NU1M_TRIRU
ID NU1M_TRIRU Reviewed; 343 AA.
AC Q9ZZ38;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=NADH-ubiquinone oxidoreductase chain 1;
DE EC=7.1.1.2;
DE AltName: Full=NADH dehydrogenase subunit 1;
GN Name=ND1; Synonyms=NADH1;
OS Trichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum).
OG Mitochondrion.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=5551;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=IP 1817.89;
RX PubMed=10022946; DOI=10.1007/s002940050429;
RA de Bievre C., Dujon B.;
RT "Organisation of the mitochondrial genome of Trichophyton rubrum III. DNA
RT sequence analysis of the NADH dehydrogenase subunits 1, 2, 3, 4, 5 and the
RT cytochrome b gene.";
RL Curr. Genet. 35:30-35(1999).
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 1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y18476; CAA77189.1; -; Genomic_DNA.
DR PIR; T14245; T14245.
DR AlphaFoldDB; Q9ZZ38; -.
DR SMR; Q9ZZ38; -.
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 HAMAP; MF_01350; NDH1_NuoH; 1.
DR InterPro; IPR001694; NADH_UbQ_OxRdtase_su1/FPO.
DR InterPro; IPR018086; NADH_UbQ_OxRdtase_su1_CS.
DR PANTHER; PTHR11432; PTHR11432; 1.
DR Pfam; PF00146; NADHdh; 1.
DR PROSITE; PS00667; COMPLEX1_ND1_1; 1.
DR PROSITE; PS00668; COMPLEX1_ND1_2; 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..343
FT /note="NADH-ubiquinone oxidoreductase chain 1"
FT /id="PRO_0000117491"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 343 AA; 38240 MW; D29CD3BF97CFED64 CRC64;
MYTLISIIGK YISCLPALLI VAFLTISERK TMASMQRRLG QNIVGYYGLL QAFADALKLL
LKEYVAPTQA NIILLFLGPI ITLIFSLLGY RVIPYGSGLF ISDFNLGILY ILAVSSLATY
GILLAGWSAN SKYAFLGSLR STAQLISYEL LLRFYILLVI LFTGSLNLTT IIESQKVVYF
ILPLLPIFLI FFIGCIAETN RAPFDLAEAE SELVSGFMTE HSAVIFMIFF FLAQYASIVL
ICILSSVLFL GGYLNILPLN TYNVCDFNSL FSDYLINGLS SLNLAIKTAF LIFVFIWVRA
SFPRIRFDQL MSVCWTILLP IIIAYVVLLP CIVIGLNSSI LLI
