RBL2_HALNC
ID RBL2_HALNC Reviewed; 459 AA.
AC Q9ZHZ4; D0KZQ8;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Ribulose bisphosphate carboxylase {ECO:0000255|HAMAP-Rule:MF_01339};
DE Short=RuBisCO {ECO:0000255|HAMAP-Rule:MF_01339};
DE EC=4.1.1.39 {ECO:0000255|HAMAP-Rule:MF_01339};
DE AltName: Full=Form II RuBisCO {ECO:0000303|PubMed:9696760};
GN Name=cbbM {ECO:0000255|HAMAP-Rule:MF_01339}; OrderedLocusNames=Hneap_1095;
OS Halothiobacillus neapolitanus (strain ATCC 23641 / c2) (Thiobacillus
OS neapolitanus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC Halothiobacillaceae; Halothiobacillus.
OX NCBI_TaxID=555778;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Shively J.M.;
RT "A form II Rubisco gene and associated genes in Thiobacillus
RT neapolitanus.";
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23641 / c2;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Davenport K., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Kerfeld C., Cannon G., Heinhort S.;
RT "Complete sequence of Halothiobacillus neapolitanus c2.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=ATCC 23641 / c2;
RX PubMed=9696760; DOI=10.1128/jb.180.16.4133-4139.1998;
RA Baker S.H., Jin S., Aldrich H.C., Howard G.T., Shively J.M.;
RT "Insertion mutation of the form I cbbL gene encoding ribulose bisphosphate
RT carboxylase/oxygenase (RuBisCO) in Thiobacillus neapolitanus results in
RT expression of form II RuBisCO, loss of carboxysomes, and an increased CO2
RT requirement for growth.";
RL J. Bacteriol. 180:4133-4139(1998).
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_01339}.
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_01339};
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_01339};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01339};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01339};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01339}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:9696760}.
CC -!- INDUCTION: Form II RuBisCO is expressed in the presence of form I, when
CC grown in air with or without 5% CO(2), although it is not the major
CC activity. When the form I gene is disrupted the RuBisCO form II
CC activity increases, but is not found in carboxysomes (at protein
CC level). {ECO:0000269|PubMed:9696760}.
CC -!- MISCELLANEOUS: The basic functional RuBisCO is composed of a large
CC chain homodimer in a 'head-to-tail' conformation. In contrast to form I
CC RuBisCO, the form II RuBisCO are composed solely of large subunits.
CC {ECO:0000255|HAMAP-Rule:MF_01339}.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type II
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01339}.
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DR EMBL; AF046932; AAD02442.1; -; Genomic_DNA.
DR EMBL; CP001801; ACX95931.1; -; Genomic_DNA.
DR RefSeq; WP_012823967.1; NC_013422.1.
DR AlphaFoldDB; Q9ZHZ4; -.
DR SMR; Q9ZHZ4; -.
DR STRING; 555778.Hneap_1095; -.
DR EnsemblBacteria; ACX95931; ACX95931; Hneap_1095.
DR KEGG; hna:Hneap_1095; -.
DR eggNOG; COG1850; Bacteria.
DR HOGENOM; CLU_031450_3_1_6; -.
DR OMA; NQYLHYH; -.
DR OrthoDB; 848380at2; -.
DR Proteomes; UP000009102; Chromosome.
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-KW.
DR CDD; cd08211; RuBisCO_large_II; 1.
DR Gene3D; 3.20.20.110; -; 1.
DR Gene3D; 3.30.70.150; -; 1.
DR HAMAP; MF_01339; RuBisCO_L_type2; 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; IPR020871; RuBisCO_lsuII.
DR PANTHER; PTHR42704; PTHR42704; 1.
DR Pfam; PF00016; RuBisCO_large; 1.
DR Pfam; PF02788; RuBisCO_large_N; 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; Reference proteome.
FT CHAIN 1..459
FT /note="Ribulose bisphosphate carboxylase"
FT /id="PRO_0000062670"
FT ACT_SITE 166
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
FT ACT_SITE 287
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
FT BINDING 111
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
FT BINDING 191
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
FT BINDING 193
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
FT BINDING 194
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
FT BINDING 288
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
FT BINDING 321
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
FT BINDING 368
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
FT SITE 329
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
FT MOD_RES 191
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339"
SQ SEQUENCE 459 AA; 50573 MW; 84101EDB69A063FF CRC64;
MDQSARYADL SLKEEDLIAG GKHILVAYKM KPKAGHGYLE ASAHFAAESS TGTNVEVSTT
DDFTKGVDAL VYYIDEATED MRIAYPMDLF DRNVTDGRMM LVSVLTLIIG NNQGMGDIEH
AKIHDIYFPE RAIQLFDGPS KDISDMWRIL GRPIENGGYI AGTIIKPKLG LRPEPFAAAA
YQFWLGGDFI KNDEPQGNQV FCPLKKVLPL VYDSMKRAQD ETGQAKLFSM NITADDHYEM
MARADFGLET FGPDADKLAF LVDGFVGGPG MITTARRQYP NQYLHYHRAG HGMITSPSAK
RGYTAFVLAK ISRLQGASGI HVGTMGYGKM EGEGDDRNIA YMIERDEAQG PVYFQKWYGM
KPTTPIISGG MNALRLPGFF ENLGHGNVIN TAGGGSYGHI DSPAAGAISL KQAYECWKAG
ADPIEFAKEH KEFARAFESF PKDADAIFPG WREKLGVHK
