NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2247456 [NCBI, ExPASy, EBI, Israel, Japan]
Stein J.L., Haygood M., Felbeck H.;
"Nucleotide sequence and expression of a deep-sea ribulose-1,5-bisphosphate carboxylase gene cloned from a chemoautotrophic bacterial endosymbiont.";
Proc. Natl. Acad. Sci. U.S.A. 87:8850-8854(1990).

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.
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: Heterohexadecamer of 8 large chains and 8 small chains (By similarity).
MISCELLANEOUS: The basic functional RuBisCO is composed of a large chain homodimer in a "head-to-tail" conformation. In form I RuBisCO this homodimer is arranged in a barrel-like tetramer with the small subunits forming a tetrameric "cap" on each end of the "barrel" (By similarity).
SIMILARITY: Belongs to the RuBisCO large chain family. Type I 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

M34536; AAA27387.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A38262; A38262.

3D structure databases

HSSP

O93627; 1GEH. [HSSP ENTRY / PDB]

SMR

P24672; 5-466.

ModBase

P24672.

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_01338; -; 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.

ProtoNet

P24672.

Other

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`	`1 471`	`471`	`Ribulose bisphosphate carboxylase large chain.`	`PRO_0000062618`
`ACT_SITE`	`167 167`		`Proton acceptor (By similarity).`
`ACT_SITE`	`286 286`		`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`	`115 115`		`Substrate; in homodimeric partner (By similarity).`
`BINDING`	`165 165`		`Substrate (By similarity).`
`BINDING`	`169 169`		`Substrate (By similarity).`
`BINDING`	`287 287`		`Substrate (By similarity).`
`BINDING`	`319 319`		`Substrate (By similarity).`
`BINDING`	`371 371`		`Substrate (By similarity).`
`SITE`	`326 326`	`1`	`Transition state stabilizer (By similarity).`
`MOD_RES`	`193 193`		`N6-carboxylysine (By similarity).`

Sequence information

Length: 471 AA [This is the length of the unprocessed precursor]

Molecular weight: 52770 Da [This is the MW of the unprocessed precursor]

CRC64: 990F5E9B5E55C504 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAKKYDAGVK DYRETYWMPD YTPKETDLLA CFKIIPQPGV PREEARAAVA AESSTGTWTT 

        70         80         90        100        110        120 
VWTDLLTDLD HYKGRAYAIE DVPGDEEAFY AFIAYPIDLF EEGSVVNVFT SLVGNVFGFK 

       130        140        150        160        170        180 
AIRALRLEDV RFPIAYVMTC NGPPHGIQVE RDIMNKYGRP LLGCTIKPKL GLSAKNYGRA 

       190        200        210        220        230        240 
VYECLRGGLD FTKDDENVNS QPFMRWRHGF DFVMEAIEKA ERETGERKGH YLNVTAPTPD 

       250        260        270        280        290        300 
EMFKRAEYAK EIGAPIIMHD YITGGFTANT GLAQWCRDNG VLLHIHRAMH AVLDRNPHHG 

       310        320        330        340        350        360 
IHFRVLTKIL RLSGGDHLHT GTVVGKLEGD REATLGWIDL LRESYIKEDR SRGIFFDQDW 

       370        380        390        400        410        420 
GSMPGVFAAC SGGIHVWHMP ALVTIFGEHA VLQFGGGTLG HPWGNAGAAA NRVALEACVE 

       430        440        450        460        470 
ARNEGHELEK EGKDILIQAA KHSPELKTAM ETWKEIKFEF DTVDKLDVAH K

P24672 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