Skip Header

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

Ribulose bisphosphate carboxylase large chain 2

Gene

cbbL2

Organism
Nitrobacter winogradskyi (strain Nb-255 / ATCC 25391)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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.UniRule annotation

Catalytic activityi

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

Cofactori

Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei128 – 1281Substrate; in homodimeric partnerUniRule annotation
Binding sitei178 – 1781SubstrateUniRule annotation
Active sitei180 – 1801Proton acceptorUniRule annotation
Binding sitei182 – 1821SubstrateUniRule annotation
Metal bindingi206 – 2061Magnesium; via carbamate groupUniRule annotation
Metal bindingi208 – 2081MagnesiumUniRule annotation
Metal bindingi209 – 2091MagnesiumUniRule annotation
Active sitei298 – 2981Proton acceptorUniRule annotation
Binding sitei299 – 2991SubstrateUniRule annotation
Binding sitei331 – 3311SubstrateUniRule annotation
Sitei338 – 3381Transition state stabilizerUniRule annotation
Binding sitei383 – 3831SubstrateUniRule annotation

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

BioCyciNWIN323098:GJEG-2980-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase large chain 2UniRule annotation (EC:4.1.1.39UniRule annotation)
Short name:
RuBisCO large subunit 2UniRule annotation
Gene namesi
Name:cbbL2UniRule annotation
Ordered Locus Names:Nwi_2929
OrganismiNitrobacter winogradskyi (strain Nb-255 / ATCC 25391)
Taxonomic identifieri323098 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeNitrobacter
ProteomesiUP000002531: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 489489Ribulose bisphosphate carboxylase large chain 2PRO_0000251452Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei206 – 2061N6-carboxylysineUniRule annotation

Interactioni

Subunit structurei

Heterohexadecamer of 8 large chains and 8 small chains.UniRule annotation

Protein-protein interaction databases

STRINGi323098.Nwi_2929.

Structurei

3D structure databases

ProteinModelPortaliQ3SNG2.
SMRiQ3SNG2. Positions 26-469.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiITAGWMA.
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.

Q3SNG2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNVQNEKSMT VRGKDRYKSG VMSYKKMGYW EPDYTPKDTD VICLFRVTPQ
60 70 80 90 100
DGVDPIEASA AVAGESSTAT WTVVWTDRLT AAEKYRAKCY RVDPVPGAEG
110 120 130 140 150
QYFAYIAYDL DLFEPGSISN LTASVIGNVF GFKPLKALRL EDMRLPVAYV
160 170 180 190 200
KTFKGPPTGI VVERERLDKF GRPLLGATVK PKLGLSGRNY GRVVYEALKG
210 220 230 240 250
GLDFTKDDEN INSQPFMHWR ERFLYCMEAV NRAQAATGEI KGSYLNVTAA
260 270 280 290 300
TMEDMYERAE FAKELGSVVV MIDLVIGYTA IQSMSNWARK NDMILHLHRA
310 320 330 340 350
GHSTYTRQRS HGVSFRVISK WMRLAGVDHI HAGTVVGKLE GDPLTTRGFY
360 370 380 390 400
DICREEYNPT QLEHGIFFDQ NWASLNKVMP VASGGIHAGQ MHQLIQHLGE
410 420 430 440 450
DVVLQFGGGT IGHPMGIQAG ATANRVALEA MILARNEGRD YVSEGPEILA
460 470 480
KAAASCTPLK QALEVWKDVT FDYASTDAPD YVPTAVPAA
Length:489
Mass (Da):54,148
Last modified:October 11, 2005 - v1
Checksum:iE7A0458BCD485A9E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000115 Genomic DNA. Translation: ABA06179.1.
RefSeqiYP_319531.1. NC_007406.1.

Genome annotation databases

EnsemblBacteriaiABA06179; ABA06179; Nwi_2929.
GeneIDi3674284.
KEGGinwi:Nwi_2929.
PATRICi22702997. VBINitWin102302_3305.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000115 Genomic DNA. Translation: ABA06179.1.
RefSeqiYP_319531.1. NC_007406.1.

3D structure databases

ProteinModelPortaliQ3SNG2.
SMRiQ3SNG2. Positions 26-469.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi323098.Nwi_2929.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABA06179; ABA06179; Nwi_2929.
GeneIDi3674284.
KEGGinwi:Nwi_2929.
PATRICi22702997. VBINitWin102302_3305.

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiITAGWMA.
OrthoDBiEOG6ZKXMS.

Enzyme and pathway databases

BioCyciNWIN323098:GJEG-2980-MONOMER.

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. "Genome sequence of the chemolithoautotrophic nitrite-oxidizing bacterium Nitrobacter winogradskyi Nb-255."
    Starkenburg S.R., Chain P.S.G., Sayavedra-Soto L.A., Hauser L., Land M.L., Larimer F.W., Malfatti S.A., Klotz M.G., Bottomley P.J., Arp D.J., Hickey W.J.
    Appl. Environ. Microbiol. 72:2050-2063(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Nb-255 / ATCC 25391.

Entry informationi

Entry nameiRBL1B_NITWN
AccessioniPrimary (citable) accession number: Q3SNG2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: October 11, 2005
Last modified: January 7, 2015
This is version 59 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".UniRule annotation

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.