Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q0K1E0

- RBL1C_CUPNH

UniProt

Q0K1E0 - RBL1C_CUPNH

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Ribulose bisphosphate carboxylase large chain, chromosomal

Gene

cbbL1

Organism
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript 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 By similarity.By similarity

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.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei126 – 1261Substrate; in homodimeric partnerBy similarity
Binding sitei176 – 1761SubstrateBy similarity
Active sitei178 – 1781Proton acceptorBy similarity
Binding sitei180 – 1801SubstrateBy similarity
Metal bindingi204 – 2041Magnesium; via carbamate groupBy similarity
Metal bindingi206 – 2061MagnesiumBy similarity
Metal bindingi207 – 2071MagnesiumBy similarity
Active sitei296 – 2961Proton acceptorBy similarity
Binding sitei297 – 2971SubstrateBy similarity
Binding sitei329 – 3291SubstrateBy similarity
Sitei336 – 3361Transition state stabilizerBy similarity
Binding sitei381 – 3811SubstrateBy similarity

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

Enzyme and pathway databases

BioCyciCNEC381666:GJUJ-5100-MONOMER.

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
Ordered Locus Names:H16_B1395
OrganismiCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
Taxonomic identifieri381666 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
ProteomesiUP000008210: Chromosome 2

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 486486Ribulose bisphosphate carboxylase large chain, chromosomalPRO_0000273254Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei204 – 2041N6-carboxylysineBy similarity

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

Expressioni

Inductioni

Total RuBisCO activity (both chromosome and plasmid-derived enzyme) is high under lithoautotrophic growth conditions, intermediate when grown on fructose and poor when grown on pyruvate.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi381666.H16_B1395.

Structurei

3D structure databases

ProteinModelPortaliQ0K1E0.
SMRiQ0K1E0. Positions 24-467.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiCTPLKQA.
OrthoDBiEOG6ZKXMS.

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.

Q0K1E0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNAPESVQAK PRKRYDAGVM KYKEMGYWDG DYEPKDTDLL 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 KSLGSVIIMI DLIVGWTCIQ SMSNWCRQND MILHLHRAGH
310 320 330 340 350
GTYTRQKNHG VSFRVIAKWL RLAGVDHMHT GTAVGKLEGD PLTVQGYYNV
360 370 380 390 400
CRDAYTHADL SRGLFFDQDW ASLRKVMPVA SGGIHAGQMH QLISLFGDDV
410 420 430 440 450
VLQFGGGTIG HPQGIQAGAT ANRVALEAMV LARNEGRDIL NEGPEILRDA
460 470 480
ARWCGPLRAA LDTWGDISFN YTPTDTSDFA PTASVA
Length:486
Mass (Da):53,729
Last modified:October 3, 2006 - v1
Checksum:i47C20867581EDDB4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti83 – 886YRAKAY → SVQGL in AAA83745. (PubMed:7543477)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U20584 Genomic DNA. Translation: AAA83745.1.
AM260480 Genomic DNA. Translation: CAJ96184.1.
M65065 Genomic DNA. Translation: AAA21981.1.
PIRiI39557.
RefSeqiYP_840914.1. NC_008314.1.

Genome annotation databases

EnsemblBacteriaiCAJ96184; CAJ96184; H16_B1395.
GeneIDi4456354.
KEGGireh:H16_B1395.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U20584 Genomic DNA. Translation: AAA83745.1 .
AM260480 Genomic DNA. Translation: CAJ96184.1 .
M65065 Genomic DNA. Translation: AAA21981.1 .
PIRi I39557.
RefSeqi YP_840914.1. NC_008314.1.

3D structure databases

ProteinModelPortali Q0K1E0.
SMRi Q0K1E0. Positions 24-467.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 381666.H16_B1395.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAJ96184 ; CAJ96184 ; H16_B1395 .
GeneIDi 4456354.
KEGGi reh:H16_B1395.

Phylogenomic databases

eggNOGi COG1850.
HOGENOMi HOG000230831.
KOi K01601.
OMAi CTPLKQA.
OrthoDBi EOG6ZKXMS.

Enzyme and pathway databases

BioCyci CNEC381666:GJUJ-5100-MONOMER.

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

« Hide 'large scale' publications
  1. "Characterization of the duplicate ribulose-1,5-bisphosphate carboxylase genes and cbb promoters of Alcaligenes eutrophus."
    Kusian B., Bednarski R., Husemann M., Bowien B.
    J. Bacteriol. 177:4442-4450(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], EXPRESSION UNDER DIFFERENT GROWTH CONDITIONS.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.
  3. "Identification of cfxR, an activator gene of autotrophic CO2 fixation in Alcaligenes eutrophus."
    Windhoevel U., Bowien B.
    Mol. Microbiol. 5:2695-2705(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.

Entry informationi

Entry nameiRBL1C_CUPNH
AccessioniPrimary (citable) accession number: Q0K1E0
Secondary accession number(s): P09657, P77811
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: October 3, 2006
Last modified: October 1, 2014
This is version 53 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" By similarity.By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3