RBL2_HYDMR
ID RBL2_HYDMR Reviewed; 463 AA.
AC Q59462; Q75W26;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Ribulose bisphosphate carboxylase;
DE Short=RuBisCO;
DE EC=4.1.1.39;
GN Name=cbbM {ECO:0000303|PubMed:7765489}; Synonyms=cbbL-3;
OS Hydrogenovibrio marinus.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Hydrogenovibrio.
OX NCBI_TaxID=28885;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND OPERON ORGANIZATION.
RC STRAIN=DSM 11271 / JCM 7688 / MH-110;
RX PubMed=7765489; DOI=10.1271/bbb.58.1733;
RA Yaguchi T., Chung S.Y., Igarashi Y., Kodama T.;
RT "Cloning and sequence of the L2 form of RubisCO from a marine obligately
RT autotrophic hydrogen-oxidizing bacterium, Hydrogenovibrio marinus strain
RT MH-110.";
RL Biosci. Biotechnol. Biochem. 58:1733-1737(1994).
RN [2]
RP PROTEIN SEQUENCE OF 2-31, AND SUBUNIT.
RC STRAIN=DSM 11271 / JCM 7688 / MH-110;
RX PubMed=8319883; DOI=10.1111/j.1574-6968.1993.tb06142.x;
RA Chung S.Y., Yaguchi T., Nishihara H., Igarashi Y., Kodama T.;
RT "Purification of form L2 RubisCO from a marine obligately autotrophic
RT hydrogen-oxidizing bacterium, Hydrogenovibrio marinus strain MH-110.";
RL FEMS Microbiol. Lett. 109:49-53(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION OF EXPRESSION BY CO(2) IN
RP H.MARINUS.
RC STRAIN=DSM 11271 / JCM 7688 / MH-110;
RX PubMed=15317772; DOI=10.1128/jb.186.17.5685-5691.2004;
RA Yoshizawa Y., Toyoda K., Arai H., Ishii M., Igarashi Y.;
RT "CO2-responsive expression and gene organization of three ribulose-1,5-
RT bisphosphate carboxylase/oxygenase enzymes and carboxysomes in
RT Hydrogenovibrio marinus strain MH-110.";
RL J. Bacteriol. 186:5685-5691(2004).
RN [4]
RP CHARACTERIZATION IN E.COLI, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RC STRAIN=DSM 11271 / JCM 7688 / MH-110;
RX DOI=10.1016/S0922-338X(97)86759-1;
RA Hayashi N.R., Oguni A., Yaguchi T., Chung S.-Y., Nishihara H., Kodama T.,
RA Igarashi Y.;
RT "Different properties of gene products of three sets ribulose 1,5-
RT bisphosphate carboxylase/oxygenase from a marine obligately autotrophic
RT hydrogen-oxidizing bacterium, Hydrogenovibrio marinus strain MH-110.";
RL J. Ferment. Bioeng. 85:150-155(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:0000269|Ref.4}.
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:0000269|Ref.4};
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:0000269|Ref.4};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=0.003 umol/min/mg enzyme with CO(2) as substrate, expressed in
CC E.coli {ECO:0000269|Ref.4};
CC Note=The CO(2)/O(2) specificity factor (tau) is 14.8.
CC {ECO:0000269|Ref.4};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8319883, ECO:0000269|Ref.4}.
CC -!- INDUCTION: mRNA expression is constant at all CO(2) concentrations
CC tested, however more protein accumulates at 15% and 2% CO(2) than at
CC 0.15% and 0.03% CO(2) (at protein level).
CC {ECO:0000269|PubMed:15317772}.
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 (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type II
CC subfamily. {ECO:0000305|PubMed:7765489, ECO:0000305|PubMed:8319883}.
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DR EMBL; D28135; BAA05677.1; -; Genomic_DNA.
DR EMBL; AB122071; BAD15326.1; -; Genomic_DNA.
DR PIR; JC2307; JC2307.
DR RefSeq; WP_029912625.1; NZ_JMIU01000001.1.
DR AlphaFoldDB; Q59462; -.
DR SMR; Q59462; -.
DR STRING; 28885.EI16_09265; -.
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; Direct protein sequencing; Lyase;
KW Magnesium; Metal-binding; Monooxygenase; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8319883"
FT CHAIN 2..463
FT /note="Ribulose bisphosphate carboxylase"
FT /id="PRO_0000062662"
FT ACT_SITE 171
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 294
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 328
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 375
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 336
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 196
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250"
FT CONFLICT 379
FT /note="D -> N (in Ref. 3; BAD15326)"
FT /evidence="ECO:0000305"
FT CONFLICT 422
FT /note="A -> D (in Ref. 3; BAD15326)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="E -> D (in Ref. 3; BAD15326)"
FT /evidence="ECO:0000305"
FT CONFLICT 433..435
FT /note="APR -> YAKEHP (in Ref. 3; BAD15326)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 463 AA; 50729 MW; A7F8E289FF92E996 CRC64;
MDQSNRYADL TLTEEKLVAD GNHLLVAYRL KPAAGYGFLE VAAHVAAESS TGTNVEVSTT
DDFTRGVDAL VYEIDEAAFG DKGGLMKIAY PVDLFDPNLI DGHYNVSHMW SLILGNNQGM
GDHEGLRMLD FLVPEKMVKR FDGPATDISD LWKVLGRPEV DGGYIAGTII KPKLGLRPEP
FAKACYDFWL GGDFIKNDEP QANQNFCPME VVIPKVAEAM DRAQQATGQA KLFSANVTAD
FHEEMIKRGE YVLGEFAKYG NEKHVAFLVD GFVTGPAGVT TSRRAFPDTY LHFHRAGHGA
VTSYKSPMGM DPLCYMKLAR LMGASGIHTG TMGYGKMEGH NDERVLAYML ERDECQGPYF
YQKWYGMKPT TPIISGGMDA LRLPGFFENL GHGNVINTCG GGSFGHIDSP AAGGISLGQA
YACWKTGAEP IEAPREFARA FESFPGDADK IFPGWREKLG VHK
