Skip Header

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

Q6N0W9

- RBL2_RHOPA

UniProt

Q6N0W9 - RBL2_RHOPA

(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

Gene

cbbM

Organism
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Status
Reviewed - Annotation score: 3 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.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 sitei112 – 1121Substrate; in homodimeric partnerUniRule annotation
Active sitei167 – 1671Proton acceptorUniRule annotation
Binding sitei169 – 1691SubstrateUniRule annotation
Metal bindingi192 – 1921Magnesium; via carbamate groupUniRule annotation
Metal bindingi194 – 1941MagnesiumUniRule annotation
Metal bindingi195 – 1951MagnesiumUniRule annotation
Active sitei288 – 2881Proton acceptorUniRule annotation
Binding sitei289 – 2891SubstrateUniRule annotation
Binding sitei322 – 3221SubstrateUniRule annotation
Sitei330 – 3301Transition state stabilizerUniRule annotation
Binding sitei369 – 3691SubstrateUniRule 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, Photosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

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:RPA4641
OrganismiRhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Taxonomic identifieri258594 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeRhodopseudomonas
ProteomesiUP000001426: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 461461Ribulose bisphosphate carboxylasePRO_0000062665Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei192 – 1921N6-carboxylysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi258594.RPA4641.

Structurei

Secondary structure

1
461
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 74Combined sources
Helixi14 – 207Combined sources
Beta strandi23 – 3210Combined sources
Helixi39 – 4911Combined sources
Turni50 – 523Combined sources
Helixi63 – 675Combined sources
Beta strandi71 – 766Combined sources
Turni77 – 804Combined sources
Beta strandi81 – 877Combined sources
Helixi88 – 903Combined sources
Turni95 – 973Combined sources
Helixi102 – 1098Combined sources
Helixi112 – 1154Combined sources
Beta strandi119 – 12810Combined sources
Helixi131 – 1344Combined sources
Helixi144 – 1518Combined sources
Beta strandi155 – 1573Combined sources
Beta strandi161 – 1655Combined sources
Beta strandi167 – 1704Combined sources
Helixi174 – 18512Combined sources
Beta strandi189 – 1924Combined sources
Beta strandi198 – 2003Combined sources
Helixi205 – 22319Combined sources
Beta strandi228 – 2325Combined sources
Helixi238 – 25215Combined sources
Helixi253 – 2586Combined sources
Beta strandi259 – 2646Combined sources
Helixi265 – 2684Combined sources
Helixi270 – 27910Combined sources
Beta strandi283 – 2886Combined sources
Turni290 – 2923Combined sources
Helixi293 – 2964Combined sources
Beta strandi302 – 3043Combined sources
Helixi306 – 31611Combined sources
Beta strandi319 – 3224Combined sources
Beta strandi328 – 3325Combined sources
Helixi335 – 3373Combined sources
Helixi338 – 3458Combined sources
Beta strandi346 – 3505Combined sources
Beta strandi355 – 3573Combined sources
Beta strandi365 – 3717Combined sources
Helixi374 – 3763Combined sources
Helixi377 – 3848Combined sources
Beta strandi389 – 3924Combined sources
Helixi394 – 3985Combined sources
Helixi404 – 42017Combined sources
Helixi424 – 4274Combined sources
Helixi428 – 4303Combined sources
Helixi432 – 4409Combined sources
Helixi442 – 4487Combined sources
Helixi452 – 4554Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4LF1X-ray2.38A/B/C/D/E/F1-461[»]
4LF2X-ray2.38A/B/C/D/E/F1-461[»]
ProteinModelPortaliQ6N0W9.
SMRiQ6N0W9. 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.
PhylomeDBiQ6N0W9.

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.

Q6N0W9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDQSNRYANL NLKESELIAG GRHVLCAYIM KPKAGFGNFI QTAAHFAAES
60 70 80 90 100
STGTNVEVST TDDFTRGVDA LVYEVDEANS LMKIAYPIEL FDRNVIDGRA
110 120 130 140 150
MIASFLTLTI GNNQGMGDVE YAKMYDFYVP PAYLKLFDGP STTIKDLWRV
160 170 180 190 200
LGRPVINGGF IVGTIIKPKL GLRPQPFANA CYDFWLGGDF IKNDEPQGNQ
210 220 230 240 250
VFAPFKDTVR AVADAMRRAQ DKTGEAKLFS FNITADDHYE MLARGEFILE
260 270 280 290 300
TFADNADHIA FLVDGYVAGP AAVTTARRAF PKQYLHYHRA GHGAVTSPQS
310 320 330 340 350
KRGYTAFVLS KMARLQGASG IHTGTMGFGK MEGEAADRAI AYMITEDAAD
360 370 380 390 400
GPYFHQEWLG MNPTTPIISG GMNALRMPGF FDNLGHSNLI MTAGGGAFGH
410 420 430 440 450
VDGGAAGAKS LRQAEQCWKQ GADPVEFAKD HREFARAFES FPQDADKLYP
460
NWRAKLKPQA A
Length:461
Mass (Da):50,485
Last modified:July 5, 2004 - v1
Checksum:i907EFB041943AABC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti75 – 751V → I in AAN52766. (PubMed:12900023)Curated
Sequence conflicti79 – 802NS → KG in AAN52766. (PubMed:12900023)Curated
Sequence conflicti145 – 1451K → R in AAN52766. (PubMed:12900023)Curated
Sequence conflicti156 – 1561I → V in AAN52766. (PubMed:12900023)Curated
Sequence conflicti348 – 3481A → S in AAN52766. (PubMed:12900023)Curated
Sequence conflicti361 – 3611M → L in AAN52766. (PubMed:12900023)Curated
Sequence conflicti442 – 4432PQ → AH in AAK39106. (PubMed:15259271)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY155466 Genomic DNA. Translation: AAN52766.1.
AF355197 Genomic DNA. Translation: AAK39106.1.
BX572607 Genomic DNA. Translation: CAE30081.1.
RefSeqiNP_949975.1. NC_005296.1.
WP_011160173.1. NC_005296.1.

Genome annotation databases

EnsemblBacteriaiCAE30081; CAE30081; RPA4641.
GeneIDi2692140.
KEGGirpa:RPA4641.
PATRICi23293933. VBIRhoPal84835_4873.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY155466 Genomic DNA. Translation: AAN52766.1 .
AF355197 Genomic DNA. Translation: AAK39106.1 .
BX572607 Genomic DNA. Translation: CAE30081.1 .
RefSeqi NP_949975.1. NC_005296.1.
WP_011160173.1. NC_005296.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4LF1 X-ray 2.38 A/B/C/D/E/F 1-461 [» ]
4LF2 X-ray 2.38 A/B/C/D/E/F 1-461 [» ]
ProteinModelPortali Q6N0W9.
SMRi Q6N0W9. Positions 2-456.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 258594.RPA4641.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAE30081 ; CAE30081 ; RPA4641 .
GeneIDi 2692140.
KEGGi rpa:RPA4641.
PATRICi 23293933. VBIRhoPal84835_4873.

Phylogenomic databases

eggNOGi COG1850.
HOGENOMi HOG000230831.
KOi K01601.
OMAi AKEHREF.
OrthoDBi EOG66QKT8.
PhylomeDBi Q6N0W9.

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

« Hide 'large scale' publications
  1. "Construction of a genetically engineered microorganism for CO2 fixation using a Rhodopseudomonas/Escherichia coli shuttle vector."
    Du C., Zhou J., Wang J., Yan B., Lu H., Hou H.
    FEMS Microbiol. Lett. 225:69-73(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: DH.
  2. "Analysis of diversity among 3-chlorobenzoate-degrading strains of Rhodopseudomonas palustris."
    Oda Y., Meijer W.G., Gibson J.L., Gottschal J.C., Forney L.J.
    Microb. Ecol. 47:68-79(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: DCP3.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-98 / CGA009.

Entry informationi

Entry nameiRBL2_RHOPA
AccessioniPrimary (citable) accession number: Q6N0W9
Secondary accession number(s): Q8GJP8, Q93TJ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: July 5, 2004
Last modified: November 26, 2014
This is version 71 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

3D-structure, Complete proteome, Reference proteome

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