ID   NU3M_CANPA              Reviewed;         131 AA.
AC   P48909;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=NADH-ubiquinone oxidoreductase chain 3;
DE            EC=7.1.1.2;
DE   AltName: Full=NADH dehydrogenase subunit 3;
GN   Name=ND3; Synonyms=NAD3;
OS   Candida parapsilosis (Yeast).
OG   Mitochondrion.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5480;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SR2;
RX   PubMed=7521869; DOI=10.1128/jb.176.18.5622-5630.1994;
RA   Nosek J., Fukuhara H.;
RT   "NADH dehydrogenase subunit genes in the mitochondrial DNA of yeasts.";
RL   J. Bacteriol. 176:5622-5630(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SR23 / CBS 7157;
RX   PubMed=15449175; DOI=10.1007/s00438-004-1046-0;
RA   Nosek J., Novotna M., Hlavatovicova Z., Ussery D.W., Fajkus J., Tomaska L.;
RT   "Complete DNA sequence of the linear mitochondrial genome of the pathogenic
RT   yeast Candida parapsilosis.";
RL   Mol. Genet. Genomics 272:173-180(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 46-131.
RC   STRAIN=SR23 / CBS 7157;
RX   PubMed=7715605; DOI=10.1007/bf00425822;
RA   Nosek J., Dinouel N., Kovac L., Fukuhara H.;
RT   "Linear mitochondrial DNAs from yeasts: telomeres with large tandem
RT   repetitions.";
RL   Mol. Gen. Genet. 247:61-72(1995).
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 membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 3 family. {ECO:0000305}.
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DR   EMBL; X74411; CAE54593.1; -; Genomic_DNA.
DR   PIR; S54752; S54752.
DR   RefSeq; NP_943630.1; NC_005253.2.
DR   AlphaFoldDB; P48909; -.
DR   SMR; P48909; -.
DR   GeneID; 2657789; -.
DR   CGD; CAL0000145117; CapafMp01.
DR   VEuPathDB; FungiDB:CapafMp01; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031966; C:mitochondrial 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   Gene3D; 1.20.58.1610; -; 1.
DR   InterPro; IPR000440; NADH_UbQ/plastoQ_OxRdtase_su3.
DR   InterPro; IPR038430; NDAH_ubi_oxred_su3_sf.
DR   PANTHER; PTHR11058; PTHR11058; 1.
DR   Pfam; PF00507; Oxidored_q4; 1.
PE   3: Inferred from homology;
KW   Electron transport; Membrane; Mitochondrion; NAD; Respiratory chain;
KW   Translocase; Transmembrane; Transmembrane helix; Transport; Ubiquinone.
FT   CHAIN           1..131
FT                   /note="NADH-ubiquinone oxidoreductase chain 3"
FT                   /id="PRO_0000117724"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        52..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   131 AA;  14682 MW;  5E79B13E66C87572 CRC64;
     MFTAYLILCP IIAVVLVGLN WLLATSNSYI EKDGPFECGF TSFQQSRSAF SVAFILVAIL
     FLPFDLEISS ILPFVISPYS NGLYGLVILV IFLILLIVAF VVEIQLKALQ LNRTYTNDLP
     HTELYDININ D