ID   RBL_GALSU               Reviewed;         493 AA.
AC   P23755;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   24-JAN-2024, entry version 121.
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};
GN   Name=rbcL {ECO:0000255|HAMAP-Rule:MF_01338};
OS   Galdieria sulphuraria (Red alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Galdieriales; Galdieriaceae;
OC   Galdieria.
OX   NCBI_TaxID=130081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=14-1-1 / Isolate 107.79/Goettingen;
RX   PubMed=2274041; DOI=10.1007/bf00633849;
RA   Valentin K.-U., Zetsche K.;
RT   "Structure of the Rubisco operon from the unicellular red alga Cyanidium
RT   caldarium: evidence for a polyphyletic origin of the plastids.";
RL   Mol. Gen. Genet. 222:425-430(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=UTEX 2393;
RA   Whitney S.M., Andrews J.;
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0007744|PDB:4F0H, ECO:0007744|PDB:4F0K, ECO:0007744|PDB:4F0M}
RP   X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF UNACTIVATED HOLOENZYME IN COMPLEX
RP   WITH O2 OR CO2 AND MAGNESIUM, FUNCTION, SUBUNIT, AND S-NITROSYLATION AT
RP   CYS-181 AND CYS-460.
RX   PubMed=23112176; DOI=10.1073/pnas.1210754109;
RA   Stec B.;
RT   "Structural mechanism of RuBisCO activation by carbamylation of the active
RT   site lysine.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:18785-18790(2012).
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 (Probable).
CC       Carbon dioxide and oxygen bind in the same pocket of the enzyme in a
CC       similar manner (PubMed:23112176). {ECO:0000255|HAMAP-Rule:MF_01338,
CC       ECO:0000269|PubMed:23112176, ECO:0000305|PubMed:23112176}.
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, ECO:0000305|PubMed:23112176};
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         ECO:0000305|PubMed:23112176};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         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       {ECO:0000255|HAMAP-Rule:MF_01338, ECO:0000269|PubMed:23112176}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {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 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, ECO:0000269|PubMed:23112176}.
CC   -!- MISCELLANEOUS: Although originally identified as Cyanidium caldarium,
CC       these sequences derive from Galdieria sulphuraria. {ECO:0000305}.
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; X55524; CAA39140.1; -; Genomic_DNA.
DR   EMBL; AF233069; AAF81681.1; -; Genomic_DNA.
DR   PDB; 4F0H; X-ray; 1.96 A; A=1-493.
DR   PDB; 4F0K; X-ray; 2.05 A; A=1-493.
DR   PDB; 4F0M; X-ray; 2.25 A; A=1-493.
DR   PDBsum; 4F0H; -.
DR   PDBsum; 4F0K; -.
DR   PDBsum; 4F0M; -.
DR   AlphaFoldDB; P23755; -.
DR   SMR; P23755; -.
DR   DIP; DIP-60089N; -.
DR   IntAct; P23755; 1.
DR   eggNOG; ENOG502QTI9; Eukaryota.
DR   BRENDA; 4.1.1.39; 2381.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniRule.
DR   CDD; cd08212; RuBisCO_large_I; 1.
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   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; 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; SFLDG01052; RuBisCO; 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   1: Evidence at protein level;
KW   3D-structure; Calvin cycle; Carbon dioxide fixation; Chloroplast; Lyase;
KW   Magnesium; Metal-binding; Monooxygenase; Oxidoreductase; Photorespiration;
KW   Photosynthesis; Plastid; S-nitrosylation.
FT   CHAIN           1..493
FT                   /note="Ribulose bisphosphate carboxylase large chain"
FT                   /id="PRO_0000062476"
FT   ACT_SITE        184
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   ACT_SITE        302
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         132
FT                   /ligand="substrate"
FT                   /note="in homodimeric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         182
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         186
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         210
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         212
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         213
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         303
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         335
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         387
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   SITE            342
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   MOD_RES         181
FT                   /note="S-nitrosocysteine"
FT                   /evidence="ECO:0000269|PubMed:23112176,
FT                   ECO:0007744|PDB:4F0H, ECO:0007744|PDB:4F0K,
FT                   ECO:0007744|PDB:4F0M"
FT   MOD_RES         210
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   MOD_RES         460
FT                   /note="S-nitrosocysteine"
FT                   /evidence="ECO:0000269|PubMed:23112176,
FT                   ECO:0007744|PDB:4F0H, ECO:0007744|PDB:4F0K,
FT                   ECO:0007744|PDB:4F0M"
FT   HELIX           29..33
FT                   /evidence="ECO:0007829|PDB:4F0H"
FT   STRAND          45..53
FT                   /evidence="ECO:0007829|PDB:4F0H"
FT   HELIX           59..69
FT                   /evidence="ECO:0007829|PDB:4F0H"
FT   HELIX           79..83
FT                   /evidence="ECO:0007829|PDB:4F0H"
FT   HELIX           86..89
FT                   /evidence="ECO:0007829|PDB:4F0H"
FT   STRAND          92..99
FT                   /evidence="ECO:0007829|PDB:4F0H"
FT   STRAND          102..112
FT                   /evidence="ECO:0007829|PDB:4F0H"
FT   HELIX           114..116
FT                   /evidence="ECO:0007829|PDB:4F0H"
FT   HELIX           122..130
FT                   /evidence="ECO:0007829|PDB:4F0H"
FT   HELIX           133..135
FT                   /evidence="ECO:0007829|PDB:4F0H"
FT   TURN            136..138
FT                   /evidence="ECO:0007829|PDB:4F0K"
FT   STRAND          139..148
FT                   /evidence="ECO:0007829|PDB:4F0H"
FT   HELIX           151..154
FT                   /evidence="ECO:0007829|PDB:4F0H"
FT   HELIX           163..171
FT                   /evidence="ECO:0007829|PDB:4F0H"
FT   STRAND          178..182
FT                   /evidence="ECO:0007829|PDB:4F0H"
FT   STRAND          184..187
FT                   /evidence="ECO:0007829|PDB:4F0H"
FT   HELIX           191..204
FT                   /evidence="ECO:0007829|PDB:4F0H"
FT   STRAND          207..210
FT                   /evidence="ECO:0007829|PDB:4F0H"
FT   STRAND          216..218
FT                   /evidence="ECO:0007829|PDB:4F0H"
FT   HELIX           223..241
FT                   /evidence="ECO:0007829|PDB:4F0H"
FT   STRAND          246..250
FT                   /evidence="ECO:0007829|PDB:4F0H"
FT   HELIX           256..269
FT                   /evidence="ECO:0007829|PDB:4F0H"
FT   STRAND          272..277
FT                   /evidence="ECO:0007829|PDB:4F0H"
FT   HELIX           278..280
FT                   /evidence="ECO:0007829|PDB:4F0H"
FT   HELIX           282..294
FT                   /evidence="ECO:0007829|PDB:4F0H"
FT   STRAND          298..302
FT                   /evidence="ECO:0007829|PDB:4F0H"
FT   TURN            304..306
FT                   /evidence="ECO:0007829|PDB:4F0H"
FT   HELIX           307..310
FT                   /evidence="ECO:0007829|PDB:4F0H"
FT   STRAND          311..317
FT                   /evidence="ECO:0007829|PDB:4F0H"
FT   HELIX           319..329
FT                   /evidence="ECO:0007829|PDB:4F0H"
FT   STRAND          332..335
FT                   /evidence="ECO:0007829|PDB:4F0H"
FT   STRAND          339..341
FT                   /evidence="ECO:0007829|PDB:4F0H"
FT   HELIX           347..358
FT                   /evidence="ECO:0007829|PDB:4F0H"
FT   STRAND          360..362
FT                   /evidence="ECO:0007829|PDB:4F0H"
FT   TURN            366..369
FT                   /evidence="ECO:0007829|PDB:4F0H"
FT   STRAND          383..386
FT                   /evidence="ECO:0007829|PDB:4F0H"
FT   HELIX           392..394
FT                   /evidence="ECO:0007829|PDB:4F0H"
FT   HELIX           395..402
FT                   /evidence="ECO:0007829|PDB:4F0H"
FT   STRAND          407..411
FT                   /evidence="ECO:0007829|PDB:4F0H"
FT   HELIX           412..415
FT                   /evidence="ECO:0007829|PDB:4F0H"
FT   HELIX           421..440
FT                   /evidence="ECO:0007829|PDB:4F0H"
FT   HELIX           445..458
FT                   /evidence="ECO:0007829|PDB:4F0H"
FT   HELIX           461..469
FT                   /evidence="ECO:0007829|PDB:4F0H"
FT   TURN            470..473
FT                   /evidence="ECO:0007829|PDB:4F0K"
SQ   SEQUENCE   493 AA;  54989 MW;  B69EE280D47C6FA2 CRC64;
     MSQSLEEKSV QERTRIKNSR YESGVIPYAK MGYWNPDYQV KDTDVLALFR VTPQPGVDPI
     EAAAAVAGES STATWTVVWT DLLTAADLYR AKAYKVDQVP NNPEQYFAYI AYELDLFEEG
     SIANLTASII GNVFGFKAVK ALRLEDMRLP FAYIKTFQGP ATGVILERER LDKFGRPLLG
     CTTKPKLGLS GKNYGRVVYE ALKGGLDFVK DDENINSQPF MRWRERYLFV MEAVNKAAAA
     TGEVKGHYLN VTAATMEEMY ARAQLAKELG SVIIMIDLVI GYTAIQTMAK WARDNDMILH
     LHRAGNSTYS RQKNHGMNFR VICKWMRMAG VDHIHAGTVV GKLEGDPIIT RGFYKTLLLP
     KLERNLQEGL FFDMDWASLR KVMPVASGGI HAGQMHQLIH YLGEDVVLQF GGGTIGHPDG
     IQSGATANRV ALEAMILARN ENRDFLTEGP EILREAAKNC GALRTALDLW KDITFNYTST
     DTSDFVETPT ANI
//