Reviewed, UniProtKB/Swiss-Prot P29278 (RBL2_RHOSH)

Names and origin

Protein names

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

Gene names

Name:	cbbM
Synonyms:	cbbL2, rbpL

Organism

Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides)

Taxonomic identifier

1063 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter

Protein attributes

Sequence length	459 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
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 – 459	459	Ribulose bisphosphate carboxylase HAMAP MF_01339		PRO_0000062667
Sites
	Active site	166	1	Proton acceptor By similarity
	Active site	287	1	Proton acceptor By similarity
	Metal binding	191	1	Magnesium; via carbamate group By similarity
	Metal binding	193	1	Magnesium By similarity
	Metal binding	194	1	Magnesium By similarity
	Binding site	111	1	Substrate; in homodimeric partner By similarity
	Binding site	168	1	Substrate By similarity
	Binding site	288	1	Substrate By similarity
	Binding site	321	1	Substrate By similarity
	Binding site	368	1	Substrate By similarity
	Site	329	1	Transition state stabilizer By similarity
Amino acid modifications
	Modified residue	191	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P29278-1 [UniParc]. Last modified July 1, 1993. Version 3. Checksum: 299ABAA836BD683E	FASTA	459	50,519
	10 20 30 40 50 60 MDQSNRYARL DLQEADLIAG GRHVLCAYVM KPKAGYGYLE TAAHFAAESS TGTNVEVSTT 70 80 90 100 110 120 DDFTRGVDAL VYEIDPEKEI MKIAYPVELF DRNIIDGRAM LCSFLTLTIG NNQGMGDVEY 130 140 150 160 170 180 AKMHDFYVPP CYLRLFDGPS MNIADMWRVL GRDVRNGGMV VGTIIKPKLG LRPKPFADAC 190 200 210 220 230 240 HEFWLGADFI KNDEPQGNQT FAPLKETIRL VADAMKRAQD ETGEAKLFSA NITADDHYEM 250 260 270 280 290 300 VARGEYILET FGENADHVAF LVDGYVTGPA AITTARRQFP RQFLHYHRAG HGAVTSPQSM 310 320 330 340 350 360 RGYTAFVLSK MARLQGASGI HTGTMGYGKM EGEAADKIMA YMLTDEAAEG PFYRQTGWGS 370 380 390 400 410 420 KATTPIISGG MNALRLPGFF DNLGHSNVIQ TSGGGAFGHL DGGTAGAKSL RQSHEAWMAG 430 440 450 VDLVTYAREH RELARAFESF PADADKFYPG WRDRLHRAA

References

[1]	"Nucleotide and deduced amino acid sequence of the Rhodobacter sphaeroides gene encoding form II ribulose-1,5-biphosphate carboxylase/oxygenase and comparison with other deduced forms I and II sequences." Wagner S.J., Stevens S.E. Jr., Nixon B.T., Lambert D.H., Quivey R.G. Jr., Tabita F.R. FEMS Microbiol. Lett. 55:217-222(1988) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Identification, expression, and deduced primary structure of transketolase and other enzymes encoded within the form II CO2 fixation operon of Rhodobacter sphaeroides." Chen J.-H., Gibson J.L., McCue L.A., Tabita F.R. J. Biol. Chem. 266:20447-20452(1991) [PubMed: 1939098] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M68914 Genomic DNA. Translation: AAA26158.1. Sequence problems.
PIR	E41080.
3D structure databases
HSSP	HSSP built from PDB template 1RBA based on UniProtKB P04718.
SMR	P29278. Positions 2-455.
ModBase	Search...
Enzyme and pathway databases
BRENDA	4.1.1.39. 2796.
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_RHOSH

Accession

Primary (citable) accession number: P29278

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	July 1, 1993
Last modified:	March 24, 2009
This is version 58 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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