Reviewed, UniProtKB/Swiss-Prot Q2J1J9 (RBL2_RHOP2)

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:	RPB_0951

Organism

Rhodopseudomonas palustris (strain HaA2) [Complete proteome] [HAMAP]

Taxonomic identifier

316058 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bradyrhizobiaceae › Rhodopseudomonas

Protein attributes

Sequence length	461 AA.
Sequence status	Complete.
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. HAMAP MF_01339
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. HAMAP MF_01339
Subunit structure	Homodimer By similarity. HAMAP MF_01339
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. HAMAP MF_01339
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
Cellular component	plastid Inferred from electronic annotation. Source: InterPro
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_0000251409
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)
	Q2J1J9-1 [UniParc]. Last modified March 7, 2006. Version 1. Checksum: 78A84C7343DE90E9	FASTA	461	50,522
	10 20 30 40 50 60 MDQSSRYANL NLKESDLIAG GRHVLCAYIM KPKDGFGNFL QTAAHFSAES STGTNVEVST 70 80 90 100 110 120 TDDFTRGVDA LVYEIDEANN VMKIAYPIEL FDRNVIDGRA MIASFLTLTI GNNQGMGDVE 130 140 150 160 170 180 YAKMHDFYVP PAYLRLFDGP STTIRDLWRV LGRPVVDGGF IVGTIIKPKL GLRPQPFADA 190 200 210 220 230 240 CYDFWLGGDF IKNDEPQGNQ VFAPFKETVR AVNEAMRRAQ DKTGEPKLFS FNITADDHYE 250 260 270 280 290 300 MVARGEYILE TFADNADHVA FLVDGYVAGP AAVTTARRAF PKQYLHYHRA GHGAVTSPQS 310 320 330 340 350 360 KRGYTAFVLS KMARLQGASG IHTGTMGFGK MEGEAADRAM AYMITEDSAD GPFFHQEWLG 370 380 390 400 410 420 MNPTTPIISG GMNALRMPGF FDNLGHSNLI MTAGGGAFGH IDGGAAGAKS LRQAEQCWKA 430 440 450 460 GADPVEFAKD HREFARAFES FPHDADALYP NWRNSLKLAA A

References

[1]

"Complete sequence of Rhodopseudomonas palustris HaA2." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., 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 (JAN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000250 Genomic DNA. Translation: ABD05661.1.
RefSeq	YP_484572.1.
3D structure databases
SMR	Q2J1J9. Positions 2-456.
ModBase	Search...
Protein-protein interaction databases
STRING	Q2J1J9.
Genome annotation databases
GeneID	3909306.
GenomeReviews	Gene locus RPB_0951 in contig CP000250_GR.
KEGG	rpb:RPB_0951.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1850.
HOGENOM	HBG405441.
OMA	NVEVCTT.
Family and domain databases
HAMAP	MF_01339. RuBisCO_L_type2. [Tree]
InterPro	IPR020871. RuBisCO. IPR020878. RuBisCo_large_chain_AS. 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_RHOP2

Accession

Primary (citable) accession number: Q2J1J9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2006
Last sequence update:	March 7, 2006
Last modified:	January 19, 2010
This is version 31 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)