ID NDUS1_ACACA Reviewed; 675 AA. AC Q37373; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 24-JAN-2024, entry version 119. DE RecName: Full=NADH-ubiquinone oxidoreductase 75 kDa subunit; DE EC=7.1.1.2; DE AltName: Full=Complex I-75kD; DE Short=CI-75kD; DE AltName: Full=NADH dehydrogenase subunit 11; GN Name=NAD11; OS Acanthamoeba castellanii (Amoeba). OG Mitochondrion. OC Eukaryota; Amoebozoa; Discosea; Longamoebia; Centramoebida; OC Acanthamoebidae; Acanthamoeba. OX NCBI_TaxID=5755; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 30010 / Neff; RX PubMed=7844823; DOI=10.1006/jmbi.1994.0043; RA Burger G., Plante I., Lonergan K.M., Gray M.W.; RT "The mitochondrial DNA of the amoeboid protozoon, Acanthamoeba castellanii: RT complete sequence, gene content and genome organization."; RL J. Mol. Biol. 245:522-537(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). 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 30 different subunits. CC {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}. 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; U12386; AAD11824.1; -; Genomic_DNA. DR PIR; S53832; S53832. DR RefSeq; NP_042531.1; NC_001637.1. DR AlphaFoldDB; Q37373; -. DR SMR; Q37373; -. DR GeneID; 1734026; -. 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; cd02774; MopB_Res-Cmplx1_Nad11-M; 1. DR Gene3D; 3.10.20.740; -; 1. DR Gene3D; 3.30.70.20; -; 1. DR Gene3D; 3.40.50.740; -; 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 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 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; PS51839; 4FE4S_HC3; 1. DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1. DR PROSITE; PS00642; COMPLEX1_75K_2; 1. DR PROSITE; PS00643; COMPLEX1_75K_3; 1. PE 3: Inferred from homology; KW 2Fe-2S; 4Fe-4S; Electron transport; Iron; Iron-sulfur; Membrane; KW Metal-binding; Mitochondrion; Mitochondrion inner membrane; NAD; KW Oxidoreductase; Respiratory chain; Translocase; Transport; Ubiquinone. FT CHAIN 1..675 FT /note="NADH-ubiquinone oxidoreductase 75 kDa subunit" FT /id="PRO_0000118536" FT DOMAIN 2..80 FT /note="2Fe-2S ferredoxin-type" FT DOMAIN 80..119 FT /note="4Fe-4S His(Cys)3-ligated-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184" FT DOMAIN 217..273 FT /note="4Fe-4S Mo/W bis-MGD-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004" FT BINDING 36 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000250" FT BINDING 47 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000250" FT BINDING 50 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000250" FT BINDING 64 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000250" FT BINDING 96 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184" FT BINDING 100 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184" FT BINDING 103 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184" FT BINDING 109 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184" FT BINDING 148 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 151 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 154 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 198 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000250" SQ SEQUENCE 675 AA; 77554 MW; 3870F3BC9E8B9807 CRC64; MKNISFKVND FQYTINNKLT LIQACLKNKV DISRFCFHEK LSIAGNCRMC LVEDLKQVKP LASCAINVSN SMNIYTNTLK VKKARESVLE FLLANHPLDC PICDQGGECD LQDQSVVFGS DRGRFYEFKR SVEDKDCGPL IKTIMNRCIH CTRCVRFSNE VAGVNILGVT GRGSKMEIGF YIENLMRSEL SGNVIDLCPV GALTSKPFAF TSRPWELKSY NSIDVLDSLH SNIRVDIRGT KIMRILPRVN SELNEDWITD KIRFSYDSFR RQRLYDPMVK ISGSFLKIGW KKAMLFIKKF FCNFLGFNHS SFIPLRGYIG DYLDLETIYT FKKFLLLNGS NFFLPSSSYN DLTALYSFNT PLTRLDEGDF CILLDVNLRV ELPIVNSRIK QLVSKKMLPV FVLGFYSNFN YFVKHISNSS KTLLHVLEGS HWLSAKISKK FSSKPIFLIG DSSSLLKGSL IVPLFNFTNV ICDNWNGLNI ISNDSSYLST KEFNLSSSHS QNSHLLNFPI NFVLNYDKAV LVDSSAFQIY QGHHGDTNAI NSNLIFPSTS FIEKNSFYSN SLAIVQKTKK ILFSPGNSRD DWKILNALID NFGFSYFKVR NSFDLVSFLS ESTPFILYKR SFSFKCFGFY EQLVYHFFNY FSVNNNYYIY DSITRNSKIM SLCFNKFKMK GYNFF //