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Protein

Ribulose bisphosphate carboxylase large chain 2

Gene

cbbL2

Organism
Nitrobacter hamburgensis (strain X14 / DSM 10229)
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

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

Enzyme and pathway databases

BioCyciNHAM323097:GHP7-4115-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:Nham_4049
Encoded oniPlasmid 10 Publication
OrganismiNitrobacter hamburgensis (strain X14 / DSM 10229)
Taxonomic identifieri323097 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeNitrobacter
ProteomesiUP000001953 Componenti: Plasmid pNITHX1

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 488488Ribulose bisphosphate carboxylase large chain 2PRO_0000251447Add
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

STRINGi323097.Nham_3751.

Structurei

3D structure databases

ProteinModelPortaliQ1QGD4.
SMRiQ1QGD4. 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.
OMAiQACDAYL.
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.

Q1QGD4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNVLNEKSLT VRGKDRYKSG VMSYKKMGYW EPDYTPKDTD IICLFRVTPQ
60 70 80 90 100
DGVDPIEAAA 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
GHSTYTRQRN HGVSFRVISK WMRLAGVDHI HAGTVVGKLE GDPLTTRGYY
360 370 380 390 400
DICREEHNPM QLEHGIFFDQ NWASLNKMMP VASGGIHAGQ MHQLIQHLGE
410 420 430 440 450
DVVLQFGGGT IGHPMGIQAG ATANRVALEA MILARNEGRD YVSEGPDILA
460 470 480
KAAASCTPLK QALEVWKDVT FNYQSTDAPD YVTTPAVA
Length:488
Mass (Da):54,167
Last modified:May 16, 2006 - v1
Checksum:iD9BE53686D953C91
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000320 Genomic DNA. Translation: ABE64713.1.
RefSeqiWP_011505022.1. NC_007959.1.

Genome annotation databases

EnsemblBacteriaiABE64713; ABE64713; Nham_4049.
KEGGinha:Nham_4049.
PATRICi22685933. VBINitHam61822_0013.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000320 Genomic DNA. Translation: ABE64713.1.
RefSeqiWP_011505022.1. NC_007959.1.

3D structure databases

ProteinModelPortaliQ1QGD4.
SMRiQ1QGD4. Positions 26-469.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi323097.Nham_3751.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABE64713; ABE64713; Nham_4049.
KEGGinha:Nham_4049.
PATRICi22685933. VBINitHam61822_0013.

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiQACDAYL.
OrthoDBiEOG6ZKXMS.

Enzyme and pathway databases

BioCyciNHAM323097:GHP7-4115-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: X14 / DSM 10229.

Entry informationi

Entry nameiRBL1B_NITHX
AccessioniPrimary (citable) accession number: Q1QGD4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: May 16, 2006
Last modified: July 22, 2015
This is version 60 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, Plasmid, 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.