NU2M_PODAN
ID NU2M_PODAN Reviewed; 556 AA.
AC P15578;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=NADH-ubiquinone oxidoreductase chain 2;
DE EC=7.1.1.2;
DE AltName: Full=NADH dehydrogenase subunit 2;
GN Name=ND2;
OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS (Pleurage anserina).
OG Mitochondrion.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC Podospora anserina.
OX NCBI_TaxID=515849;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A, and s;
RX PubMed=2975708; DOI=10.1016/0022-2836(88)90044-7;
RA Cummings D.J., Domenico J.M.;
RT "Sequence analysis of mitochondrial DNA from Podospora anserina.
RT Pervasiveness of a class I intron in three separate genes.";
RL J. Mol. Biol. 204:815-839(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=s;
RX PubMed=2357736; DOI=10.1007/bf00334517;
RA Cummings D.J., McNally K.L., Domenico J.M., Matsuura E.T.;
RT "The complete DNA sequence of the mitochondrial genome of Podospora
RT anserina.";
RL Curr. Genet. 17:375-402(1990).
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; X55026; CAA38765.1; -; Genomic_DNA.
DR EMBL; X14485; CAA32646.1; -; Genomic_DNA.
DR PIR; S02154; S02154.
DR RefSeq; NP_074912.1; NC_001329.3.
DR AlphaFoldDB; P15578; -.
DR SMR; P15578; -.
DR STRING; 515849.P15578; -.
DR GeneID; 802484; -.
DR KEGG; pan:PoanfMp04; -.
DR Proteomes; UP000001197; Mitochondrion.
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 GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR HAMAP; MF_00445; NDH1_NuoN_1; 1.
DR InterPro; IPR010096; NADH-Q_OxRdtase_suN/2.
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; Reference proteome; Respiratory chain; Translocase; Transmembrane;
KW Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..556
FT /note="NADH-ubiquinone oxidoreductase chain 2"
FT /id="PRO_0000117627"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 358..378
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 455..475
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 517..537
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 556 AA; 62554 MW; 5613ACB0D2324BAF CRC64;
MIFISIIGLL LSNAVTLRQD MSVNFNRIAL IDLIYCILHD TMSLSIINKG IGLHGGLLHI
TNITLIFHIF IFFLSILILQ LTSFYPRKAW IPEHSSLKDI IYQKFLNYRT KIFNKMGEHM
KIIEYPLILL FVISGAVFLM STNDLVSIFL SIELQSYGLY LLSTIYRNSE LSTAGGLIYF
LLGGLSSCFI LLGTSLLYIN SGTTSLDGLY ILNSISDVKD GAADMPALTS WYKSYYLNFA
LLVFSIGFLF KVSAAPFHFW SPDVYDAIPT IVTTFVAIIA KISIFIFLLE LVYHTNNYLS
EFSWTYLLLI SSLFSLIIGT VVGLTQFRIK RLLAYSTISH VGFILLALSG CSIESTQAFI
FYLIQYSISN LNVFIIIITI GFSLYGYITT NKEYKDLLDK NNSPIQVISQ LKGYFYINPL
LSLSLAITIF SFVGIPPLVG FFAKQMVLSA ALDNGYIFLT LIAILTSVIG AVYYLNIIKK
IFFYLPDHSI NPSIGEFLFK KGLIFEAGDF KGRITLISSP FSITISIITL VILLFIFMNK
EWLSMGTILV QVLFSN