NU4C_TOBAC
ID NU4C_TOBAC Reviewed; 500 AA.
AC P06262;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=NAD(P)H-quinone oxidoreductase chain 4, chloroplastic;
DE EC=7.1.1.-;
DE AltName: Full=NAD(P)H dehydrogenase, chain 4;
DE AltName: Full=NADH-plastoquinone oxidoreductase chain 4;
GN Name=ndhD; Synonyms=ndh4;
OS Nicotiana tabacum (Common tobacco).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Bright Yellow 4;
RX PubMed=16453699; DOI=10.1002/j.1460-2075.1986.tb04464.x;
RA Shinozaki K., Ohme M., Tanaka M., Wakasugi T., Hayashida N.,
RA Matsubayashi T., Zaita N., Chunwongse J., Obokata J.,
RA Yamaguchi-Shinozaki K., Ohto C., Torazawa K., Meng B.-Y., Sugita M.,
RA Deno H., Kamogashira T., Yamada K., Kusuda J., Takaiwa F., Kato A.,
RA Tohdoh N., Shimada H., Sugiura M.;
RT "The complete nucleotide sequence of the tobacco chloroplast genome: its
RT gene organization and expression.";
RL EMBO J. 5:2043-2049(1986).
RN [2]
RP RNA EDITING OF INITIATOR CODON.
RX PubMed=8076816; DOI=10.1016/0378-1119(94)90290-9;
RA Neckermann K., Zeltz P., Igloi G.L., Koessel H., Maier R.M.;
RT "The role of RNA editing in conservation of start codons in chloroplast
RT genomes.";
RL Gene 146:177-182(1994).
RN [3]
RP RNA EDITING.
RX PubMed=10589833; DOI=10.1007/s004380051106;
RA Hirose T., Kusumegi T., Tsudzuki T., Sugiura M.;
RT "RNA editing sites in tobacco chloroplast transcripts: editing as a
RT possible regulator of chloroplast RNA polymerase activity.";
RL Mol. Gen. Genet. 262:462-467(1999).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n
CC H(+)(out) + NAD(+); Xref=Rhea:RHEA:42608, Rhea:RHEA-COMP:9561,
CC Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62192;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a plastoquinone + (n+1) H(+)(in) + NADPH = a plastoquinol + n
CC H(+)(out) + NADP(+); Xref=Rhea:RHEA:42612, Rhea:RHEA-COMP:9561,
CC Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:62192;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- RNA EDITING: Modified_positions=1 {ECO:0000269|PubMed:10589833,
CC ECO:0000269|PubMed:8076816}, 42 {ECO:0000269|PubMed:10589833,
CC ECO:0000269|PubMed:8076816}; Note=The initiator methionine is created
CC by RNA editing.;
CC -!- SIMILARITY: Belongs to the complex I subunit 4 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA77432.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z00044; CAA77432.1; ALT_INIT; Genomic_DNA.
DR EMBL; X76975; CAA54280.1; -; mRNA.
DR PIR; A00444; DENTN4.
DR RefSeq; NP_054557.2; NC_001879.2.
DR AlphaFoldDB; P06262; -.
DR SMR; P06262; -.
DR GeneID; 800483; -.
DR KEGG; nta:800483; -.
DR OMA; ITRWGNQ; -.
DR OrthoDB; 996580at2759; -.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR HAMAP; MF_00491; NDH1_NuoM; 1.
DR InterPro; IPR022997; NADH_Q_OxRdtase_chain4.
DR InterPro; IPR010227; NADH_Q_OxRdtase_chainM/4.
DR InterPro; IPR003918; NADH_UbQ_OxRdtase.
DR InterPro; IPR001750; ND/Mrp_mem.
DR PANTHER; PTHR43507; PTHR43507; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR PRINTS; PR01437; NUOXDRDTASE4.
DR TIGRFAMs; TIGR01972; NDH_I_M; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; Membrane; NAD; NADP; Plastid; Plastoquinone; Quinone;
KW RNA editing; Thylakoid; Translocase; Transmembrane; Transmembrane helix.
FT CHAIN 1..500
FT /note="NAD(P)H-quinone oxidoreductase chain 4,
FT chloroplastic"
FT /id="PRO_0000118031"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 411..431
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 462..482
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 500 AA; 56350 MW; E83A130C7B9BCFEC CRC64;
MNYFPWLTII VVFPIFAGSL IFFLPHKGNR VIRWYTICIC ILELLLTTYA FCYHFQSDDP
LIQLVEDYKW INFFDFHWRL GIDGLSIGPI LLTGFITTLA TLAAWPVTRD SRLFHFLMLA
MYSGQIGSFS SRDLLLFFIM WELELIPVYL LLCMWGGKKR LYSATKFILY TAGGSVFLLM
GVLGLALYGS NEPTLNFETS VNQSYPVVLE IIFYIGFFIA FAVKSPIIPL HTWLPDTHGE
AHYSTCMLLA GILLKMGAYG LIRINMELLP HAHSIFSPWL MIIGTIQIIY AALTSLGQRN
LKKRIAYSSV SHMGFIIIGI SSLTDTGLNG ALLQIISHGF IGAALFFLAG TTYDRIRLVY
LDEMGGIAIP MPKMFTMFSS FSMASLALPG MSGFVAELIV FFGIITGQKY LLIPKILITF
VMAIGMILTP IYSLSMSRQM FYGYKLFNAP KDSFFDSGPR ELFLSISIFL PVIGIGIYPD
FVLSLAVDKV EVILSNFFYR
