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NU5M_ASPNG
ID   NU5M_ASPNG              Reviewed;         656 AA.
AC   Q6QU67;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=NADH-ubiquinone oxidoreductase chain 5;
DE            EC=7.1.1.2;
GN   Name=nad5;
OS   Aspergillus niger.
OG   Mitochondrion.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=N909;
RX   PubMed=15600010; DOI=10.1016/j.femsle.2004.10.025;
RA   Juhasz A., Laday M., Gacser A., Kucsera J., Pfeiffer I., Kevei F.,
RA   Hamari Z.;
RT   "Mitochondrial DNA organisation of the mtDNA type 2b of Aspergillus
RT   tubingensis compared to the Aspergillus niger mtDNA type 1a.";
RL   FEMS Microbiol. Lett. 241:119-126(2004).
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 (By
CC       similarity). {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 5 family. {ECO:0000305}.
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DR   EMBL; AY525764; AAS66787.1; -; Genomic_DNA.
DR   RefSeq; YP_337890.1; NC_007445.1.
DR   AlphaFoldDB; Q6QU67; -.
DR   SMR; Q6QU67; -.
DR   GeneID; 3703575; -.
DR   KEGG; ang:Asnifp15; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respirasome; 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   InterPro; IPR010934; NADH_DH_su5_C.
DR   InterPro; IPR018393; NADHpl_OxRdtase_5_subgr.
DR   InterPro; IPR001750; ND/Mrp_mem.
DR   InterPro; IPR003945; NU5C-like.
DR   InterPro; IPR001516; Proton_antipo_N.
DR   PANTHER; PTHR42829; PTHR42829; 1.
DR   Pfam; PF06455; NADH5_C; 1.
DR   Pfam; PF00361; Proton_antipo_M; 1.
DR   Pfam; PF00662; Proton_antipo_N; 1.
DR   TIGRFAMs; TIGR01974; NDH_I_L; 1.
PE   3: Inferred from homology;
KW   Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   NAD; Respiratory chain; Translocase; Transmembrane; Transmembrane helix;
KW   Transport; Ubiquinone.
FT   CHAIN           1..656
FT                   /note="NADH-ubiquinone oxidoreductase chain 5"
FT                   /id="PRO_0000118064"
FT   TRANSMEM        4..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        28..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        81..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        112..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        133..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        176..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        208..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        243..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        272..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        301..319
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        329..351
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        364..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        409..431
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        452..471
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        514..536
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        603..625
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        629..651
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   656 AA;  73072 MW;  3DA662B67104AEF1 CRC64;
     MYLTLIILPL LGSIVSGFFG RKVGVKGAHL ITCVSVITTT FLAILAFFEV GFNNIPVTIN
     VARWVDVESL YVLWNFRFDS LTVSMFITVL IVSSLVHIYS ISYMSHDPHN QRFFSYLSLF
     TFMMIILVTG NNYLIMFVGW EGVGVCSYLL VNFWFTRIAA NQSSLSALLT NREGDTLLTV
     GMFAILWSFG NIDYSTVFAL APYYNENIIT IIGICLLIGA TAKSSQVGLH IWLPQAMEGP
     TPVSALIHAA TMVTAGVYLL MRSSPLIEYS STVLVLCLWL GAITTVFSSL IGLFQQDIKK
     VIAYSTMSQL GMMVIAVGLS SYNLALFHLV NHAFYKALLF LGAGSVIHAV ADNQDFRKYG
     GLREFLPLTY SVMLIASLSL VAVPFMTGFY SKDFILESAY GQYYLSSTIV YFVATIGAMF
     TTLYSAKVLY LTFLTNPNGP LVNYKHAHEG DLFMTIPLII LAIFSIFFGY LTKDIFIGLG
     TGFFTDNSLF IHPSHEIMLD TEFAVPTFFK LLPFVFTVSL SLLSVLLSEF LPKLLINFKF
     SRLGYNIFSF FNQRFYIELF YNKYIVEGVL KLGGQTSKNL NKGPVKLLGP YGLEKGGLAL
     SNSLGNLSTG IVTTYALYIL IGLIFDISLL YFSYNDNNLL ILIIFTLFAL LNSNKK
 
 
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