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Q2JIP3

- RBL_SYNJB

UniProt

Q2JIP3 - RBL_SYNJB

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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium Yellowstone B-Prime)
Status
Reviewed - 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

Binds 1 magnesium ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei122 – 1221Substrate; in homodimeric partnerUniRule annotation
Binding sitei172 – 1721SubstrateUniRule annotation
Active sitei174 – 1741Proton acceptorUniRule annotation
Binding sitei176 – 1761SubstrateUniRule annotation
Metal bindingi200 – 2001Magnesium; via carbamate groupUniRule annotation
Metal bindingi202 – 2021MagnesiumUniRule annotation
Metal bindingi203 – 2031MagnesiumUniRule annotation
Active sitei293 – 2931Proton acceptorUniRule annotation
Binding sitei294 – 2941SubstrateUniRule annotation
Binding sitei326 – 3261SubstrateUniRule annotation
Sitei333 – 3331Transition state stabilizerUniRule annotation
Binding sitei378 – 3781SubstrateUniRule 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

Lyase, Monooxygenase, Oxidoreductase

Keywords - Biological processi

Calvin cycle, Carbon dioxide fixation, Photorespiration, Photosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciSSP321332:GH1B-2579-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:CYB_2579
OrganismiSynechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium Yellowstone B-Prime)
Taxonomic identifieri321332 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
ProteomesiUP000001938: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 474474Ribulose bisphosphate carboxylase large chainPRO_0000251462Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei200 – 2001N6-carboxylysineUniRule annotation
Disulfide bondi246 – 246Interchain; 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 bond

Proteomic databases

PRIDEiQ2JIP3.

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

Protein-protein interaction databases

STRINGi321332.CYB_2579.

Structurei

3D structure databases

ProteinModelPortaliQ2JIP3.
SMRiQ2JIP3. Positions 8-474.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiFTQDWAS.
OrthoDBiEOG6ZKXMS.

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.

Q2JIP3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAYSATQSKS GYQAGVKDYR LTYYTPDYTP KDTDVLACFR VTPQPGVPPE
60 70 80 90 100
EAGAAVAAES STGTWTTVWT DLLTDLDRYK GRCYDIEPVP GEDNQYFCFV
110 120 130 140 150
AYPLDLFEEG SVTNMLTSIV GNVFGFKALK ALRLEDVRIP VAYLKTFQGP
160 170 180 190 200
PHGIQVERDK LNKYGRPLLG CTIKPKLGLS AKNYGRAVYE ALRGGLDFTK
210 220 230 240 250
DDENINSQPF QRWRDRYLFV MEAVHKAQAE TGEIKGHYLN VTAPTCEEMF
260 270 280 290 300
KRAEFAKELG APIIMHDYLT AGFTANTSLA KWCRDNGILL HIHRAMHAVI
310 320 330 340 350
DRQKNHGIHF RVLAKCLRMS GGDHLHSGTV VGKLEGDRAI TMGFVDLMRE
360 370 380 390 400
NYVEADRSRG IFFTQDWASM PGVMPVASGG IHVWHMPALV EIFGDDSVLQ
410 420 430 440 450
FGGGTLGHPW GNAPGATANR VALEACIQAR NEGRDLAREG NDIIREAAKW
460 470
SPELAAACEL WKEIKFEFKA VDTL
Length:474
Mass (Da):52,727
Last modified:March 7, 2006 - v1
Checksum:i159EB8C81B3EA67A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000240 Genomic DNA. Translation: ABD03511.1.
RefSeqiWP_011434138.1. NC_007776.1.
YP_478774.1. NC_007776.1.

Genome annotation databases

EnsemblBacteriaiABD03511; ABD03511; CYB_2579.
GeneIDi3901300.
KEGGicyb:CYB_2579.
PATRICi23807514. VBISynSp29577_2582.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000240 Genomic DNA. Translation: ABD03511.1 .
RefSeqi WP_011434138.1. NC_007776.1.
YP_478774.1. NC_007776.1.

3D structure databases

ProteinModelPortali Q2JIP3.
SMRi Q2JIP3. Positions 8-474.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 321332.CYB_2579.

Proteomic databases

PRIDEi Q2JIP3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABD03511 ; ABD03511 ; CYB_2579 .
GeneIDi 3901300.
KEGGi cyb:CYB_2579.
PATRICi 23807514. VBISynSp29577_2582.

Phylogenomic databases

eggNOGi COG1850.
HOGENOMi HOG000230831.
KOi K01601.
OMAi FTQDWAS.
OrthoDBi EOG6ZKXMS.

Enzyme and pathway databases

BioCyci SSP321332:GH1B-2579-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. "Population level functional diversity in a microbial community revealed by comparative genomic and metagenomic analyses."
    Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N., Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.
    ISME J. 1:703-713(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: JA-2-3B'a(2-13).

Entry informationi

Entry nameiRBL_SYNJB
AccessioniPrimary (citable) accession number: Q2JIP3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: March 7, 2006
Last modified: October 1, 2014
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

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 proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3