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NU2C2_ANTAG
ID   NU2C2_ANTAG             Reviewed;         500 AA.
AC   P0CC31; Q85CP2;
DT   09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT   09-FEB-2010, sequence version 1.
DT   25-MAY-2022, entry version 30.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase subunit 2 B, chloroplastic {ECO:0000255|HAMAP-Rule:MF_00445};
DE            EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_00445};
DE   AltName: Full=NAD(P)H dehydrogenase, subunit 2 B {ECO:0000255|HAMAP-Rule:MF_00445};
DE   AltName: Full=NADH-plastoquinone oxidoreductase subunit 2 B {ECO:0000255|HAMAP-Rule:MF_00445};
GN   Name=ndhB2 {ECO:0000255|HAMAP-Rule:MF_00445};
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_00445}.
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_00445};
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_00445};
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_00445}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000255|HAMAP-Rule:MF_00445}; Multi-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_00445}.
CC   -!- RNA EDITING: Modified_positions=89 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 120 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 145 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 157 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 158 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 167 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 174 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 180 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 197 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 294 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 310 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 335 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 341 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 368 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 373 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 379 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 399 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 402 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 454 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 476 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}; Note=The nonsense codon at position 157
CC       is modified to a sense codon.;
CC   -!- SIMILARITY: Belongs to the complex I subunit 2 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00445}.
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DR   EMBL; AB086179; BAC55413.1; -; Genomic_DNA.
DR   RefSeq; NP_777457.1; NC_004543.1.
DR   RefSeq; NP_777476.1; NC_004543.1.
DR   AlphaFoldDB; P0CC31; -.
DR   SMR; P0CC31; -.
DR   GeneID; 2553494; -.
DR   GeneID; 2553495; -.
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   GO; GO:0019684; P:photosynthesis, light reaction; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00445; NDH1_NuoN_1; 1.
DR   InterPro; IPR010096; NADH-Q_OxRdtase_suN/2.
DR   InterPro; IPR001750; ND/Mrp_mem.
DR   InterPro; IPR045693; Ndh2_N.
DR   Pfam; PF19530; Ndh2_N; 1.
DR   Pfam; PF00361; Proton_antipo_M; 1.
DR   TIGRFAMs; TIGR01770; NDH_I_N; 1.
PE   2: Evidence at transcript level;
KW   Chloroplast; Membrane; NAD; NADP; Plastid; Plastoquinone; Quinone;
KW   RNA editing; Thylakoid; Translocase; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..500
FT                   /note="NAD(P)H-quinone oxidoreductase subunit 2 B,
FT                   chloroplastic"
FT                   /id="PRO_0000391253"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        78..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        116..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        166..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        211..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        242..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        277..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        305..325
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        335..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        376..396
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        409..429
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        467..487
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
SQ   SEQUENCE   500 AA;  55243 MW;  0ED218E87D474C86 CRC64;
     MKLDFGSFLS DGSSILPECI LISSLIIILL IDLTSEKKTY WLYFISLTSL IISITVLLFQ
     LKEEPIFSFS GSFQTDGFNG IFRISIAFSS LLCIPLSMEY MKCTKMAITE SLIFLLTATI
     GGMFLCGAND LIIIFITLEC LSLSSYLLSG YTKKDVRSNE AAMKYLLMGG ASSSILAYGF
     SWLYGLSGGK IQLQEIFNGL INTQMYNSTS ISIVLIFIIA GIAFKLSLVP FHQWTPDVYE
     GAPTSVIAFF SVTSKIAGLA LATRIFNTVF FSSLNEWHLI LEIIAILSMI LGNFIAITQT
     SMKRMLAYSS ISQIGYFMIG VIAGDSNGYA SMITYMLFYI FMNLGTFACI TLFGLRTGTD
     NIRDYAGLYK KDPLLASFLA LSLLSLGGIP PLAGFFGKLY LFWCGWKAGL YLSVSVGLFT
     SVISIYYYLR IVKLIVTKEN EETTSYIRKY KTSSNYLVSK SPIEFSIIIC VIGSTFSGIV
     INPVIAIVEK TISLSSFINN
 
 
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