ID   NDUS3_BETVU             Reviewed;         192 AA.
AC   Q37787;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   24-OCT-2003, sequence version 3.
DT   25-MAY-2022, entry version 105.
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   Beta vulgaris (Sugar beet).
OG   Mitochondrion.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Betoideae; Beta.
OX   NCBI_TaxID=161934;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND RNA EDITING.
RC   STRAIN=cv. TK81-O; TISSUE=Tap root;
RX   PubMed=8246903; DOI=10.1007/bf00284703;
RA   Kubo T., Mikami T., Kinoshita T.;
RT   "The sugar beet mitochondrial genome contains an ORF sharing sequence
RT   homology with the gene for the 30 kDa subunit of bovine mitochondrial
RT   complex I.";
RL   Mol. Gen. Genet. 241:479-481(1993).
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; Peripheral membrane
CC       protein; Matrix side.
CC   -!- RNA EDITING: Modified_positions=31 {ECO:0000269|PubMed:8246903}, 38
CC       {ECO:0000269|PubMed:8246903}, 100 {ECO:0000269|PubMed:8246903}, 110
CC       {ECO:0000269|PubMed:8246903}, 123 {ECO:0000269|PubMed:8246903};
CC   -!- SIMILARITY: Belongs to the complex I 30 kDa subunit family.
CC       {ECO:0000305}.
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DR   EMBL; D38016; BAA07213.2; -; Genomic_DNA.
DR   PIR; S62130; S62130.
DR   RefSeq; NP_063974.2; NC_002511.2.
DR   AlphaFoldDB; Q37787; -.
DR   SMR; Q37787; -.
DR   GeneID; 809510; -.
DR   KEGG; bvg:809510; -.
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   2: Evidence at transcript level;
KW   Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   NAD; Oxidoreductase; Respiratory chain; RNA editing; Translocase;
KW   Transport; Ubiquinone.
FT   CHAIN           1..192
FT                   /note="NADH dehydrogenase [ubiquinone] iron-sulfur protein
FT                   3"
FT                   /id="PRO_0000118639"
SQ   SEQUENCE   192 AA;  23151 MW;  6D111D64E4C71CCE CRC64;
     MDNQFIFKYS WETLPKKWVK KIEKSEHGNR FDTNTDYLFQ LLCFLKLHTY TRFQVLIDIC
     GVDYPSRKRR FEVVYNLLST RYNSRIRLQT CADEVTRISL VVSLFPSAGW WEREVWDMFG
     VSFINHPDLR RILTDYGFEG HPLRKDFPLS GYVEVRYDDP EKRVVSEPIE MTQEFRYFDF
     ASPWEQRNGN EG