NDHH_ANTAG
ID NDHH_ANTAG Reviewed; 393 AA.
AC Q85UU0; Q85WB4;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit H, chloroplastic {ECO:0000255|HAMAP-Rule:MF_01358};
DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01358};
DE AltName: Full=NAD(P)H dehydrogenase subunit H;
DE AltName: Full=NADH-plastoquinone oxidoreductase 49 kDa subunit {ECO:0000255|HAMAP-Rule:MF_01358};
DE AltName: Full=NADH-plastoquinone oxidoreductase subunit H {ECO:0000255|HAMAP-Rule:MF_01358};
GN Name=ndhH {ECO:0000255|HAMAP-Rule:MF_01358};
OS Anthoceros angustus (Hornwort) (Anthoceros formosae).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Anthocerotophyta;
OC Anthocerotopsida; Anthocerotidae; Anthocerotales; Anthocerotaceae;
OC Anthoceros.
OX NCBI_TaxID=48387;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND RNA EDITING.
RX PubMed=12527781; DOI=10.1093/nar/gkg155;
RA Kugita M., Kaneko A., Yamamoto Y., Takeya Y., Matsumoto T., Yoshinaga K.;
RT "The complete nucleotide sequence of the hornwort (Anthoceros formosae)
RT chloroplast genome: insight into the earliest land plants.";
RL Nucleic Acids Res. 31:716-721(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND RNA EDITING.
RC TISSUE=Thallus;
RX PubMed=12711687; DOI=10.1093/nar/gkg327;
RA Kugita M., Yamamoto Y., Fujikawa T., Matsumoto T., Yoshinaga K.;
RT "RNA editing in hornwort chloroplasts makes more than half the genes
RT functional.";
RL Nucleic Acids Res. 31:2417-2423(2003).
CC -!- FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN
CC and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain
CC and possibly in a chloroplast respiratory chain. The immediate electron
CC acceptor for the enzyme in this species is believed to be
CC plastoquinone. Couples the redox reaction to proton translocation, and
CC thus conserves the redox energy in a proton gradient.
CC {ECO:0000255|HAMAP-Rule:MF_01358}.
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_01358};
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_01358};
CC -!- SUBUNIT: NDH is composed of at least 16 different subunits, 5 of which
CC are encoded in the nucleus. {ECO:0000255|HAMAP-Rule:MF_01358}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_01358}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01358}; Stromal side {ECO:0000255|HAMAP-
CC Rule:MF_01358}.
CC -!- RNA EDITING: Modified_positions=32 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 42 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 75 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 110 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 128 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 130 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 147 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 157 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 169 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 170 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 182 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 202 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 209 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 215 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 230 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 234 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 260 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 290 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 293 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 341 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 349 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 393 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}; Note=The nonsense codons at positions
CC 128, 202, 230 and 293 are modified to sense codons.;
CC -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family.
CC {ECO:0000255|HAMAP-Rule:MF_01358}.
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DR EMBL; AB087490; BAC55507.1; -; mRNA.
DR EMBL; AB086179; BAC55407.2; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_777470.1; NC_004543.1.
DR AlphaFoldDB; Q85UU0; -.
DR SMR; Q85UU0; -.
DR GeneID; 2553501; -.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-UniRule.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0019684; P:photosynthesis, light reaction; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.645.10; -; 1.
DR HAMAP; MF_01358; NDH1_NuoD; 1.
DR InterPro; IPR001135; NADH_Q_OxRdtase_suD.
DR InterPro; IPR014029; NADH_UbQ_OxRdtase_49kDa_CS.
DR InterPro; IPR022885; NDH1_su_D/H.
DR InterPro; IPR029014; NiFe-Hase_large.
DR PANTHER; PTHR11993; PTHR11993; 1.
DR Pfam; PF00346; Complex1_49kDa; 1.
DR SUPFAM; SSF56762; SSF56762; 1.
DR TIGRFAMs; TIGR01962; NuoD; 1.
DR PROSITE; PS00535; COMPLEX1_49K; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; Membrane; NAD; NADP; Plastid; Plastoquinone; Quinone;
KW RNA editing; Thylakoid; Translocase; Transport.
FT CHAIN 1..393
FT /note="NAD(P)H-quinone oxidoreductase subunit H,
FT chloroplastic"
FT /id="PRO_0000118597"
SQ SEQUENCE 393 AA; 45334 MW; 9858E72DD68C3941 CRC64;
MTMLAAKADP MTLSMGPHHP SMHGVLRLIV TLDGENVTDC EPILGYLHRG MEKIAENRTI
VQYLPYVTRW DYLATMFTEA ITVNAPEKLT NIQVPKRASY IRIIMLELSR IASHLLWLGP
FMADIGAQTP FFYILREREM IYDLFEAATG MRMMHNFFRI GGVAVDLPYG WVDKCLDFCD
YFSLKVDEYE RLITYNSIFL KRVEGVGTIS REEAINWGLS GLMLRASGVQ WDLRKVDHYE
CYDELDWQVQ SQTEGDSLAR YLVRIGEMRE SVKIIQQALK VIPGGPYENL EARRLNQGKD
SEWNDFEYQF ISKKPSPTFK LPKQEHYIRV EAPKGELGIY LIGDDSVFPW RWKIRPPGFI
NLQILPQLVK GMKLADIMTI LGSIDIIMGE VDR
