NU1M_ANOGA
ID NU1M_ANOGA Reviewed; 314 AA.
AC P34846;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=NADH-ubiquinone oxidoreductase chain 1;
DE EC=7.1.1.2;
DE AltName: Full=NADH dehydrogenase subunit 1;
GN Name=mt:ND1; Synonyms=ND1;
OS Anopheles gambiae (African malaria mosquito).
OG Mitochondrion.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G3;
RX PubMed=9087549; DOI=10.1111/j.1365-2583.1993.tb00131.x;
RA Beard C.B., Hamm D.M., Collins F.H.;
RT "The mitochondrial genome of the mosquito Anopheles gambiae: DNA sequence,
RT genome organization, and comparisons with mitochondrial sequences of other
RT insects.";
RL Insect Mol. Biol. 2:103-124(1993).
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 EMBL; L20934; AAD12202.1; -; Genomic_DNA.
DR PIR; T09813; T09813.
DR RefSeq; NP_008081.1; NC_002084.1.
DR AlphaFoldDB; P34846; -.
DR SMR; P34846; -.
DR STRING; 7165.AGAP028389-PA; -.
DR GeneID; 1267425; -.
DR KEGG; aga:ND1; -.
DR CTD; 4535; -.
DR VEuPathDB; VectorBase:AGAP028389; -.
DR eggNOG; KOG4770; Eukaryota.
DR HOGENOM; CLU_015134_0_1_1; -.
DR InParanoid; P34846; -.
DR OMA; WSGWASN; -.
DR OrthoDB; 1214989at2759; -.
DR Proteomes; UP000007062; Mitochondrion.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IBA:GO_Central.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
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; Reference proteome; Respiratory chain; Translocase; Transmembrane;
KW Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..314
FT /note="NADH-ubiquinone oxidoreductase chain 1"
FT /id="PRO_0000117341"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 314 AA; 36100 MW; 512CABE0AA4E1DB7 CRC64;
MFDGIMPLIG SLLLVICVMV GVAFLTLLER KVLGYIQIRK GPNKVGFNGL LQPFSDAVKL
FTKEQTYPLL SNYISYYFSP VFSLFLSLLI WMCIPYLIKL YSFNLGVLFF LCCTSLGVYT
VMIAGWSSNS NYALLGGLRA VAQTISYEVS LALILLSFIF LVGNYNFLSF YFYQDYVWFI
FFCFPLGLVW LASCLAETNR TPFDFAEGES ELVSGFNVEY SSGGFALIFL AEYSSILFMS
MLFVVIFLGS DIYSFMFFLK LSFISFIFIW VRGTLPRFRY DKLMYLAWKS FLPLSLNYLF
FFVGLKIFFI SLLF