RBL1A_HYDCU
ID RBL1A_HYDCU Reviewed; 472 AA.
AC Q31IK0;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
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, ECO:0000269|PubMed:18974784};
DE AltName: Full=Non-carboxysomal form I RuBisCO large subunit {ECO:0000303|PubMed:28115547};
GN Name=cbbL1 {ECO:0000255|HAMAP-Rule:MF_01338}; OrderedLocusNames=Tcr_0427;
OS Hydrogenovibrio crunogenus (strain DSM 25203 / XCL-2) (Thiomicrospira
OS crunogena).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Hydrogenovibrio.
OX NCBI_TaxID=317025;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25203 / XCL-2;
RX PubMed=17105352; DOI=10.1371/journal.pbio.0040383;
RA Scott K.M., Sievert S.M., Abril F.N., Ball L.A., Barrett C.J., Blake R.A.,
RA Boller A.J., Chain P.S.G., Clark J.A., Davis C.R., Detter C., Do K.F.,
RA Dobrinski K.P., Faza B.I., Fitzpatrick K.A., Freyermuth S.K., Harmer T.L.,
RA Hauser L.J., Huegler M., Kerfeld C.A., Klotz M.G., Kong W.W., Land M.,
RA Lapidus A., Larimer F.W., Longo D.L., Lucas S., Malfatti S.A., Massey S.E.,
RA Martin D.D., McCuddin Z., Meyer F., Moore J.L., Ocampo L.H. Jr., Paul J.H.,
RA Paulsen I.T., Reep D.K., Ren Q., Ross R.L., Sato P.Y., Thomas P.,
RA Tinkham L.E., Zeruth G.T.;
RT "The genome of deep-sea vent chemolithoautotroph Thiomicrospira crunogena
RT XCL-2.";
RL PLoS Biol. 4:1-17(2006).
RN [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=DSM 25203 / XCL-2;
RX PubMed=18974784; DOI=10.1371/journal.pone.0003570;
RA Menon B.B., Dou Z., Heinhorst S., Shively J.M., Cannon G.C.;
RT "Halothiobacillus neapolitanus carboxysomes sequester heterologous and
RT chimeric RubisCO species.";
RL PLoS ONE 3:e3570-e3570(2008).
RN [3]
RP INDUCTION.
RC STRAIN=DSM 25203 / XCL-2;
RX PubMed=28115547; DOI=10.1128/jb.00871-16;
RG USF MCB4404L;
RA Mangiapia M., Brown T.W., Chaput D., Haller E., Harmer T.L., Hashemy Z.,
RA Keeley R., Leonard J., Mancera P., Nicholson D., Stevens S., Wanjugi P.,
RA Zabinski T., Pan C., Scott K.M.;
RT "Proteomic and Mutant Analysis of the CO2 Concentrating Mechanism of
RT Hydrothermal Vent Chemolithoautotroph Thiomicrospira crunogena.";
RL J. Bacteriol. 199:0-0(2017).
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 (By similarity). Can replace the endogenous type I
CC ccbL gene in H.neapolitanus, constituting an active RuBisCO, however
CC the active enzyme is not targeted to carboxysomes (PubMed:18974784).
CC {ECO:0000255|HAMAP-Rule:MF_01338, ECO:0000269|PubMed:18974784}.
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:0000269|PubMed:18974784};
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:18974784}.
CC -!- INDUCTION: Induced by growth in high levels of dissolved inorganic
CC carbon and low NH(3) levels (at protein level).
CC {ECO:0000269|PubMed:28115547}.
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}.
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DR EMBL; CP000109; ABB41023.1; -; Genomic_DNA.
DR RefSeq; WP_011369848.1; NC_007520.2.
DR AlphaFoldDB; Q31IK0; -.
DR SMR; Q31IK0; -.
DR STRING; 317025.Tcr_0427; -.
DR EnsemblBacteria; ABB41023; ABB41023; Tcr_0427.
DR KEGG; tcx:Tcr_0427; -.
DR eggNOG; COG1850; Bacteria.
DR HOGENOM; CLU_031450_2_0_6; -.
DR OMA; EYRETYW; -.
DR OrthoDB; 848380at2; -.
DR GO; GO:0005737; C:cytoplasm; 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 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 Calvin cycle; Carbon dioxide fixation; Cytoplasm; Lyase; Magnesium;
KW Metal-binding; Monooxygenase; Oxidoreductase.
FT CHAIN 1..472
FT /note="Ribulose bisphosphate carboxylase large chain 1"
FT /id="PRO_0000251466"
FT ACT_SITE 167
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT ACT_SITE 286
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 115
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 193
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 195
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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 287
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 319
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 371
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT SITE 326
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT MOD_RES 193
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
SQ SEQUENCE 472 AA; 52568 MW; 5E70D6B51D425EC2 CRC64;
MAKTYNAGVK EYRETYWMPE YEPKDSDFLA CFKVIPQDGV PREEIAAAVA AESSTGTWTT
VWTDLLTDLD YYKGRAYKIE DVPGDDAAFY AFIAYPIDLF EEGSVVSVMT SLVGNVFGFK
ALRACRLEDI RFPLAYVMTC GGPPHGIQVE RDKMDKYGRP MLGCTIKPKL GLSAKNYGRA
VYECLRGGLD FTKDDENVTS QPFMRWRDRF LFCQDAIEKA QAETGERKGH YLNCTAGTPE
EMYERAEFAK EIGTPIIMHD YLTGGFTANT GLANYCRKNG LLLHIHRAMH GVIDRNPHHG
IHFRVLTKAL RLSGGDHLHS GTVVGKLEGD REATLGWIDL MRDSFIPEDR SRGIMFDQDF
GAMPGVMPVA SGGIHVWHMP ALVSIFGDDS VLQFGGGTLG HPWGNAAGAA ANRVALEACV
QARNEGKEVE KEGKEILTNA AKHSPELKIA METWKEIKFE FDTVDKLDVK HK
