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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Paracoccus denitrificans (strain Pd 1222)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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.UniRule annotation

Catalytic activityi

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

Cofactori

Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei127 – 1271Substrate; in homodimeric partnerUniRule annotation
Binding sitei177 – 1771SubstrateUniRule annotation
Active sitei179 – 1791Proton acceptorUniRule annotation
Binding sitei181 – 1811SubstrateUniRule annotation
Metal bindingi205 – 2051Magnesium; via carbamate groupUniRule annotation
Metal bindingi207 – 2071MagnesiumUniRule annotation
Metal bindingi208 – 2081MagnesiumUniRule annotation
Active sitei297 – 2971Proton acceptorUniRule annotation
Binding sitei298 – 2981SubstrateUniRule annotation
Binding sitei330 – 3301SubstrateUniRule annotation
Sitei337 – 3371Transition state stabilizerUniRule annotation
Binding sitei382 – 3821SubstrateUniRule annotation

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

BioCyciPDEN318586:GCVQ-1717-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase large chainUniRule annotation (EC:4.1.1.39UniRule annotation)
Short name:
RuBisCO large subunitUniRule annotation
Gene namesi
Name:cbbLUniRule annotation
Ordered Locus Names:Pden_1699
OrganismiParacoccus denitrificans (strain Pd 1222)
Taxonomic identifieri318586 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus
ProteomesiUP000000361 Componenti: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 487487Ribulose bisphosphate carboxylase large chainPRO_0000299967Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei205 – 2051N6-carboxylysineUniRule annotation

Interactioni

Subunit structurei

Heterohexadecamer of 8 large chains and 8 small chains.UniRule annotation

Protein-protein interaction databases

STRINGi318586.Pden_1699.

Structurei

3D structure databases

ProteinModelPortaliA1B2Q2.
SMRiA1B2Q2. Positions 12-481.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RuBisCO large chain family. Type I subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiHAAFTRN.
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.

A1B2Q2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNEMSKSEIT DKKKRYAAGV LKYAQMGYWD GDYQPKDTDI LALFRITPQD
60 70 80 90 100
GVDPIEAAAA VAGESSTATW TVVWTDRLTA CDQYRAKAYK VEPVPGQEGQ
110 120 130 140 150
YFCYVAYDLI LFEEGSIANV TASIIGNVFS FKPLLAARLE DMRFPVAYMK
160 170 180 190 200
TFAGPPTGIV VERERLDKFG RPLLGATTKP KLGLSGKNYG RVVYEGLKGG
210 220 230 240 250
LDFMKDDENI NSQPFMHWRD RFLYCMEAVN KATAVTGEVK GHYLNITAGT
260 270 280 290 300
MEEMYRRAEL AKELGSVIVM VDLIVGWTAI QSISNWCRQN DMILHMHRAG
310 320 330 340 350
HGTYTRQKNH GISFRVIAKW LRMAGVDHLH CGTAVGKLEG DPLTVQGYYN
360 370 380 390 400
TCREMVNEVD LPRGIFFEQD WGNLKKVMPV ASGGIHAGQM HQLLDLFGDD
410 420 430 440 450
VVLQFGGGTI GHPMGIQAGA TANRVALEAM VLARNEGVDL KTEGPEVLRR
460 470 480
AAKWCKPLEA ALDVWGNITF NYTSTDTSDF VPTASVS
Length:487
Mass (Da):53,971
Last modified:January 23, 2007 - v1
Checksum:i07BD6810EEA63615
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000489 Genomic DNA. Translation: ABL69796.1.
RefSeqiWP_011747994.1. NC_008686.1.
YP_915492.1. NC_008686.1.

Genome annotation databases

EnsemblBacteriaiABL69796; ABL69796; Pden_1699.
KEGGipde:Pden_1699.
PATRICi22854475. VBIParDen97112_1626.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000489 Genomic DNA. Translation: ABL69796.1.
RefSeqiWP_011747994.1. NC_008686.1.
YP_915492.1. NC_008686.1.

3D structure databases

ProteinModelPortaliA1B2Q2.
SMRiA1B2Q2. Positions 12-481.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi318586.Pden_1699.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABL69796; ABL69796; Pden_1699.
KEGGipde:Pden_1699.
PATRICi22854475. VBIParDen97112_1626.

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiHAAFTRN.
OrthoDBiEOG6ZKXMS.

Enzyme and pathway databases

BioCyciPDEN318586:GCVQ-1717-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

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Pd 1222.

Entry informationi

Entry nameiRBL_PARDP
AccessioniPrimary (citable) accession number: A1B2Q2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: January 23, 2007
Last modified: April 1, 2015
This is version 54 of the entry and version 1 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".UniRule annotation

Keywords - Technical termi

Complete proteome, 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.