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Database: UniProt
Entry: C6GJY3_9MARC
LinkDB: C6GJY3_9MARC
Original site: C6GJY3_9MARC 
ID   C6GJY3_9MARC            Unreviewed;       320 AA.
AC   C6GJY3;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   22-FEB-2023, entry version 37.
DE   RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000256|ARBA:ARBA00017725, ECO:0000256|RuleBase:RU000302};
DE            EC=4.1.1.39 {ECO:0000256|ARBA:ARBA00012287, ECO:0000256|RuleBase:RU000302};
DE   Flags: Fragment;
GN   Name=rbcL {ECO:0000313|EMBL:ACR82667.1};
OS   Solenostoma speciosum subsp. villosum.
OG   Plastid; Chloroplast {ECO:0000313|EMBL:ACR82667.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Jungermanniopsida; Jungermanniidae; Jungermanniales; Jungermanniineae;
OC   Solenostomataceae; Solenostoma; Solenostoma subgen. Solenostoma.
OX   NCBI_TaxID=644118 {ECO:0000313|EMBL:ACR82667.1};
RN   [1] {ECO:0000313|EMBL:ACR82667.1}
RP   NUCLEOTIDE SEQUENCE.
RX   AGRICOLA=IND44218742; DOI=10.1007/s00606-009-0187-3;
RA   Feldberg K., Hentschel J., Bombosch A., Long D.G., Vana J., Heinrichs J.;
RT   "Transfer of Gottschelia grollei, G. patoniae and Scaphophyllum speciosum
RT   to Solenostoma based on chloroplast DNA rbcL sequences.";
RL   Plant Syst. Evol. 280:243-250(2009).
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|ARBA:ARBA00001067,
CC         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|ARBA:ARBA00000537,
CC         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. Type I
CC       subfamily. {ECO:0000256|ARBA:ARBA00006204}.
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DR   EMBL; FJ984951; ACR82667.1; -; Genomic_DNA.
DR   AlphaFoldDB; C6GJY3; -.
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   Gene3D; 3.20.20.110; Ribulose bisphosphate carboxylase, large subunit, C-terminal domain; 1.
DR   Gene3D; 3.30.70.150; RuBisCO large subunit, N-terminal domain; 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; RIBULOSE BISPHOSPHATE CARBOXYLASE; 1.
DR   PANTHER; PTHR42704:SF9; RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN; 1.
DR   Pfam; PF00016; RuBisCO_large; 1.
DR   Pfam; PF02788; RuBisCO_large_N; 1.
DR   SFLD; SFLDS00014; RuBisCO; 1.
DR   SFLD; SFLDG00301; RuBisCO-like_proteins; 1.
DR   SUPFAM; SSF51649; RuBisCo, C-terminal domain; 1.
DR   SUPFAM; SSF54966; RuBisCO, large subunit, small (N-terminal) domain; 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, ECO:0000313|EMBL:ACR82667.1};
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|ARBA:ARBA00023238,
KW   ECO:0000256|RuleBase:RU000302};
KW   Photosynthesis {ECO:0000256|RuleBase:RU000302};
KW   Plastid {ECO:0000256|ARBA:ARBA00022640, ECO:0000313|EMBL:ACR82667.1}.
FT   DOMAIN          5..73
FT                   /note="Ribulose bisphosphate carboxylase large subunit
FT                   ferrodoxin-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02788"
FT   DOMAIN          83..319
FT                   /note="Ribulose bisphosphate carboxylase large subunit C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00016"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACR82667.1"
FT   NON_TER         320
FT                   /evidence="ECO:0000313|EMBL:ACR82667.1"
SQ   SEQUENCE   320 AA;  35823 MW;  5E2616A5D8E88F4F CRC64;
     DGLTSLDRYK GRCYDIEPVA GEENQYIAYV AYPLDLFEEG SVTNLFTSIV GNVFGFKALR
     ALRLEDLRIP PAYVKTFQGP PHGIQVERDK LNKYGRPLLG CTIKPKLGLS AKNYGRAVYE
     CLRGGLDFTK DDENVNSQPF MRWRDRFLFV AEALFKSQAE TGEIKGHYLN ATAGTCEEML
     KRAACARELG VPIIMHDYLT GGFTANTTLA HYSRDNGLLL HIHRAMHAVI DRQKNHGMHF
     RVLAKALRLS GGDHIHAGTV VGKLEGERDV TLGFVDLLRD DYIEKDRSRG IYFTQDWVSL
     PGVLPVASGG IHVWHMPALT
//
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