Ribulose bisphosphate carboxylase large chain

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Reviewed, UniProtKB/Swiss-Prot P27997 (RBL1_RHOSH)

Last modified March 24, 2009. Version 57. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Ribulose bisphosphate carboxylase large chain
      Short name=RuBisCO large subunit
    EC=4.1.1.39

Gene names

Name:	cbbL
Synonyms:	cbbL1, rbcL

Organism

Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides)

Taxonomic identifier

1063 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter

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Protein attributes

Sequence length	486 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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_01338 3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O₂. HAMAP MF_01338
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Subunit structure	Heterohexadecamer of 8 large chains and 8 small chains By similarity.
Induction	Expression of this operon predominates when carbon dioxide is limiting. HAMAP MF_01338
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.
Sequence similarities	Belongs to the RuBisCO large chain family. Type I subfamily.
biophysicochemical properties	Kinetic parameters: The CO₂/O₂ specificity factor (tau) is 56. K_M=50 µM for ribulose 1,5-bisphosphate Ref.2 K_M=22 µM for CO₂ V_max=2.5 µmol/min/mg enzyme with CO₂ as substrate

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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...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 486

486

Ribulose bisphosphate carboxylase large chain HAMAP MF_01338

PRO_0000062647

Sites

Active site

177

Proton acceptor By similarity

Active site

295

Proton acceptor By similarity

Metal binding

203

Magnesium; via carbamate group By similarity

Metal binding

205

Magnesium By similarity

Metal binding

206

Magnesium By similarity

Binding site

125

Substrate; in homodimeric partner By similarity

Binding site

175

Substrate By similarity

Binding site

179

Substrate By similarity

Binding site

296

Substrate By similarity

Binding site

328

Substrate By similarity

Binding site

380

Substrate By similarity

Site

335

Transition state stabilizer By similarity

Amino acid modifications

Modified residue

203

N6-carboxylysine By similarity

Experimental info

Mutagenesis

341

L → M: Increases KM for CO(2), decreases KM for ribulose 1,5-bisphosphate. HAMAP MF_01338

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Sequences

Sequence

Length

Mass (Da)

Tools

P27997-1 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 82B91D700303C3C0
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FASTA

486

53,686

        10         20         30         40         50         60 
MDTKTTEIKG KERYKAGVLK YAQMGYWDGD YVPKDTDVLA LFRITPQEGV DPVEAAAAVA 

        70         80         90        100        110        120 
GESSTATWTV VWTDRLTACD SYRAKAYRVE PVPGTPGQYF CYVAYDLILF EEGSIANLTA 

       130        140        150        160        170        180 
SIIGNVFSFK PLKAARLEDM RFPVAYVKTY KGPPTGIVGE RERLDKFGKP LLGATTKPKL 

       190        200        210        220        230        240 
GLSGKNYGRV VYEGLKGGLD FMKDDENINS QPFMHWRDRF LYVMEAVNLA SAQTGEVKGH 

       250        260        270        280        290        300 
YLNITAGTME EMYRRAEFAK SLGSVIVMVD LIIGYTAIQS ISEWCRQNDM ILHMHRAGHG 

       310        320        330        340        350        360 
TYTRQKNHGI SFRVIAKWLR LAGVDHLHCG TAVGKLEGDP LTVQGYYNVC REPFNTVDLP 

       370        380        390        400        410        420 
RGIFFEQDWA DLRKVMPVAS GGIHAGQMHQ LLSLFGDDVV LQFGGGTIGH PMGIQAGATA 

       430        440        450        460        470        480 
NRVALEAMVL ARNEGRNIDV EGPEILRAAA KWCKPLEAAL DTWGNITFNY TSTDTSDFVP 


TASVAM

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References

[1]	"Nucleotide sequence, transcriptional analysis, and expression of genes encoded within the form I CO2 fixation operon of Rhodobacter sphaeroides." Gibson J.L., Falcone D.L., Tabita F.R. J. Biol. Chem. 266:14646-14653(1991) [PubMed: 1907281] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: HR.
[2]	"Closely related form I ribulose bisphosphate carboxylase/oxygenase molecules that possess different CO2/O2 substrate specificities." Horken K.M., Tabita F.R. Arch. Biochem. Biophys. 361:183-194(1999) [PubMed: 9882445] [Abstract] Cited for: KINETIC CHARACTERIZATION, MUTAGENESIS. Strain: FI.

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Cross-references

Sequence databases
	M64624 Genomic DNA. Translation: AAA26115.1.
PIR	RKRFAL. D40767.
3D structure databases
HSSP	HSSP built from PDB template 1BXN based on UniProtKB P09657.
SMR	P27997. Positions 13-479.
ModBase	Search...
Enzyme and pathway databases
BRENDA	4.1.1.39. 2796.
Family and domain databases
HAMAP	MF_01338. [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...

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Entry information

Entry name

RBL1_RHOSH

Accession

Primary (citable) accession number: P27997

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	March 24, 2009
This is version 57 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)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents