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P0C2C2

- RBL1C_CUPNE

UniProt

P0C2C2 - RBL1C_CUPNE

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Protein

Ribulose bisphosphate carboxylase large chain, chromosomal

Gene

cbbL1

Organism
Cupriavidus necator (Alcaligenes eutrophus) (Ralstonia eutropha)
Status
Reviewed - 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

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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:
EMBL
GenBank
DDBJ
Links Updated
M17744 Genomic DNA. Translation: AAC28129.1.
PIRiA26954. RKALLE.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M17744 Genomic DNA. Translation: AAC28129.1 .
PIRi A26954. RKALLE.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BXN X-ray 2.70 A/C/E/G 1-486 [» ]
ProteinModelPortali P0C2C2.
SMRi P0C2C2. Positions 24-467.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P0C2C2.

Family and domain databases

Gene3Di 3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPi MF_01338. RuBisCO_L_type1.
InterProi IPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view ]
Pfami PF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view ]
SUPFAMi SSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEi PS00157. RUBISCO_LARGE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(1987) [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 (AUG-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(1999) [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: October 1, 2014
This is version 41 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