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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein 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 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 sitei118 – 1181Substrate; in homodimeric partnerUniRule annotation
Binding sitei168 – 1681SubstrateUniRule annotation
Active sitei170 – 1701Proton acceptorUniRule annotation
Binding sitei172 – 1721SubstrateUniRule annotation
Metal bindingi196 – 1961Magnesium; via carbamate groupUniRule annotation
Metal bindingi198 – 1981MagnesiumUniRule annotation
Metal bindingi199 – 1991MagnesiumUniRule annotation
Active sitei289 – 2891Proton acceptorUniRule annotation
Binding sitei290 – 2901SubstrateUniRule annotation
Binding sitei322 – 3221SubstrateUniRule annotation
Sitei329 – 3291Transition state stabilizerUniRule annotation
Binding sitei374 – 3741SubstrateUniRule 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. photorespiration Source: UniProtKB-KW
  2. reductive pentose-phosphate cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Lyase, Monooxygenase, Oxidoreductase

Keywords - Biological processi

Calvin cycle, Carbon dioxide fixation, Photorespiration, Photosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-750.
SABIO-RKP54205.

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
Synonyms:rbcLUniRule annotation
Ordered Locus Names:slr0009
OrganismiSynechocystis sp. (strain PCC 6803 / Kazusa)
Taxonomic identifieri1111708 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis
ProteomesiUP000001425: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 470470Ribulose bisphosphate carboxylase large chainPRO_0000062655Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei196 – 1961N6-carboxylysineUniRule annotation
Disulfide bondi242 – 242Interchain; in linked formUniRule annotation

Post-translational modificationi

The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover.UniRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP54205.
PRIDEiP54205.

Interactioni

Subunit structurei

Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers.UniRule annotation

Binary interactionsi

WithEntry#Exp.IntActNotes
trxAP522313EBI-862277,EBI-862916

Protein-protein interaction databases

IntActiP54205. 4 interactions.
STRINGi1148.slr0009.

Structurei

3D structure databases

ProteinModelPortaliP54205.
SMRiP54205. Positions 6-464.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
InParanoidiP54205.
KOiK01601.
OMAiHAAFTRN.
OrthoDBiEOG6ZKXMS.
PhylomeDBiP54205.

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.

P54205-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVQAKAGFKA GVQDYRLTYY TPDYTPKDTD LLACFRMTPQ PGVPAEEAAA
60 70 80 90 100
AVAAESSTGT WTTVWTDNLT DLDRYKGRCY DLEAVPNEDN QYFAFIAYPL
110 120 130 140 150
DLFEEGSVTN VLTSLVGNVF GFKALRALRL EDIRFPVALI KTFQGPPHGI
160 170 180 190 200
TVERDKLNKY GRPLLGCTIK PKLGLSAKNY GRAVYECLRG GLDFTKDDEN
210 220 230 240 250
INSQPFMRWR DRFLFVQEAI EKAQAETNEM KGHYLNVTAG TCEEMMKRAE
260 270 280 290 300
FAKEIGTPII MHDFFTGGFT ANTTLARWCR DNGILLHIHR AMHAVVDRQK
310 320 330 340 350
NHGIHFRVLA KCLRLSGGDH LHSGTVVGKL EGERGITMGF VDLMREDYVE
360 370 380 390 400
EDRSRGIFFT QDYASMPGTM PVASGGIHVW HMPALVEIFG DDSCLQFGGG
410 420 430 440 450
TLGHPWGNAP GATANRVALE ACVQARNEGR NLAREGNDVI REACRWSPEL
460 470
AAACELWKEI KFEFEAMDTL
Length:470
Mass (Da):52,491
Last modified:October 1, 1996 - v1
Checksum:i45B9322482745B2B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65960 Genomic DNA. Translation: CAA46773.1.
BA000022 Genomic DNA. Translation: BAA10190.1.
PIRiS39561.
RefSeqiNP_442120.1. NC_000911.1.
YP_005652178.1. NC_017277.1.
YP_007451997.1. NC_020286.1.

Genome annotation databases

EnsemblBacteriaiBAA10190; BAA10190; BAA10190.
GeneIDi952593.
KEGGisyn:slr0009.
PATRICi23841842. VBISynSp132158_2465.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65960 Genomic DNA. Translation: CAA46773.1.
BA000022 Genomic DNA. Translation: BAA10190.1.
PIRiS39561.
RefSeqiNP_442120.1. NC_000911.1.
YP_005652178.1. NC_017277.1.
YP_007451997.1. NC_020286.1.

3D structure databases

ProteinModelPortaliP54205.
SMRiP54205. Positions 6-464.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP54205. 4 interactions.
STRINGi1148.slr0009.

Proteomic databases

PaxDbiP54205.
PRIDEiP54205.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA10190; BAA10190; BAA10190.
GeneIDi952593.
KEGGisyn:slr0009.
PATRICi23841842. VBISynSp132158_2465.

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
InParanoidiP54205.
KOiK01601.
OMAiHAAFTRN.
OrthoDBiEOG6ZKXMS.
PhylomeDBiP54205.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-750.
SABIO-RKP54205.

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. "Construction of a Synechocystis PCC6803 mutant suitable for the study of variant hexadecameric ribulose bisphosphate carboxylase/oxygenase enzymes."
    Amichay D., Levitz R., Gurevitz M.
    Plant Mol. Biol. 23:465-476(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region from map positions 64% to 92% of the genome."
    Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N., Sugiura M., Tabata S.
    DNA Res. 2:153-166(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 27184 / PCC 6803 / N-1.
  3. "Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
    Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.
    , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PCC 6803 / Kazusa.

Entry informationi

Entry nameiRBL_SYNY3
AccessioniPrimary (citable) accession number: P54205
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: January 7, 2015
This is version 108 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
  2. Synechocystis PCC 6803
    Synechocystis (strain PCC 6803): entries and gene names

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.