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H0PB08

- H0PB08_9SYNC

UniProt

H0PB08 - H0PB08_9SYNC

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Protein

Ribulose bisphosphate carboxylase large chain

Gene

rbcL

Organism
Synechocystis sp. PCC 6803 substr. PCC-N
Status
Unreviewed - 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

Note: Binds 1 magnesium 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

LyaseUniRule annotation, MonooxygenaseUniRule annotation, Oxidoreductase

Keywords - Biological processi

Calvin cycleUniRule annotation, Carbon dioxide fixationUniRule annotation, PhotorespirationUniRule annotation

Keywords - Ligandi

MagnesiumUniRule annotation, Metal-bindingUniRule annotation

Enzyme and pathway databases

BioCyciSSP1080229:GLM2-2255-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:rbcLUniRule annotation
Synonyms:cbbLUniRule annotation
ORF Names:SYNPCCN_2223Imported
OrganismiSynechocystis sp. PCC 6803 substr. PCC-NImported
Taxonomic identifieri1080229 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis
ProteomesiUP000007108: Chromosome

PTM / Processingi

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 bondUniRule annotation

Proteomic databases

PRIDEiH0PB08.

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

Structurei

3D structure databases

ProteinModelPortaliH0PB08.
SMRiH0PB08. Positions 6-464.
ModBaseiSearch...
MobiDBiSearch...

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.

H0PB08-1 [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:February 22, 2012 - v1
Checksum:i45B9322482745B2B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP012277 Genomic DNA. Translation: BAL33140.1.
RefSeqiWP_010873418.1. NC_017052.1.
YP_005409862.1. NC_017052.1.

Genome annotation databases

EnsemblBacteriaiBAL33140; BAL33140; SYNPCCN_2223.
GeneIDi12011000.
KEGGisys:SYNPCCN_2223.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP012277 Genomic DNA. Translation: BAL33140.1 .
RefSeqi WP_010873418.1. NC_017052.1.
YP_005409862.1. NC_017052.1.

3D structure databases

ProteinModelPortali H0PB08.
SMRi H0PB08. Positions 6-464.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi H0PB08.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAL33140 ; BAL33140 ; SYNPCCN_2223 .
GeneIDi 12011000.
KEGGi sys:SYNPCCN_2223.

Phylogenomic databases

KOi K01601.

Enzyme and pathway databases

BioCyci SSP1080229:GLM2-2255-MONOMER.

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. "Identification of substrain-specific mutations by massively parallel whole-genome resequencing of Synechocystis sp. PCC 6803."
    Kanesaki Y., Shiwa Y., Tajima N., Suzuki M., Watanabe S., Sato N., Ikeuchi M., Yoshikawa H.
    DNA Res. 19:67-79(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Entry informationi

Entry nameiH0PB08_9SYNC
AccessioniPrimary (citable) accession number: H0PB08
Entry historyi
Integrated into UniProtKB/TrEMBL: February 22, 2012
Last sequence update: February 22, 2012
Last modified: November 26, 2014
This is version 24 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 proteomeImported

External Data

Dasty 3