ID A0A0F5YKI8_9CYAN Unreviewed; 476 AA.
AC A0A0F5YKI8;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000256|HAMAP-Rule:MF_01338};
DE Short=RuBisCO large subunit {ECO:0000256|HAMAP-Rule:MF_01338};
DE EC=4.1.1.39 {ECO:0000256|HAMAP-Rule:MF_01338};
GN Name=rbcL {ECO:0000256|HAMAP-Rule:MF_01338,
GN ECO:0000313|EMBL:KKD39434.1};
GN Synonyms=cbbL {ECO:0000256|HAMAP-Rule:MF_01338};
GN ORFNames=WN50_03480 {ECO:0000313|EMBL:KKD39434.1};
OS Limnoraphis robusta CS-951.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Sirenicapillariaceae; Limnoraphis.
OX NCBI_TaxID=1637645 {ECO:0000313|EMBL:KKD39434.1, ECO:0000313|Proteomes:UP000033607};
RN [1] {ECO:0000313|EMBL:KKD39434.1, ECO:0000313|Proteomes:UP000033607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS-951 {ECO:0000313|EMBL:KKD39434.1,
RC ECO:0000313|Proteomes:UP000033607};
RA Willis A., Parks M., Burford M.A.;
RT "Draft genome assembly of filamentous brackish cyanobacterium Limnoraphis
RT robusta strain CS-951.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_01338}.
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, ECO:0000256|HAMAP-
CC Rule:MF_01338};
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|HAMAP-Rule:MF_01338};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01338};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-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 subunit
CC homodimers. {ECO:0000256|HAMAP-Rule:MF_01338}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000256|ARBA:ARBA00023587,
CC ECO:0000256|HAMAP-Rule:MF_01338}.
CC -!- PTM: The disulfide bond which can form in the large chain dimeric
CC partners within the hexadecamer appears to be associated with oxidative
CC stress and protein turnover. {ECO:0000256|HAMAP-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:0000256|HAMAP-Rule:MF_01338}.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01338}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKD39434.1}.
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DR EMBL; LATL02000144; KKD39434.1; -; Genomic_DNA.
DR RefSeq; WP_046277111.1; NZ_LATL02000144.1.
DR AlphaFoldDB; A0A0F5YKI8; -.
DR PATRIC; fig|1637645.4.peg.2931; -.
DR OrthoDB; 9770811at2; -.
DR Proteomes; UP000033607; Unassembled WGS sequence.
DR GO; GO:0031470; C:carboxysome; 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:0009853; P:photorespiration; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Bacterial microcompartment {ECO:0000256|ARBA:ARBA00024446};
KW Calvin cycle {ECO:0000256|ARBA:ARBA00022567, ECO:0000256|HAMAP-
KW Rule:MF_01338};
KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP-
KW Rule:MF_01338};
KW Carboxysome {ECO:0000256|ARBA:ARBA00023669, ECO:0000256|HAMAP-
KW Rule:MF_01338}; Disulfide bond {ECO:0000256|HAMAP-Rule:MF_01338};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01338};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01338};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01338};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033, ECO:0000256|HAMAP-
KW Rule:MF_01338};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01338}; Photorespiration {ECO:0000256|HAMAP-Rule:MF_01338};
KW Reference proteome {ECO:0000313|Proteomes:UP000033607}.
FT DOMAIN 25..145
FT /note="Ribulose bisphosphate carboxylase large subunit
FT ferrodoxin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02788"
FT DOMAIN 155..463
FT /note="Ribulose bisphosphate carboxylase large subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF00016"
FT ACT_SITE 176
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT ACT_SITE 295
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT BINDING 124
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT BINDING 202
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT BINDING 204
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT BINDING 205
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT BINDING 328
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT BINDING 380
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT SITE 335
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT MOD_RES 202
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
FT DISULFID 248
FT /note="Interchain; in linked form"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338"
SQ SEQUENCE 476 AA; 53233 MW; 17BE98C1667B0828 CRC64;
MAYSQTRTQS KAGYKAGVQD YKLTYYTPDY TPKDTDILAA FRVTPQPGVP PEEAGAAVAA
ESSTGTWTTV WTDLLTDLDR YKGRCYDIEP VPGEDNQYIC FIAYPLDLFE EGSVTNLLTS
LVGNVFGFKA LRALRLEDLR IPIAYLKTFQ GPPHGITVER DKLNKYGRPL LGCTIKPKLG
LSAKNYGRAV YECLRGGLDF TKDDENINSQ PFMRWRDRFL FVQEAIEKAQ AETGEVKGHY
LNVTAPTCEE MLERAEFAKE LKTPIIMHDY LTGGFTANTT LAKWCRRNGI LLHIHRAMHA
VIDRQKNHGI HFRVLAKCLR MSGGDHLHSG TVVGKLEGEK GITMGFVDLM REDHIEQDRD
RGIYFTQDWA SMPGVMPVAS GGIHIWHMPA LVEIFGDDSC LQFGGGTLGH PWGNAPGATA
NRVALEACIQ ARNEGRNLFR EGGDVIREAA KWSPELAVAC ELWKEIKFEF EAMDTL
//
