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Database: UniProt/SWISS-PROT
Entry: RBL_PHYPA
LinkDB: RBL_PHYPA
Original site: RBL_PHYPA 
ID   RBL_PHYPA               Reviewed;         475 AA.
AC   P34915; Q95FY7;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   07-NOV-2003, sequence version 2.
DT   25-OCT-2017, entry version 108.
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: Precursor;
GN   Name=rbcL {ECO:0000255|HAMAP-Rule:MF_01338};
OS   Physcomitrella patens subsp. patens (Moss).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC   Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae;
OC   Physcomitrella.
OX   NCBI_TaxID=3218;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Kruse S., Martin W., Wehe M., Reski R.;
RT   "An open reading frame (ycf11) is evolutionary conserved from
RT   Cyanobacteria to the plastid DNAs of Archegoniates and Gymnosperms is
RT   modified in the plastid DNAs of Dicots and is not plastome encoded in
RT   Monocots.";
RL   J. Plant Physiol. 146:258-262(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Protonema;
RA   Sugita M., Sugiura C.;
RT   "Physcomitrella patens chloroplast genes.";
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Gransden 2004;
RX   PubMed=12954768; DOI=10.1093/nar/gkg726;
RA   Sugiura C., Kobayashi Y., Setsuyuki A., Sugita C., Sugita M.;
RT   "Complete chloroplast DNA sequence of the moss Physcomitrella patens:
RT   evidence for the loss and relocation of rpoA from the chloroplast to
RT   the nucleus.";
RL   Nucleic Acids Res. 31:5324-5331(2003).
RN   [4]
RP   PROTEIN SEQUENCE OF 184-195.
RC   TISSUE=Protonema;
RX   PubMed=9129336; DOI=10.1007/s004250050065;
RA   Kasten B., Buck F., Nuske J., Reski R.;
RT   "Cytokinin affects nuclear- and plastome-encoded energy-converting
RT   plastid enzymes.";
RL   Planta 201:261-272(1997).
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: 2 3-phospho-D-glycerate + 2 H(+) = D-ribulose
CC       1,5-bisphosphate + CO(2) + H(2)O. {ECO:0000255|HAMAP-
CC       Rule:MF_01338}.
CC   -!- CATALYTIC ACTIVITY: 3-phospho-D-glycerate + 2-phosphoglycolate =
CC       D-ribulose 1,5-bisphosphate + O(2). {ECO:0000255|HAMAP-
CC       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-
CC       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
CC       subunit 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
CC       oxidative stress and protein turnover. {ECO:0000255|HAMAP-
CC       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
CC       RuBisCO this homodimer is arranged in a barrel-like tetramer with
CC       the small subunits forming a tetrameric "cap" on each end of the
CC       "barrel". {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}.
DR   EMBL; X74156; CAA52269.1; -; Genomic_DNA.
DR   EMBL; AB066207; BAB62086.1; -; Genomic_DNA.
DR   EMBL; AP005672; BAC85044.1; -; Genomic_DNA.
DR   PIR; S34663; S34663.
DR   RefSeq; NP_904194.1; NC_005087.1.
DR   ProteinModelPortal; P34915; -.
DR   SMR; P34915; -.
DR   PRIDE; P34915; -.
DR   GeneID; 2546763; -.
DR   KEGG; ppp:PhpapaCp031; -.
DR   InParanoid; P34915; -.
DR   KO; K01601; -.
DR   Proteomes; UP000006727; Chloroplast.
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   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   1: Evidence at protein level;
KW   Acetylation; Calvin cycle; Carbon dioxide fixation; Chloroplast;
KW   Complete proteome; Direct protein sequencing; Disulfide bond; Lyase;
KW   Magnesium; Metal-binding; Methylation; Monooxygenase; Oxidoreductase;
KW   Photorespiration; Photosynthesis; Plastid; Reference proteome.
FT   PROPEP        1      2       {ECO:0000255|HAMAP-Rule:MF_01338}.
FT                                /FTId=PRO_0000031347.
FT   CHAIN         3    475       Ribulose bisphosphate carboxylase large
FT                                chain.
FT                                /FTId=PRO_0000031348.
FT   ACT_SITE    175    175       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   ACT_SITE    294    294       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   METAL       201    201       Magnesium; via carbamate group.
FT                                {ECO:0000255|HAMAP-Rule:MF_01338}.
FT   METAL       203    203       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   METAL       204    204       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     123    123       Substrate; in homodimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_01338}.
FT   BINDING     173    173       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     177    177       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     295    295       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     327    327       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   BINDING     379    379       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   SITE        334    334       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_01338}.
FT   MOD_RES       3      3       N-acetylproline. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   MOD_RES      14     14       N6,N6,N6-trimethyllysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01338}.
FT   MOD_RES     201    201       N6-carboxylysine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01338}.
FT   DISULFID    247    247       Interchain; in linked form.
FT                                {ECO:0000255|HAMAP-Rule:MF_01338}.
FT   CONFLICT      9      9       A -> T (in Ref. 1; CAA52269).
FT                                {ECO:0000305}.
FT   CONFLICT     30     30       Q -> H (in Ref. 1; CAA52269).
FT                                {ECO:0000305}.
FT   CONFLICT     50     50       A -> L (in Ref. 1; CAA52269).
FT                                {ECO:0000305}.
FT   CONFLICT    190    190       Y -> N (in Ref. 1; CAA52269).
FT                                {ECO:0000305}.
FT   CONFLICT    251    251       I -> L (in Ref. 1; CAA52269).
FT                                {ECO:0000305}.
FT   CONFLICT    255    256       QF -> PC (in Ref. 1; CAA52269).
FT                                {ECO:0000305}.
FT   CONFLICT    301    301       L -> V (in Ref. 1; CAA52269).
FT                                {ECO:0000305}.
FT   CONFLICT    339    339       R -> L (in Ref. 1; CAA52269).
FT                                {ECO:0000305}.
FT   CONFLICT    372    374       PGV -> QVF (in Ref. 1; CAA52269).
FT                                {ECO:0000305}.
FT   CONFLICT    385    385       W -> G (in Ref. 1; CAA52269).
FT                                {ECO:0000305}.
FT   CONFLICT    414    414       A -> T (in Ref. 1; CAA52269).
FT                                {ECO:0000305}.
SQ   SEQUENCE   475 AA;  52705 MW;  30A91B8A714507AF CRC64;
     MSPRPEIKAG VGFKAGVKDY RLTYYTPDYQ TKDTDILAAF RMTPQPGVPA EECGAAVAAE
     SSTGTWTTVW TDGLTSLDRY KGRCYAIEPV AGEENQYIAY VAYPLDLFEE GSVTNLFTSI
     VGNVFGFKAL RALRLEDLRI PPAYSKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL
     SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF CAEAIYKSQG ETGEIKGHYL
     NATAGTCEEM IKRAQFAREL GMPIVMHDYL TGGFTANTSL AHYCRDNGLL LHIHRAMHAV
     LDRQKNHGMH FRVLAKALRL SGGDHIHSGT VVGKLEGERQ VTLGFVDLLR DDYIEKDRSR
     GIYFTQDWVS LPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN
     RVALEACVQA RNEGRDLARE GNEIIREAAK WSPELAAACE VWKEIKFEFD TVDTL
//
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