ID   NDUS2_PROWI             Reviewed;         400 AA.
AC   Q37619;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-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   Prototheca wickerhamii.
OG   Mitochondrion.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Chlorellales; Chlorellaceae; Prototheca.
OX   NCBI_TaxID=3111;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=263-11;
RX   PubMed=8133522; DOI=10.1006/jmbi.1994.1210;
RA   Wolff G., Plante I., Lang B.F., Kueck U., Burger G.;
RT   "Complete sequence of the mitochondrial DNA of the chlorophyte alga
RT   Prototheca wickerhamii. Gene content and genome organization.";
RL   J. Mol. Biol. 237:75-86(1994).
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       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}.
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DR   EMBL; U02970; AAD12640.1; -; Genomic_DNA.
DR   PIR; T11921; T11921.
DR   RefSeq; NP_042252.1; NC_001613.1.
DR   AlphaFoldDB; Q37619; -.
DR   SMR; Q37619; -.
DR   PRIDE; Q37619; -.
DR   GeneID; 802126; -.
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..400
FT                   /note="NADH-ubiquinone oxidoreductase 49 kDa subunit"
FT                   /id="PRO_0000118591"
SQ   SEQUENCE   400 AA;  45810 MW;  7227458FE80BC9D2 CRC64;
     MALEKIITAP KYKNFTINFG PQHPAAHGVL RLVLEMNGEV VQRSDPHIGL LHRGTEKLIE
     YKNYLQALPY FDRLDYVSMM CQEHAYSLAV EKLLNISKDI PLRAQYIRVL FSEITRILNH
     LLAVTCHAMD VGALTPFLWG FEEREKLMEF YERVSGARMH AAYIRPGGVA LDLPLGLCED
     IYKFSKQFAS RIDEIEEMLT SNRIWKQRLV DVGVVSAEQA LDWSFSGVLL RGSGIAWDLR
     KTQPYEVYDR MKFNIPVGTR GDCYDRYLIR VQEMRESLRI VMQTINEMSK GIIRLDDRKI
     TPPTRDQMKQ SMESLIHHFK FYTGGFVVPA GETYTAVEAP KGEFGVYLVS NGTSKPYRCK
     IRAPGFAHLQ GLDFMARNHM LADVVTIIGT QDIVFGEVDR