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A1VNQ9

- RBL2_POLNA

UniProt

A1VNQ9 - RBL2_POLNA

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Protein

Ribulose bisphosphate carboxylase

Gene

cbbM

Organism
Polaromonas naphthalenivorans (strain CJ2)
Status
Reviewed - 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 Mg(2+) ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei111 – 1111Substrate; in homodimeric partnerUniRule annotation
Active sitei166 – 1661Proton acceptorUniRule annotation
Binding sitei168 – 1681SubstrateUniRule annotation
Metal bindingi191 – 1911Magnesium; via carbamate groupUniRule annotation
Metal bindingi193 – 1931MagnesiumUniRule annotation
Metal bindingi194 – 1941MagnesiumUniRule annotation
Active sitei287 – 2871Proton acceptorUniRule annotation
Binding sitei288 – 2881SubstrateUniRule annotation
Binding sitei321 – 3211SubstrateUniRule annotation
Sitei329 – 3291Transition state stabilizerUniRule annotation
Binding sitei368 – 3681SubstrateUniRule 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

BioCyciPNAP365044:GJ8X-2009-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylaseUniRule annotation (EC:4.1.1.39UniRule annotation)
Short name:
RuBisCOUniRule annotation
Gene namesi
Name:cbbMUniRule annotation
Ordered Locus Names:Pnap_1978
OrganismiPolaromonas naphthalenivorans (strain CJ2)
Taxonomic identifieri365044 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaePolaromonas
ProteomesiUP000000644: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 459459Ribulose bisphosphate carboxylasePRO_1000067649Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei191 – 1911N6-carboxylysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi365044.Pnap_1978.

Structurei

3D structure databases

ProteinModelPortaliA1VNQ9.
SMRiA1VNQ9. Positions 2-456.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiAKEHREF.
OrthoDBiEOG66QKT8.

Family and domain databases

Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01339. RuBisCO_L_type2.
InterProiIPR020871. RuBisCO.
IPR020878. RuBisCo_large_chain_AS.
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.

A1VNQ9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDQSNRYADL SLKEEDLIAG GRHILVAYKM KPKAGHGYLE AAAHFAAESS
60 70 80 90 100
TGTNVEVSTT DEFTKGVDAL VYLIDEATEE MRIAFPMDLF DRNILDGRMM
110 120 130 140 150
IVSFLTLVIG NNQGMGDIQH AKIYDFFMPP RAIQLFDGPS KDISDMWRIL
160 170 180 190 200
GRPVKDGGYI AGTIIKPKLG LRPEPFAQAA YQFWLGGDFI KNDEPQGNQT
210 220 230 240 250
FAPMNKVMPL VHDAMKRAMD ETGEAKLFSA NITADDHYEM LARGDYILRT
260 270 280 290 300
FGPDADKVAF LVDGYVGGPG MITTARRAFP NQYLHYHRAG HGAVTSPSAK
310 320 330 340 350
RGYDAYVLAK MSRLQGASGI HVGTMGYGKM EGTHDDRAIA YIIERDSYTG
360 370 380 390 400
PAYHQEWYGM KPTTPIISGG MNALRLPGFF ENLGHGNVIN TSGGGAYGHI
410 420 430 440 450
DSPAAGATSL RQAYECWKAK ADPIEWAKEH PEFARAFASF PGDADMLFPG

WRDKLASHR
Length:459
Mass (Da):50,571
Last modified:February 6, 2007 - v1
Checksum:i6FEEDE1CB0783D9D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000529 Genomic DNA. Translation: ABM37287.1.
RefSeqiYP_982208.1. NC_008781.1.

Genome annotation databases

EnsemblBacteriaiABM37287; ABM37287; Pnap_1978.
GeneIDi4688038.
KEGGipna:Pnap_1978.
PATRICi22948612. VBIPolNap76733_2845.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000529 Genomic DNA. Translation: ABM37287.1 .
RefSeqi YP_982208.1. NC_008781.1.

3D structure databases

ProteinModelPortali A1VNQ9.
SMRi A1VNQ9. Positions 2-456.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 365044.Pnap_1978.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABM37287 ; ABM37287 ; Pnap_1978 .
GeneIDi 4688038.
KEGGi pna:Pnap_1978.
PATRICi 22948612. VBIPolNap76733_2845.

Phylogenomic databases

eggNOGi COG1850.
HOGENOMi HOG000230831.
KOi K01601.
OMAi AKEHREF.
OrthoDBi EOG66QKT8.

Enzyme and pathway databases

BioCyci PNAP365044:GJ8X-2009-MONOMER.

Family and domain databases

Gene3Di 3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPi MF_01339. RuBisCO_L_type2.
InterProi IPR020871. RuBisCO.
IPR020878. RuBisCo_large_chain_AS.
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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CJ2.

Entry informationi

Entry nameiRBL2_POLNA
AccessioniPrimary (citable) accession number: A1VNQ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 6, 2007
Last modified: November 26, 2014
This is version 51 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 contrast to form I RuBisCO, the form II RuBisCO are composed solely of large subunits.UniRule annotation

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3