ID E8WX47_GRATM Unreviewed; 480 AA.
AC E8WX47;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=FAD-dependent pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:ADW69689.1};
GN OrderedLocusNames=AciX9_2665 {ECO:0000313|EMBL:ADW69689.1};
OS Granulicella tundricola (strain ATCC BAA-1859 / DSM 23138 / MP5ACTX9).
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Granulicella.
OX NCBI_TaxID=1198114 {ECO:0000313|Proteomes:UP000000343};
RN [1] {ECO:0000313|Proteomes:UP000000343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP5ACTX9 {ECO:0000313|Proteomes:UP000000343};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Ovchinnikova G., Pagani I., Rawat S.R., Mannisto M.,
RA Haggblom M.M., Woyke T.;
RT "Complete sequence of chromosome of Acidobacterium sp. MP5ACTX9.";
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000350-3};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000350-3};
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532}.
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DR EMBL; CP002480; ADW69689.1; -; Genomic_DNA.
DR AlphaFoldDB; E8WX47; -.
DR STRING; 1198114.AciX9_2665; -.
DR PaxDb; 1198114-AciX9_2665; -.
DR KEGG; acm:AciX9_2665; -.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_1_2_0; -.
DR Proteomes; UP000000343; 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; IPR001100; Pyr_nuc-diS_OxRdtase.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR PANTHER; PTHR43014; MERCURIC REDUCTASE; 1.
DR PANTHER; PTHR43014:SF4; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE RCLA-RELATED; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PIRSF; PIRSF000350; Mercury_reductase_MerA; 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 FAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000350-3};
KW NAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000000343}.
FT DOMAIN 24..339
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 365..471
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 463
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT BINDING 70
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 133
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 162..164
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 199..206
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 222
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 286
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 327
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 61..66
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 480 AA; 51154 MW; C7FE2A4E7347814E CRC64;
MTGGSAGRTL TCMSAPLADP VEHYDLLVLG SGEAGKYIAW AMATSGKKAA VIERRYIGGS
CPNIACLPSK NFVHSAKVAH YASQAAQFRL PVATGPIDME VVRGRKRKMV DGLVQMHEGR
FAQTGAELIL GTGTFTAPRT LHVLTNTGMT RMLTAETVVI STGSRAAIDP IPGLLEAQPL
THIEMLETGQ VPPHLTILGG GYIGLEFAQA MRRLGSEVTV VERNPRLLHR EDEDVITTLT
GVLSREGIEI LTSTSVERVT GRSGSSVTVH TSAGEITGTH ILVATGRTPN TDGIGLDLAG
VTLGKDGHIQ VDEHLRTSAE NVFAVGDCAG SPHFTHIAFD DHRVVKSVLL GKSGSTPRST
KDRQVPFCLF TDPEFAHIGL SESEAKRQGI SYRLAKLPML AVLRTRTMDE SEGFLKALIS
TQDDSILGFT AVGVGSGEML AAVQLAMSAN LPYTALRDLI VTHPTLNEGL VYLFSSTPPR
//
