NU2M_CANAL
ID NU2M_CANAL Reviewed; 475 AA.
AC Q9B8D2;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 2.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=NADH-ubiquinone oxidoreductase chain 2;
DE EC=7.1.1.2;
DE AltName: Full=NADH dehydrogenase subunit 2;
GN Name=NAD2; OrderedLocusNames=CM_00310W {ECO:0000312|CGD:CAL0000182977};
GN ORFNames=CaalfMp09;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OG Mitochondrion.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=11208783; DOI=10.1128/jb.183.3.865-872.2001;
RA Anderson J.B., Wickens C., Khan M., Cowen L.E., Federspiel N.A., Jones T.,
RA Kohn L.M.;
RT "Infrequent genetic exchange and recombination in the mitochondrial genome
RT of Candida albicans.";
RL J. Bacteriol. 183:865-872(2001).
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 2 family. {ECO:0000305}.
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DR EMBL; AF285261; AAG59594.2; -; Genomic_DNA.
DR RefSeq; NP_075037.2; NC_002653.1.
DR AlphaFoldDB; Q9B8D2; -.
DR SMR; Q9B8D2; -.
DR STRING; 237561.Q9B8D2; -.
DR GeneID; 802559; -.
DR KEGG; cal:CaalfMp09; -.
DR CGD; CAL0000182977; NAD2.
DR VEuPathDB; FungiDB:CM_00310W; -.
DR InParanoid; Q9B8D2; -.
DR Proteomes; UP000000559; Mitochondrion.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; ISS:CGD.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; ISS:CGD.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; ISS:CGD.
DR InterPro; IPR001750; ND/Mrp_mem.
DR Pfam; PF00361; Proton_antipo_M; 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..475
FT /note="NADH-ubiquinone oxidoreductase chain 2"
FT /id="PRO_0000356876"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 447..467
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 475 AA; 53320 MW; 4D69C55652703418 CRC64;
MVVHITTDND IGVRITLRRM LLLTLVTYIV YIAYNQRDIL HINRLAVLAL SFVAYLAWES
IGIQYSNFTL LNDWFQYTPG NAPIVLLLII LVITLLVYLT TTQRYITPNK WIALLMLVNL
IGLILFPMVN DLIPLYVIIE LQSYSLYLLT GVYNKSYNAT RAAILYFVTG GIASVLILLS
SAEVYEATGL TNLSEISTYY SISGINTWTS FDILLIALVF KMGLAPLHAW SISVYSYAPL
YITAYISIVA KVSIMSFIYL NIHLFSTQLL ILAFYLSVAV AAYTPLYQVN IKSILAYSGI
LNFGYLLTAV LTNDNAYYIY IIQYSLTHVT IFLCILAITE YTNKPASYWS PIVNVNQLVV
PNKALCIALI VCLFSLIGIP PLPGFYGKYY IIVGLMSNGL NLEALTIIVF SVIATYYYAY
IIKQLASNLY NNNTNVIATP INSTLGFIIS ILMVILITFY MYLPTLLDGL TLLHS