NU2M_DICCI
ID NU2M_DICCI Reviewed; 491 AA.
AC Q2LCP8;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 25-MAY-2022, entry version 50.
DE RecName: Full=NADH-ubiquinone oxidoreductase chain 2;
DE EC=7.1.1.2;
DE AltName: Full=NADH dehydrogenase subunit 2;
GN Name=nad2;
OS Dictyostelium citrinum (Slime mold).
OG Mitochondrion.
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=361072;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=18413355; DOI=10.1093/molbev/msn088;
RA Heidel A.J., Gloeckner G.;
RT "Mitochondrial genome evolution in the social amoebae.";
RL Mol. Biol. Evol. 25:1440-1450(2008).
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 -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane
CC protein.
CC -!- SIMILARITY: Belongs to the complex I subunit 2 family. {ECO:0000305}.
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DR EMBL; DQ336395; ABC60395.1; -; Genomic_DNA.
DR RefSeq; YP_492644.1; NC_007787.2.
DR AlphaFoldDB; Q2LCP8; -.
DR SMR; Q2LCP8; -.
DR GeneID; 3912632; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR InterPro; IPR001750; ND/Mrp_mem.
DR Pfam; PF00361; Proton_antipo_M; 1.
PE 3: Inferred from homology;
KW Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW NAD; Respiratory chain; Translocase; Transmembrane; Transmembrane helix;
KW Transport; Ubiquinone.
FT CHAIN 1..491
FT /note="NADH-ubiquinone oxidoreductase chain 2"
FT /id="PRO_0000312391"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 411..433
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 463..483
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 491 AA; 55392 MW; 4DD82BDBB5377F46 CRC64;
MVCLFENLMN MIKYSIYILP LIILIVLSIS IKKDVQRVHI IIQSLKLTLI VIMIVIGIEE
SIYVKLNGHL IKTELIKLFE YLLLGVSYMI IKMFEEGVTE GKKTKITDEG LILIYSSIIG
MLISMEAHNL ITLFLSLEIS SICFYILALN KNSRKGIEGG LKYYIIGGIA TTILLLGIVS
IYKSTGSLMY TDLLVIVMEN TDDYRIQMGI ALIVLGLILK LGIAPFHGWL IDVYEGAGML
MTFYLTITQK LVTLMVLINL YQNLIIYTNA IMFTNGLIIL ILVTLVVGTI GSLRQQKLIR
FIAYSAIVNS ALLILMLAGS MSEELMVNSV YYLINYIIGL TVLMSLIMGF LRLNDRGTIE
DIYQLKNMWV INMFGAIVYI LVLMYLAGLP PMTNFISKIL ILLPYMVLGR VYLTMLAFFL
SVGVMIYYMN LVKIIIIDKV QTHEQGVAEL EITSKPTKGG RRIVLGVMWL IFSQLYLDEI
LNVIKVIVAL I