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 27-MAR-2024, entry version 145. 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}. 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; 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.P80269; -. DR PaxDb; 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; AIRYDID; -. DR OrthoDB; 176717at2759; -. 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: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 Gene3D; 3.30.70.3270; -; 1. 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 NCBIfam; TIGR01971; NuoI; 1. DR PANTHER; PTHR10849:SF20; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 8, MITOCHONDRIAL; 1. DR PANTHER; PTHR10849; NADH DEHYDROGENASE UBIQUINONE IRON-SULFUR PROTEIN 8, MITOCHONDRIAL; 1. DR Pfam; PF12838; Fer4_7; 1. DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 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 //