ID   NDUS3_BETTR             Reviewed;         192 AA.
AC   Q33994;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   13-SEP-2023, 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   Beta trigyna (Caucasian wild beet).
OG   Mitochondrion.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Betoideae; Beta.
OX   NCBI_TaxID=19769;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. SP753012-O; TISSUE=Leaf;
RX   PubMed=7736615; DOI=10.1007/bf00326162;
RA   Kubo T., Yanai Y., Kinoshita T., Mikami T.;
RT   "The chloroplast trnP-trnW-petG gene cluster in the mitochondrial genomes
RT   of Beta vulgaris, B. trigyna and B. webbiana: evolutionary aspects.";
RL   Curr. Genet. 27:285-289(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). {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:0000250}, 38 {ECO:0000250}, 100
CC       {ECO:0000250}, 110 {ECO:0000250}, 123 {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the complex I 30 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; D38017; BAA07214.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; Q33994; -.
DR   SMR; Q33994; -.
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; NADH:ubiquinone oxidoreductase, 30kDa subunit; 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   NCBIfam; TIGR01961; NuoC_fam; 1.
DR   PANTHER; PTHR10884:SF14; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 3, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR10884; NADH DEHYDROGENASE UBIQUINONE IRON-SULFUR PROTEIN 3; 1.
DR   Pfam; PF00329; Complex1_30kDa; 1.
DR   SUPFAM; SSF143243; Nqo5-like; 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; RNA editing; Translocase;
KW   Transport; Ubiquinone.
FT   CHAIN           1..192
FT                   /note="NADH dehydrogenase [ubiquinone] iron-sulfur protein
FT                   3"
FT                   /id="PRO_0000118638"
SQ   SEQUENCE   192 AA;  23109 MW;  12C3F3F5AA32A925 CRC64;
     MDNQFIFKYS WETLPKKWVK KIEKSEHGNR FDTNTDYLFQ LLCFLKLHTY TRFQVLIDIC
     GVDYPSRKRR FEVVYNLLST RYNSRIRLQT SADEVTRISS VVSLFPSAGW WEREVWDMFG
     VSFINHPDLR RILTDYGFEG HPLRKDFPLS GYVEVRYDDP EKRVVSEPIE MTQEFRYFDF
     ASPWEQRNGN EG
//