Reviewed, UniProtKB/Swiss-Prot O84917 (RBL2_THIIN)

Names and origin

Protein names

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

Gene names

Name:

cbbM

Organism

Thiomonas intermedia (Thiobacillus intermedius)

Taxonomic identifier

926 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Thiomonas

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.
Caution	No expression of this protein has been seen during autotrophic and mixotrophic growth, however the protein is probably expressed under other conditions. In a related bacteria (T.neapolitanus) expression has been seen when the form I enzyme has been knocked out.

Ontologies

Keywords
Biological process	Calvin cycle Carbon dioxide fixation
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
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_0000062669
Sites
	Active site	168	1	Proton acceptor By similarity
	Active site	289	1	Proton acceptor By similarity
	Metal binding	193	1	Magnesium; via carbamate group By similarity
	Metal binding	195	1	Magnesium By similarity
	Metal binding	196	1	Magnesium By similarity
	Binding site	113	1	Substrate; in homodimeric partner By similarity
	Binding site	170	1	Substrate By similarity
	Binding site	290	1	Substrate By similarity
	Binding site	323	1	Substrate By similarity
	Binding site	370	1	Substrate By similarity
	Site	331	1	Transition state stabilizer By similarity
Amino acid modifications
	Modified residue	193	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	O84917-1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: D470D17F356800E2	FASTA	461	50,818
	10 20 30 40 50 60 MAHDQSSRYA NLDLKESDLI AGGKHILVAY KMKPKAGYDY LATAAHFAAE SSTGTNVEVS 70 80 90 100 110 120 TTDDFTKGVD ALVYFIDEAT EDMRIAYPIE LFDRNVIDGR FMIVSFLTLV IGNNQGMGDV 130 140 150 160 170 180 EYGKMIDFYV PERAIQMFDG PATDISNLWR ILGRPIKDGG YIAGTIIKPK LGLRPEPFAQ 190 200 210 220 230 240 AAYQFWLGGD FIKNDEPQGN QVFAPVKKVI PLVYDAMKRA QDETGEAKLF SMNITADDYH 250 260 270 280 290 300 EMCARADFAL EVFGPDADKL AFLVDGYVGG PGMVTTARRQ YPNQYLHYHR AGHGAITSPS 310 320 330 340 350 360 SKRGYTAFVL AKMSRLQGAS GIHVGTMGYG KMEGEGDDRN IAYMIERDEC QGPVYFQKWY 370 380 390 400 410 420 GMKPTTPIIS GGMNALRLPG FFENLGHGNV INTAGGGSYG HIDSPAAGAK SLRQAYECWK 430 440 450 460 AGADPIEYAK EHKEFARAFE SFPGDADKLF PGWRDKLGVH K

References

[1]	"A form II Rubisco gene and associated genes in Thiobacillus intermedius." Shively J.M., Soyer F. Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Cloning and expression of the D-ribulose-1,5-bisphosphate carboxylase/oxygenase form II gene from Thiobacillus intermedius in Escherichia coli." Stoner M.T., Shively J.M. FEMS Microbiol. Lett. 107:287-292(1993) [PubMed: 8472910] [Abstract] Cited for: EXPRESSION IN T.INTERMEDIUS.
[3]	Shively J.M. Unpublished observations (OCT-2005) Cited for: PROBABLE EXPRESSION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF012127 Genomic DNA. Translation: AAC24964.1.
3D structure databases
SMR	O84917. Positions 4-459.
ModBase	Search...
Enzyme and pathway databases
BRENDA	4.1.1.39. 294944.
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_THIIN

Accession

Primary (citable) accession number: O84917

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 22, 2005
Last sequence update:	November 1, 1998
Last modified:	January 19, 2010
This is version 46 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)