ID   NDUS7_SOLTU             Reviewed;         213 AA.
AC   Q43844;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial;
DE            EC=7.1.1.2;
DE   AltName: Full=Complex I-20kD;
DE            Short=CI-20kD;
DE   AltName: Full=NADH-ubiquinone oxidoreductase 20 kDa subunit;
DE   Flags: Precursor;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Desiree; TISSUE=Leaf;
RX   PubMed=8914535; DOI=10.1007/bf00040836;
RA   Heiser V., Grohmann L., Brennicke A.;
RT   "The plant mitochondrial 22 kDa (PSST) subunit of respiratory chain complex
RT   I is encoded by a nuclear gene with enhanced transcript levels in
RT   flowers.";
RL   Plant Mol. Biol. 31:1195-1204(1996).
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   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305};
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.
CC   -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family.
CC       {ECO:0000305}.
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DR   EMBL; X96671; CAA65451.1; -; mRNA.
DR   PIR; T07603; T07603.
DR   AlphaFoldDB; Q43844; -.
DR   SMR; Q43844; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   GO; GO:0005747; C:mitochondrial respiratory chain complex I; IBA:GO_Central.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IBA:GO_Central.
DR   GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR   GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
DR   GO; GO:0015990; P:electron transport coupled proton transport; IBA:GO_Central.
DR   GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IBA:GO_Central.
DR   HAMAP; MF_01356; NDH1_NuoB; 1.
DR   InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa.
DR   InterPro; IPR006138; NADH_UQ_OxRdtase_20Kd_su.
DR   Pfam; PF01058; Oxidored_q6; 1.
DR   TIGRFAMs; TIGR01957; nuoB_fam; 1.
DR   PROSITE; PS01150; COMPLEX1_20K; 1.
PE   2: Evidence at transcript level;
KW   4Fe-4S; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW   Mitochondrion; NAD; Oxidoreductase; Reference proteome; Respiratory chain;
KW   Transit peptide; Translocase; Transport; Ubiquinone.
FT   TRANSIT         1..31
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..213
FT                   /note="NADH dehydrogenase [ubiquinone] iron-sulfur protein
FT                   7, mitochondrial"
FT                   /id="PRO_0000020035"
FT   REGION          30..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         88
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         89
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         153
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         183
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   213 AA;  23396 MW;  8047FAB323418FCB CRC64;
     MALIARNAKL LTGTAPFLQR AATIHTTLPS LSQQPASSPA TSGGAQPPSM NTPAGISKPA
     EYVISKVDDL MNWARRGSIW PMTFGLACCA VEMMHAGAAR YDFDRFGIIF RPSPRQSDVM
     IVAGTLTNKM APALRKVYDQ MPEPRWVISM GSCANGGGYY HYSYAVVRGC DRIVPVDIYV
     PGCPPTAEAL LYGILQLQKK INRRKDLLMW WTQ