NU5M_HYPJE
ID NU5M_HYPJE Reviewed; 692 AA.
AC Q8SHP7;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=NADH-ubiquinone oxidoreductase chain 5;
DE EC=7.1.1.2;
GN Name=nd5;
OS Hypocrea jecorina (Trichoderma reesei).
OG Mitochondrion.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=51453;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11825887; DOI=10.1074/jbc.m107651200;
RA Chambergo F.S., Bonaccorsi E.D., Ferreira A.J.S., Ramos A.S.P.,
RA Ferreira J.R. Jr., Abrahao-Neto J., Farah J.P.S., El-Dorry H.;
RT "Elucidation of the metabolic fate of glucose in the filamentous fungus
RT Trichoderma reesei using expressed sequence tag (EST) analysis and cDNA
RT microarrays.";
RL J. Biol. Chem. 277:13983-13988(2002).
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; AF447590; AAL74164.1; -; Genomic_DNA.
DR RefSeq; NP_570156.1; NC_003388.1.
DR AlphaFoldDB; Q8SHP7; -.
DR SMR; Q8SHP7; -.
DR GeneID; 804634; -.
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; 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; 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..692
FT /note="NADH-ubiquinone oxidoreductase chain 5"
FT /id="PRO_0000118157"
FT TRANSMEM 5..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 30..52
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 168..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..222
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 511..528
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 535..557
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 615..637
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 692 AA; 77172 MW; 89821FAAFCBA6C81 CRC64;
MYLSIIILPL LGSIVSGFFG RKVGVTGSRI LGCLSIITTT ILAIISFFEV GFNNNPISIN
LFKWLDSESF NMVWNFQFDS LTVSMLIPVL VISSLVHFYS IGYMSHDPHS QRFFSYLSLF
TFMMIILVTG NNYLLMFVGW EGVGVCSYLL VSFWFTRIAA NQSSLSAFLT NRVGDCFLTI
GMFVILWSLG NLDYSTVFSL APYINENIIT IIGICLLIGA MAKSSQVGLH IWLPMAMEGP
TPVSALIHAA TMVTAGVYLL IRSSPLIEYS STVLLICLWL GAVTTVFSSL IGLFQQDIKK
IIAYSTMSQL GMMVIAIGLS SYNVAIFHLI NHAFYKGLLF LGAGAVIHAV VDNQDLRKYG
GLISFLPLTY TVILIASLSL VAFPFMTGFF SKDFILESAY GQYHFSSINV YFIATIGAVF
TTLYSVKVIY LTFLANPNGS VNYYKNAHEG DIFLSLPLVI LAIFSIYFGY LTKDIYIGLG
SGFFIDNSIF IHPMREILID TEFGVPTIFK LLPFFLTIFF SVLSIVYYEY MPKVVVDFNL
TNLGYYIYGF FNQRFLVEFF YNKYIVNTVL DLGGQTTKIL DKGSVEWIGP YGFGIALVKA
SKTVSGLGKG VVTDYALYIL IGACFYLSIF TFISIFFDLA NSITLSCVLV LLGVNNYVKL
NKNDNINENS LTSSFLWSNT KEMSKYTTKI II