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Protein

Ribulose bisphosphate carboxylase large chain, chromosomal

Gene

cbbL1

Organism
Cupriavidus necator (Alcaligenes eutrophus) (Ralstonia eutropha)
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. Both reactions occur simultaneously and in competition at the same active site.

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei126Substrate; in homodimeric partner1
Binding sitei176Substrate1
Active sitei178Proton acceptor1
Binding sitei180Substrate1
Metal bindingi204Magnesium; via carbamate group1
Metal bindingi206Magnesium1
Metal bindingi207Magnesium1
Active sitei296Proton acceptor1
Binding sitei297Substrate1
Binding sitei329Substrate1
Sitei336Transition state stabilizer1
Binding sitei381Substrate1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase, Monooxygenase, Oxidoreductase

Keywords - Biological processi

Calvin cycle, Carbon dioxide fixation

Keywords - Ligandi

Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase large chain, chromosomal (EC:4.1.1.39)
Short name:
RuBisCO large subunit
Gene namesi
Name:cbbL1
Synonyms:cbbL, cbxLC, cfxLC
OrganismiCupriavidus necator (Alcaligenes eutrophus) (Ralstonia eutropha)
Taxonomic identifieri106590 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000626411 – 486Ribulose bisphosphate carboxylase large chain, chromosomalAdd BLAST486

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei204N6-carboxylysine1 Publication1

Post-translational modificationi

A disulfide bond might be able to form between Cys-278 in the large chain dimeric partners within the hexadecamer.1 Publication

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Heterohexadecamer of 8 large chains and 8 small chains. A disulfide link might be formed within the large subunit homodimers.1 Publication

Protein-protein interaction databases

STRINGi381666.H16_B1395.

Structurei

Secondary structure

1486
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni25 – 27Combined sources3
Beta strandi38 – 47Combined sources10
Helixi53 – 62Combined sources10
Turni63 – 66Combined sources4
Helixi75 – 78Combined sources4
Helixi81 – 83Combined sources3
Beta strandi86 – 92Combined sources7
Beta strandi100 – 107Combined sources8
Helixi108 – 110Combined sources3
Helixi116 – 124Combined sources9
Helixi127 – 129Combined sources3
Beta strandi133 – 135Combined sources3
Beta strandi137 – 142Combined sources6
Helixi145 – 148Combined sources4
Helixi158 – 165Combined sources8
Beta strandi172 – 176Combined sources5
Helixi185 – 197Combined sources13
Beta strandi201 – 204Combined sources4
Helixi217 – 235Combined sources19
Beta strandi240 – 244Combined sources5
Helixi250 – 262Combined sources13
Beta strandi266 – 271Combined sources6
Helixi272 – 274Combined sources3
Helixi276 – 287Combined sources12
Turni288 – 290Combined sources3
Beta strandi292 – 296Combined sources5
Turni298 – 300Combined sources3
Helixi301 – 304Combined sources4
Beta strandi309 – 311Combined sources3
Helixi313 – 323Combined sources11
Beta strandi326 – 329Combined sources4
Beta strandi335 – 338Combined sources4
Helixi341 – 352Combined sources12
Beta strandi354 – 356Combined sources3
Helixi360 – 362Combined sources3
Beta strandi377 – 383Combined sources7
Helixi386 – 388Combined sources3
Helixi389 – 396Combined sources8
Beta strandi401 – 404Combined sources4
Helixi406 – 409Combined sources4
Helixi414 – 435Combined sources22
Helixi439 – 453Combined sources15
Helixi455 – 463Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BXNX-ray2.70A/C/E/G1-486[»]
ProteinModelPortaliP0C2C2.
SMRiP0C2C2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C2C2.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105DT1. Bacteria.
COG1850. LUCA.

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.

P0C2C2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNAPETIQAK PRKRYDAGVM KYKEMGYWDG DYVPKDTDVL ALFRITPQDG
60 70 80 90 100
VDPVEAAAAV AGESSTATWT VVWTDRLTAC DMYRAKAYRV DPVPNNPEQF
110 120 130 140 150
FCYVAYDLSL FEEGSIANLT ASIIGNVFSF KPIKAARLED MRFPVAYVKT
160 170 180 190 200
FAGPSTGIIV ERERLDKFGR PLLGATTKPK LGLSGRNYGR VVYEGLKGGL
210 220 230 240 250
DFMKDDENIN SQPFMHWRDR FLFVMDAVNK ASAATGEVKG SYLNVTAGTM
260 270 280 290 300
EEMYRRAEFA KSLGSVIIMV DLIVGWTCIQ SMSNWCRQND MILHLHRAGH
310 320 330 340 350
GTYTRQKNHG VSFRVIAKWL RLAGVDHMHT GTAVGKLEGD PLTVQGYYNV
360 370 380 390 400
CRDAYTQTDL TRGLFFDQDW ASLRKVMPVA SGGIHAGQMH QLIHLFGDDV
410 420 430 440 450
VLQFGGGTIG HPQGIQAGAT ANRVALEAMV LARNEGRDIL NEGPEILRDA
460 470 480
ARWCAPLRAA LDTWGDITFN YTPTDTSDFV PTASVA
Length:486
Mass (Da):53,840
Last modified:January 23, 2007 - v1
Checksum:i66EAB4A11982FAB5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17744 Genomic DNA. Translation: AAC28129.1.
PIRiA26954. RKALLE.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17744 Genomic DNA. Translation: AAC28129.1.
PIRiA26954. RKALLE.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BXNX-ray2.70A/C/E/G1-486[»]
ProteinModelPortaliP0C2C2.
SMRiP0C2C2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi381666.H16_B1395.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105DT1. Bacteria.
COG1850. LUCA.

Miscellaneous databases

EvolutionaryTraceiP0C2C2.

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 nameiRBL1C_CUPNE
AccessioniPrimary (citable) accession number: P0C2C2
Secondary accession number(s): P09657, P77811
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 51 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".

Keywords - Technical termi

3D-structure

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.