SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

F7US61

- F7US61_SYNYG

UniProt

F7US61 - F7US61_SYNYG

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Ribulose bisphosphate carboxylase large chain

Gene
cbbL, rbcL, SYNGTS_2225
Organism
Synechocystis sp. (strain PCC 6803 / GT-S)
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 sitei118 – 1181Substrate; in homodimeric partner By similarityUniRule annotation
Binding sitei168 – 1681Substrate By similarityUniRule annotation
Active sitei170 – 1701Proton acceptor By similarityUniRule annotation
Binding sitei172 – 1721Substrate By similarityUniRule annotation
Metal bindingi196 – 1961Magnesium; via carbamate group By similarityUniRule annotation
Metal bindingi198 – 1981Magnesium By similarityUniRule annotation
Metal bindingi199 – 1991Magnesium By similarityUniRule annotation
Active sitei289 – 2891Proton acceptor By similarityUniRule annotation
Binding sitei290 – 2901Substrate By similarityUniRule annotation
Binding sitei322 – 3221Substrate By similarityUniRule annotation
Sitei329 – 3291Transition state stabilizer By similarityUniRule annotation
Binding sitei374 – 3741Substrate 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 annotation, 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

BioCyciSSP1148:GJOT-2263-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:SYNGTS_2225Imported
OrganismiSynechocystis sp. (strain PCC 6803 / GT-S)
Taxonomic identifieri1111707 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis
ProteomesiUP000008187: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei196 – 1961N6-carboxylysine By similarityUniRule annotation
Disulfide bondi242 – 242Interchain; 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

Proteomic databases

PRIDEiF7US61.

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

Structurei

3D structure databases

ProteinModelPortaliF7US61.
SMRiF7US61. Positions 6-464.

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.

F7US61-1 [UniParc]FASTAAdd to Basket

« Hide

MVQAKAGFKA GVQDYRLTYY TPDYTPKDTD LLACFRMTPQ PGVPAEEAAA    50
AVAAESSTGT WTTVWTDNLT DLDRYKGRCY DLEAVPNEDN QYFAFIAYPL 100
DLFEEGSVTN VLTSLVGNVF GFKALRALRL EDIRFPVALI KTFQGPPHGI 150
TVERDKLNKY GRPLLGCTIK PKLGLSAKNY GRAVYECLRG GLDFTKDDEN 200
INSQPFMRWR DRFLFVQEAI EKAQAETNEM KGHYLNVTAG TCEEMMKRAE 250
FAKEIGTPII MHDFFTGGFT ANTTLARWCR DNGILLHIHR AMHAVVDRQK 300
NHGIHFRVLA KCLRLSGGDH LHSGTVVGKL EGERGITMGF VDLMREDYVE 350
EDRSRGIFFT QDYASMPGTM PVASGGIHVW HMPALVEIFG DDSCLQFGGG 400
TLGHPWGNAP GATANRVALE ACVQARNEGR NLAREGNDVI REACRWSPEL 450
AAACELWKEI KFEFEAMDTL 470
Length:470
Mass (Da):52,491
Last modified:September 21, 2011 - v1
Checksum:i45B9322482745B2B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP012205 Genomic DNA. Translation: BAK50973.1.
RefSeqiNP_442120.1. NC_000911.1.
YP_005652178.1. NC_017277.1.
YP_007451997.1. NC_020286.1.

Genome annotation databases

EnsemblBacteriaiBAK50973; BAK50973; SYNGTS_2225.
GeneIDi952593.
KEGGisyn:slr0009.
syy:SYNGTS_2225.
syz:MYO_122490.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP012205 Genomic DNA. Translation: BAK50973.1 .
RefSeqi NP_442120.1. NC_000911.1.
YP_005652178.1. NC_017277.1.
YP_007451997.1. NC_020286.1.

3D structure databases

ProteinModelPortali F7US61.
SMRi F7US61. Positions 6-464.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi F7US61.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAK50973 ; BAK50973 ; SYNGTS_2225 .
GeneIDi 952593.
KEGGi syn:slr0009.
syy:SYNGTS_2225.
syz:MYO_122490.

Phylogenomic databases

KOi K01601.

Enzyme and pathway databases

BioCyci SSP1148:GJOT-2263-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. "Genomic structure of the cyanobacterium Synechocystis sp. PCC 6803 strain GT-S."
    Tajima N., Sato S., Maruyama F., Kaneko T., Sasaki N.V., Kurokawa K., Ohta H., Kanesaki Y., Yoshikawa H., Tabata S., Ikeuchi M., Sato N.
    DNA Res. 18:393-399(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PCC 6803 / GT-S.

Entry informationi

Entry nameiF7US61_SYNYG
AccessioniPrimary (citable) accession number: F7US61
Entry historyi
Integrated into UniProtKB/TrEMBL: September 21, 2011
Last sequence update: September 21, 2011
Last modified: July 9, 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" By similarity.UniRule annotation

Keywords - Technical termi

Complete proteome

External Data

Dasty 3

Similar proteinsi