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NDUS1_NEUCR
ID   NDUS1_NEUCR             Reviewed;         744 AA.
AC   P24918; Q7RV66; Q9P6E0;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 2.
DT   03-AUG-2022, entry version 178.
DE   RecName: Full=NADH-ubiquinone oxidoreductase 78 kDa subunit, mitochondrial;
DE            EC=7.1.1.2;
DE   AltName: Full=Complex I-78kD;
DE            Short=CI-78kD;
DE   Flags: Precursor;
GN   Name=nuo78; ORFNames=B17C10.90, NCU01765;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 34-64.
RC   STRAIN=74-ORS-6a / FGSC 4200;
RX   PubMed=1832016; DOI=10.1016/0167-4781(91)90049-r;
RA   Preis D., Weidner U., Conzen C., Azevedo J.E., Nehls U., Roehlen D.-A.,
RA   van der Pas J.C., Sackmann U., Schneider R., Werner S., Weiss H.;
RT   "Primary structures of two subunits of NADH: ubiquinone reductase from
RT   Neurospora crassa concerned with NADH-oxidation. Relationship to a soluble
RT   NAD-reducing hydrogenase of Alcaligenes eutrophus.";
RL   Biochim. Biophys. Acta 1090:133-138(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory chain
CC       NADH dehydrogenase (Complex I) that is believed to belong to the
CC       minimal assembly required for catalysis. Complex I functions in the
CC       transfer of electrons from NADH to the respiratory chain. The immediate
CC       electron acceptor for the enzyme is believed to be ubiquinone. This is
CC       the largest subunit of complex I and it is a component of the iron-
CC       sulfur (IP) fragment of the enzyme. It may form part of the active site
CC       crevice where NADH is oxidized.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) +
CC         NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-
CC         COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2;
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250};
CC       Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC       Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Complex I is composed of about 40 different subunits.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane.
CC   -!- SIMILARITY: Belongs to the complex I 75 kDa subunit family.
CC       {ECO:0000305}.
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DR   EMBL; X57602; CAA40828.1; -; mRNA.
DR   EMBL; AL355926; CAB91229.1; -; Genomic_DNA.
DR   EMBL; CM002237; EAA27952.3; -; Genomic_DNA.
DR   PIR; S17664; S17664.
DR   PIR; T49428; T49428.
DR   RefSeq; XP_957188.3; XM_952095.3.
DR   AlphaFoldDB; P24918; -.
DR   SMR; P24918; -.
DR   STRING; 5141.EFNCRP00000001842; -.
DR   TCDB; 3.D.1.6.2; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR   PRIDE; P24918; -.
DR   EnsemblFungi; EAA27952; EAA27952; NCU01765.
DR   GeneID; 3873340; -.
DR   KEGG; ncr:NCU01765; -.
DR   VEuPathDB; FungiDB:NCU01765; -.
DR   HOGENOM; CLU_000422_11_6_1; -.
DR   InParanoid; P24918; -.
DR   Proteomes; UP000001805; Chromosome 6, Linkage Group II.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR   CDD; cd00207; fer2; 1.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR   InterPro; IPR000283; NADH_UbQ_OxRdtase_75kDa_su_CS.
DR   InterPro; IPR010228; NADH_UbQ_OxRdtase_Gsu.
DR   InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
DR   InterPro; IPR015405; NuoG_C.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR   Pfam; PF09326; NADH_dhqG_C; 1.
DR   SMART; SM00929; NADH-G_4Fe-4S_3; 1.
DR   SUPFAM; SSF54292; SSF54292; 1.
DR   TIGRFAMs; TIGR01973; NuoG; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS51839; 4FE4S_HC3; 1.
DR   PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR   PROSITE; PS00641; COMPLEX1_75K_1; 1.
DR   PROSITE; PS00642; COMPLEX1_75K_2; 1.
DR   PROSITE; PS00643; COMPLEX1_75K_3; 1.
PE   1: Evidence at protein level;
KW   2Fe-2S; 4Fe-4S; Direct protein sequencing; Electron transport; Iron;
KW   Iron-sulfur; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion inner membrane; NAD; Oxidoreductase; Reference proteome;
KW   Respiratory chain; Transit peptide; Translocase; Transport; Ubiquinone.
FT   TRANSIT         1..33
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:1832016"
FT   CHAIN           34..744
FT                   /note="NADH-ubiquinone oxidoreductase 78 kDa subunit,
FT                   mitochondrial"
FT                   /id="PRO_0000019974"
FT   DOMAIN          34..112
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   DOMAIN          112..151
FT                   /note="4Fe-4S His(Cys)3-ligated-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT   DOMAIN          251..307
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         68
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
FT   BINDING         79
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
FT   BINDING         82
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
FT   BINDING         96
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
FT   BINDING         128
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT   BINDING         132
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT   BINDING         135
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT   BINDING         141
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT   BINDING         182
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         185
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         188
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         232
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        125
FT                   /note="L -> P (in Ref. 1; CAA40828)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        152
FT                   /note="G -> R (in Ref. 1; CAA40828)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        164
FT                   /note="R -> Q (in Ref. 1; CAA40828)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        340
FT                   /note="P -> A (in Ref. 1; CAA40828)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        379..388
FT                   /note="SGHKPLAHGV -> FGPQTSCSWC (in Ref. 1; CAA40828)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        493
FT                   /note="A -> R (in Ref. 1; CAA40828)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        527..534
FT                   /note="SRVGAFEV -> PESAPSRL (in Ref. 1; CAA40828)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        666..667
FT                   /note="PS -> SL (in Ref. 1; CAA40828)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        722
FT                   /note="P -> S (in Ref. 1; CAA40828)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        727..729
FT                   /note="MAP -> IGS (in Ref. 1; CAA40828)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        740
FT                   /note="I -> Y (in Ref. 1; CAA40828)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   744 AA;  81602 MW;  D842DDCE80510929 CRC64;
     MLRSTLSRSA WRTGRHQAAR NASRAFSATA QRPAEVELTI DGKKVSIEAG SALIQACEKA
     GVTIPRYCYH EKLMIAGNCR MCLVEVEKVP KPVASCAWPV QPGMVVKTNS PLTHKAREGV
     MEFLLANHPL DCPICDQGGE CDLQDQSMRY GGDRGRFHEV GGKRAVEDKN MGPLIKTSMN
     RCIQCTRCVR FANDIAGAPE LGSTGRGNDL QIGTYLEKNL DSELSGNVID LCPVGALTSK
     PYAFRARPWE LKKTESIDVL DGLGSNIRVD TRGLEVMRIL PRLNDEVNEE WINDKTRFAC
     DGLKTQRLTI PLVRREGKFE PASWDQALTE IAHAYQTLNP QGNEFKAIAG QLTEVESLVA
     MKDLANRLGS ENLALDMPSG HKPLAHGVDV RSNYIFNSSI VGIESADVIL LVGTNPRHEA
     AVLNARIRKQ WLRSDLEIGV VGQTWDSTFE FEHLGTDHAA LQKALEGDFG KKLQSAKNPM
     IIVGSGVTDH GDANAFYETV GKFVDSNASN FLTEEWNGYN VLQRAASRVG AFEVGFTVPS
     AEIAQTKPKF VWLLGADEFN EADIPKDAFI VYQGHHGDRG AQIADIVLPG AAYTEKAGTY
     VNTEGRVQMT RAATGLPGAA RTDWKILRAV SEYLGVRLPY DDVAQLRDRM VEISPALSSY
     DIIEPPSLQQ LSKVQLVEQN QGATATNEPL KKVIENFYFT DAISRSSPTM ARCSAAKKTG
     DPRTNFMAPG MEEDRPMGQI AYGA
 
 
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