NU1M_ARATH
ID NU1M_ARATH Reviewed; 325 AA.
AC P92558; Q42576;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 4.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=NADH-ubiquinone oxidoreductase chain 1;
DE EC=7.1.1.2;
DE AltName: Full=NADH dehydrogenase subunit 1;
GN Name=ND1; Synonyms=NAD1;
GN OrderedLocusNames=AtMg00516/AtMg01120/AtMg01275
GN {ECO:0000312|Araport:ATMG00516, ECO:0000312|Araport:ATMG01120,
GN ECO:0000312|Araport:ATMG01275};
GN and
GN OrderedLocusNames=At2g07785 {ECO:0000312|Araport:AT2G07785};
GN and
GN OrderedLocusNames=At2g07786 {ECO:0000312|Araport:AT2G07786};
OS Arabidopsis thaliana (Mouse-ear cress).
OG Mitochondrion.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. C24;
RA Schuster W.;
RL Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. C24;
RX PubMed=8988169; DOI=10.1038/ng0197-57;
RA Unseld M., Marienfeld J.R., Brandt P., Brennicke A.;
RT "The mitochondrial genome of Arabidopsis thaliana contains 57 genes in
RT 366,924 nucleotides.";
RL Nat. Genet. 15:57-61(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (AT2G07785 AND AT2G07786).
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
RP GENOME REANNOTATION (AT2G07785 AND AT2G07786).
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP RNA EDITING.
RX PubMed=10611383; DOI=10.1073/pnas.96.26.15324;
RA Giege P., Brennicke A.;
RT "RNA editing in Arabidopsis mitochondria effects 441 C to U changes in
RT ORFs.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:15324-15329(1999).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=14671022; DOI=10.1105/tpc.016055;
RA Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA Millar A.H.;
RT "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT signaling and regulatory components, provides assessment of targeting
RT prediction programs, and indicates plant-specific mitochondrial proteins.";
RL Plant Cell 16:241-256(2004).
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 -!- SUBUNIT: Complex I is composed of at least 49 different subunits.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- RNA EDITING: Modified_positions=1 {ECO:0000269|PubMed:10611383}, 56
CC {ECO:0000269|PubMed:10611383}, 89 {ECO:0000269|PubMed:10611383}, 103
CC {ECO:0000269|PubMed:10611383}, 126 {ECO:0000269|PubMed:10611383}, 164
CC {ECO:0000269|PubMed:10611383}, 165 {ECO:0000269|PubMed:10611383}, 167
CC {ECO:0000269|PubMed:10611383}, 179 {ECO:0000269|PubMed:10611383}, 191
CC {ECO:0000269|PubMed:10611383}, 194 {ECO:0000269|PubMed:10611383}, 212
CC {ECO:0000269|PubMed:10611383}, 225 {ECO:0000269|PubMed:10611383}, 242
CC {ECO:0000269|PubMed:10611383}, 248 {ECO:0000269|PubMed:10611383}, 252
CC {ECO:0000269|PubMed:10611383}, 275 {ECO:0000269|PubMed:10611383}, 300
CC {ECO:0000269|PubMed:10611383}, 310 {ECO:0000269|PubMed:10611383}, 313
CC {ECO:0000269|PubMed:10611383}; Note=The initiator methionine is created
CC by RNA editing.;
CC -!- MISCELLANEOUS: A stretch of 270 kb of the mitochondrial genome is
CC duplicated within the centromere of chromosome 2 resulting in the
CC duplication of the gene. The expression of the duplicated genes
CC (At2g07785 and At2g07786) is not demonstrated. They are also probably
CC not RNA edited and therefore differs in all the positions known to be
CC edited.
CC -!- SIMILARITY: Belongs to the complex I subunit 1 family. {ECO:0000305}.
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DR EMBL; X82618; CAA57940.1; -; mRNA.
DR EMBL; Y08501; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC007729; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002685; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S49576; S49576.
DR PDB; 7A23; EM; 3.70 A; H=1-325.
DR PDB; 7A24; EM; 3.80 A; H=1-325.
DR PDB; 7AR7; EM; 3.72 A; H=2-325.
DR PDBsum; 7A23; -.
DR PDBsum; 7A24; -.
DR PDBsum; 7AR7; -.
DR AlphaFoldDB; P92558; -.
DR SMR; P92558; -.
DR IntAct; P92558; 2.
DR STRING; 3702.ATMG00516.1; -.
DR PaxDb; P92558; -.
DR PeptideAtlas; P92558; -.
DR PRIDE; P92558; -.
DR Araport; AT2G07785; -.
DR Araport; AT2G07786; -.
DR Araport; ATMG00516; -.
DR Araport; ATMG01120; -.
DR Araport; ATMG01275; -.
DR eggNOG; KOG4770; Eukaryota.
DR InParanoid; P92558; -.
DR BioCyc; ARA:ATMG01120-MON; -.
DR BioCyc; MetaCyc:ATMG01120-MON; -.
DR BRENDA; 7.1.1.2; 399.
DR PRO; PR:P92558; -.
DR Proteomes; UP000006548; Chromosome 2.
DR Proteomes; UP000006548; Mitochondrion (cv. C24).
DR ExpressionAtlas; P92558; baseline and differential.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IBA:GO_Central.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
DR HAMAP; MF_01350; NDH1_NuoH; 1.
DR InterPro; IPR001694; NADH_UbQ_OxRdtase_su1/FPO.
DR InterPro; IPR018086; NADH_UbQ_OxRdtase_su1_CS.
DR PANTHER; PTHR11432; PTHR11432; 1.
DR Pfam; PF00146; NADHdh; 1.
DR PROSITE; PS00667; COMPLEX1_ND1_1; 1.
DR PROSITE; PS00668; COMPLEX1_ND1_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Electron transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; NAD; Reference proteome; Respiratory chain;
KW RNA editing; Translocase; Transmembrane; Transmembrane helix; Transport;
KW Ubiquinone.
FT CHAIN 1..325
FT /note="NADH-ubiquinone oxidoreductase chain 1"
FT /id="PRO_0000117344"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 325 AA; 36030 MW; 436447F5DAB7EBEF CRC64;
MYIAVPAEIL GIILPLLLGV AFLVLAERKV MAFVQRRKGP DVVGSFGLLQ PLADGLKLIL
KEPISPSSAN FFLFRMAPVA TFMLSLVAWA VVPFDYGMVL SDLNIGLLYL FAISSLGVYG
IIIAGWSSNS KYAFLGALRS AAQMVSYEVS IGLILITVLI CVGSCNLSEI VMAQKQIWFG
IPLFPVLVMF FISCLAETNR APFDLPEAEA ELVAGYNVEY SSMGFALFFL GEYANMILMS
GLCTLFFLGG WLPILDLPIF KKIPGSIWFS IKVLFFLFLY IWVRAAFPRY RYDQLMGLGW
KVFLPLSLAW VVSVSGLLVT FQWLP
