RBL2_RHOCA
ID RBL2_RHOCA Reviewed; 458 AA.
AC P50922;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
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; Synonyms=cbbL2, rbpL;
OS Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=1061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 11166 / DSM 1710 / CCUG 31484 / JCM 21090 / LMG 2962 / NBRC
RC 16435 / NCIMB 8254 / ATH 2.3.1;
RA Larimer F.W., Lu T.-Y.S., Buley D.M.;
RT "Sequence and expression of the form II ribulose-bisphosphate
RT carboxylase/oxygenase (RuBisCO) gene from Rhodobacter capsulatus.";
RL FASEB J. 9:A1275-A1275(1997).
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.
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 -!- 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;
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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U23145; AAB82048.1; -; Genomic_DNA.
DR PIR; T10506; T10506.
DR AlphaFoldDB; P50922; -.
DR SMR; P50922; -.
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 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; Photosynthesis.
FT CHAIN 1..458
FT /note="Ribulose bisphosphate carboxylase"
FT /id="PRO_0000062664"
FT ACT_SITE 166
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 287
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 288
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 321
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 368
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 329
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 191
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 458 AA; 50092 MW; 2C63CDD57C653FAA CRC64;
MDQSNRYARL DLKEADLIAG GRHVLCAYIM KPKAGYGYLE TAAHFAAESS TGTNVEVSTT
DDFTRGVDAL VYEIDPEKEI MKIAYPVELF DRNIIDGGAM LCSFLTLTIG NNQGMGDVEY
AKMHDFYVPP CYLRLFDGPS MNIADMWRVL GRPVVDGGMV VGTIIKPKLG LRPKPFADAC
YEFWLGGDFI KNDEPQGNQT FAPLKETIRL VADAMKRAQD ETGEAKLFSA NITADDHYEM
VARGEYILET FGENADHVAF LVDGYVTGPA AITTARRSFP RQFLHYHRAG HGAVTSPQSM
RGYTAFVLSK MSRLQGASGI HTGTMGYGKM EGDASDKIMA YMLNDEAAQG PFYHQDWLGM
KATTPIISGG MNALRLPGFF DNLGHSNVIQ TSGGGAFGHL DGATAGAKSL RQSCDAWKAG
VDLVTYAKSH RELARAFESF PNDADKLYPG WRVALGVN
