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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Cyanobacterium aponinum (strain PCC 10605)
Status
Unreviewed-Annotation score: Annotation score: 4 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)DescriptionActionsGraphical viewLength
Binding sitei116Substrate; in homodimeric partnerUniRule annotation1
Binding sitei166SubstrateUniRule annotation1
Active sitei168Proton acceptorUniRule annotation1
Binding sitei170SubstrateUniRule annotation1
Metal bindingi194Magnesium; via carbamate groupUniRule annotation1
Metal bindingi196MagnesiumUniRule annotation1
Metal bindingi197MagnesiumUniRule annotation1
Active sitei287Proton acceptorUniRule annotation1
Binding sitei288SubstrateUniRule annotation1
Binding sitei320SubstrateUniRule annotation1
Sitei327Transition state stabilizerUniRule annotation1
Binding sitei372SubstrateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

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

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:Cyan10605_0644Imported
OrganismiCyanobacterium aponinum (strain PCC 10605)Imported
Taxonomic identifieri755178 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesCyanobacteriaceaeCyanobacterium
Proteomesi
  • UP000010480 Componenti: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei194N6-carboxylysineUniRule annotation1
Disulfide bondi240Interchain; 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 bondUniRule annotation

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini17 – 136RuBisCO_large_NInterPro annotationAdd BLAST120
Domaini147 – 455RuBisCO_largeInterPro annotationAdd BLAST309

Sequence similaritiesi

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

Phylogenomic databases

KOiK01601.
OMAiFTQDWAS.
OrthoDBiPOG091H14UZ.

Family and domain databases

CDDicd08212. RuBisCO_large_I. 1 hit.
Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01338. RuBisCO_L_type1. 1 hit.
InterProiIPR033966. RuBisCO.
IPR020878. RuBisCo_large_chain_AS.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR020888. RuBisCO_lsuI.
[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.

K9Z349-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQAGFKAGV QDYRLTYYTP DYTPKDTDLL ACFRMTPQPG VPPEECAAAV
60 70 80 90 100
AAESSTGTWT TVWTDGLTDL DRYKGRCYSV EPVPGEDNQY FCFVAYPLDL
110 120 130 140 150
FEEGSITNVL TSLVGNVFGF KALRALRLED IRFPVALIKT YQGPPHGITV
160 170 180 190 200
ERDLLNKYGR PLLGCTIKPK LGLSAKNYGR AVYECLRGGL DFTKDDENIN
210 220 230 240 250
SQPFMRWRDR FLFVQEAIEK AQAETNEIKG HYLNVTAGTC EEMLKRAEFA
260 270 280 290 300
KEIGTPIIMH DFLTGGFTAN TTLAKWCRDN GVLLHIHRAM HAVIDRQKNH
310 320 330 340 350
GIHFRVLAKC LRLSGGDHLH SGTVVGKLEG DRAATLGFVD LMREDYVEED
360 370 380 390 400
RSRGVFFTQD YASLPGTMPV ASGGIHVWHM PALVEIFGDD SCLQFGGGTL
410 420 430 440 450
GHPWGNAPGA TANRVALEAC VQARNEGRSL AREGNEVIRE ACRWSPELAA
460
ACELWKEIKF EFDTVDTL
Length:468
Mass (Da):52,005
Last modified:March 6, 2013 - v1
Checksum:iC6002D758ABF66F5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP003947 Genomic DNA. Translation: AFZ52783.1.
RefSeqiWP_015218514.1. NC_019776.1.

Genome annotation databases

EnsemblBacteriaiAFZ52783; AFZ52783; Cyan10605_0644.
KEGGican:Cyan10605_0644.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP003947 Genomic DNA. Translation: AFZ52783.1.
RefSeqiWP_015218514.1. NC_019776.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAFZ52783; AFZ52783; Cyan10605_0644.
KEGGican:Cyan10605_0644.

Phylogenomic databases

KOiK01601.
OMAiFTQDWAS.
OrthoDBiPOG091H14UZ.

Family and domain databases

CDDicd08212. RuBisCO_large_I. 1 hit.
Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01338. RuBisCO_L_type1. 1 hit.
InterProiIPR033966. RuBisCO.
IPR020878. RuBisCo_large_chain_AS.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR020888. RuBisCO_lsuI.
[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...

Entry informationi

Entry nameiK9Z349_CYAAP
AccessioniPrimary (citable) accession number: K9Z349
Entry historyi
Integrated into UniProtKB/TrEMBL: March 6, 2013
Last sequence update: March 6, 2013
Last modified: November 30, 2016
This is version 32 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

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 one 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.