NDUS1_ACACA
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 03-AUG-2022, entry version 114.
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}.
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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 PRIDE; 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 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 Pfam; PF00384; Molybdopterin; 2.
DR Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR SMART; SM00929; NADH-G_4Fe-4S_3; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR TIGRFAMs; TIGR01973; NuoG; 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
