Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ribulose bisphosphate carboxylase large chain, plasmid

Gene

cbbL2

Organism
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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 activityi

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O.
3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2.

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei126 – 1261Substrate; in homodimeric partnerBy similarity
Binding sitei176 – 1761SubstrateBy similarity
Active sitei178 – 1781Proton acceptorBy similarity
Binding sitei180 – 1801SubstrateBy similarity
Metal bindingi204 – 2041Magnesium; via carbamate groupBy similarity
Metal bindingi206 – 2061MagnesiumBy similarity
Metal bindingi207 – 2071MagnesiumBy similarity
Active sitei296 – 2961Proton acceptorBy similarity
Binding sitei297 – 2971SubstrateBy similarity
Binding sitei329 – 3291SubstrateBy similarity
Sitei336 – 3361Transition state stabilizerBy similarity
Binding sitei381 – 3811SubstrateBy similarity

GO - Molecular functioni

  1. magnesium ion binding Source: UniProtKB-HAMAP
  2. monooxygenase activity Source: UniProtKB-KW
  3. ribulose-bisphosphate carboxylase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. reductive pentose-phosphate cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Lyase, Monooxygenase, Oxidoreductase

Keywords - Biological processi

Calvin cycle, Carbon dioxide fixation

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciCNEC381666:GJUJ-6701-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase large chain, plasmid (EC:4.1.1.39)
Short name:
RuBisCO large subunit
Gene namesi
Name:cbbL2
Synonyms:cbbL, cbxLP, cfxLP
Ordered Locus Names:PHG427
Encoded oniPlasmid megaplasmid pHG10 Publication
OrganismiCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
Taxonomic identifieri381666 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
ProteomesiUP000008210 Componenti: Plasmid megaplasmid pHG1

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 486486Ribulose bisphosphate carboxylase large chain, plasmidPRO_0000062642Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei204 – 2041N6-carboxylysineBy similarity

Expressioni

Inductioni

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.

Interactioni

Subunit structurei

Heterohexadecamer of 8 large chains and 8 small chains.By similarity

Protein-protein interaction databases

STRINGi381666.PHG427.

Structurei

3D structure databases

ProteinModelPortaliP42721.
SMRiP42721. Positions 24-467.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiITAGWMA.
OrthoDBiEOG6ZKXMS.

Family and domain databases

Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01338. RuBisCO_L_type1.
InterProiIPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view]
PfamiPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
SUPFAMiSSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEiPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P42721-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNAPESVQAK PRKRYDAGVM KYKEMGYWDG DYEPKDTDLL ALFRITPQDG
60 70 80 90 100
VDPVEAAAAV AGESSTATWT VVWTDRLTAC DMYRAKAYRV DPVPNNPEQF
110 120 130 140 150
FCYVAYDLSL FEEGSIANLT ASIIGNVFSF KPIKAARLED MRFPVAYVKT
160 170 180 190 200
FAGPSTGIIV ERERLDKFGR PLLGATTKPK LGLSGRNYGR VVYEGLKGGL
210 220 230 240 250
DFMKDDENIN SQPFMHWRDR FLFVMDAVNK ASAATGEVKG SYLNVTAGTM
260 270 280 290 300
EEMYRRAEFA KSLGSVVIMI DLIVGWTCIQ SMSNWCRQND MILHLHRAGH
310 320 330 340 350
GTYTRQKNHG VSFRVIAKWL RLAGVDHMHT GTAVGKLEGD PLTVQGYYNV
360 370 380 390 400
CRDAYTHTDL TRGLFFDQDW ASLRKVMPVA SGGIHAGQMH QLIHLFGDDV
410 420 430 440 450
VLQFGGGTIG HPQGIQAGAT ANRVALEAMV LARNEGRDIL NEGPEILRDA
460 470 480
ARWCGPLRAA LDTWGDISFN YTPTDTSDFA PTASVA
Length:486
Mass (Da):53,809
Last modified:January 4, 2005 - v3
Checksum:i38443E663E0EEE13
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti198 – 1981G → R in AAA83747 (PubMed:7543477).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U20585 Genomic DNA. Translation: AAA83747.1.
AY305378 Genomic DNA. Translation: AAP86176.1.
M65064 Genomic DNA. Translation: AAA21980.1.
PIRiI39559.
RefSeqiNP_943062.1. NC_005241.1.
YP_009074696.1. NG_034727.1.

Genome annotation databases

EnsemblBacteriaiAAP86176; AAP86176; PHG427.
KEGGireh:PHG427.
PATRICi35229366. VBIRalEut6770_0355.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U20585 Genomic DNA. Translation: AAA83747.1.
AY305378 Genomic DNA. Translation: AAP86176.1.
M65064 Genomic DNA. Translation: AAA21980.1.
PIRiI39559.
RefSeqiNP_943062.1. NC_005241.1.
YP_009074696.1. NG_034727.1.

3D structure databases

ProteinModelPortaliP42721.
SMRiP42721. Positions 24-467.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi381666.PHG427.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAP86176; AAP86176; PHG427.
KEGGireh:PHG427.
PATRICi35229366. VBIRalEut6770_0355.

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiITAGWMA.
OrthoDBiEOG6ZKXMS.

Enzyme and pathway databases

BioCyciCNEC381666:GJUJ-6701-MONOMER.

Family and domain databases

Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01338. RuBisCO_L_type1.
InterProiIPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view]
PfamiPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
SUPFAMiSSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEiPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.

Entry informationi

Entry nameiRBL1P_CUPNH
AccessioniPrimary (citable) accession number: P42721
Secondary accession number(s): Q7WWS4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 4, 2005
Last modified: April 1, 2015
This is version 101 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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).By similarity

Keywords - Technical termi

Complete proteome, Plasmid, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.