ID   NDUS1_SOLTU             Reviewed;         738 AA.
AC   Q43644;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   24-JAN-2024, entry version 149.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 1, mitochondrial;
DE            EC=7.1.1.2;
DE   AltName: Full=76 kDa mitochondrial complex I subunit;
DE   AltName: Full=Complex I-76kD;
DE            Short=CI-76kD;
DE   AltName: Full=NADH-ubiquinone oxidoreductase 76 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=9615461; DOI=10.1093/oxfordjournals.pcp.a029380;
RA   Rasmusson A.G., Heiser V., Irrgang K.D., Brennicke A., Grohmann L.;
RT   "Molecular characterisation of the 76 kDa iron-sulphur protein subunit of
RT   potato mitochondrial complex I.";
RL   Plant Cell Physiol. 39:373-381(1998).
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). This is the largest subunit of complex I and it is a
CC       component of the iron-sulfur (IP) fragment of the enzyme. It may form
CC       part of the active site crevice where NADH is oxidized (By similarity).
CC       {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=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250};
CC       Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000250};
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 {ECO:0000250}.
CC       Note=Matrix and cytoplasmic side of the mitochondrial inner membrane.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the complex I 75 kDa subunit family.
CC       {ECO:0000305}.
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DR   EMBL; X85808; CAA59818.1; -; mRNA.
DR   PIR; S52737; S52737.
DR   RefSeq; NP_001275317.1; NM_001288388.1.
DR   AlphaFoldDB; Q43644; -.
DR   SMR; Q43644; -.
DR   IntAct; Q43644; 1.
DR   STRING; 4113.Q43644; -.
DR   CarbonylDB; Q43644; -.
DR   PaxDb; 4113-PGSC0003DMT400034638; -.
DR   ProMEX; Q43644; -.
DR   GeneID; 102594243; -.
DR   KEGG; sot:102594243; -.
DR   eggNOG; KOG2282; Eukaryota.
DR   InParanoid; Q43644; -.
DR   OrthoDB; 19999at2759; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; Q43644; baseline.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
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:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR   CDD; cd00207; fer2; 1.
DR   CDD; cd02773; MopB_Res-Cmplx1_Nad11; 1.
DR   Gene3D; 3.10.20.740; -; 1.
DR   Gene3D; 3.30.70.20; -; 1.
DR   Gene3D; 3.40.50.740; -; 2.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR   InterPro; IPR000283; NADH_UbQ_OxRdtase_75kDa_su_CS.
DR   InterPro; IPR010228; NADH_UbQ_OxRdtase_Gsu.
DR   InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
DR   InterPro; IPR015405; NDUFS1-like_C.
DR   NCBIfam; TIGR01973; NuoG; 1.
DR   PANTHER; PTHR43105:SF13; NADH-UBIQUINONE OXIDOREDUCTASE 75 KDA SUBUNIT, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR   Pfam; PF13510; Fer2_4; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR   Pfam; PF09326; NADH_dhqG_C; 1.
DR   SMART; SM00929; NADH-G_4Fe-4S_3; 1.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS51839; 4FE4S_HC3; 1.
DR   PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR   PROSITE; PS00641; COMPLEX1_75K_1; 1.
DR   PROSITE; PS00642; COMPLEX1_75K_2; 1.
DR   PROSITE; PS00643; COMPLEX1_75K_3; 1.
PE   2: Evidence at transcript level;
KW   2Fe-2S; 4Fe-4S; Electron transport; Iron; Iron-sulfur; Membrane;
KW   Metal-binding; Mitochondrion; Mitochondrion inner membrane; NAD;
KW   Oxidoreductase; Reference proteome; Respiratory chain; Transit peptide;
KW   Translocase; Transport; Ubiquinone.
FT   TRANSIT         1..27
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           28..738
FT                   /note="NADH dehydrogenase [ubiquinone] iron-sulfur protein
FT                   1, mitochondrial"
FT                   /id="PRO_0000019973"
FT   DOMAIN          66..144
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   DOMAIN          144..183
FT                   /note="4Fe-4S His(Cys)3-ligated-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT   DOMAIN          281..337
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT   BINDING         100
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
FT   BINDING         111
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
FT   BINDING         114
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
FT   BINDING         128
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
FT   BINDING         160
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT   BINDING         164
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT   BINDING         167
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT   BINDING         173
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT   BINDING         212
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         215
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         218
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         262
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   738 AA;  79970 MW;  4AA955A62EEAD2E8 CRC64;
     MGLGLLASRA LRSSRIIRNS TRTIVSTPEL KNADAAAAAA AADAPSDLPK RHPVGGARVH
     LPNPEDVIEV FVDGYPVKIP KGMTVLQACE IAGVDIPRFC YHSRLSIAGN CRMCLVEVEK
     SPKPVASCAM PALPGMKIKT DTPIAKKARE GVMEFLLMNH PLDCPICDQG GECDLQDQSM
     AFGSDRGRFT EMKRSVVDKN LGPLVKTVMT RCIQCTRCVR FASEVAGVED LGMLGRGSGE
     EIGTYVEKLM TSELSGNVID ICPVGALTSK PFAFKARNWE LKGTESIDVT DAVGSNIRID
     SRGPEVMRVV PRLNEDINEE WISDKTRFFY DGLKRQRLND PMIRGADGRF QAVSWRDALA
     IVAEVMHQIK PEEIVGVAGK LSDAESMMAL KDLLNKMGSN NIFCEGNGMH PNADLRSGYI
     MNTSISGLEK ADAFLLVGTQ PRVEAAMVNA RIHKTVKATN AKVGYVGPAA DFNYDHEHLG
     TDPQTLVEIA EGRHPFSSAL KNAKNPVIIV GAGVFDRDDK DAVFAAVDTI AKNNNVVRPD
     WNGLNVLLLN AAQVAALDLG LVPESDKCIE SAKFVYLMGA DDVNLDKLPD DAFVVYQGHH
     GDRGVYRANV ILPASAFTEK EGIYENTEGC AQITLPAVPT VGDARDDWKI VRALSEVAGV
     GLPYDSLGAI RSRIKTVAPN LLEVDERQPA TFSTSLRPEV SQKVSATPFT PAVENFYMTD
     AITRASKIMA QCSALLKK
//