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K9PU29

- K9PU29_9CYAN

UniProt

K9PU29 - K9PU29_9CYAN

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Protein
Ribulose bisphosphate carboxylase large chain
Gene
cbbL, rbcL, Lepto7376_0178
Organism
Leptolyngbya sp. PCC 7376
Status
Unreviewed - 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 By similarity.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

Binds 1 magnesium ion per subunit By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei119 – 1191Substrate; in homodimeric partner By similarityUniRule annotation
Binding sitei169 – 1691Substrate By similarityUniRule annotation
Active sitei171 – 1711Proton acceptor By similarityUniRule annotation
Binding sitei173 – 1731Substrate By similarityUniRule annotation
Metal bindingi197 – 1971Magnesium; via carbamate group By similarityUniRule annotation
Metal bindingi199 – 1991Magnesium By similarityUniRule annotation
Metal bindingi200 – 2001Magnesium By similarityUniRule annotation
Active sitei290 – 2901Proton acceptor By similarityUniRule annotation
Binding sitei291 – 2911Substrate By similarityUniRule annotation
Binding sitei323 – 3231Substrate By similarityUniRule annotation
Sitei330 – 3301Transition state stabilizer By similarityUniRule annotation
Binding sitei375 – 3751Substrate By similarityUniRule 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

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: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei197 – 1971N6-carboxylysine By similarityUniRule annotation
Disulfide bondi243 – 243Interchain; in linked form By similarityUniRule 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 By similarity.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 By similarity.UniRule annotation

Family & Domainsi

Sequence similaritiesi

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

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MVQTKSAGFK AGVQDYRLTY YTPDYTPKDT DLLACFRMTP QAGVPAEECA    50
AAVAAESSTG TWTTVWTDGL TDLDRYKGRC YHVEPVAGED NQYFCFVAYP 100
LDLFEEGSIT NVLTSLVGNV FGFKALRALR LEDIRFPVAF IKTCPGNPHG 150
ITVERDLLNK YGRPLLGCTI KPKLGLSAKN YGRAVYECLR GGLDFTKDDE 200
NINSQPFMRW RDRFLFVQEA IEKAQAETNE VKGHYLNVTA ATCEEMIERA 250
EFAKEIGTPI VMHDFITGGF TANTSLSKWC RKNGLLLHIH RAMHAVIDRQ 300
KNHGIHFRVL AKCLRLSGGD HLHSGTVVGK LEGDRQGTLG FVDLMREDYV 350
EEDRSRGVFF TQDWASAPGT MPVASGGIHV WHMPALVDIF GDDSCLQFGG 400
GTLGHPWGNA PGATANRVAL EACVQARNEG RSLAREGNDV LREAGKWSPE 450
LAAALNLWKE IKFEFDTVDT L 471
Length:471
Mass (Da):52,214
Last modified:March 6, 2013 - v1
Checksum:iC9C386CD54825A21
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP003946 Genomic DNA. Translation: AFY36623.1.
RefSeqiWP_015132410.1. NC_019683.1.
YP_007069457.1. NC_019683.1.

Genome annotation databases

EnsemblBacteriaiAFY36623; AFY36623; Lepto7376_0178.
GeneIDi14086091.
KEGGilep:Lepto7376_0178.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP003946 Genomic DNA. Translation: AFY36623.1 .
RefSeqi WP_015132410.1. NC_019683.1.
YP_007069457.1. NC_019683.1.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AFY36623 ; AFY36623 ; Lepto7376_0178 .
GeneIDi 14086091.
KEGGi lep:Lepto7376_0178.

Phylogenomic databases

KOi K01601.

Family and domain databases

Gene3Di 3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPi MF_01338. RuBisCO_L_type1.
InterProi IPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view ]
Pfami PF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view ]
SUPFAMi SSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEi PS00157. RUBISCO_LARGE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 12 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" By similarity.UniRule annotation

Keywords - Technical termi

Complete proteome

External Data

Dasty 3

Similar proteinsi