Reviewed, UniProtKB/Swiss-Prot Q213J3 (RBL2_RHOPB)

Names and origin

Protein names

Recommended name:
    Ribulose bisphosphate carboxylase
      Short name=RuBisCO
    EC=4.1.1.39

Gene names

Name:	cbbM
Ordered Locus Names:	RPC_2895

Organism

Rhodopseudomonas palustris (strain BisB18) [Complete proteome] [HAMAP]

Taxonomic identifier

316056 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bradyrhizobiaceae › Rhodopseudomonas

Protein attributes

Sequence length	461 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site By similarity.
Catalytic activity	2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O. HAMAP MF_01339 3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2. HAMAP MF_01339
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Subunit structure	Homodimer By similarity.
Miscellaneous	The basic functional RuBisCO is composed of a large chain homodimer in a "head-to-tail" conformation. In contrast to form I RuBisCO, the form II RuBisCO are composed solely of large subunits By similarity.
Sequence similarities	Belongs to the RuBisCO large chain family. Type II subfamily.

Ontologies

Keywords
Biological process	Calvin cycle Carbon dioxide fixation Photosynthesis
Ligand	Magnesium Metal-binding
Molecular function	Lyase Monooxygenase Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW reductive pentose-phosphate cycle Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW monooxygenase activity Inferred from electronic annotation. Source: UniProtKB-KW ribulose-bisphosphate carboxylase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 461	461	Ribulose bisphosphate carboxylase HAMAP MF_01339		PRO_0000251410
Sites
	Active site	167	1	Proton acceptor By similarity
	Active site	288	1	Proton acceptor By similarity
	Metal binding	192	1	Magnesium; via carbamate group By similarity
	Metal binding	194	1	Magnesium By similarity
	Metal binding	195	1	Magnesium By similarity
	Binding site	112	1	Substrate; in homodimeric partner By similarity
	Binding site	169	1	Substrate By similarity
	Binding site	289	1	Substrate By similarity
	Binding site	322	1	Substrate By similarity
	Binding site	369	1	Substrate By similarity
	Site	330	1	Transition state stabilizer By similarity
Amino acid modifications
	Modified residue	192	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q213J3-1 [UniParc]. Last modified April 18, 2006. Version 1. Checksum: 33252C39508E66E4	FASTA	461	50,554
	10 20 30 40 50 60 MDQSNRYANL NLTEKDLIAG GRHVLCAYIM KPKAGFGNFL QTAAHFAAES STGTNVEVST 70 80 90 100 110 120 TDDFTRGVDA LVYEIDEAKQ LMKIAYPIDL FDRNIIDGRA MIASFLTLTI GNNQGMGDVE 130 140 150 160 170 180 YAKMYDFYVP PAYLKLFDGP STTIKDLWRV LGRPVVDGGF IVGTIIKPKL GLRPQPFANA 190 200 210 220 230 240 CYDFWLGGDF IKNDEPQGNQ VFAPFKETVR LVNDAMRRAQ DKTGQPKLFS FNITADDHHE 250 260 270 280 290 300 MVARGEYILE TFADNADHIA FLVDGYVAGP AAVTTARRRF PKQYLHYHRA GHGAVTSPQA 310 320 330 340 350 360 KRGYTAFVLS KMARLQGASG IHTGTMGFGK MEGEAADRAM AYMITEDSAD GPYFHQEWLG 370 380 390 400 410 420 MNPTTPIISG GMNALRMPGF FKNLGHSNLI MTAGGGAFGH IDGGAAGAKS LRQAEQCWKE 430 440 450 460 GADPVAFAKE HREFARAFES FPHDADALYP NWRGQLGLAA A

References

[1]

"Complete sequence of Rhodopseudomonas palustris BisB18." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. , Hauser L., Pelletier D.A., Kyrpides N., Anderson I., Oda Y., Harwood C.S., Richardson P. Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000301 Genomic DNA. Translation: ABD88443.1.
RefSeq	YP_532762.1.
3D structure databases
SMR	Q213J3. Positions 2-458.
ModBase	Search...
Genome annotation databases
GeneID	3971923.
GenomeReviews	Gene locus RPC_2895 in contig CP000301_GR.
KEGG	rpc:RPC_2895.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q213J3.
OMA	Q213J3. LRLPGFF.
Enzyme and pathway databases
BioCyc	RPAL316056:RPC_2895-MON.
Family and domain databases
HAMAP	MF_01339. [Tree]
InterPro	IPR000685. RuBisCO_lsu_C. IPR017443. RuBisCO_lsu_fd_N. IPR017444. RuBisCO_lsu_N. [Graphical view]
Gene3D	G3DSA:3.20.20.110. RuBisCO_large. 1 hit. G3DSA:3.30.70.150. RuBisCO_large. 1 hit.
Pfam	PF00016. RuBisCO_large. 1 hit. PF02788. RuBisCO_large_N. 1 hit. [Graphical view]
PROSITE	PS00157. RUBISCO_LARGE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RBL2_RHOPB

Accession

Primary (citable) accession number: Q213J3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2006
Last sequence update:	April 18, 2006
Last modified:	June 16, 2009
This is version 25 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)