Q07N61 (RBL2_RHOP5) Reviewed, UniProtKB/Swiss-Prot

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:	RPE_2686

Organism

Rhodopseudomonas palustris (strain BisA53) [Complete proteome] [HAMAP]

Taxonomic identifier

316055 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bradyrhizobiaceae › Rhodopseudomonas › Rhodopseudomonas palustris

Protein attributes

Sequence length	460 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-Rule MF_01339
Catalytic activity	2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O. HAMAP-Rule MF_01339 3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2. HAMAP-Rule 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. HAMAP-Rule 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	reductive pentose-phosphate cycle Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	magnesium ion binding Inferred from electronic annotation. Source: HAMAP 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 – 460	460	Ribulose bisphosphate carboxylase HAMAP-Rule MF_01339		PRO_1000067650
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)
	Q07N61 [UniParc]. Last modified October 31, 2006. Version 1. Checksum: 4AED8610E910F883	FASTA	460	50,252
	10 20 30 40 50 60 MDQSSRYANL NLKEKDLIAG GRHVLCAYIV KPKAGFGDFL QTAAHFAAES STGTNVEVST 70 80 90 100 110 120 TDDFTRGVDA LVYEIDESKE LMKIAYPVEL FDRNVIDGRA MIASFLTLTI GNNQGMGDVE 130 140 150 160 170 180 YAKMYDFYVP PAYLKLFDGP STTIKDLWRV LGRPVVDGGF IVGTIIKPKL GLRPQPFANA 190 200 210 220 230 240 CFDFWLGGDF IKNDEPQGNQ VFAPFKETVR AVNEAMRRAQ DATGQAKLFS FNITADDHYE 250 260 270 280 290 300 MLARGEYILE TFGENADHIA FLVDGYVAGP AAVTTARRAF PKQYLHYHRA GHGAVTSPQS 310 320 330 340 350 360 KRGYTAFVLS KMARLQGASG IHTGTMGFGK MEGEAADRAM AFMITEDSAD GPYFHQEWLG 370 380 390 400 410 420 MNPTTPIISG GMNALRMPGF FTNLGHSNLI MTAGGGAFGH LDGGAAGAKS LRQAEQCWKL 430 440 450 460 GADPVQFAKE HHEFARAFES FSHDADKLFP GWRGQLGLAA

References

[1]

"Complete sequence of Rhodopseudomonas palustris BisA53." US DOE Joint Genome Institute 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., Kim E., Harwood C.S., Oda Y., Richardson P. Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: BisA53.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000463 Genomic DNA. Translation: ABJ06623.1.
RefSeq	YP_781603.1. NC_008435.1.
3D structure databases
ProteinModelPortal	Q07N61.
SMR	Q07N61. Positions 2-458.
ModBase	Search...
Protein-protein interaction databases
STRING	316055.RPE_2686.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABJ06623; ABJ06623; RPE_2686.
GeneID	4360364.
KEGG	rpe:RPE_2686.
PATRIC	23259930. VBIRhoPal93214_2710.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1850.
HOGENOM	HOG000230831.
KO	K01601.
OMA	NQYLHYH.
ProtClustDB	PRK13475.
Enzyme and pathway databases
BioCyc	RPAL316055:GHR9-2742-MONOMER.
Family and domain databases
Gene3D	3.20.20.110. 1 hit. 3.30.70.150. 1 hit.
HAMAP	MF_01339. RuBisCO_L_type2.
InterPro	IPR020871. RuBisCO. IPR020878. RuBisCo_large_chain_AS. IPR000685. RuBisCO_lsu_C. IPR017443. RuBisCO_lsu_fd_N. IPR017444. RuBisCO_lsu_N. [Graphical view]
Pfam	PF00016. RuBisCO_large. 1 hit. PF02788. RuBisCO_large_N. 1 hit. [Graphical view]
SUPFAM	SSF51649. RuBisCO_large. 1 hit. SSF54966. RuBisCO_large. 1 hit.
PROSITE	PS00157. RUBISCO_LARGE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RBL2_RHOP5

Accession

Primary (citable) accession number: Q07N61

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	October 31, 2006
Last modified:	May 1, 2013
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program