NU4M_DEBHA
ID NU4M_DEBHA Reviewed; 467 AA.
AC A9RAH8;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=NADH-ubiquinone oxidoreductase chain 4;
DE EC=7.1.1.2;
DE AltName: Full=NADH dehydrogenase subunit 4;
GN Name=ND4;
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 membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the complex I subunit 4 family. {ECO:0000305}.
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DR EMBL; DQ508940; ABF58079.1; -; Genomic_DNA.
DR RefSeq; YP_001621430.1; NC_010166.1.
DR AlphaFoldDB; A9RAH8; -.
DR SMR; A9RAH8; -.
DR STRING; 284592.A9RAH8; -.
DR GeneID; 5845852; -.
DR KEGG; dha:ND4; -.
DR InParanoid; A9RAH8; -.
DR Proteomes; UP000000599; Mitochondrion.
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 GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR InterPro; IPR010227; NADH_Q_OxRdtase_chainM/4.
DR InterPro; IPR003918; NADH_UbQ_OxRdtase.
DR InterPro; IPR001750; ND/Mrp_mem.
DR PANTHER; PTHR43507; PTHR43507; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR PRINTS; PR01437; NUOXDRDTASE4.
DR TIGRFAMs; TIGR01972; NDH_I_M; 1.
PE 3: Inferred from homology;
KW Electron transport; Membrane; Mitochondrion; NAD; Reference proteome;
KW Respiratory chain; Translocase; Transmembrane; Transmembrane helix;
KW Transport; Ubiquinone.
FT CHAIN 1..467
FT /note="NADH-ubiquinone oxidoreductase chain 4"
FT /id="PRO_0000355053"
FT TRANSMEM 21..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 467 AA; 52759 MW; EDD823BCC6A7D995 CRC64;
MTMLFVIFSG LTSMTSRLVN SMSKHMFTVA SMLMAMPTLY DWEEIDVYYT SDGMADVLML
LTMYMLPLSM ISNWNNMKST LYFELVLNLG MMLLINFMCQ DMTSFYMYFE ASLAPLFMLM
GLYGAANRDK AADYVLMYTL FSSLFMLLAM ALYEVMLDNT DYQATSLLVL SLDLQCMLFL
AMSMGIAVKT PLAPLHTWLP VVHSESPLAG SMLLAGMILK LAVFAMIRLI LPTLSDASVT
YTPFVYVMCV MTMMYTSIIT LRQTDLKVII AYSSISHMAV CMLGMLSNTM TGITGSLVLC
IAHGFVSPGL FMMVGGMLYD RYHNRLMYYF QGLISYMPYL SVYFMMLSFC NMGTPLSINF
IGEMLSLTGA INRAPVLGAM AALSVLLSAC YQMKLTNRLT GGIKTPYMSL TSDCTYRETV
LMITLIVPTM FLGFFPSWVM DFLWDAPNLL YMFMVYRTFI KMSIPWL
