[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-12, AND CHARACTERIZATION. STRAIN=KOD1; DOI=10.1074/jbc.274.8.5078; PubMed=9988755 [NCBI, ExPASy, EBI, Israel, Japan] Ezaki S., Maeda N., Kishimoto T., Atomi H., Imanaka T.; "Presence of a structurally novel type ribulose-bisphosphate carboxylase/oxygenase in the hyperthermophilic archaeon, Pyrococcus kodakaraensis KOD1."; J. Biol. Chem. 274:5078-5082(1999).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=KOD1; DOI=10.1101/gr.3003105; PubMed=15710748 [NCBI, ExPASy, EBI, Israel, Japan] Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.; "Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes."; Genome Res. 15:352-363(2005).
[3]	PROTEIN SEQUENCE OF 2-12, CHARACTERIZATION, AND CRYSTALLIZATION. STRAIN=KOD1; DOI=10.1006/jmbi.1999.3145; PubMed=10512715 [NCBI, ExPASy, EBI, Israel, Japan] Maeda N., Kitano K., Fukui T., Ezaki S., Atomi H., Miki K., Imanaka T.; "Ribulose bisphosphate carboxylase/oxygenase from the hyperthermophilic archaeon Pyrococcus kodakaraensis KOD1 is composed solely of large subunits and forms a pentagonal structure."; J. Mol. Biol. 293:57-66(1999).
[4]	SUBUNIT, AND MUTAGENESIS OF GLU-63; ARG-66 AND ASP-69. DOI=10.1074/jbc.M203117200; PubMed=12070156 [NCBI, ExPASy, EBI, Israel, Japan] Maeda N., Kanai T., Atomi H., Imanaka T.; "The unique pentagonal structure of an archaeal Rubisco is essential for its high thermostability."; J. Biol. Chem. 277:31656-31662(2002).
[5]	X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), COFACTOR, AND SUBUNIT. DOI=10.1016/S0969-2126(01)00608-6; PubMed=11435112 [NCBI, ExPASy, EBI, Israel, Japan] Kitano K., Maeda N., Fukui T., Atomi H., Imanaka T., Miki K.; "Crystal structure of a novel-type archaeal rubisco with pentagonal symmetry."; Structure 9:473-481(2001).

Comments

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.
BIOPHYSICOCHEMICAL PROPERTIES:

Temperature dependence: Optimum temperature is 90 degrees Celsius. Highly thermostable;
SUBUNIT: Homodecamer, consisting of fiver dimer units which form a ring-like pentagonal structure. This arrangement is essential for its high thermostability. Composed solely of large subunits.
MISCELLANEOUS: The basic functional RuBisCO is composed of a large chain homodimer in a "head-to-tail" conformation (By similarity).
SIMILARITY: Belongs to the RuBisCO large chain family. Type III subfamily.

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

AB018555; BAA33863.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP006878; BAD86479.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_184703.1; -.

3D structure databases

PDB

1GEH; X-ray; 2.80 A; A/B/C/D/E=1-444.

[ExPASy / RCSB / EBI]

PDBsum

1GEH; -.

ModBase

O93627.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-13272; -.
TKOD69014:TK2290-MON; -.

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:0015977;	Biological process: carbon utilization by fixation of carbon dioxide (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_01133; -; 1.
PBIL [Tree]

InterPro

IPR000685; RuBisCO_lsu_C.
IPR017712; RuBisCO_lsu_III.
IPR017444; RuBisCO_lsu_N.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.110; RuBisCO_large; 1.

Pfam

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

Genome annotation databases

3234791; -.

AP006878_GR; TK2290.

tko:TK2290; -.

fig|69014.3.peg.2291; -.

Phylogenomic databases

HOGENOM

O93627; -.

Genome annotation databases

CMR

O93627; TK2290.

Other

ProtoNet

O93627.

UniRef

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

Keywords

3D-structure; Carbon dioxide fixation; Complete proteome; Direct protein sequencing; Lyase; Magnesium; Metal-binding; Monooxygenase; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 444`	`443`	`Ribulose bisphosphate carboxylase.`	`PRO_0000062678`
`ACT_SITE`	`163 163`		`Proton acceptor.`
`ACT_SITE`	`281 281`		`Proton acceptor.`
`METAL`	`189 189`		`Magnesium; via carbamate group.`
`METAL`	`191 191`		`Magnesium.`
`METAL`	`192 192`		`Magnesium.`
`BINDING`	`111 111`		`Substrate; in homodimeric partner.`
`BINDING`	`165 165`		`Substrate.`
`BINDING`	`282 282`		`Substrate.`
`BINDING`	`314 314`		`Substrate.`
`BINDING`	`367 367`		`Substrate.`
`SITE`	`322 322`	`1`	`Transition state stabilizer.`
`MOD_RES`	`189 189`		`N6-carboxylysine.`
`MUTAGEN`	`63 63`		`E->S: Decrease in activity and in thermostability. Large decrease in activity; forms dimers; when associated with S-66 and S-69.`
`MUTAGEN`	`66 66`		`R->S: Large decrease in activity and in thermostability. Large decrease in activity; forms dimers; when associated with S-63 and S-69.`
`MUTAGEN`	`69 69`		`D->S: Slight decrease in activity; no change in thermostability. Large decrease in activity; forms dimers; when associated with S-63 and S-66.`
`TURN`	`21 23`	`3`
`STRAND`	`24 33`	`10`
`HELIX`	`39 49`	`11`
`HELIX`	`64 70`	`7`
`STRAND`	`73 76`	`4`
`STRAND`	`81 83`	`3`
`STRAND`	`85 92`	`8`
`HELIX`	`93 95`	`3`
`HELIX`	`101 108`	`8`
`HELIX`	`111 114`	`4`
`STRAND`	`118 120`	`3`
`STRAND`	`122 127`	`6`
`HELIX`	`130 133`	`4`
`HELIX`	`142 150`	`9`
`STRAND`	`157 160`	`4`
`HELIX`	`170 182`	`13`
`STRAND`	`187 189`	`3`
`HELIX`	`202 219`	`18`
`STRAND`	`225 227`	`3`
`HELIX`	`234 247`	`14`
`STRAND`	`251 255`	`5`
`HELIX`	`256 259`	`4`
`HELIX`	`261 273`	`13`
`STRAND`	`277 281`	`5`
`HELIX`	`285 287`	`3`
`STRAND`	`294 296`	`3`
`HELIX`	`298 308`	`11`
`STRAND`	`311 314`	`4`
`HELIX`	`326 338`	`13`
`STRAND`	`340 342`	`3`
`STRAND`	`363 369`	`7`
`TURN`	`372 374`	`3`
`HELIX`	`375 381`	`7`
`STRAND`	`384 389`	`6`
`HELIX`	`392 395`	`4`
`HELIX`	`401 415`	`15`
`HELIX`	`421 425`	`5`
`HELIX`	`429 436`	`8`

Sequence information

Length: 444 AA [This is the length of the unprocessed precursor]

Molecular weight: 49713 Da [This is the MW of the unprocessed precursor]

CRC64: 6E3AFF37367DD7FE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVEKFDTIYD YYVDKGYEPS KKRDIIAVFR VTPAEGYTIE QAAGAVAAES STGTWTTLYP 

        70         80         90        100        110        120 
WYEQERWADL SAKAYDFHDM GDGSWIVRIA YPFHAFEEAN LPGLLASIAG NIFGMKRVKG 

       130        140        150        160        170        180 
LRLEDLYFPE KLIREFDGPA FGIEGVRKML EIKDRPIYGV VPKPKVGYSP EEFEKLAYDL 

       190        200        210        220        230        240 
LSNGADYMKD DENLTSPWYN RFEERAEIMA KIIDKVENET GEKKTWFANI TADLLEMEQR 

       250        260        270        280        290        300 
LEVLADLGLK HAMVDVVITG WGALRYIRDL AADYGLAIHG HRAMHAAFTR NPYHGISMFV 

       310        320        330        340        350        360 
LAKLYRLIGI DQLHVGTAGA GKLEGGKWDV IQNARILRES HYKPDENDVF HLEQKFYSIK 

       370        380        390        400        410        420 
AAFPTSSGGL HPGNIQPVIE ALGTDIVLQL GGGTLGHPDG PAAGARAVRQ AIDAIMQGIP 

       430        440 
LDEYAKTHKE LARALEKWGH VTPV

O93627 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