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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Leptolyngbya sp. PCC 7376
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei119 – 1191Substrate; in homodimeric partnerUniRule annotation
Binding sitei169 – 1691SubstrateUniRule annotation
Active sitei171 – 1711Proton acceptorUniRule annotation
Binding sitei173 – 1731SubstrateUniRule annotation
Metal bindingi197 – 1971Magnesium; via carbamate groupUniRule annotation
Metal bindingi199 – 1991MagnesiumUniRule annotation
Metal bindingi200 – 2001MagnesiumUniRule annotation
Active sitei290 – 2901Proton acceptorUniRule annotation
Binding sitei291 – 2911SubstrateUniRule annotation
Binding sitei323 – 3231SubstrateUniRule annotation
Sitei330 – 3301Transition state stabilizerUniRule annotation
Binding sitei375 – 3751SubstrateUniRule annotation

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

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
ORF Names:Lepto7376_0178Imported
OrganismiLeptolyngbya sp. PCC 7376Imported
Taxonomic identifieri111781 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeOscillatorialesLeptolyngbya
ProteomesiUP000010389 Componenti: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei197 – 1971N6-carboxylysineUniRule annotation
Disulfide bondi243 – 243Interchain; 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

Sequence similaritiesi

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

Phylogenomic databases

KOiK01601.

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.

K9PU29-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVQTKSAGFK AGVQDYRLTY YTPDYTPKDT DLLACFRMTP QAGVPAEECA
60 70 80 90 100
AAVAAESSTG TWTTVWTDGL TDLDRYKGRC YHVEPVAGED NQYFCFVAYP
110 120 130 140 150
LDLFEEGSIT NVLTSLVGNV FGFKALRALR LEDIRFPVAF IKTCPGNPHG
160 170 180 190 200
ITVERDLLNK YGRPLLGCTI KPKLGLSAKN YGRAVYECLR GGLDFTKDDE
210 220 230 240 250
NINSQPFMRW RDRFLFVQEA IEKAQAETNE VKGHYLNVTA ATCEEMIERA
260 270 280 290 300
EFAKEIGTPI VMHDFITGGF TANTSLSKWC RKNGLLLHIH RAMHAVIDRQ
310 320 330 340 350
KNHGIHFRVL AKCLRLSGGD HLHSGTVVGK LEGDRQGTLG FVDLMREDYV
360 370 380 390 400
EEDRSRGVFF TQDWASAPGT MPVASGGIHV WHMPALVDIF GDDSCLQFGG
410 420 430 440 450
GTLGHPWGNA PGATANRVAL EACVQARNEG RSLAREGNDV LREAGKWSPE
460 470
LAAALNLWKE IKFEFDTVDT L
Length:471
Mass (Da):52,214
Last modified:March 6, 2013 - v1
Checksum:iC9C386CD54825A21
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP003946 Genomic DNA. Translation: AFY36623.1.
RefSeqiWP_015132410.1. NC_019683.1.

Genome annotation databases

EnsemblBacteriaiAFY36623; AFY36623; Lepto7376_0178.
KEGGilep:Lepto7376_0178.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP003946 Genomic DNA. Translation: AFY36623.1.
RefSeqiWP_015132410.1. NC_019683.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAFY36623; AFY36623; Lepto7376_0178.
KEGGilep:Lepto7376_0178.

Phylogenomic databases

KOiK01601.

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.

Entry informationi

Entry nameiK9PU29_9CYAN
AccessioniPrimary (citable) accession number: K9PU29
Entry historyi
Integrated into UniProtKB/TrEMBL: March 6, 2013
Last sequence update: March 6, 2013
Last modified: July 22, 2015
This is version 18 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.