NDUS1_DICDI
ID NDUS1_DICDI Reviewed; 688 AA.
AC Q34312;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 129.
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;
GN Name=nad11; Synonyms=ndufs1; ORFNames=DDB_G0294052;
OS Dictyostelium discoideum (Slime mold).
OG Mitochondrion.
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=X22;
RX PubMed=7807547; DOI=10.1007/bf00160403;
RA Cole R.A., Williams K.L.;
RT "The Dictyostelium discoideum mitochondrial genome: a primordial system
RT using the universal code and encoding hydrophilic proteins atypical of
RT metazoan mitochondrial DNA.";
RL J. Mol. Evol. 39:579-588(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX3;
RX PubMed=10821186; DOI=10.1007/pl00008685;
RA Ogawa S., Yoshino R., Angata K., Iwamoto M., Pi M., Kuroe K., Matsuo K.,
RA Morio T., Urushihara H., Yanagisawa K., Tanaka Y.;
RT "The mitochondrial DNA of Dictyostelium discoideum: complete sequence, gene
RT content and genome organization.";
RL Mol. Gen. Genet. 263:514-519(2000).
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.
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; U02291; AAA77667.1; -; Genomic_DNA.
DR EMBL; AB000109; BAA78086.1; -; Genomic_DNA.
DR PIR; T43783; T43783.
DR RefSeq; NP_050104.1; NC_000895.1.
DR AlphaFoldDB; Q34312; -.
DR SMR; Q34312; -.
DR GeneID; 2193950; -.
DR KEGG; ddi:DidioMp37; -.
DR dictyBase; DDB_G0294052; nad11.
DR InParanoid; Q34312; -.
DR OMA; GTHAFCK; -.
DR PhylomeDB; Q34312; -.
DR Reactome; R-DDI-6799198; Complex I biogenesis.
DR PRO; PR:Q34312; -.
DR Proteomes; UP000002195; Mitochondrion.
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; IBA:GO_Central.
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; 1.
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; 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 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; Reference proteome; Respiratory chain; Translocase;
KW Transport; Ubiquinone.
FT CHAIN 1..688
FT /note="NADH-ubiquinone oxidoreductase 75 kDa subunit"
FT /id="PRO_0000327377"
FT DOMAIN 1..85
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 85..124
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT DOMAIN 223..279
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 38
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 52
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT BINDING 105
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT BINDING 108
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT BINDING 114
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT BINDING 153
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 688 AA; 79838 MW; 7091BF41C8A055F6 CRC64;
MIIRFKINEI ECEVNEEKED ITILQACTAN GIEIPRFCYH EKLTIAGNCR MCLVYVTNEE
KLLAACGIPL DENFDDESIE TEIDEILKAR EGVMEFLLIN HPLDCPICDQ GGECDLQEQT
LAYGLDTGRF YIKKRAVEIK TFGRLIKGIM TRCIHCTRCV RFLTEIAGVN ELGVLGRGYN
MEIGTYKKNV MIESELSGNI IDLCPVGALT SAVYAYKGRP WELKNIKGID IFDTLLTPIN
YQVKGGEIFR ILPRINDRIN EEWITDKVRF HYESYKIIEK IRKETPSYKI QANKFIELTW
KTALKMVFKV LLNKKNKVDL IIGSKINSTN LRIYKELMNR LGSKNYITEN GLMFKKFNYD
LRENYINSND LYNVDKNDLV LLCGINLRVE SPLLNIKLRN VNFGDDEIES VKKIGIIGNK
FDWKHESEYI GATLNSMLKL FEGRLPYCQQ IKKSKAPLII VGPSLLTRIS LTLQEMRAIF
MKACNLKPEN ILIITQGANF GMALEEGLFK EKFSIGGNVL YSIDSNEVQV TNKINYVIYQ
GIINDKFENK IDLYLPSKHY FEDFEGDREV YMNTFGQRSE IEKLSISKGN KIKENSMIGY
IQLMYLNNKE MTRKEKEQKD IKLSYREMKK EEKRKIKVNK YLTINNIIEN YYMTDINIRL
SKNLMITGQL RKEKKIMEAG IWKNRKCI
