NDUS8_SOLTU
ID NDUS8_SOLTU Reviewed; 229 AA.
AC P80269; Q43849; Q43850;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial;
DE EC=7.1.1.2;
DE AltName: Full=Complex I-28.5kD;
DE Short=CI-28.5kD;
DE AltName: Full=NADH-ubiquinone oxidoreductase 28.5 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] (ALLELES TYKY1 AND TYKY2).
RC STRAIN=cv. Desiree; TISSUE=Leaf;
RX PubMed=9037104; DOI=10.1007/s004380050342;
RA Schmidt-Bleek K., Heiser V., Thieck O., Brennicke A., Grohmann L.;
RT "The 28.5-kDa iron-sulfur protein of mitochondrial complex I is encoded in
RT the nucleus in plants.";
RL Mol. Gen. Genet. 253:448-454(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44;
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
RN [3]
RP PROTEIN SEQUENCE OF 42-65, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Bintje; TISSUE=Tuber;
RX PubMed=8294484; DOI=10.1016/s0021-9258(17)42163-6;
RA Herz U., Schroeder W., Liddell A., Leaver C.J., Brennicke A., Grohmann L.;
RT "Purification of the NADH:ubiquinone oxidoreductase (complex I) of the
RT respiratory chain from the inner mitochondrial membrane of Solanum
RT tuberosum.";
RL J. Biol. Chem. 269:2263-2269(1994).
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). May donate electrons to ubiquinone. {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:0000250};
CC Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000250};
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 {ECO:0000269|PubMed:8294484}; Peripheral membrane protein
CC {ECO:0000305}; Matrix side {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Lowest expression found in storage tissues of
CC tubers. Higher expression in older leaves than younger ones. Highest
CC expression found in flowers.
CC -!- POLYMORPHISM: There are two alleles; TYKY1 (shown here) and TYKY2.
CC {ECO:0000305|PubMed:9037104}.
CC -!- SIMILARITY: Belongs to the complex I 23 kDa subunit family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally reported that TYKY1 and TYKY2 were two
CC different genes. {ECO:0000305|PubMed:9037104}.
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DR EMBL; X84319; CAA59062.1; -; mRNA.
DR EMBL; X84320; CAA59063.1; -; mRNA.
DR PIR; S52385; S52385.
DR PIR; S52386; S52386.
DR RefSeq; NP_001275214.1; NM_001288285.1.
DR AlphaFoldDB; P80269; -.
DR SMR; P80269; -.
DR STRING; 4113.PGSC0003DMT400084285; -.
DR EnsemblPlants; PGSC0003DMT400084285; PGSC0003DMT400084285; PGSC0003DMG400033912.
DR EnsemblPlants; RHC10H1G1669.2.1; RHC10H1G1669.2.1; RHC10H1G1669.2.
DR GeneID; 102589342; -.
DR Gramene; PGSC0003DMT400084285; PGSC0003DMT400084285; PGSC0003DMG400033912.
DR Gramene; RHC10H1G1669.2.1; RHC10H1G1669.2.1; RHC10H1G1669.2.
DR KEGG; sot:102589342; -.
DR eggNOG; KOG3256; Eukaryota.
DR HOGENOM; CLU_067218_5_0_1; -.
DR InParanoid; P80269; -.
DR OMA; TIMYPYE; -.
DR OrthoDB; 1283957at2759; -.
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; IEA:UniProtKB-EC.
DR GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IBA:GO_Central.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IBA:GO_Central.
DR HAMAP; MF_01351; NDH1_NuoI; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR010226; NADH_quinone_OxRdtase_chainI.
DR PANTHER; PTHR10849; PTHR10849; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR TIGRFAMs; TIGR01971; NuoI; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 1: Evidence at protein level;
KW 4Fe-4S; Direct protein sequencing; Electron transport; Iron; Iron-sulfur;
KW Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane; NAD;
KW Oxidoreductase; Reference proteome; Repeat; Respiratory chain;
KW Transit peptide; Translocase; Transport; Ubiquinone.
FT TRANSIT 1..41
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:8294484"
FT CHAIN 42..229
FT /note="NADH dehydrogenase [ubiquinone] iron-sulfur protein
FT 8, mitochondrial"
FT /id="PRO_0000020017"
FT DOMAIN 121..150
FT /note="4Fe-4S ferredoxin-type 1"
FT DOMAIN 160..189
FT /note="4Fe-4S ferredoxin-type 2"
FT BINDING 130
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 140
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT VARIANT 23..26
FT /note="HTIE -> QAWQ (in allele TYKY2)"
FT VARIANT 30..33
FT /note="GYNR -> TPNG (in allele TYKY2)"
FT VARIANT 57
FT /note="E -> R (in strain: cv. Bintje)"
FT VARIANT 62
FT /note="E -> K (in strain: cv. Bintje)"
FT VARIANT 65
FT /note="K -> T (in strain: cv. Bintje)"
FT VARIANT 121
FT /note="R -> H (in allele TYKY2)"
FT VARIANT 216
FT /note="T -> I (in allele TYKY2)"
SQ SEQUENCE 229 AA; 26378 MW; D995415DBE064A93 CRC64;
MAAILARKSL SALRSRQLVL AGHTIEGTNG YNRTLLGTRS FATKHSFSTD KDDEEREQLA
KELSKDWNSV FERSINTLFL TEMVRGLMLT LKYFFEKKVT INYPFEKGPL SPRFRGEHAL
RRYATGEERC IACKLCEAIC PAQAITIEAE EREDGSRRTT RYDIDMTKCI YCGFCQEACP
VDAIVEGPNF EFATETHEEL LYDKEKLLEN GDRWETEIAE NLRSESLYR
