[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=K12; Shively J.M., Soyer F.; "A form II Rubisco gene and associated genes in Thiobacillus intermedius."; Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
[2]	EXPRESSION IN T.INTERMEDIUS. DOI=10.1016/0378-1097(93)90324-U; PubMed=8472910 [NCBI, ExPASy, EBI, Israel, Japan] Stoner M.T., Shively J.M.; "Cloning and expression of the D-ribulose-1,5-bisphosphate carboxylase/oxygenase form II gene from Thiobacillus intermedius in Escherichia coli."; FEMS Microbiol. Lett. 107:287-292(1993).
[3]	PROBABLE EXPRESSION. Shively J.M.; Unpublished observations (OCT-2005).

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.
CATALYTIC ACTIVITY: 3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O₂.
COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
SUBUNIT: 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).
SIMILARITY: 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.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF012127; AAC24964.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P04718; 2RUS. [HSSP ENTRY / PDB]

SMR

O84917; 4-459.

ModBase

O84917.

Ontologies

GO:0009573;	Cellular component: chloroplast ribulose bisphosphate carboxylase complex (inferred from electronic annotation from InterPro).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004497;	Molecular function: monooxygenase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0016984;	Molecular function: ribulose-bisphosphate carboxylase activity (inferred from electronic annotation from HAMAP).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0019253;	Biological process: reductive pentose-phosphate cycle (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_01339; -; 1.
PBIL [Tree]

InterPro

IPR000685; RuBisCO_lsu_C.
IPR017443; RuBisCO_lsu_fd_N.
IPR017444; RuBisCO_lsu_N.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.110; RuBisCO_large; 1.
G3DSA:3.30.70.150; RuBisCO_large; 1.

Pfam

PF00016; RuBisCO_large; 1.
PF02788; RuBisCO_large_N; 1.
Pfam graphical view of domain structure.

PROSITE

PS00157; RUBISCO_LARGE; 1.

Other

ProtoNet

O84917.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Calvin cycle; Carbon dioxide fixation; Lyase; Magnesium; Metal-binding; Monooxygenase; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 461`	`461`	`Ribulose bisphosphate carboxylase.`	`PRO_0000062669`
`ACT_SITE`	`168 168`		`Proton acceptor (By similarity).`
`ACT_SITE`	`289 289`		`Proton acceptor (By similarity).`
`METAL`	`193 193`		`Magnesium; via carbamate group (By similarity).`
`METAL`	`195 195`		`Magnesium (By similarity).`
`METAL`	`196 196`		`Magnesium (By similarity).`
`BINDING`	`113 113`		`Substrate; in homodimeric partner (By similarity).`
`BINDING`	`170 170`		`Substrate (By similarity).`
`BINDING`	`290 290`		`Substrate (By similarity).`
`BINDING`	`323 323`		`Substrate (By similarity).`
`BINDING`	`370 370`		`Substrate (By similarity).`
`SITE`	`331 331`	`1`	`Transition state stabilizer (By similarity).`
`MOD_RES`	`193 193`		`N6-carboxylysine (By similarity).`

Sequence information

Length: 461 AA [This is the length of the unprocessed precursor]

Molecular weight: 50818 Da [This is the MW of the unprocessed precursor]

CRC64: D470D17F356800E2 [This is a checksum on the sequence]

        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

O84917 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools