NDUS2_CAEEL
ID NDUS2_CAEEL Reviewed; 482 AA.
AC Q93873;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Probable NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial;
DE EC=7.1.1.2;
DE AltName: Full=Complex I-49kD;
DE Short=CI-49kD;
DE AltName: Full=NADH-ubiquinone oxidoreductase 49 kDa subunit;
DE Flags: Precursor;
GN Name=gas-1; ORFNames=K09A9.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(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). {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 1 [4Fe-4S] cluster. {ECO:0000250};
CC -!- SUBUNIT: Complex I is composed of 45 different subunits. Component of
CC the iron-sulfur (IP) fragment of the enzyme (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Matrix side {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; Z79601; CAB01886.1; -; Genomic_DNA.
DR PIR; T23532; T23532.
DR RefSeq; NP_510569.1; NM_078168.4.
DR AlphaFoldDB; Q93873; -.
DR SMR; Q93873; -.
DR BioGRID; 46540; 45.
DR STRING; 6239.K09A9.5; -.
DR EPD; Q93873; -.
DR PaxDb; Q93873; -.
DR PeptideAtlas; Q93873; -.
DR EnsemblMetazoa; K09A9.5.1; K09A9.5.1; WBGene00001520.
DR GeneID; 181646; -.
DR KEGG; cel:CELE_K09A9.5; -.
DR UCSC; K09A9.5; c. elegans.
DR CTD; 181646; -.
DR WormBase; K09A9.5; CE11980; WBGene00001520; gas-1.
DR eggNOG; KOG2870; Eukaryota.
DR GeneTree; ENSGT00390000009529; -.
DR HOGENOM; CLU_015134_1_1_1; -.
DR InParanoid; Q93873; -.
DR OMA; IMGTSME; -.
DR OrthoDB; 444312at2759; -.
DR PhylomeDB; Q93873; -.
DR Reactome; R-CEL-6799198; Complex I biogenesis.
DR PRO; PR:Q93873; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00001520; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:WormBase.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; ISS:WormBase.
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:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IBA:GO_Central.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IMP:WormBase.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:WormBase.
DR Gene3D; 1.10.645.10; -; 1.
DR HAMAP; MF_01358; NDH1_NuoD; 1.
DR InterPro; IPR001135; NADH_Q_OxRdtase_suD.
DR InterPro; IPR014029; NADH_UbQ_OxRdtase_49kDa_CS.
DR InterPro; IPR022885; NDH1_su_D/H.
DR InterPro; IPR029014; NiFe-Hase_large.
DR PANTHER; PTHR11993; PTHR11993; 1.
DR Pfam; PF00346; Complex1_49kDa; 1.
DR SUPFAM; SSF56762; SSF56762; 1.
DR TIGRFAMs; TIGR01962; NuoD; 1.
DR PROSITE; PS00535; COMPLEX1_49K; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion inner membrane; NAD; Oxidoreductase;
KW Reference proteome; Respiratory chain; Transit peptide; Translocase;
KW Transport; Ubiquinone.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..482
FT /note="Probable NADH dehydrogenase [ubiquinone] iron-sulfur
FT protein 2, mitochondrial"
FT /id="PRO_0000019983"
FT BINDING 345
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 351
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 366
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
SQ SEQUENCE 482 AA; 54563 MW; ACF06535338418B1 CRC64;
MLGRKIAGTC LRANVPSVAA TSSTPATQTR NSHTIWYPDA KFERQFKTGG TLGKLWMSER
VSDFDEKIGL DKLEKLAYSD PVMSDNYSGK QREKNLENMI LNFGPQHPAA HGVLRLVLKL
EGEVIIKAIP HIGLLHRATE KLIEHKTYTQ ALPYFDRLDY VSMMCNEQAW SLAVEKLLGI
DIPTRAKYIR TLMGELTRIQ NHIMGITTHA LDVGAMTPFF WMFEEREKLF EFSERVSGAR
MHANYVRPGG VAWDLPIGLM DDIYDWAIKF PERIDELEDM LTENRIWKAR TIDIGLVSAA
DALNWGFSGV MVRGSGIKQD VRKTEPYDAY ADMEFDVPIG TKGDCYDRYL CRIEEMRQSL
NIVHQCLNKM PAGEIKVDDH KVVPPKRAEM KENMESLIHH FKFFTEGFQV PPGATYVPIE
APKGEFGVYL VADGTGKPYR CFIRAPGFAH LAAIHDVCYM SLIADIVAVI GTMDIVFGEV
DR
