ID   NDUS2_TRYBB             Reviewed;         386 AA.
AC   P21301;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=NADH-ubiquinone oxidoreductase 49 kDa subunit homolog;
DE            EC=7.1.1.2;
DE   AltName: Full=NADH dehydrogenase subunit 7 homolog;
GN   Name=NAD7; Synonyms=MURF 3;
OS   Trypanosoma brucei brucei.
OG   Mitochondrion.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=5702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2393904; DOI=10.1016/0092-8674(90)90265-g;
RA   Koslowsky D.J., Bhat G., Jayarama Perrollaz A.L., Feagin J.E., Stuart K.;
RT   "The MURF3 gene of T. brucei contains multiple domains of extensive editing
RT   and is homologous to a subunit of NADH dehydrogenase.";
RL   Cell 62:901-911(1990).
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; M55645; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; A35693; A35693.
DR   AlphaFoldDB; P21301; -.
DR   SMR; P21301; -.
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   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; 2.
DR   SUPFAM; SSF56762; SSF56762; 1.
DR   PROSITE; PS00535; COMPLEX1_49K; 1.
PE   2: Evidence at transcript level;
KW   Electron transport; Mitochondrion; NAD; Oxidoreductase; Respiratory chain;
KW   Translocase; Transport; Ubiquinone.
FT   CHAIN           1..386
FT                   /note="NADH-ubiquinone oxidoreductase 49 kDa subunit
FT                   homolog"
FT                   /id="PRO_0000118594"
SQ   SEQUENCE   386 AA;  45098 MW;  448F5D52DC572071 CRC64;
     MLFLVVFLHL YRFTFGPQHP AAHGVLCCLL YFCGEFIVYI DCIIGYLHRG TEKLCEYKSV
     EQCLPYFDRL DYVSVCCNEH LLSLCFEYML RCCLSLRCAF MRLLIVEFTR SFNGLLCISC
     MVLDLGCLSP LLWSFEERDK LMTFFDLCCG CRMHLAFMVL LGILDDFVFG FVDFLLLLII
     SCLFVMDCYD LLFVGNRLFY LRLRGLSFFD LYDLVFNSLS GVLSRSLGMV WDCRLFSCYE
     LYFMFCYDYC FCFIGDAFDR LFLRLFDMRM SLLICKQCFF VGFFVFGFVC LFDYLYCDIT
     IETIIMLFYS LWCCCLPGIS FACVEHPKGE YCLLLCFCVG LCSRLRLRCA DFLHICLLDV
     CLRGFLLHDL VAVLGNIDVV FGSVDR