ID K6WXE1_9MICO Unreviewed; 487 AA.
AC K6WXE1;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE SubName: Full=Putative oxidoreductase {ECO:0000313|EMBL:GAB96752.1};
GN ORFNames=KILIM_047_00140 {ECO:0000313|EMBL:GAB96752.1};
OS Kineosphaera limosa NBRC 100340.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermatophilaceae;
OC Kineosphaera.
OX NCBI_TaxID=1184609 {ECO:0000313|EMBL:GAB96752.1, ECO:0000313|Proteomes:UP000008366};
RN [1] {ECO:0000313|EMBL:GAB96752.1, ECO:0000313|Proteomes:UP000008366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100340 {ECO:0000313|EMBL:GAB96752.1,
RC ECO:0000313|Proteomes:UP000008366};
RA Yoshida I., Isaki S., Hosoyama A., Tsuchikane K., Katsumata H., Ando Y.,
RA Ohji S., Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Kineosphaera limosa NBRC 100340.";
RL Submitted (AUG-2012) 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}.
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:GAB96752.1}.
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DR EMBL; BAHD01000047; GAB96752.1; -; Genomic_DNA.
DR AlphaFoldDB; K6WXE1; -.
DR STRING; 1184609.KILIM_047_00140; -.
DR eggNOG; COG1249; Bacteria.
DR Proteomes; UP000008366; 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; IPR001100; Pyr_nuc-diS_OxRdtase.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR PANTHER; PTHR43014; MERCURIC REDUCTASE; 1.
DR PANTHER; PTHR43014:SF1; NAD(P)H DEHYDROGENASE (QUINONE); 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:UP000008366}.
FT DOMAIN 18..350
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 371..478
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT BINDING 63
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 140
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 207..214
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 294
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 335
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
SQ SEQUENCE 487 AA; 50327 MW; 63C03F40F2448C20 CRC64;
MALNVGIAWK DERVSSDSVV IVGGGPGGYE AALVAAALGA NVDIVESDGM GGAAVLTDCV
PSKALVATGG YLGRVGDGAA RMGVRHHVEG AQTDDPVQDL VPRVDLGAVN DRIMAVAQAQ
SHDIRQGLER AGVTVHSGRG RLLDERTVGI VGARGEVGER LSADMILLAT GASPRVLPTA
QPDGARILTW QQVWALREVP RRLIVVGSGV TGAEFAQAYL HLGSEVVLVS SRDRVLPGED
PDAAEVIEDV FRRRGMEVLN RSRAESVERH GEEVEVRLVD GRTVTGSHAL LAVGSVPQTQ
GLGLAEVGVA TADSGHISVD RVSRTSVRGI YAAGDCTGVL PLASVAATQG RIAVAHALGD
TVHPLSIQGI SANIFTDPEI ATVGITAADA DADADNVRSV MMPLATNARA KMDNIGEGFV
KLFARSGSNA VIGGVVVAPR ASELIFPIAL AVQQQLTVDQ MAGTITVYPS LSGSLAEAAR
RLHAVDG
//
