NDUS3_MARPO
ID NDUS3_MARPO Reviewed; 195 AA.
AC P34944;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 3;
DE EC=7.1.1.2;
DE AltName: Full=NADH dehydrogenase subunit 9;
GN Name=NAD9;
OS Marchantia polymorpha (Liverwort) (Marchantia aquatica).
OG Mitochondrion.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=3197;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1731062; DOI=10.1016/0022-2836(92)90708-r;
RA Oda K., Yamato K., Ohta E., Nakamura Y., Takemura M., Nozato N., Akashi K.,
RA Kanegae T., Ogura Y., Kohchi T., Ohyama K.;
RT "Gene organization deduced from the complete sequence of liverwort
RT Marchantia polymorpha mitochondrial DNA. A primitive form of plant
RT mitochondrial genome.";
RL J. Mol. Biol. 223:1-7(1992).
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 -!- SUBUNIT: Complex I is composed of about 45 different subunits. This is
CC a component of the iron-sulfur (IP) fragment of the enzyme (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane.
CC -!- SIMILARITY: Belongs to the complex I 30 kDa subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC09443.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M68929; AAC09443.1; ALT_INIT; Genomic_DNA.
DR PIR; S25996; S25996.
DR RefSeq; NP_054446.1; NC_001660.1.
DR AlphaFoldDB; P34944; -.
DR SMR; P34944; -.
DR GeneID; 2948426; -.
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 Gene3D; 3.30.460.80; -; 1.
DR HAMAP; MF_01357; NDH1_NuoC; 1.
DR InterPro; IPR010218; NADH_DH_suC.
DR InterPro; IPR037232; NADH_quin_OxRdtase_su_C/D-like.
DR InterPro; IPR001268; NADH_UbQ_OxRdtase_30kDa_su.
DR InterPro; IPR020396; NADH_UbQ_OxRdtase_CS.
DR Pfam; PF00329; Complex1_30kDa; 1.
DR SUPFAM; SSF143243; SSF143243; 1.
DR TIGRFAMs; TIGR01961; NuoC_fam; 1.
DR PROSITE; PS00542; COMPLEX1_30K; 1.
PE 3: Inferred from homology;
KW Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW NAD; Oxidoreductase; Respiratory chain; Translocase; Transport; Ubiquinone.
FT CHAIN 1..195
FT /note="NADH dehydrogenase [ubiquinone] iron-sulfur protein
FT 3"
FT /id="PRO_0000118641"
SQ SEQUENCE 195 AA; 23354 MW; D123890812812ABB CRC64;
MDNQLFFKSL IATLPKWIHK CQTSKHENIL YTNPNSLFQL LYFLKYHTNT RFKVLIDICG
VDYPSRKRRF EVVYNLLSID YNTRIRILTS VDEITPICSV VSIFPSAGWW ERETWDMFGV
YFSNHPDLRR ILTDYGFEGH PLRKDFPLSG YVEVRYDDSE KRVVSEPIEM TQEFRYFDFA
SPWEQMSRSD ESNQK