Ribulose bisphosphate carboxylase large chain, plasmid - Ralstonia eutropha (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)

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Reviewed, UniProtKB/Swiss-Prot P42721 (RBL1P_RALEH)

Last modified September 1, 2009. Version 69. 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, plasmid
      Short name=RuBisCO large subunit
    EC=4.1.1.39

Gene names

Name:	cbbL2
Synonyms:	cbbL, cbxLP, cfxLP
Ordered Locus Names:	PHG427

Encoded on

Plasmid megaplasmid pHG1

Organism

Ralstonia eutropha (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)) [Complete proteome] [HAMAP]

Taxonomic identifier

381666 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus

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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 transcript 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. HAMAP MF_01338
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	Total RuBisCO activity (both chromosome and plasmid-derived enzyme) is high under lithoautotrophic growth conditions, intermediate when grown on fructose and poor when grown on pyruvate. 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.

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Ontologies

Keywords
Biological process	Calvin cycle Carbon dioxide fixation
Ligand	Magnesium Metal-binding
Molecular function	Lyase Monooxygenase Oxidoreductase
Technical term	Complete proteome Plasmid
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, plasmid HAMAP MF_01338

PRO_0000062642

Sites

Active site

178

Proton acceptor By similarity

Active site

296

Proton acceptor By similarity

Metal binding

204

Magnesium; via carbamate group By similarity

Metal binding

206

Magnesium By similarity

Metal binding

207

Magnesium By similarity

Binding site

126

Substrate; in homodimeric partner By similarity

Binding site

176

Substrate By similarity

Binding site

180

Substrate By similarity

Binding site

297

Substrate By similarity

Binding site

329

Substrate By similarity

Binding site

381

Substrate By similarity

Site

336

Transition state stabilizer By similarity

Amino acid modifications

Modified residue

204

N6-carboxylysine By similarity

Experimental info

Sequence conflict

198

G → R in AAA83747. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

P42721-1 [UniParc].

Last modified January 4, 2005. Version 3.
Checksum: 38443E663E0EEE13
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FASTA

486

53,809

        10         20         30         40         50         60 
MNAPESVQAK PRKRYDAGVM KYKEMGYWDG DYEPKDTDLL ALFRITPQDG VDPVEAAAAV 

        70         80         90        100        110        120 
AGESSTATWT VVWTDRLTAC DMYRAKAYRV DPVPNNPEQF FCYVAYDLSL FEEGSIANLT 

       130        140        150        160        170        180 
ASIIGNVFSF KPIKAARLED MRFPVAYVKT FAGPSTGIIV ERERLDKFGR PLLGATTKPK 

       190        200        210        220        230        240 
LGLSGRNYGR VVYEGLKGGL DFMKDDENIN SQPFMHWRDR FLFVMDAVNK ASAATGEVKG 

       250        260        270        280        290        300 
SYLNVTAGTM EEMYRRAEFA KSLGSVVIMI DLIVGWTCIQ SMSNWCRQND MILHLHRAGH 

       310        320        330        340        350        360 
GTYTRQKNHG VSFRVIAKWL RLAGVDHMHT GTAVGKLEGD PLTVQGYYNV CRDAYTHTDL 

       370        380        390        400        410        420 
TRGLFFDQDW ASLRKVMPVA SGGIHAGQMH QLIHLFGDDV VLQFGGGTIG HPQGIQAGAT 

       430        440        450        460        470        480 
ANRVALEAMV LARNEGRDIL NEGPEILRDA ARWCGPLRAA LDTWGDISFN YTPTDTSDFA 


PTASVA

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of the duplicate ribulose-1,5-bisphosphate carboxylase genes and cbb promoters of Alcaligenes eutrophus." Kusian B., Bednarski R., Husemann M., Bowien B. J. Bacteriol. 177:4442-4450(1995) [PubMed: 7543477] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], EXPRESSION UNDER DIFFERENT GROWTH CONDITIONS.
[2]	"Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16 megaplasmid encoding key enzymes of H(2)-based lithoautotrophy and anaerobiosis." Schwartz E., Henne A., Cramm R., Eitinger T., Friedrich B., Gottschalk G. J. Mol. Biol. 332:369-383(2003) [PubMed: 12948488] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Identification of cfxR, an activator gene of autotrophic CO2 fixation in Alcaligenes eutrophus." Windhoevel U., Bowien B. Mol. Microbiol. 5:2695-2705(1991) [PubMed: 1779759] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.

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Cross-references

Sequence databases
	U20585 Genomic DNA. Translation: AAA83747.1. AY305378 Genomic DNA. Translation: AAP86176.1. M65064 Genomic DNA. Translation: AAA21980.1.
PIR	I39559.
RefSeq	NP_943062.1.
3D structure databases
SMR	P42721. Positions 14-479.
ModBase	Search...
Protein-protein interaction databases
STRING	P42721.
Genome annotation databases
GeneID	2656546.
GenomeReviews	Gene locus PHG427 in contig AY305378_GR.
KEGG	reh:PHG427.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P42721.
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

RBL1P_RALEH

Accession

Primary (citable) accession number: P42721
Secondary accession number(s): Q7WWS4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	January 4, 2005
Last modified:	September 1, 2009
This is version 69 of the entry and version 3 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

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents