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NU1M_LEITA
ID   NU1M_LEITA              Reviewed;         313 AA.
AC   P15576;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=NADH-ubiquinone oxidoreductase chain 1;
DE            EC=7.1.1.2;
DE   AltName: Full=NADH dehydrogenase subunit 1;
GN   Name=ND1;
OS   Leishmania tarentolae (Sauroleishmania tarentolae).
OG   Mitochondrion.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania;
OC   lizard Leishmania.
OX   NCBI_TaxID=5689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=3032958; DOI=10.1016/s0021-9258(18)45555-x;
RA   Simpson L., Neckelmann N., de la Cruz V.F., Simpson A.M., Feagin J.E.,
RA   Jasmer D.P., Stuart K.;
RT   "Comparison of the maxicircle (mitochondrial) genomes of Leishmania
RT   tarentolae and Trypanosoma brucei at the level of nucleotide sequence.";
RL   J. Biol. Chem. 262:6182-6196(1987).
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}.
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DR   PIR; D26696; D26696.
DR   AlphaFoldDB; P15576; -.
DR   SMR; P15576; -.
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   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; 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..313
FT                   /note="NADH-ubiquinone oxidoreductase chain 1"
FT                   /id="PRO_0000117418"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        31..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        62..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        84..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        142..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        183..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        216..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        250..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        286..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   313 AA;  35807 MW;  CE7ADF8883EEA37F CRC64;
     MLNIDIIIII IIDILVVLIL TGFVSLCERR ILALVQIRIG PALCFFGILT PITDGIKLFI
     KFIIFVISFD IIYLIGAMII TACCIFLGWF YFPIGFILLL DTGFTLTVML CVHVFCSMFS
     TFFVGCFLFS SCFVYLSAMR TMFFSIISES GIFLLYTTIY SLDYFSFFGI KDVCVGQIYI
     TNFYIAGVLF ISVFWVSMLL DGLKLPFDYM ECESELVAGL ITELSGFFFV LYSVLEINHI
     LLTTLLFASL CFGGLFICFK AILILIFGFF YPRVIGYRLK ITTAQAFILI FLFYMCVLMF
     IWLFTTKIIA MLF
 
 
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