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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans)
Status
Reviewed-Annotation score: Annotation score: 5 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.2 Publications

Catalytic activityi

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O.2 Publications
3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2.1 Publication

Cofactori

Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit.1 Publication

Kineticsi

The CO2/O2 specificity factor (tau) is 39.

  1. KM=39 µM for ribulose 1,5-bisphosphate1 Publication
  2. KM=173 µM for CO21 Publication
  1. Vmax=2.5 µmol/min/mg enzyme with CO2 as substrate1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei120Substrate; in homodimeric partner1
Binding sitei170Substrate1
Active sitei172Proton acceptor1
Binding sitei174Substrate1
Metal bindingi198Magnesium; via carbamate group1 Publication1
Metal bindingi200Magnesium1 Publication1
Metal bindingi201Magnesium1 Publication1
Active sitei291Proton acceptor1
Binding sitei292Substrate1
Binding sitei324Substrate1
Sitei331Transition state stabilizer1
Binding sitei376Substrate1

GO - Molecular functioni

GO - Biological processi

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

SABIO-RKP00880.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase large chain (EC:4.1.1.392 Publications)
Short name:
RuBisCO large subunit
Gene namesi
Name:cbbL
Synonyms:rbcA, rbcL
Ordered Locus Names:syc0130_c
OrganismiSynechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans)
Taxonomic identifieri269084 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesSynechococcaceaeSynechococcus
Proteomesi
  • UP000001175 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000626511 – 472Ribulose bisphosphate carboxylase large chainAdd BLAST472

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei198N6-carboxylysine1 Publication1
Disulfide bondi244Interchain; in linked form1 Publication

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.1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP00880.

Interactioni

Subunit structurei

Heterohexadecamer of 8 large chains and 8 small chains (PubMed:9882445, PubMed:7922027); disulfide-linked (PubMed:8245022). The disulfide link is formed within the large subunit homodimers (PubMed:8245022).1 Publication2 Publications

Protein-protein interaction databases

DIPiDIP-6210N.
STRINGi269084.syc0130_c.

Structurei

Secondary structure

1472
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi18 – 21Combined sources4
Beta strandi32 – 41Combined sources10
Helixi47 – 57Combined sources11
Turni58 – 60Combined sources3
Beta strandi63 – 65Combined sources3
Helixi67 – 71Combined sources5
Helixi74 – 77Combined sources4
Beta strandi80 – 86Combined sources7
Beta strandi94 – 100Combined sources7
Helixi102 – 104Combined sources3
Helixi110 – 118Combined sources9
Helixi121 – 123Combined sources3
Beta strandi127 – 136Combined sources10
Helixi139 – 142Combined sources4
Helixi152 – 159Combined sources8
Beta strandi166 – 168Combined sources3
Beta strandi172 – 175Combined sources4
Helixi179 – 191Combined sources13
Beta strandi195 – 198Combined sources4
Beta strandi204 – 206Combined sources3
Helixi211 – 229Combined sources19
Beta strandi234 – 238Combined sources5
Helixi244 – 256Combined sources13
Beta strandi260 – 265Combined sources6
Helixi266 – 269Combined sources4
Helixi271 – 284Combined sources14
Beta strandi287 – 291Combined sources5
Helixi295 – 299Combined sources5
Beta strandi302 – 306Combined sources5
Helixi308 – 318Combined sources11
Beta strandi321 – 324Combined sources4
Beta strandi328 – 332Combined sources5
Helixi336 – 347Combined sources12
Beta strandi349 – 351Combined sources3
Helixi355 – 357Combined sources3
Beta strandi372 – 378Combined sources7
Helixi381 – 383Combined sources3
Helixi384 – 391Combined sources8
Beta strandi396 – 398Combined sources3
Helixi401 – 404Combined sources4
Helixi410 – 430Combined sources21
Helixi434 – 448Combined sources15
Helixi450 – 459Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RBLX-ray2.20A/B/C/D/E/F/G/H6-472[»]
1RSCX-ray2.30A/B/C/D/E/F/G/H1-472[»]
2WVWelectron microscopy9.00A/B/C/D/E/F/G/H1-472[»]
3RG6X-ray3.20A/B1-472[»]
ProteinModelPortaliP00880.
SMRiP00880.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00880.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105DT1. Bacteria.
COG1850. LUCA.
HOGENOMiHOG000230831.
KOiK01601.
OMAiFTQDWAS.
OrthoDBiPOG091H14UZ.

Family and domain databases

CDDicd08212. RuBisCO_large_I. 1 hit.
Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01338. RuBisCO_L_type1. 1 hit.
InterProiIPR033966. RuBisCO.
IPR020878. RuBisCo_large_chain_AS.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR020888. RuBisCO_lsuI.
[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.

P00880-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKTQSAAGY KAGVKDYKLT YYTPDYTPKD TDLLAAFRFS PQPGVPADEA
60 70 80 90 100
GAAIAAESST GTWTTVWTDL LTDMDRYKGK CYHIEPVQGE ENSYFAFIAY
110 120 130 140 150
PLDLFEEGSV TNILTSIVGN VFGFKAIRSL RLEDIRFPVA LVKTFQGPPH
160 170 180 190 200
GIQVERDLLN KYGRPMLGCT IKPKLGLSAK NYGRAVYECL RGGLDFTKDD
210 220 230 240 250
ENINSQPFQR WRDRFLFVAD AIHKSQAETG EIKGHYLNVT APTCEEMMKR
260 270 280 290 300
AEFAKELGMP IIMHDFLTAG FTANTTLAKW CRDNGVLLHI HRAMHAVIDR
310 320 330 340 350
QRNHGIHFRV LAKCLRLSGG DHLHSGTVVG KLEGDKASTL GFVDLMREDH
360 370 380 390 400
IEADRSRGVF FTQDWASMPG VLPVASGGIH VWHMPALVEI FGDDSVLQFG
410 420 430 440 450
GGTLGHPWGN APGATANRVA LEACVQARNE GRDLYREGGD ILREAGKWSP
460 470
ELAAALDLWK EIKFEFETMD KL
Length:472
Mass (Da):52,448
Last modified:February 15, 2005 - v2
Checksum:iCDD8519AA9D493C9
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti38 – 39RF → PV in K00486 (PubMed:6307620).Curated2
Sequence conflicti353A → R in K00486 (PubMed:6307620).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K00486 Genomic DNA. No translation available.
X03220 Genomic DNA. Translation: CAA26972.1.
AP008231 Genomic DNA. Translation: BAD78320.1.
PIRiA90941. RKYCL.
RefSeqiWP_011242444.1. NC_006576.1.

Genome annotation databases

EnsemblBacteriaiBAD78320; BAD78320; syc0130_c.
KEGGisyc:syc0130_c.
PATRICi32485757. VBISynElo117686_0157.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K00486 Genomic DNA. No translation available.
X03220 Genomic DNA. Translation: CAA26972.1.
AP008231 Genomic DNA. Translation: BAD78320.1.
PIRiA90941. RKYCL.
RefSeqiWP_011242444.1. NC_006576.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RBLX-ray2.20A/B/C/D/E/F/G/H6-472[»]
1RSCX-ray2.30A/B/C/D/E/F/G/H1-472[»]
2WVWelectron microscopy9.00A/B/C/D/E/F/G/H1-472[»]
3RG6X-ray3.20A/B1-472[»]
ProteinModelPortaliP00880.
SMRiP00880.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6210N.
STRINGi269084.syc0130_c.

Proteomic databases

PRIDEiP00880.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD78320; BAD78320; syc0130_c.
KEGGisyc:syc0130_c.
PATRICi32485757. VBISynElo117686_0157.

Phylogenomic databases

eggNOGiENOG4105DT1. Bacteria.
COG1850. LUCA.
HOGENOMiHOG000230831.
KOiK01601.
OMAiFTQDWAS.
OrthoDBiPOG091H14UZ.

Enzyme and pathway databases

SABIO-RKP00880.

Miscellaneous databases

EvolutionaryTraceiP00880.

Family and domain databases

CDDicd08212. RuBisCO_large_I. 1 hit.
Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01338. RuBisCO_L_type1. 1 hit.
InterProiIPR033966. RuBisCO.
IPR020878. RuBisCo_large_chain_AS.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR020888. RuBisCO_lsuI.
[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...

Entry informationi

Entry nameiRBL_SYNP6
AccessioniPrimary (citable) accession number: P00880
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 15, 2005
Last modified: November 30, 2016
This is version 137 of the entry and version 2 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".1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.