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   27-MAR-2024, entry version 168.
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; 46.
DR   STRING; 6239.K09A9.5.1; -.
DR   EPD; Q93873; -.
DR   PaxDb; 6239-K09A9-5; -.
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   AGR; WB:WBGene00001520; -.
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; 191at2759; -.
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 cell types or 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; IEA:UniProtKB-EC.
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; Cytochrome-c3 Hydrogenase, chain B; 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   NCBIfam; TIGR01962; NuoD; 1.
DR   PANTHER; PTHR11993:SF10; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11993; NADH-UBIQUINONE OXIDOREDUCTASE 49 KDA SUBUNIT; 1.
DR   Pfam; PF00346; Complex1_49kDa; 1.
DR   SUPFAM; SSF56762; HydB/Nqo4-like; 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
//