ID   NDUS2_ACACA             Reviewed;         401 AA.
AC   Q37384;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=NADH-ubiquinone oxidoreductase 49 kDa subunit;
DE            EC=7.1.1.2;
DE   AltName: Full=NADH dehydrogenase subunit 7;
GN   Name=NAD7;
OS   Acanthamoeba castellanii (Amoeba).
OG   Mitochondrion.
OC   Eukaryota; Amoebozoa; Discosea; Longamoebia; Centramoebida;
OC   Acanthamoebidae; Acanthamoeba.
OX   NCBI_TaxID=5755;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 30010 / Neff;
RX   PubMed=7844823; DOI=10.1006/jmbi.1994.0043;
RA   Burger G., Plante I., Lonergan K.M., Gray M.W.;
RT   "The mitochondrial DNA of the amoeboid protozoon, Acanthamoeba castellanii:
RT   complete sequence, gene content and genome organization.";
RL   J. Mol. Biol. 245:522-537(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). Component of the iron-sulfur (IP) fragment of the enzyme.
CC       {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.
CC   -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U12386; AAD11854.1; -; Genomic_DNA.
DR   PIR; S53862; S53862.
DR   RefSeq; NP_042561.1; NC_001637.1.
DR   AlphaFoldDB; Q37384; -.
DR   SMR; Q37384; -.
DR   PRIDE; Q37384; -.
DR   GeneID; 1734056; -.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR   Gene3D; 1.10.645.10; -; 1.
DR   HAMAP; MF_01358; NDH1_NuoD; 1.
DR   InterPro; IPR001135; NADH_Q_OxRdtase_suD.
DR   InterPro; IPR014029; NADH_UbQ_OxRdtase_49kDa_CS.
DR   InterPro; IPR022885; NDH1_su_D/H.
DR   InterPro; IPR029014; NiFe-Hase_large.
DR   PANTHER; PTHR11993; PTHR11993; 1.
DR   Pfam; PF00346; Complex1_49kDa; 1.
DR   SUPFAM; SSF56762; SSF56762; 1.
DR   TIGRFAMs; TIGR01962; NuoD; 1.
DR   PROSITE; PS00535; COMPLEX1_49K; 1.
PE   3: Inferred from homology;
KW   Electron transport; Mitochondrion; NAD; Oxidoreductase; Respiratory chain;
KW   Translocase; Transport; Ubiquinone.
FT   CHAIN           1..401
FT                   /note="NADH-ubiquinone oxidoreductase 49 kDa subunit"
FT                   /id="PRO_0000118587"
SQ   SEQUENCE   401 AA;  46096 MW;  BA929F88024C0DF8 CRC64;
     MRKNQISPYI KTSKIKNFTM NFGPQHPAAH GVLRLILELD GELVRKADPH IGLLHRGTEK
     LIEYKTYIQA LPYFDRLDYV SMMSQEHAYS LAIEKLLNCN VPIRAQYIRV IYSELTRILN
     HILAVTTHAM DVGALTPFLW LFEEREKLME FYERVSGARM HAAYIRPGGV AQDFPLGLWN
     DIMQFVEQFF WRLVEVEELL NGNRIWKQRL VDVGIVTAEE ALSHGFSGVM LRGSGIAWDL
     RKNNPYEVYN KLNFNIPIGK NGDCYDRYLI RVYEMYESLN IIKQCLTAMP AGLIKVNDKK
     ITPPERTDMK YSMESLIHHF KLYSEGFNVP ENETYACVEA PKGEFGVYVV SDGSNKPYRC
     KIKAPGFLHL QSLNSMSKGH MIADVVTIIG TQDIVFGEID R