ID A0A9D3ZQ01_9ROSI Unreviewed; 598 AA.
AC A0A9D3ZQ01;
DT 03-MAY-2023, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2023, sequence version 1.
DT 28-JAN-2026, entry version 12.
DE RecName: Full=NADH:ubiquinone reductase (non-electrogenic) {ECO:0000256|ARBA:ARBA00012637};
DE EC=1.6.5.9 {ECO:0000256|ARBA:ARBA00012637};
GN ORFNames=J1N35_034203 {ECO:0000313|EMBL:KAH1056138.1};
OS Gossypium stocksii.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=47602 {ECO:0000313|EMBL:KAH1056138.1, ECO:0000313|Proteomes:UP000828251};
RN [1] {ECO:0000313|EMBL:KAH1056138.1, ECO:0000313|Proteomes:UP000828251}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. E1 {ECO:0000313|Proteomes:UP000828251};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAH1056138.1};
RX PubMed=34170607;
RA Yu D., Ke L., Zhang D., Wu Y., Sun Y., Mei J., Sun J., Sun Y.;
RT "Multi-omics assisted identification of the key and species-specific
RT regulatory components of drought-tolerant mechanisms in Gossypium
RT stocksii.";
RL Plant Biotechnol. J. 19:1690-1692(2021).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + NADH + H(+) = 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:ARBA00047599};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ubiquinone + NADH + H(+) = 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:ARBA00049010};
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}.
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:KAH1056138.1}.
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DR EMBL; JAIQCV010000010; KAH1056138.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9D3ZQ01; -.
DR OrthoDB; 3244603at2759; -.
DR Proteomes; UP000828251; Unassembled WGS sequence.
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:0050136; F:NADH dehydrogenase (quinone) (non-electrogenic) activity; IEA:UniProtKB-EC.
DR FunFam; 3.50.50.100:FF:000002; External alternative NAD(P)H-ubiquinone oxidoreductase B1, mitochondrial; 1.
DR FunFam; 3.50.50.100:FF:000008; External alternative NAD(P)H-ubiquinone oxidoreductase B1, mitochondrial; 1.
DR Gene3D; 3.50.50.100; -; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
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 InterPro; IPR054585; NDH2-like_C.
DR PANTHER; PTHR43706:SF47; EXTERNAL NADH-UBIQUINONE OXIDOREDUCTASE 1, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR43706; NADH DEHYDROGENASE; 1.
DR Pfam; PF00036; EF-hand_1; 1.
DR Pfam; PF22366; NDH2_C; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR SMART; SM00054; EFh; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000828251};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 396..431
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
SQ SEQUENCE 598 AA; 67241 MW; 5F84975FF48D3D3F CRC64;
MRNFNFFGRL SRAFNDYPSL SKIIVVSTIS GGSLIAYAEA NAFNGSKGHI AHADALASND
DRRIASSEQV PKKKKVVLLG TGWGGMSFLK SLNNPNYEVQ VVSPRNFFVF TPLLPSVTCG
KVEARSIVEP IRNIIRKKNV NISYSEAECV KIDPNNKKIY CRATIDSRSK GEEVFAVDYD
YLIIAVGAQV NTFNTPGVME NCHFLKEIDD AQKIRKNVID SFEKASLPNL SDEERKKILH
FVVVGGGPTG VEFAAELHDF VNDDVVKLYP NVQDLVKITL LEATDHILNM FDKRITNFAE
QKFGRDGIDV KLGSMVTGIN ENEISTKVRG NGEKTSTPYG MVLWSTGIGP RPLIKEFMKQ
IGQGNRRALA TDEWLRVEGF GNIYALGDCA TVNQRKVMED ISEIFRKADK DNSGTLTVKE
FQEIIDDICE RYPQVELYLK NKQVRNMVDL LKEAKGDAAK ESMELNIEEF KSALSEVDSQ
MKNLPATAQV ANQQGAYLAK CFNRMEECEK NPEGPPRFRG TGRHRFHPFR YRHLGQFAPL
GGEQTAAQLP GDWVSIGHSE QWLWYSVYAS KQVSWRTRAL VVSDWIRRFI FGRDTSGI
//
