ID A0A437A5T5_9PEZI Unreviewed; 607 AA.
AC A0A437A5T5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=NADH:ubiquinone reductase (non-electrogenic) {ECO:0000256|ARBA:ARBA00012637};
DE EC=1.6.5.9 {ECO:0000256|ARBA:ARBA00012637};
GN ORFNames=DFL_004831 {ECO:0000313|EMBL:RVD86562.1};
OS Arthrobotrys flagrans.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Arthrobotrys.
OX NCBI_TaxID=97331 {ECO:0000313|EMBL:RVD86562.1, ECO:0000313|Proteomes:UP000283090};
RN [1] {ECO:0000313|EMBL:RVD86562.1, ECO:0000313|Proteomes:UP000283090}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS H-5679 {ECO:0000313|EMBL:RVD86562.1,
RC ECO:0000313|Proteomes:UP000283090};
RA Youssar L., Wernet V., Hensel N., Hildebrandt H.-G., Fischer R.;
RT "Intercellular communication is required for trap formation in the
RT nematode-trapping fungus Duddingtonia flagrans.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + H(+) + NADH = a quinol + NAD(+);
CC Xref=Rhea:RHEA:46160, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; EC=1.6.5.9;
CC Evidence={ECO:0000256|ARBA:ARBA00000864};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ubiquinone + H(+) + NADH = a ubiquinol + NAD(+);
CC Xref=Rhea:RHEA:23152, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000256|ARBA:ARBA00000891};
CC -!- SIMILARITY: Belongs to the NADH dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00005272}.
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:RVD86562.1}.
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DR EMBL; SAEB01000006; RVD86562.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A437A5T5; -.
DR STRING; 97331.A0A437A5T5; -.
DR VEuPathDB; FungiDB:DFL_004831; -.
DR Proteomes; UP000283090; Unassembled WGS sequence.
DR GO; GO:0003954; F:NADH dehydrogenase activity; IEA:InterPro.
DR GO; GO:0006116; P:NADH oxidation; IEA:InterPro.
DR Gene3D; 3.50.50.100; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR045024; NDH-2.
DR PANTHER; PTHR43706:SF3; EXTERNAL NADH-UBIQUINONE OXIDOREDUCTASE 1, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR43706; NADH DEHYDROGENASE; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000283090}.
FT DOMAIN 140..474
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT REGION 43..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 607 AA; 67660 MW; B80E35EF3EEBAE4F CRC64;
MVLRTPPAAI AAASSRRSIL QSTIRTNPSG CLLLRPHRTS QFSTSLHRSL KPRQSTASSS
ALRQQPRRQI SNIAEPKNES SSATATVSTP IPKKQRFRVL RFLWRLTWLS TLGGAAYLTY
HIYDSKHPPE QLPLDPTKKT LVILGSGWGS VSLLKKLDTE DYNVIVISPR NFFLFTPLLP
SCTTGTIEHR SIMEPLRHII RHKKRAVKYY EAEATKIDVD RRVVKINDFS DVKGNVSETE
VPFDYLVVGV GAENATFGIP GVRENACFLK EIGDAQQIRK KVMDCIETAT FKDQTEEEKD
RLLHMVVVGG GPTGIEFAAE LQDFFEEDLR KWVPDITDRF KVTLVEALPN VLPMFSKALI
DYTEKTFKDE NISVRTKTMV KKVTDKSIEV EATQPDGSKV KESINYGLLV WATGNAVRGV
VRDLMSQVPA QKNSRRGLAV NDYLVVDGTD GIWALGDCSA TKYAPTAQVA SQQGNFLARL
FNSMAKTQAV EEELRSLDAR LQASTDEAEK TLLTAEINAK GRSLSKVKQL SPFQYSHQGS
LAYIGADRAV ADLNWFGGAI SSATGGELTY LFWRSAYVSM VFSLRNRILV LTDWLKTKAF
GRDVSRE
//