ID A0A498HFN5_MALDO Unreviewed; 1307 AA.
AC A0A498HFN5;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=NADH:ubiquinone reductase (non-electrogenic) {ECO:0000256|ARBA:ARBA00012637};
DE EC=1.6.5.9 {ECO:0000256|ARBA:ARBA00012637};
GN ORFNames=DVH24_028284 {ECO:0000313|EMBL:RXH68137.1};
OS Malus domestica (Apple) (Pyrus malus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX NCBI_TaxID=3750 {ECO:0000313|EMBL:RXH68137.1, ECO:0000313|Proteomes:UP000290289};
RN [1] {ECO:0000313|EMBL:RXH68137.1, ECO:0000313|Proteomes:UP000290289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC TISSUE=Young leaf {ECO:0000313|EMBL:RXH68137.1};
RA Hu J.;
RT "A high-quality apple genome assembly.";
RL Submitted (OCT-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}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|ARBA:ARBA00008684}.
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:RXH68137.1}.
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DR EMBL; RDQH01000343; RXH68137.1; -; Genomic_DNA.
DR STRING; 3750.A0A498HFN5; -.
DR Proteomes; UP000290289; Chromosome 17.
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:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0003954; F:NADH dehydrogenase activity; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0006116; P:NADH oxidation; IEA:InterPro.
DR Gene3D; 3.50.50.100; -; 2.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR045024; NDH-2.
DR InterPro; IPR002885; Pentatricopeptide_rpt.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR NCBIfam; TIGR00756; PPR; 2.
DR PANTHER; PTHR43706; NADH DEHYDROGENASE; 1.
DR PANTHER; PTHR43706:SF48; NADH:UBIQUINONE REDUCTASE (NON-ELECTROGENIC); 1.
DR Pfam; PF00036; EF-hand_1; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF13041; PPR_2; 1.
DR Pfam; PF13812; PPR_3; 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 SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS51375; PPR; 3.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 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 Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00022707};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Myristate {ECO:0000256|ARBA:ARBA00022707};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000290289};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 1..144
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 728..763
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REPEAT 1117..1151
FT /note="PPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00708"
FT REPEAT 1152..1186
FT /note="PPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00708"
FT REPEAT 1187..1221
FT /note="PPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00708"
SQ SEQUENCE 1307 AA; 145712 MW; B287A0722BDAD53A CRC64;
MAKIFKINQT EANINRVVGT SNGYMSPEYT RDMTIFSEKL DVFSFGVLLL EIVSGKKNAA
FYHFEHSPTL AGWAWELWKE GRGMEVIDES VRETCRPDEA LRCIHVGFLC VQEAPADRPT
MSSVIRMLQS TEATSLPPSK KPAFSTYRNS SFVPSSQTPT SFSHSSVTTS LPEAMDTEPI
SLFEFSIILL HVFPKSRISV AVDTISENNS LSGGIFELGF KSGQLSNYYI GIWYSKHVVS
ERTIVWVANR DIHFQSIVGD YKWKEECCFL LISKFSNSCR MELWKEGKGK EVMMDQQGKH
GGLIHVGFLC VQEAPDDRLT TSSVVHMLQG NEATPPSLSK KPAFSMWGQS FFETASRLFH
QRSSLSKILV VVTVSGGGLA TFHETKPVHT VYADSAQEAE TSRKKKVVVL GTGWAGVSFL
KNLRSSSYDV EVVSPKNYFM FTPLLPSVTC GTVEARSIVE PIRKITEKKG LDVEFREAEC
YRIDPKNKKV LCRSTQHSNL GLKEAEFSVD YDYLIVAMGA KTNTFNTPGV EQYAHFLKGI
EDAVRIRQTV IDCFERASLP SASEEEKKKL LSFVCVGGGP AGVEFAAELH DFVKDDLAKL
YPSVTGYVKI TVIEASDHIL NMFDKRITAF AEGKFFRDGI DVKTGSLVVK LTDKEVSAKD
RDTGKISNIP YGMVLWATGI GPRPEIIDFM KQIGQTNRRV LATDEWLRVE GCDGVYALGD
CATVNQRRVV DDIVSIFRKA DKDNSGTLSL EEFQEVMEDL MVRYPQLSLH LKSKHMRNID
ELLENSWKNP KDEIDIETFK AALSQADSQM KNLPATAQVA AQQGAYLADC FNRMEECEKY
PEGPLKFRDV GRHRFQPFRY KHFGMFAPLG GEQTAAHLPG DWVSIGQSTQ WLWYSQASEL
AHKGAGGFGL GKAIYFRKGH QCLRCYIAAA ASDVRALTFL PNSAPIRRPN HNPPPFSTSV
DPPLFSTATR FISSSRTSSS PEQEATLNQI LSSIQNAATL LESLYENRLF LSPKSFNSVL
VAAAAESGDL SLLSQLLQVA IASSQPLNSA CFLTVAKAFA KSDDCAELLR LTKQVMELTA
PSMTVINRIL FAFGECGETE KALLIFSQMK TLAFVPDLYT HNTVLEILGC AGRIDELVGQ
FGVMKEAGIV PDVVSYNTVL NNLRKLGKFD VCLFYFKEMG ENGVEADLLT YTAVIESLGR
SGNVEEALRF FDEMKAREIR PSLYVYRSLI TNLKKMGKVD LALSLTEEMN SCDSELAGPM
DFKRNKRFEM ICIKHDSNST VFFEQSCSYL QTDDTQITGP NYFEQSS
//