NU2M_OENBE
ID NU2M_OENBE Reviewed; 488 AA.
AC P93401;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=NADH-ubiquinone oxidoreductase chain 2;
DE EC=7.1.1.2;
DE AltName: Full=NADH dehydrogenase subunit 2;
GN Name=ND2; Synonyms=NAD2;
OS Oenothera berteroana (Bertero's evening primrose).
OG Mitochondrion.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Onagraceae; Onagroideae; Onagreae; Oenothera.
OX NCBI_TaxID=3950;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND RNA EDITING.
RX PubMed=1559998; DOI=10.1016/s0021-9258(18)42560-4;
RA Binder S., Marchfelder A., Brennicke A., Wissinger B.;
RT "RNA editing in trans-splicing intron sequences of nad2 mRNAs in Oenothera
RT mitochondria.";
RL J. Biol. Chem. 267:7615-7623(1992).
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 -!- RNA EDITING: Modified_positions=9 {ECO:0000269|PubMed:1559998}, 19
CC {ECO:0000269|PubMed:1559998}, 75 {ECO:0000269|PubMed:1559998}, 103
CC {ECO:0000269|PubMed:1559998}, 104 {ECO:0000269|PubMed:1559998}, 119
CC {ECO:0000269|PubMed:1559998}, 121 {ECO:0000269|PubMed:1559998}, 123
CC {ECO:0000269|PubMed:1559998}, 132 {ECO:0000269|PubMed:1559998}, 134
CC {ECO:0000269|PubMed:1559998}, 143 {ECO:0000269|PubMed:1559998}, 166
CC {ECO:0000269|PubMed:1559998}, 175 {ECO:0000269|PubMed:1559998}, 221
CC {ECO:0000269|PubMed:1559998}, 263 {ECO:0000269|PubMed:1559998}, 267
CC {ECO:0000269|PubMed:1559998}, 270 {ECO:0000269|PubMed:1559998}, 307
CC {ECO:0000269|PubMed:1559998}, 310 {ECO:0000269|PubMed:1559998}, 320
CC {ECO:0000269|PubMed:1559998}, 321 {ECO:0000269|PubMed:1559998}, 353
CC {ECO:0000269|PubMed:1559998}, 375 {ECO:0000269|PubMed:1559998}, 376
CC {ECO:0000269|PubMed:1559998}, 416 {ECO:0000269|PubMed:1559998}, 433
CC {ECO:0000269|PubMed:1559998}, 467 {ECO:0000269|PubMed:1559998}, 468
CC {ECO:0000269|PubMed:1559998}, 486 {ECO:0000269|PubMed:1559998};
CC -!- MISCELLANEOUS: Exons a and b and c, d and e are cis-spliced, while a
CC trans-splicing reaction is required to link exons b and c.
CC -!- SIMILARITY: Belongs to the complex I subunit 2 family. {ECO:0000305}.
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DR EMBL; M81726; AAB18755.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M81725; AAB18755.1; JOINED; Genomic_DNA.
DR AlphaFoldDB; P93401; -.
DR SMR; P93401; -.
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:0009536; C:plastid; IEA:UniProt.
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.
DR TIGRFAMs; TIGR01770; NDH_I_N; 1.
PE 2: Evidence at transcript level;
KW Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW NAD; Respiratory chain; RNA editing; Translocase; Transmembrane;
KW Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..488
FT /note="NADH-ubiquinone oxidoreductase chain 2"
FT /id="PRO_0000117613"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 400..420
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 456..476
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 488 AA; 54050 MW; 915F5622AAC093A1 CRC64;
MFNLFLAVFP EIFIINATFI LLIHGVVFST SKKDDYPPLV SNVGWLGLLS VLITLLLLAA
GAPLLTIAHL FWNNFFRRDN FTYFCQILLL LSTAGTISMC FDFFEQERFD AFEFIVLILL
STCSMLFMIS AYDLIAMYLA IELQSLCFYV LAASKRKSEF STEAGLKYLI LGAFSSGILL
FGCSMIYGST GATHFDQLAK ILTGYEITGA RSSGIFMGIL FIAVGFLFKI TAVPFHMWAP
DIYEGSPTPV TAFLSIAPKI SIFANILRVF IYGSYGATLQ QIFFFCSIAS MILGALAAMA
QTKVKRLLAY SSIGHVGYIC IGFSCGTIEG IQSLLIGLFI YALTTINAFA IVLALRQTRV
KYIADLGALA KTNPILAITF SITMFSYAGI PPLAGFCSKF YLFFAALGCG AYFLASVGVV
TSVIGCFYYI RLVKRMFFDT PRTWILYEPM DRNKSLLLAM TSSFITLFFL YPSPLFSVTH
QMALSLYL
