ID I1M2C9_SOYBN Unreviewed; 575 AA.
AC I1M2C9;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=NADH:ubiquinone reductase (non-electrogenic) {ECO:0000256|ARBA:ARBA00012637};
DE EC=1.6.5.9 {ECO:0000256|ARBA:ARBA00012637};
GN Name=100797657 {ECO:0000313|EnsemblPlants:KRH21577};
GN ORFNames=GLYMA_13G246600 {ECO:0000313|EMBL:KRH21577.1};
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:KRH21577.1};
RN [1] {ECO:0000313|EMBL:KRH21577.1, ECO:0000313|EnsemblPlants:KRH21577}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH21577};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH21577.1};
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:KRH21577}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH21577};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH21577.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH21577.1};
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: Mitochondrion inner membrane
CC {ECO:0000256|ARBA:ARBA00004137}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004137}; Intermembrane side
CC {ECO:0000256|ARBA:ARBA00004137}. Peroxisome
CC {ECO:0000256|ARBA:ARBA00004275}.
CC -!- SIMILARITY: Belongs to the NADH dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00005272}.
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DR EMBL; CM000846; KRH21577.1; -; Genomic_DNA.
DR RefSeq; XP_006594629.1; XM_006594566.2.
DR AlphaFoldDB; I1M2C9; -.
DR EnsemblPlants; KRH21577; KRH21577; GLYMA_13G246600.
DR GeneID; 100797657; -.
DR Gramene; KRH21577; KRH21577; GLYMA_13G246600.
DR HOGENOM; CLU_021377_1_0_1; -.
DR OMA; EISSMPY; -.
DR OrthoDB; 48029at2759; -.
DR Proteomes; UP000008827; Chromosome 13.
DR ExpressionAtlas; I1M2C9; baseline and differential.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; -; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR045024; NDH-2.
DR PANTHER; PTHR43706; NADH DEHYDROGENASE; 1.
DR PANTHER; PTHR43706:SF22; NADH:UBIQUINONE REDUCTASE (NON-ELECTROGENIC); 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR PROSITE; PS50222; EF_HAND_2; 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 Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000008827};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 373..408
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
SQ SEQUENCE 575 AA; 64708 MW; 3CE81CA59ACC6B2C CRC64;
MSSITFFHRL SSAFRDNQSH LKLVLLCTAV SGGGLWAYGE SVAPEEAVTE KKKVVVLGTG
WAATSFMKNL NNPKYEIQVV SPRNYFAFTP LLPSVTCGTV EARSIVEPVR NIFKKKVDVQ
FSEAECFKID AENRKVYCRS SVNNNLDGKE EFVVDYDYLI VAVGANVNTF NTPGVTENCH
FLKEVEDAQK IRRTVIDCFE RANLPDVSED EKKRILHFAI VGGGPTGVEF AASLHDFVNE
DLVRLYPGIK DLVKITLLEA GNHILGMFDK RITAFAEDKF RRDGIDVKTG SMVVKVSEKE
ISTKELKNGE IKTIPYGMAV WSTGIGTRPF IKDFMAQIGQ ASRRALATDE WLRVEGCNNV
YALGDCATIN QRKVMEDIVA IFKKADKDNS GTLTVIQFQE VMKDICERYP QVELYLKNKQ
MGNIADLLKE AKGDDKKESI ELNIEELKTA LSKVDSQMKF LPATAQVASQ QGTYLAKCFN
RMEECEKNPE GPLRFRGEGH HRFKPFRYKH LGQFAPLGGE QTAAQLPGDW VSIGHSSQWL
WYSVYASKQV SWRTRALVVS DWTRRFIFGR DSSSI
//
