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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Cyanothece sp. (strain ATCC 51142)
Status
Reviewed-Annotation score: -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

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

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

Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei119Substrate; in homodimeric partnerUniRule annotation1
Binding sitei169SubstrateUniRule annotation1
Active sitei171Proton acceptorUniRule annotation1
Binding sitei173SubstrateUniRule annotation1
Metal bindingi197Magnesium; via carbamate groupUniRule annotation1
Metal bindingi199MagnesiumUniRule annotation1
Metal bindingi200MagnesiumUniRule annotation1
Active sitei290Proton acceptorUniRule annotation1
Binding sitei291SubstrateUniRule annotation1
Binding sitei323SubstrateUniRule annotation1
Sitei330Transition state stabilizerUniRule annotation1
Binding sitei375SubstrateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLyase, Monooxygenase, Oxidoreductase
Biological processCalvin cycle, Carbon dioxide fixation, Photorespiration, Photosynthesis
LigandMagnesium, Metal-binding

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:cce_3166
OrganismiCyanothece sp. (strain ATCC 51142)
Taxonomic identifieri43989 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeOscillatorialesCyanothecaceaeCyanothece
Proteomesi

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003557491 – 471Ribulose bisphosphate carboxylase large chainAdd BLAST471

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei197N6-carboxylysineUniRule annotation1
Disulfide bondi243Interchain; 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

PRIDEiB1WXH3

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

STRINGi43989.cce_3166

Structurei

3D structure databases

ProteinModelPortaliB1WXH3
SMRiB1WXH3
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105DT1 Bacteria
COG1850 LUCA
HOGENOMiHOG000230831
KOiK01601
OMAiHRAMHAA
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
InterProiView protein in InterPro
IPR033966 RuBisCO
IPR020878 RuBisCo_large_chain_AS
IPR000685 RuBisCO_lsu_C
IPR036376 RuBisCO_lsu_C_sf
IPR017443 RuBisCO_lsu_fd_N
IPR036422 RuBisCO_lsu_N_sf
IPR020888 RuBisCO_lsuI
PfamiView protein in Pfam
PF00016 RuBisCO_large, 1 hit
PF02788 RuBisCO_large_N, 1 hit
SFLDiSFLDS00014 RuBisCO, 1 hit
SUPFAMiSSF51649 SSF51649, 1 hit
SSF54966 SSF54966, 1 hit
PROSITEiView protein in PROSITE
PS00157 RUBISCO_LARGE, 1 hit

Sequencei

Sequence statusi: Complete.

B1WXH3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQATKSGFN AGVQDYRLTY YTPDYTPKDT DLLACFRMTP QPGVPPEEAG
60 70 80 90 100
AAVAAESSTG TWTTVWTDNL TDLDRYKGRC YDIEPVPNED NQYFCFIAYP
110 120 130 140 150
LDLFEEGSVT NVLTSLVGNV FGFKALRALR LEDIRFPVAL IKTFQGPPHG
160 170 180 190 200
ITVERDKLNK YGRPLLGCTI KPKLGLSAKN YGRAVYECLR GGLDFTKDDE
210 220 230 240 250
NINSQPFMRW RDRFLFVQEA IEKAQAETNE VKGHYLNVTA GTCEEMMKRA
260 270 280 290 300
EFAKEIGTPI VMHDFLTGGF TANTTLAKFC RDNGILLHIH RAMHAVIDRQ
310 320 330 340 350
KNHGIHFRVL AKCLRLSGGD HLHSGTVVGK LEGERGITMG FVDLMREDYV
360 370 380 390 400
EEDRSRGIFF TQDYASMPGT MPVASGGIHV WHMPALVEIF GDDSCLQFGG
410 420 430 440 450
GTLGHPWGNA PGATANRVAL EACIQARNEG RNLAREGNDV IREACKWSPE
460 470
LAAACELWKE ITFEFEAMDT L
Length:471
Mass (Da):52,462
Last modified:May 20, 2008 - v1
Checksum:i549FB4FF3AFDE916
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000806 Genomic DNA Translation: ACB52514.1
RefSeqiWP_009547487.1, NC_010546.1

Genome annotation databases

EnsemblBacteriaiACB52514; ACB52514; cce_3166
KEGGicyt:cce_3166

Entry informationi

Entry nameiRBL_CYAA5
AccessioniPrimary (citable) accession number: B1WXH3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: May 20, 2008
Last modified: May 23, 2018
This is version 59 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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