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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Cyanothece sp. (strain PCC 7822)
Status
Unreviewed-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 sitei120 – 1201Substrate; in homodimeric partnerUniRule annotation
Binding sitei170 – 1701SubstrateUniRule annotation
Active sitei172 – 1721Proton acceptorUniRule annotation
Binding sitei174 – 1741SubstrateUniRule annotation
Metal bindingi198 – 1981Magnesium; via carbamate groupUniRule annotation
Metal bindingi200 – 2001MagnesiumUniRule annotation
Metal bindingi201 – 2011MagnesiumUniRule annotation
Active sitei291 – 2911Proton acceptorUniRule annotation
Binding sitei292 – 2921SubstrateUniRule annotation
Binding sitei324 – 3241SubstrateUniRule annotation
Sitei331 – 3311Transition state stabilizerUniRule annotation
Binding sitei376 – 3761SubstrateUniRule 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

LyaseUniRule annotationImported, MonooxygenaseUniRule annotation, Oxidoreductase

Keywords - Biological processi

Calvin cycleUniRule annotation, Carbon dioxide fixationUniRule annotation, PhotorespirationUniRule annotation, PhotosynthesisUniRule annotation

Keywords - Ligandi

MagnesiumUniRule annotation, Metal-bindingUniRule annotation

Enzyme and pathway databases

BioCyciCSP497965:GJAC-2935-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
Synonyms:rbcLUniRule annotation
Ordered Locus Names:Cyan7822_2899Imported
OrganismiCyanothece sp. (strain PCC 7822)Imported
Taxonomic identifieri497965 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesCyanothece
ProteomesiUP000008206 Componenti: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei198 – 1981N6-carboxylysineUniRule annotation

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliE0U7P5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000230831.
KOiK01601.
OMAiHAAFTRN.

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.

E0U7P5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVQSKAKGGF QAGVKDYRLT YYTPDYTPKD TDLLACFRVT PQPGVPPEEA
60 70 80 90 100
GAAVAAESST GTWTTVWTDG LTDLDRYKGR CYDIEPVPNE DNQYFCFVAY
110 120 130 140 150
PLDLFEEGSV TNILTSIVGN VFGFKALRAL RLEDIRFPVA LLKTFQGPPH
160 170 180 190 200
GITVERDKLN KYGRPLLGCT IKPKLGLSAK NYGRAVYECL RGGLDFTKDD
210 220 230 240 250
ENINSQPFMR WRDRFLFVQE AIEKAQAETN EIKGHYLNVT AGTLEEMMKR
260 270 280 290 300
AEFAKEIKTP IIMHDYLTGG FTANTTLAKF CRDNGLLLHI HRAMHAVIDR
310 320 330 340 350
QKNHGIHFRV LAKCLRMSGG DHLHSGTVVG KLEGERGITM GFVDLMREDY
360 370 380 390 400
VEEDRARGIF FTQDWASMPG VMPVASGGIH VWHMPALVEI FGDDSCLQFG
410 420 430 440 450
GGTLGHPWGN APGATANRVA LEACIQARNE GRSLAREGNE VIREAARWSP
460 470
ELAAACELWK EIKFEFEAMD TL
Length:472
Mass (Da):52,657
Last modified:November 2, 2010 - v1
Checksum:iCE42E983A700A93A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002198 Genomic DNA. Translation: ADN14857.1.
RefSeqiWP_013322960.1. NC_014501.1.
YP_003888132.1. NC_014501.1.

Genome annotation databases

EnsemblBacteriaiADN14857; ADN14857; Cyan7822_2899.
KEGGicyj:Cyan7822_2899.
PATRICi42286569. VBICyaSp18455_3032.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002198 Genomic DNA. Translation: ADN14857.1.
RefSeqiWP_013322960.1. NC_014501.1.
YP_003888132.1. NC_014501.1.

3D structure databases

ProteinModelPortaliE0U7P5.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiADN14857; ADN14857; Cyan7822_2899.
KEGGicyj:Cyan7822_2899.
PATRICi42286569. VBICyaSp18455_3032.

Phylogenomic databases

HOGENOMiHOG000230831.
KOiK01601.
OMAiHAAFTRN.

Enzyme and pathway databases

BioCyciCSP497965:GJAC-2935-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. "Novel metabolic attributes of the genus Cyanothece, comprising a group of unicellular nitrogen-fixing Cyanobacteria."
    Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H., Sherman L.A., Pakrasi H.B.
    MBio 2:E214-E214(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PCC 7822Imported.

Entry informationi

Entry nameiE0U7P5_CYAP2
AccessioniPrimary (citable) accession number: E0U7P5
Entry historyi
Integrated into UniProtKB/TrEMBL: November 2, 2010
Last sequence update: November 2, 2010
Last modified: April 1, 2015
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

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 proteomeImported

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.