RBL_GALSU
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 03-AUG-2022, entry version 117.
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; Cyanidiales; Cyanidiaceae; 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;
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 {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 STRING; 130081.XP_005705051.1; -.
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; -; 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 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
