NU4C_ADICA
ID NU4C_ADICA Reviewed; 497 AA.
AC Q85FH5;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=NAD(P)H-quinone oxidoreductase chain 4, chloroplastic {ECO:0000255|HAMAP-Rule:MF_00491};
DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_00491};
DE AltName: Full=NAD(P)H dehydrogenase, chain 4 {ECO:0000255|HAMAP-Rule:MF_00491};
DE AltName: Full=NADH-plastoquinone oxidoreductase chain 4 {ECO:0000255|HAMAP-Rule:MF_00491};
GN Name=ndhD {ECO:0000255|HAMAP-Rule:MF_00491};
OS Adiantum capillus-veneris (Maidenhair fern).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Polypodiopsida; Polypodiidae; Polypodiales; Pteridineae; Pteridaceae;
OC Vittarioideae; Adiantum.
OX NCBI_TaxID=13818;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12755170; DOI=10.1093/dnares/10.2.59;
RA Wolf P.G., Rowe C.A., Sinclair R.B., Hasebe M.;
RT "Complete nucleotide sequence of the chloroplast genome from a
RT leptosporangiate fern, Adiantum capillus-veneris L.";
RL DNA Res. 10:59-65(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND RNA EDITING.
RC TISSUE=Frond;
RX PubMed=15363849; DOI=10.1016/j.gene.2004.06.018;
RA Wolf P.G., Rowe C.A., Hasebe M.;
RT "High levels of RNA editing in a vascular plant chloroplast genome:
RT analysis of transcripts from the fern Adiantum capillus-veneris.";
RL Gene 339:89-97(2004).
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00491};
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00491};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_00491}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00491}.
CC -!- RNA EDITING: Modified_positions=7 {ECO:0000269|PubMed:15363849}, 47
CC {ECO:0000269|PubMed:15363849}, 458 {ECO:0000269|PubMed:15363849};
CC -!- SIMILARITY: Belongs to the complex I subunit 4 family.
CC {ECO:0000255|HAMAP-Rule:MF_00491}.
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DR EMBL; AY178864; AAP29441.2; -; Genomic_DNA.
DR RefSeq; NP_848110.3; NC_004766.1.
DR AlphaFoldDB; Q85FH5; -.
DR SMR; Q85FH5; -.
DR GeneID; 807448; -.
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..497
FT /note="NAD(P)H-quinone oxidoreductase chain 4,
FT chloroplastic"
FT /id="PRO_0000118008"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 331..351
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 387..407
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 463..483
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
SQ SEQUENCE 497 AA; 55663 MW; 235A4B6699AEB413 CRC64;
MISNVPWLTV IVSLPIFAGL MIPILPRNGN RVTRWYTLGI CILEFLLITY IFYCHFRIDY
QSIQLLETFN WINNIHLHWS LGIDGLSLGL VILTGFATTL ATLSAWPITR NTRLFYFLML
IMYGGQIGLF VSRDILLFFF MWEIELIPVY LLLCLWGGKR RLYSATKFVL YTAGGSIFLL
VAALTMSFYG SEVPSFNIQD LIHKSYPLSL EVLIYVGFLV AYAVKLPIFP FHTWLPDTHG
EAHYSTCMLL AGVLLKMGGY GLIRINLELL THAHFLLGSW MMLFGAIQII YASLISMSQR
NFKRRIAYSS ISHMGFVTIG IGSFTETGIN GAILQMISHG LIGAALFFLA GTCYDRTRTY
LLDQLGGAAI SMPKLFTMFS TLSLASLALP GMSGFVSELL VFLGVVTSNQ YSFAFKAGIT
VLEGIGTVLT PIYLLSMLRQ LFYGYRFFDK SNPYSIDLGP RELFILICFL LPILGIGLYP
NLILSIGSTE IPSLPLT
