RBL1A_ACIF2
ID RBL1A_ACIF2 Reviewed; 473 AA.
AC B7JB30; P28895; Q9X5Z0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Ribulose bisphosphate carboxylase large chain 1 {ECO:0000255|HAMAP-Rule:MF_01338};
DE Short=RuBisCO large subunit 1 {ECO:0000255|HAMAP-Rule:MF_01338};
DE EC=4.1.1.39 {ECO:0000255|HAMAP-Rule:MF_01338};
GN Name=cbbL1 {ECO:0000255|HAMAP-Rule:MF_01338};
GN Synonyms=rbcL1 {ECO:0000255|HAMAP-Rule:MF_01338};
GN OrderedLocusNames=AFE_1691;
OS Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768
OS / NCIMB 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270)).
OC Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=243159;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12520366; DOI=10.1007/s00284-002-3825-3;
RA Cannon G.C., Baker S.H., Soyer F., Johnson D.R., Bradburne C.E.,
RA Mehlman J.L., Davies P.S., Jiang Q.L., Heinhorst S., Shively J.M.;
RT "Organization of carboxysome genes in the thiobacilli.";
RL Curr. Microbiol. 46:115-119(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455;
RX PubMed=19077236; DOI=10.1186/1471-2164-9-597;
RA Valdes J., Pedroso I., Quatrini R., Dodson R.J., Tettelin H., Blake R. II,
RA Eisen J.A., Holmes D.S.;
RT "Acidithiobacillus ferrooxidans metabolism: from genome sequence to
RT industrial applications.";
RL BMC Genomics 9:597-597(2008).
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. Both reactions occur simultaneously and in competition at
CC the same active site. {ECO:0000255|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; Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_01338};
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}.
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}.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01338}.
CC -!- CAUTION: In A.ferrooxidans two similar set of genes code for RuBisCO
CC large and small chains: the rbcL1-rbcS1 and the rbcL2-rbcS2 sets.
CC {ECO:0000305}.
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DR EMBL; AF129925; AAD30508.1; -; Genomic_DNA.
DR EMBL; CP001219; ACK79627.1; -; Genomic_DNA.
DR RefSeq; WP_012536704.1; NC_011761.1.
DR AlphaFoldDB; B7JB30; -.
DR SMR; B7JB30; -.
DR STRING; 243159.AFE_1691; -.
DR PaxDb; B7JB30; -.
DR PRIDE; B7JB30; -.
DR EnsemblBacteria; ACK79627; ACK79627; AFE_1691.
DR GeneID; 66433214; -.
DR KEGG; afr:AFE_1691; -.
DR eggNOG; COG1850; Bacteria.
DR HOGENOM; CLU_031450_2_0_6; -.
DR OMA; IHGHPDG; -.
DR OrthoDB; 848380at2; -.
DR Proteomes; UP000001362; Chromosome.
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 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 3: Inferred from homology;
KW Calvin cycle; Carbon dioxide fixation; Lyase; Magnesium; Metal-binding;
KW Monooxygenase; Oxidoreductase; Reference proteome.
FT CHAIN 1..473
FT /note="Ribulose bisphosphate carboxylase large chain 1"
FT /id="PRO_0000369190"
FT ACT_SITE 168
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT ACT_SITE 287
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 116
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 194
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 196
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 197
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 288
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 320
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 372
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT SITE 327
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT MOD_RES 194
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
SQ SEQUENCE 473 AA; 52793 MW; 245C8C1715FEFA46 CRC64;
MAVKKYEAGV KEYRQTYWAP EYVPLDSDIL ACFKITPQPG VDREEAAAAV AAESSTGTWT
TVWTDLLTDM DYYKGRAYRI EDVPGDDTSF YAFIAYPIDL FEEGSVVNVF TSLVGNVFGF
KAVRALRLED VRFPLAYVKT CNGPPHGIQV ERDKMNKYGR PMLGCTIKPK LGLSAKNYGR
AVYECLRGGL DFTKDDENVN SQPFMRWRDR FLFVADAIHT AEAETGERKG HYLNVTAPSP
EEMYERAEFA KELNMPIIMH DFLTGGFCAN TGLARWCRKT GTLLHIHRAM HAVVDRNPHH
GIHFRVLVKA LRLSGGDHLH TGTVVGKLEG DRASTQGWVD LLRESFVPED RSRGIFFDQD
WGSMPGVFAV ASGGIHVWHM PSLLAIFGDD AVFQFGGGTL GHPWGNAAGA AANRVALEAC
VEARNEGRDL EREGKDILTN AAKDSPELKI ALETWKEIKF EFDTVDKLDV VNR
