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NU1C_ANTAG
ID   NU1C_ANTAG              Reviewed;         366 AA.
AC   Q85BI5;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic {ECO:0000255|HAMAP-Rule:MF_01350};
DE            EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01350};
DE   AltName: Full=NAD(P)H dehydrogenase subunit 1 {ECO:0000255|HAMAP-Rule:MF_01350};
DE            Short=NDH subunit 1 {ECO:0000255|HAMAP-Rule:MF_01350};
DE   AltName: Full=NADH-plastoquinone oxidoreductase subunit 1 {ECO:0000255|HAMAP-Rule:MF_01350};
GN   Name=ndhA {ECO:0000255|HAMAP-Rule:MF_01350};
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_01350}.
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_01350};
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_01350};
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_01350}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000255|HAMAP-Rule:MF_01350}; Multi-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_01350}.
CC   -!- RNA EDITING: Modified_positions=35 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 89 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 103 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 147 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 159 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 160 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 167 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 168 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 175 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 182 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 213 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 231 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 241 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 321 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 356 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 357 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}; Note=The nonsense codon at position 168
CC       is modified to a sense codon.;
CC   -!- SIMILARITY: Belongs to the complex I subunit 1 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01350}.
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DR   EMBL; AB086179; BAC55406.1; -; Genomic_DNA.
DR   EMBL; AB087489; BAC55506.1; -; mRNA.
DR   RefSeq; NP_777469.1; NC_004543.1.
DR   AlphaFoldDB; Q85BI5; -.
DR   SMR; Q85BI5; -.
DR   GeneID; 2553493; -.
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: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   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   2: Evidence at transcript level;
KW   Chloroplast; Membrane; NAD; NADP; Plastid; Plastoquinone; Quinone;
KW   RNA editing; Thylakoid; Translocase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..366
FT                   /note="NAD(P)H-quinone oxidoreductase subunit 1,
FT                   chloroplastic"
FT                   /id="PRO_0000117505"
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        97..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        130..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        166..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        254..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        307..327
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        340..360
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
SQ   SEQUENCE   366 AA;  40514 MW;  74282550B38FD56E CRC64;
     MVFNMNLKEQ AMSLFYESGF PKDFFSFLWI TASILILVSG VVIGVLVIVW LERKISAGIQ
     QRIGPEYAGP LGIIQALADG TKLLLKEDII PSRGDALLFS IGPAIVVIPV LLSYLVIPFG
     HNIILADLNI GVFFWIAVSS IAPLGLFMAG YGSNNKYSFL GGLRAVAQAI SYEIPLALCV
     LSISLLSNSL STVDIVEIQS KFGFWGWNVW RQPIGFIAFL IASLAECERL PFDLPEAEEE
     LVAGYQTEYS GIKFGLFYVA SYLNLLVSSL FVTVLYLGGW NLSIPFLPNF PYLEWKFTAE
     TSEVINVIIG IIITLAKAYS FLFISIVTRW TLPRVRMDQL LNLGWKFLLP IALGNLLLTA
     SFQLIA
 
 
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