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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Thiobacillus denitrificans (strain ATCC 25259)
Status
Reviewed-Annotation score: 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. Both reactions occur simultaneously and in competition at the same active site.1 Publication

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".

Catalytic activityi

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

Cofactori

Mg2+Note: Binds 1 Mg2+ ion per subunit.

Kineticsi

The CO2/O2 specificity factor (tau) is 46.
  1. KM=43 µM for ribulose 1,5-bisphosphate1 Publication
  2. KM=138 µM for CO21 Publication
  3. KM=1637 µM for O21 Publication
  1. Vmax=1.8 µmol/min/mg enzyme with CO2 as substrate1 Publication
  2. Vmax=0.5 µmol/min/mg enzyme with O2 as substrate1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei116Substrate; in homodimeric partner1
Binding sitei166Substrate1
Active sitei168Proton acceptor1
Binding sitei170Substrate1
Metal bindingi194Magnesium; via carbamate group1
Metal bindingi196Magnesium1
Metal bindingi197Magnesium1
Active sitei287Proton acceptor1
Binding sitei288Substrate1
Binding sitei320Substrate1
Sitei327Transition state stabilizer1
Binding sitei372Substrate1

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase large chain (EC:4.1.1.39)
Short name:
RuBisCO large subunit
Gene namesi
Name:cbbL
Synonyms:cbbL1
Ordered Locus Names:Tbd_2624
OrganismiThiobacillus denitrificans (strain ATCC 25259)
Taxonomic identifieri292415 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesThiobacillaceaeThiobacillus
Proteomesi
  • UP000008291 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000626561 – 473Ribulose bisphosphate carboxylase large chainAdd BLAST473

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei194N6-carboxylysine1

Interactioni

Subunit structurei

Heterohexadecamer of 8 large chains and 8 small chains (By similarity). In R.sphaeroides the complex is approximately 500 kDa.1 Publication

Protein-protein interaction databases

STRINGi292415.Tbd_2624.

Structurei

3D structure databases

ProteinModelPortaliQ56259.
SMRiQ56259.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

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

Family and domain databases

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.

Q56259-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVKTYSAGV KEYRQTYWMP EYTPLDTDIL ACFKITPQAG VDREEAAAAV
60 70 80 90 100
AAESSTGTWT TVWTDLLTDL DYYKGRAYAI EDVPGDDTCF YAFIAYPIDL
110 120 130 140 150
FEEGSVVNVF TSLVGNVFGF KAVRALRLED VRFPIAYVKT CGGPPHGIQV
160 170 180 190 200
ERDVMNKYGR PLLGCTIKPK LGLSAKNYGR AVYECLRGGL DFTKDDENVN
210 220 230 240 250
SQPFMRWRQR FDFVMEAIQK SERETGERKG HYLNVTAPTP EEMYKRAEYA
260 270 280 290 300
KEIGAPIIMH DYITGGFCAN TGLANWCRDN GMLLHIHRAM HAVLDRNPHH
310 320 330 340 350
GIHFRVLTKI LRLSGGDHLH SGTVVGKLEG DREATLGWID MMRDSFVKED
360 370 380 390 400
RSRGIFFDQD WGSMPGVFPV ASGGIHVWHM PALVTIFGDD SVLQFGGGTL
410 420 430 440 450
GHPWGNAAGA AANRVALEAC VEARNKGVAI EKEGKTVLTE AAKNSPELKI
460 470
AMETWKEIKF EFDTVDKLDV AHK
Length:473
Mass (Da):52,694
Last modified:January 1, 1998 - v2
Checksum:i470DC11519D580A7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42940 Genomic DNA. Translation: AAB70697.1.
CP000116 Genomic DNA. Translation: AAZ98577.1.
RefSeqiWP_011313136.1. NC_007404.1.

Genome annotation databases

EnsemblBacteriaiAAZ98577; AAZ98577; Tbd_2624.
KEGGitbd:Tbd_2624.

Similar proteinsi

Entry informationi

Entry nameiRBL1_THIDA
AccessioniPrimary (citable) accession number: Q56259
Secondary accession number(s): Q3SFM9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: October 25, 2017
This is version 112 of the entry and version 2 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