AC D3P8V0;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 24-JAN-2024, entry version 68.
DE SubName: Full=FAD-dependent pyridine nucleotide-disulphide oxidoreductase {ECO:0000313|EMBL:BAI81140.1};
GN OrderedLocusNames=DEFDS_1684 {ECO:0000313|EMBL:BAI81140.1};
OS Deferribacter desulfuricans (strain DSM 14783 / JCM 11476 / NBRC 101012 /
OS SSM1).
OC Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC Deferribacteraceae; Deferribacter.
OX NCBI_TaxID=639282 {ECO:0000313|EMBL:BAI81140.1, ECO:0000313|Proteomes:UP000001520};
RN [1] {ECO:0000313|EMBL:BAI81140.1, ECO:0000313|Proteomes:UP000001520}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14783 / JCM 11476 / NBRC 101012 / SSM1
RC {ECO:0000313|Proteomes:UP000001520};
RX PubMed=20189949; DOI=10.1093/dnares/dsq005;
RA Takaki Y., Shimamura S., Nakagawa S., Fukuhara Y., Horikawa H., Ankai A.,
RA Harada T., Hosoyama A., Oguchi A., Fukui S., Fujita N., Takami H.,
RA Takai K.;
RT "Bacterial lifestyle in a deep-sea hydrothermal vent chimney revealed by
RT the genome sequence of the thermophilic bacterium Deferribacter
RT desulfuricans SSM1.";
RL DNA Res. 17:123-137(2010).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00006442}.
CC -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00009130}.
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DR EMBL; AP011529; BAI81140.1; -; Genomic_DNA.
DR RefSeq; WP_013008386.1; NC_013939.1.
DR AlphaFoldDB; D3P8V0; -.
DR STRING; 639282.DEFDS_1684; -.
DR KEGG; ddf:DEFDS_1684; -.
DR eggNOG; COG0446; Bacteria.
DR HOGENOM; CLU_003291_1_0_0; -.
DR OMA; DKNHTNY; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000001520; 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; PTHR43429:SF3; NITRITE REDUCTASE [NAD(P)H]; 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; PR00469; PNDRDTASEII.
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 Reference proteome {ECO:0000313|Proteomes:UP000001520}.
FT DOMAIN 2..284
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 323..421
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 440 AA; 47828 MW; A89F45220D8F748C CRC64;
MKKVVIIGGG PTGRVVVHSL HAAEGEFDIT LIKDEEINVN RCAVPYGIID KKPVEKFCIP
NSLVTDFGAK LVIDTATEIN TENNFVLTEK GDRYDYDYLL LATGSKPFIP PIEGVNLGNI
TTVRSKQDME RLREFAKKYK KCVIVGGGYI GVEVAVVLKR LGLDVTIVEM LDHILLATMD
DDFAIEVENH VKDEGINVVT GDKVIAFEGD ESVKKVVLES GEKIDTDFVV ISVGVVPNVE
LAEKSGIEVS KFGVKTDEYL RTNIENIFAA GDCAEKKSFI TKKPTRGEFG TNAVFMGKVV
GANIAGKNVK FPGVINANVS TAFEYSFGSA GLIEKAAKNE GIDVVVGESE VMDMYPMMDG
VSKIKTKLVF ERSTGKLIGG SVLRKGHCVA ANVDFISFAI QKSATIEEIL VHQYSTHPEL
AAKPSDNIYV FAAKDALKKM
//