ID I6YI10_LINUS Unreviewed; 1272 AA.
AC I6YI10;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=NADH:ubiquinone reductase (non-electrogenic) {ECO:0000256|ARBA:ARBA00012637};
DE EC=1.6.5.9 {ECO:0000256|ARBA:ARBA00012637};
OS Linum usitatissimum (Flax) (Linum humile).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Linaceae; Linum.
OX NCBI_TaxID=4006 {ECO:0000313|EMBL:AFN53706.1};
RN [1] {ECO:0000313|EMBL:AFN53706.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=22757964; DOI=10.1111/j.1365-313X.2012.05093.x;
RA Wang Z., Hobson N., Galindo L., Zhu S., Shi D., McDill J., Yang L.,
RA Hawkins S., Neutelings G., Datla R., Lambert G., Galbraith D.W.,
RA Grassa C.J., Geraldes A., Cronk Q.C., Cullis C., Dash P.K., Kumar P.A.,
RA Cloutier S., Sharpe A.G., Wong G.K., Wang J., Deyholos M.K.;
RT "The genome of flax (Linum usitatissimum) assembled de novo from short
RT shotgun sequence reads.";
RL Plant J. 72:461-473(2012).
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 DEAD box helicase family. DDX59 subfamily.
CC {ECO:0000256|ARBA:ARBA00009718}.
CC -!- SIMILARITY: Belongs to the NADH dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00005272}.
CC -!- SIMILARITY: Belongs to the syntaxin family.
CC {ECO:0000256|ARBA:ARBA00009063, ECO:0000256|RuleBase:RU003858}.
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DR EMBL; JX174448; AFN53706.1; -; Genomic_DNA.
DR AlphaFoldDB; I6YI10; -.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003954; F:NADH dehydrogenase activity; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0005484; F:SNAP receptor activity; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0006116; P:NADH oxidation; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR CDD; cd15848; SNARE_syntaxin1-like; 1.
DR CDD; cd00179; SynN; 1.
DR Gene3D; 1.20.5.110; -; 1.
DR Gene3D; 1.20.58.70; -; 1.
DR Gene3D; 3.30.60.220; -; 1.
DR Gene3D; 3.50.50.100; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
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; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR045024; NDH-2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR InterPro; IPR010989; SNARE.
DR InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR InterPro; IPR006011; Syntaxin_N.
DR InterPro; IPR000727; T_SNARE_dom.
DR InterPro; IPR007529; Znf_HIT.
DR PANTHER; PTHR43706:SF47; EXTERNAL ALTERNATIVE NAD(P)H-UBIQUINONE OXIDOREDUCTASE B2, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR43706; NADH DEHYDROGENASE; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF05739; SNARE; 1.
DR Pfam; PF00804; Syntaxin; 1.
DR Pfam; PF04438; zf-HIT; 1.
DR PRINTS; PR00368; FADPNR.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00054; EFh; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00503; SynN; 1.
DR SMART; SM00397; t_SNARE; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF47661; t-snare proteins; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
DR PROSITE; PS00914; SYNTAXIN; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:AFN53706.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1245..1264
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 203..265
FT /note="T-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50192"
FT DOMAIN 424..452
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 455..628
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 639..803
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1109..1144
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT MOTIF 424..452
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
SQ SEQUENCE 1272 AA; 141819 MW; 435AE88A3ADDD405 CRC64;
MNDLFSSSFK KYTDLKQQTQ IDDLEAGKQN TNLDKFFQDV ENVKDDMSTV AKLHKSLQES
NEEIKTVHNA KTVKDLRSRM DSDVAQVLKR VRVIKGKLEA LERSNAAARS IPGCGPGSSA
DRTRTSVVGG LGKKLKDLMD DFQNLRAKMS AEYKETVERR YFTITGEKAS EDLIENLIES
GESESFLQKA IQEQGRGQIL DTISEIQERH DAVKEIEKNL IELHQVFLDM AALVEAQGHQ
LNDIESHVAH ASSFVRRGTE QLQEAREHQK SSRKWTCIAI ILGIVFIILL LLPLLKCFVN
MKSSYGSSHR IPFEDESDEV KKSSRQQRLA LQGEPKCVIC GRYGEYICDE TDDDVCSLEC
KQVVLARTIA KDRGSISNRI VVSAKDECFY VRDSMSLTAD QTVTSRKKLD IHVKGDDTVP
PPMLSFSSWN LPSKLLQNIE SAGFDVPTPV QMQAIPIGLS GKSLLASAET GSGKTASFLV
PIITCCSRHQ NLNRKKPLGI VLTPTRELCI QVEDQAKLLG KGLLFKTALV VGGDAMAGQV
HRLQQGVELI VATPGRLIDL LTKHDIELDE VKMFVVDEVD YMLQSGFRDQ VMQIFVSLAQ
PQVLMYSATI SEEVEKLASS MIKEIVSISI GLRNRPSMAV KQLAIWVETK QKKQKLFDIL
LSKQHFVPPA VVYVGSRLGA DLLSNAITVR TGLKALSIHG EKPMKERREI MAAFLMGEAP
VIVSTGVLGR GMDLLGVRQV IVFDMPNSIE EYVHMIGRAS RMGEEGKAIA FINEENKTIF
SEFVEEKSLV LLKQCNRCGG GLVAYADANS LSHVAPPEIK KKRVVVLGTG WAGTSFLKQL
NDPSYDVQVI SPRNYFAFTP LLPSVTVGTV EPRSIVEPIR NIVKKKNVDV RYWEAECFKI
DSQSKKVHCH SNQNVDGNGK EEFVADYDYL VIAMGGRPNT FNTPGVVEHC NFLKEVEDAQ
RIRRSVVDCF EKASLPSLSD EERKKILHFV VVGGGPTGVE FAAELHDFVT EDLVKLYPAA
RKYVKITLLE AADHILTMFD KRITEFAEDK FKRDGIDVKL GSMVTKVSDN EISAKARVDG
QVTNMPYGMI VWSTGIGAHP VIRDFMKQVG QEDIDAIFKK ADKDNSGTLT VKELQEVIDD
ICERYPQVGL YLKTKKLRNI ADLLSDAQGD DSKGSIELSI EELKTALKEV DSQVKNFPAT
AQVAAQQGSY LANCFNRMET AEKNPEGPLR FRGEGRHRFR PFRLFFSWVI IFAIQIGYVA
GFDIKELIKA SV
//
