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RBL_PTYGA
ID   RBL_PTYGA               Reviewed;         440 AA.
AC   O98360; Q9GE58;
DT   11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000255|HAMAP-Rule:MF_01338};
DE            Short=RuBisCO large subunit {ECO:0000255|HAMAP-Rule:MF_01338};
DE            EC=4.1.1.39 {ECO:0000255|HAMAP-Rule:MF_01338};
DE   Flags: Fragment;
GN   Name=rbcL {ECO:0000255|HAMAP-Rule:MF_01338};
OS   Ptychomitrium gardneri (Gardner's ptychomitrium moss).
OG   Plastid; Chloroplast {ECO:0000312|EMBL:AAC96063.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC   Bryophytina; Bryopsida; Dicranidae; Grimmiales; Ptychomitriaceae;
OC   Ptychomitrium.
OX   NCBI_TaxID=61565 {ECO:0000312|EMBL:AAC96063.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Isolate Ireland 7038;
RA   Goffinet B., Bayer R.J., Vitt D.H.;
RT   "Circumscription and phylogeny of the Orthotrichales (Bryopsida) inferred
RT   from rbcL sequence analyses.";
RL   Am. J. Bot. 85:1324-1337(1998).
RN   [2] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-430.
RA   La Farge C., Mishler B.D., Wheeler J.A., Wall D.P., Johannes K.,
RA   Schaffer S., Shaw A.J.;
RT   "Phylogenetic relationships within the Haplolepideous mosses.";
RL   Bryologist 103:257-276(2000).
CC   -!- FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D-
CC       ribulose 1,5-bisphosphate, the primary event in carbon dioxide
CC       fixation, as well as the oxidative fragmentation of the pentose
CC       substrate in the photorespiration process. Both reactions occur
CC       simultaneously and in competition at the same active site.
CC       {ECO:0000255|HAMAP-Rule:MF_01338}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-
CC         bisphosphate + H2O; Xref=Rhea:RHEA:23124, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57870,
CC         ChEBI:CHEBI:58272; EC=4.1.1.39; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01338};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-ribulose 1,5-bisphosphate + O2 = (2R)-3-phosphoglycerate +
CC         2-phosphoglycolate + 2 H(+); Xref=Rhea:RHEA:36631, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:57870, ChEBI:CHEBI:58033,
CC         ChEBI:CHEBI:58272; Evidence={ECO:0000255|HAMAP-Rule:MF_01338};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01338};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01338};
CC   -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains;
CC       disulfide-linked. The disulfide link is formed within the large subunit
CC       homodimers. {ECO:0000255|HAMAP-Rule:MF_01338}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- PTM: The disulfide bond which can form in the large chain dimeric
CC       partners within the hexadecamer appears to be associated with oxidative
CC       stress and protein turnover. {ECO:0000255|HAMAP-Rule:MF_01338}.
CC   -!- MISCELLANEOUS: The basic functional RuBisCO is composed of a large
CC       chain homodimer in a 'head-to-tail' conformation. In form I RuBisCO
CC       this homodimer is arranged in a barrel-like tetramer with the small
CC       subunits forming a tetrameric 'cap' on each end of the 'barrel'.
CC       {ECO:0000255|HAMAP-Rule:MF_01338}.
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01338}.
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DR   EMBL; AF005549; AAC96063.1; -; Genomic_DNA.
DR   EMBL; AF231313; AAG13838.1; -; mRNA.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009853; P:photorespiration; IEA:UniProtKB-KW.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
DR   CDD; cd08212; RuBisCO_large_I; 1.
DR   Gene3D; 3.20.20.110; -; 1.
DR   Gene3D; 3.30.70.150; -; 1.
DR   HAMAP; MF_01338; RuBisCO_L_type1; 1.
DR   InterPro; IPR033966; RuBisCO.
DR   InterPro; IPR020878; RuBisCo_large_chain_AS.
DR   InterPro; IPR000685; RuBisCO_lsu_C.
DR   InterPro; IPR036376; RuBisCO_lsu_C_sf.
DR   InterPro; IPR017443; RuBisCO_lsu_fd_N.
DR   InterPro; IPR036422; RuBisCO_lsu_N_sf.
DR   InterPro; IPR020888; RuBisCO_lsuI.
DR   PANTHER; PTHR42704; PTHR42704; 1.
DR   Pfam; PF00016; RuBisCO_large; 1.
DR   Pfam; PF02788; RuBisCO_large_N; 1.
DR   SFLD; SFLDS00014; RuBisCO; 1.
DR   SUPFAM; SSF51649; SSF51649; 1.
DR   SUPFAM; SSF54966; SSF54966; 1.
DR   PROSITE; PS00157; RUBISCO_LARGE; 1.
PE   2: Evidence at transcript level;
KW   Calvin cycle; Carbon dioxide fixation; Chloroplast; Disulfide bond; Lyase;
KW   Magnesium; Metal-binding; Methylation; Monooxygenase; Oxidoreductase;
KW   Photorespiration; Photosynthesis; Plastid.
FT   CHAIN           <1..>440
FT                   /note="Ribulose bisphosphate carboxylase large chain"
FT                   /id="PRO_0000062578"
FT   ACT_SITE        165
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   ACT_SITE        284
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         113
FT                   /ligand="substrate"
FT                   /note="in homodimeric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         163
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         167
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         191
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         193
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         194
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         285
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         317
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         369
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   SITE            324
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   MOD_RES         4
FT                   /note="N6,N6,N6-trimethyllysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   MOD_RES         191
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   DISULFID        237
FT                   /note="Interchain; in linked form"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   NON_TER         1
FT                   /evidence="ECO:0000312|EMBL:AAC96063.1"
FT   NON_TER         440
FT                   /evidence="ECO:0000312|EMBL:AAC96063.1"
SQ   SEQUENCE   440 AA;  48737 MW;  6F398754C75686BF CRC64;
     VGFKAGVKDY RLNYYTPDYQ TKETDILAAF RMTPQPGVPP EEAGAAVAAE SSTGTWTTVW
     TDGLTSLDRY KGRCYDLEAV PGEENQYIAY VAYPLDLFEE GSVTNLFTSI VGNVFGFKAL
     RALRLEDLRI PPAYSKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL SAKNYGRAVY
     ECLRGGLDFT KDDENVNSQP FMRWRDRFLF VAEALYKSQA ETGEIKGHYL NATAGTCEEM
     LKRAEFAREL GAPIVMHDYL TGGFTANTTL AHYCRDNGLL LHIHRAMHAV IDRQKNHGMH
     FRVLAKALRL SGGDHIHAGT VVGKLEGERQ VTLGFVDLLR DDYIEKDRSR GIYFTQDWVS
     LPGVLPVASG GIHVWHXPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN RVALEACVQA
     RNEGRDLARE GNEVIREATK
 
 
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