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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Rhodopseudomonas palustris (strain BisB18)
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 in the photorespiration process. 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 sitei124 – 1241Substrate; in homodimeric partnerUniRule annotation
Binding sitei174 – 1741SubstrateUniRule annotation
Active sitei176 – 1761Proton acceptorUniRule annotation
Binding sitei178 – 1781SubstrateUniRule annotation
Metal bindingi202 – 2021Magnesium; via carbamate groupUniRule annotation
Metal bindingi204 – 2041MagnesiumUniRule annotation
Metal bindingi205 – 2051MagnesiumUniRule annotation
Active sitei294 – 2941Proton acceptorUniRule annotation
Binding sitei295 – 2951SubstrateUniRule annotation
Binding sitei327 – 3271SubstrateUniRule annotation
Sitei334 – 3341Transition state stabilizerUniRule annotation
Binding sitei379 – 3791SubstrateUniRule 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, Photosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciRPAL316056:GH3E-1342-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:RPC_1327
OrganismiRhodopseudomonas palustris (strain BisB18)
Taxonomic identifieri316056 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeRhodopseudomonas
ProteomesiUP000001948 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 485485Ribulose bisphosphate carboxylase large chainPRO_0000251457Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei202 – 2021N6-carboxylysineUniRule annotation

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi316056.RPC_1327.

Structurei

3D structure databases

ProteinModelPortaliQ219P7.
SMRiQ219P7. Positions 22-465.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
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.

Q219P7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNESVTIRGK DRYKSGVMEY KKMGYWEPDY EPKDTDIIAL FRVTPQDGVD
60 70 80 90 100
PTEASAAVAG ESSTATWTVV WTDRLTAAEK YRAKCYRVDP VPNSPGQFFA
110 120 130 140 150
YIAYDLDLFE NGSIANLSAS IIGNVFGFKP LKALRLEDMR LPVAYVKTFQ
160 170 180 190 200
GPATGIVVER ERMDKFGRPL LGATVKPKLG LSGRNYGRVV YEALKGGLDF
210 220 230 240 250
TKDDENINSQ PFMHWRERFL YCMEAVNKAQ AASGEIKGTY LNVTAGTMEE
260 270 280 290 300
MYERAEFAKQ LGSVIIMIDL VIGYTAIQSM AKWARRNDMI LHLHRAGHST
310 320 330 340 350
YTRQRNHGVS FRVIAKWMRL AGVDHIHAGT VVGKLEGDPA TTKGYYDICR
360 370 380 390 400
EDYNPMQLEH GIFFEQNWAS LNKLMPVASG GIHAGQMHQL LDHLGEDVVL
410 420 430 440 450
QFGGGTIGHP MGIQAGATAN RVALEAMIMA RNEGRDYLHE GEEILAKAAL
460 470 480
TCTPLKAALE TWKNVTFNYE STDMPDYAPT PSVSM
Length:485
Mass (Da):54,027
Last modified:October 3, 2006 - v2
Checksum:iB36E403B136F3FC4
GO

Sequence cautioni

The sequence ABD86889.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000301 Genomic DNA. Translation: ABD86889.1. Different initiation.
RefSeqiYP_531208.1. NC_007925.1.

Genome annotation databases

EnsemblBacteriaiABD86889; ABD86889; RPC_1327.
KEGGirpc:RPC_1327.
PATRICi23267326. VBIRhoPal29154_1368.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000301 Genomic DNA. Translation: ABD86889.1. Different initiation.
RefSeqiYP_531208.1. NC_007925.1.

3D structure databases

ProteinModelPortaliQ219P7.
SMRiQ219P7. Positions 22-465.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi316056.RPC_1327.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABD86889; ABD86889; RPC_1327.
KEGGirpc:RPC_1327.
PATRICi23267326. VBIRhoPal29154_1368.

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OrthoDBiEOG6ZKXMS.

Enzyme and pathway databases

BioCyciRPAL316056:GH3E-1342-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: BisB18.

Entry informationi

Entry nameiRBL_RHOPB
AccessioniPrimary (citable) accession number: Q219P7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: October 3, 2006
Last modified: April 1, 2015
This is version 53 of the entry and version 2 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.