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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei126 – 1261Substrate; in homodimeric partner
Binding sitei176 – 1761Substrate
Active sitei178 – 1781Proton acceptor
Binding sitei180 – 1801Substrate
Metal bindingi204 – 2041Magnesium; via carbamate group
Metal bindingi206 – 2061Magnesium
Metal bindingi207 – 2071Magnesium
Active sitei296 – 2961Proton acceptor
Binding sitei297 – 2971Substrate
Binding sitei329 – 3291Substrate
Sitei336 – 3361Transition state stabilizer
Binding sitei381 – 3811Substrate

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. reductive pentose-phosphate cycle Source: UniProtKB-KW
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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 486486Ribulose bisphosphate carboxylase large chain, chromosomalPRO_0000062641Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei204 – 2041N6-carboxylysine1 Publication

Post-translational modificationi

The disulfide bond which can form between Cys-278 in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover.By similarity

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers.

Structurei

Secondary structure

1
486
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni25 – 273Combined sources
Beta strandi38 – 4710Combined sources
Helixi53 – 6210Combined sources
Turni63 – 664Combined sources
Helixi75 – 784Combined sources
Helixi81 – 833Combined sources
Beta strandi86 – 927Combined sources
Beta strandi100 – 1078Combined sources
Helixi108 – 1103Combined sources
Helixi116 – 1249Combined sources
Helixi127 – 1293Combined sources
Beta strandi133 – 1353Combined sources
Beta strandi137 – 1426Combined sources
Helixi145 – 1484Combined sources
Helixi158 – 1658Combined sources
Beta strandi172 – 1765Combined sources
Helixi185 – 19713Combined sources
Beta strandi201 – 2044Combined sources
Helixi217 – 23519Combined sources
Beta strandi240 – 2445Combined sources
Helixi250 – 26213Combined sources
Beta strandi266 – 2716Combined sources
Helixi272 – 2743Combined sources
Helixi276 – 28712Combined sources
Turni288 – 2903Combined sources
Beta strandi292 – 2965Combined sources
Turni298 – 3003Combined sources
Helixi301 – 3044Combined sources
Beta strandi309 – 3113Combined sources
Helixi313 – 32311Combined sources
Beta strandi326 – 3294Combined sources
Beta strandi335 – 3384Combined sources
Helixi341 – 35212Combined sources
Beta strandi354 – 3563Combined sources
Helixi360 – 3623Combined sources
Beta strandi377 – 3837Combined sources
Helixi386 – 3883Combined sources
Helixi389 – 3968Combined sources
Beta strandi401 – 4044Combined sources
Helixi406 – 4094Combined sources
Helixi414 – 43522Combined sources
Helixi439 – 45315Combined sources
Helixi455 – 4639Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BXNX-ray2.70A/C/E/G1-486[»]
ProteinModelPortaliP0C2C2.
SMRiP0C2C2. Positions 24-467.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C2C2.

Family & Domainsi

Sequence similaritiesi

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.

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1BXNX-ray2.70A/C/E/G1-486[»]
ProteinModelPortaliP0C2C2.
SMRiP0C2C2. Positions 24-467.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP0C2C2.

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]
ProtoNetiSearch...

Publicationsi

  1. "Sequence analysis of the Alcaligenes eutrophus chromosomally encoded ribulose bisphosphate carboxylase large and small subunit genes and their gene products."
    Andersen K., Caton J.
    J. Bacteriol. 169:4547-4558(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CARBAMYLATION AT LYS-204.
    Strain: ATCC 17707 / LMG 1207 / Stanier 345 / H-20-R.
  2. Andersen K.
    Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "The crystal structure of rubisco from Alcaligenes eutrophus reveals a novel central eight-stranded beta-barrel formed by beta-strands from four subunits."
    Hansen S., Vollan V.B., Hough E., Andersen K.
    J. Mol. Biol. 288:609-621(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
    Strain: ATCC 17707 / LMG 1207 / Stanier 345 / H-20-R.

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 26, 2014
This is version 42 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

External Data

Dasty 3

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 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.