NU1M_DEBHA
ID NU1M_DEBHA Reviewed; 312 AA.
AC A9RAG3;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 56.
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 Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OG Mitochondrion.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=18673395; DOI=10.1111/j.1567-1364.2008.00409.x;
RA Sacerdot C., Casaregola S., Lafontaine I., Tekaia F., Dujon B.,
RA Ozier-Kalogeropoulos O.;
RT "Promiscuous DNA in the nuclear genomes of hemiascomycetous yeasts.";
RL FEMS Yeast Res. 8:846-857(2008).
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; DQ508940; ABF58064.1; -; Genomic_DNA.
DR RefSeq; YP_001621415.1; NC_010166.1.
DR AlphaFoldDB; A9RAG3; -.
DR SMR; A9RAG3; -.
DR STRING; 284592.A9RAG3; -.
DR GeneID; 5845857; -.
DR KEGG; dha:ND1; -.
DR InParanoid; A9RAG3; -.
DR Proteomes; UP000000599; Mitochondrion.
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; Reference proteome; Respiratory chain; Translocase; Transmembrane;
KW Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..312
FT /note="NADH-ubiquinone oxidoreductase chain 1"
FT /id="PRO_0000355050"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 312 AA; 34814 MW; 3102D12DB32B8ECD CRC64;
MNFMELLLFV LSMLLAVAFL TVAERKTLGY MQRRVGPNAV GYYGVLMAMA DAAKLLLKEM
ILPTHADKFM LIMSPMMTLM SALLCWAMIP FGPGITIMDS NYGFMLALAM GSVGVFGSLF
AGWAGNSKYS TIGSMRSTAQ LISYELVLTT VILICMLLTG TMNTSRYVEL QESMWLVVPL
LPLSLMWFMG CVAECARPPF DNVEAESELV SGHMTEYSSS MFVLFFLSEY ASMLFYSTLT
AILFFGGGTG LILGLKANFF AFTYIWVRAA TPRVRYDKLI AMCWIVFLPL LFALALFMPS
LIYIMDGYTF ME