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NDH2_YARLI
ID   NDH2_YARLI              Reviewed;         582 AA.
AC   F2Z699; O74931; Q6C0F6;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=External alternative NADH-ubiquinone oxidoreductase, mitochondrial;
DE            EC=1.6.5.9;
DE   AltName: Full=External alternative NADH dehydrogenase;
DE   AltName: Full=NADH:ubiquinone reductase (non-electrogenic);
DE   Flags: Precursor;
GN   Name=NDH2; OrderedLocusNames=YALI0F25135g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=10381390; DOI=10.1242/jcs.112.14.2347;
RA   Kerscher S.J., Okun J.G., Brandt U.;
RT   "A single external enzyme confers alternative NADH:ubiquinone
RT   oxidoreductase activity in Yarrowia lipolytica.";
RL   J. Cell Sci. 112:2347-2354(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Alternative NADH-ubiquinone oxidoreductase which catalyzes
CC       the oxidation of mitochondrial NADH does not translocate protons across
CC       the inner mitochondrial membrane. {ECO:0000269|PubMed:10381390}.
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:0000269|PubMed:10381390};
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:0000269|PubMed:10381390};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=14 uM for NADH {ECO:0000269|PubMed:10381390};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:10381390}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:10381390}; Intermembrane side
CC       {ECO:0000269|PubMed:10381390}.
CC   -!- SIMILARITY: Belongs to the NADH dehydrogenase family. {ECO:0000305}.
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DR   EMBL; AJ006852; CAA07265.1; -; Genomic_DNA.
DR   EMBL; CR382132; CAG78667.1; -; Genomic_DNA.
DR   RefSeq; XP_505856.1; XM_505856.1.
DR   AlphaFoldDB; F2Z699; -.
DR   SMR; F2Z699; -.
DR   STRING; 4952.CAG78667; -.
DR   PRIDE; F2Z699; -.
DR   EnsemblFungi; CAG78667; CAG78667; YALI0_F25135g.
DR   GeneID; 2908423; -.
DR   KEGG; yli:YALI0F25135g; -.
DR   VEuPathDB; FungiDB:YALI0_F25135g; -.
DR   HOGENOM; CLU_021377_1_0_1; -.
DR   InParanoid; F2Z699; -.
DR   OMA; VDPRSYM; -.
DR   BRENDA; 1.6.5.9; 1122.
DR   Proteomes; UP000001300; Chromosome F.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:RHEA.
DR   GO; GO:0006116; P:NADH oxidation; IEA:InterPro.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR045024; NDH-2.
DR   PANTHER; PTHR43706; PTHR43706; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   SUPFAM; SSF51905; SSF51905; 2.
PE   1: Evidence at protein level;
KW   Coiled coil; FAD; Flavoprotein; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; NAD; Oxidoreductase; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..30
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..582
FT                   /note="External alternative NADH-ubiquinone oxidoreductase,
FT                   mitochondrial"
FT                   /id="PRO_0000415492"
FT   REGION          46..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          454..501
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        48..65
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         114..144
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         277..313
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   582 AA;  65815 MW;  2BD807DD0A026562 CRC64;
     MLRLRPAVRA VSVARSVALT RSLHVSVAKF NKIEGTAPAG LPKEVKQTAG HQGHHQEIPK
     PDENHPRRKK FHFWRSLWRL TYLSAIASLG YIGYRIYVIR NPSDQLPADP SKKTLVVLGS
     GWGSVSFLKK LDTSNYNVIV VSPRNYFLFT PLLPSCPTGT IEHRSIMEPI RGIIRHKQAE
     CQYLEADATK IDHEKRIVTI RSAVSENSKE EVIKEIPFDY LVVGVGAMSS TFGIPGVQEN
     ACFLKEIPDA QQIRRTLMDC IEKAQFEKDP EVRKRLLHTV VVGGGPTGVE FAAELQDFFE
     DDLRKWIPDI RDDFKVTLVE ALPNVLPSFS KKLIDYTEKT FSDEKISILT KTMVKSVDEN
     VIRAEQTKGD GTKETLEMPY GTLVWATGNT VRPVVRELMS KIPAQKGSRR GLLVNEYLVV
     EGTEGIWALG DCSATKYAPT AQVASQEGSY LANLLNGIAK TEDLNNEITN LEKQSEHTFD
     EQERKNIFAQ LESKSRKLRR SRAMLPFEYS HQGSLAYIGS DRAVADLSFN FWGIMNWSSG
     GTMTYYFWRS AYVSMCFSMR NKILVCIDWM KVRVFGRDIS RE
 
 
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