ID   A0A4P8XU74_GUITH        Unreviewed;       344 AA.
AC   A0A4P8XU74;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   12-AUG-2020, entry version 6.
DE   RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000256|RuleBase:RU000302};
DE            EC=4.1.1.39 {ECO:0000256|RuleBase:RU000302};
DE   Flags: Fragment;
GN   Name=rbcL {ECO:0000313|EMBL:QCT05629.1};
OS   Guillardia theta (Cryptophyte) (Cryptomonas phi).
OG   Plastid {ECO:0000313|EMBL:QCT05629.1}.
OC   Eukaryota; Cryptophyceae; Pyrenomonadales; Geminigeraceae; Guillardia.
OX   NCBI_TaxID=55529 {ECO:0000313|EMBL:QCT05629.1};
RN   [1] {ECO:0000313|EMBL:QCT05629.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCMP327 {ECO:0000313|EMBL:QCT05629.1};
RX   PubMed=31088271; DOI=.1098/rspb.2019.0655;
RA   Greenwold M.J., Cunningham B.R., Lachenmyer E.M., Pullman J.M.,
RA   Richardson T.L., Dudycha J.L.;
RT   "Diversification of light capture ability was accompanied by the evolution
RT   of phycobiliproteins in cryptophyte algae.";
RL   Proc. R. Soc. B 286:20190655-20190655(2019).
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;
CC         Evidence={ECO:0000256|RuleBase:RU000302};
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:0000256|RuleBase:RU000302};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU000302};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|RuleBase:RU000302};
CC   -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains.
CC       {ECO:0000256|RuleBase:RU000302}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000256|RuleBase:RU000302}.
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family.
CC       {ECO:0000256|RuleBase:RU000302}.
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DR   EMBL; MK818447; QCT05629.1; -; Genomic_DNA.
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:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.110; -; 1.
DR   Gene3D; 3.30.70.150; -; 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   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   3: Inferred from homology;
KW   Calvin cycle {ECO:0000256|ARBA:ARBA00022567,
KW   ECO:0000256|RuleBase:RU000302};
KW   Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300,
KW   ECO:0000256|RuleBase:RU000302};
KW   Chloroplast {ECO:0000256|RuleBase:RU000302};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000302};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU000302};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU000302};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW   ECO:0000256|RuleBase:RU000302};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000302};
KW   Photorespiration {ECO:0000256|RuleBase:RU000302};
KW   Photosynthesis {ECO:0000256|RuleBase:RU000302};
KW   Plastid {ECO:0000256|ARBA:ARBA00022640, ECO:0000313|EMBL:QCT05629.1}.
FT   DOMAIN          9..129
FT                   /note="RuBisCO_large_N"
FT                   /evidence="ECO:0000259|Pfam:PF02788"
FT   DOMAIN          139..341
FT                   /note="RuBisCO_large"
FT                   /evidence="ECO:0000259|Pfam:PF00016"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:QCT05629.1"
FT   NON_TER         344
FT                   /evidence="ECO:0000313|EMBL:QCT05629.1"
SQ   SEQUENCE   344 AA;  38325 MW;  E2AA12E4C900C052 CRC64;
     VIPYAKMGYW DADYVIKDTD VLAMFRMTPQ KGVDPVECAA AIAGESSTAT WTVVWTDLLT
     ACDLYRAKAY RVDPVPGATD QYFAYIAYEL DLFEEGSLAN LTASIIGNVF GFKAVNALRL
     EDMRLPIAYL KTFQGPATGV IVERERLDKY GRPLLGATVK PKLGLSGKNY GRVVYEGLKG
     GLDFLKDDEN INSQPFMRWK ERFLFGIEGV NRAAAAAGEV KGHYFNVTAG TMEDMYERAE
     FCKEIGSVIC MIDLVIGYTA IQSMAIWARK NSMILHLHRA GNSTYSRQKT HGMNFRVICK
     WMRMAGVDHI HAGTVVGKLE GDPLMVKGFY NTLLETQTDV NLVQ
//