ID I1LLL3_SOYBN Unreviewed; 509 AA.
AC I1LLL3;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=NADH:ubiquinone reductase (non-electrogenic) {ECO:0000256|ARBA:ARBA00012637};
DE EC=1.6.5.9 {ECO:0000256|ARBA:ARBA00012637};
GN Name=100793544 {ECO:0000313|EnsemblPlants:KRH30292};
GN ORFNames=GLYMA_11G173700 {ECO:0000313|EMBL:KRH30292.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EMBL:KRH30292.1};
RN [1] {ECO:0000313|EMBL:KRH30292.1, ECO:0000313|EnsemblPlants:KRH30292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH30292};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH30292.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRH30292}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH30292};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH30292.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH30292.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) 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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
CC -!- SIMILARITY: Belongs to the NADH dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00005272}.
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DR EMBL; CM000844; KRH30292.1; -; Genomic_DNA.
DR RefSeq; XP_003538295.1; XM_003538247.3.
DR AlphaFoldDB; I1LLL3; -.
DR SMR; I1LLL3; -.
DR STRING; 3847.I1LLL3; -.
DR PaxDb; 3847-GLYMA11G27280-1; -.
DR EnsemblPlants; KRH30292; KRH30292; GLYMA_11G173700.
DR GeneID; 100793544; -.
DR Gramene; KRH30292; KRH30292; GLYMA_11G173700.
DR KEGG; gmx:100793544; -.
DR eggNOG; KOG2495; Eukaryota.
DR HOGENOM; CLU_021377_1_3_1; -.
DR InParanoid; I1LLL3; -.
DR OMA; GRAWNAK; -.
DR OrthoDB; 48029at2759; -.
DR Proteomes; UP000008827; Chromosome 11.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
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:SF13; INTERNAL ALTERNATIVE NAD(P)H-UBIQUINONE OXIDOREDUCTASE A2, MITOCHONDRIAL; 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; 1.
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:UP000008827};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 74..405
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 509 AA; 56813 MW; C22DDAB8930B66F8 CRC64;
MAWLRNLSKF ATMKRASSSS SQRPKNTDPF CLLPSFTFFS NFSTNTIEEK PCVKPVEYNN
YSGLQPTRPH EKPRVVVLGS GWAGCRLMKG LDPRVYDIVC VSPRNHMVFT PLLASTCVGT
LEFRSVAEPI GRIQPAISRE PGSYFFLANC TQIDAHNHMV HCETVTEGVE TIAPWKFTIS
YDKLVIALGS QPSTFGIQGV KEHAIFLREV HHAQEIRRKL LLNLMLSDVP GISEEEKQRL
LHCVVVGGGP TGVEFSGELS DFITKDVRQR YVHVKDYIRV TLIEANEILS SFDDRLRRYA
TKQLTKSGVR LVRGIVKDVK PQKISLNDGS EVPYGLLVWS TGVGPLPMIQ SLDLPKAPGG
RIGVDEWLRV PSVQDVFSIG DCSGFVESTG RQTLPALAQV AERQGKYLAA LLNKIGKAGA
GHANSAKEIE FGDPFVYRHL GSMATIGRYK ALVDLRQTKE AKGLALAGFL SFFIWRSAYI
TRVISWRNRF YVFVNWITTV VFGRDISRL
//
