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Q07N61

- RBL2_RHOP5

UniProt

Q07N61 - RBL2_RHOP5

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Protein

Ribulose bisphosphate carboxylase

Gene

cbbM

Organism
Rhodopseudomonas palustris (strain BisA53)
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 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

Enzyme and pathway databases

BioCyciRPAL316055:GHR9-2711-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:RPE_2686
OrganismiRhodopseudomonas palustris (strain BisA53)
Taxonomic identifieri316055 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeRhodopseudomonas
ProteomesiUP000000654: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 460460Ribulose bisphosphate carboxylasePRO_1000067650Add
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

STRINGi316055.RPE_2686.

Structurei

3D structure databases

ProteinModelPortaliQ07N61.
SMRiQ07N61. Positions 2-458.
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.

Q07N61-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDQSSRYANL NLKEKDLIAG GRHVLCAYIV KPKAGFGDFL QTAAHFAAES
60 70 80 90 100
STGTNVEVST TDDFTRGVDA LVYEIDESKE LMKIAYPVEL FDRNVIDGRA
110 120 130 140 150
MIASFLTLTI GNNQGMGDVE YAKMYDFYVP PAYLKLFDGP STTIKDLWRV
160 170 180 190 200
LGRPVVDGGF IVGTIIKPKL GLRPQPFANA CFDFWLGGDF IKNDEPQGNQ
210 220 230 240 250
VFAPFKETVR AVNEAMRRAQ DATGQAKLFS FNITADDHYE MLARGEYILE
260 270 280 290 300
TFGENADHIA FLVDGYVAGP AAVTTARRAF PKQYLHYHRA GHGAVTSPQS
310 320 330 340 350
KRGYTAFVLS KMARLQGASG IHTGTMGFGK MEGEAADRAM AFMITEDSAD
360 370 380 390 400
GPYFHQEWLG MNPTTPIISG GMNALRMPGF FTNLGHSNLI MTAGGGAFGH
410 420 430 440 450
LDGGAAGAKS LRQAEQCWKL GADPVQFAKE HHEFARAFES FSHDADKLFP
460
GWRGQLGLAA
Length:460
Mass (Da):50,252
Last modified:October 31, 2006 - v1
Checksum:i4AED8610E910F883
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000463 Genomic DNA. Translation: ABJ06623.1.
RefSeqiWP_011664101.1. NC_008435.1.
YP_781603.1. NC_008435.1.

Genome annotation databases

EnsemblBacteriaiABJ06623; ABJ06623; RPE_2686.
GeneIDi4360364.
KEGGirpe:RPE_2686.
PATRICi23259930. VBIRhoPal93214_2710.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000463 Genomic DNA. Translation: ABJ06623.1 .
RefSeqi WP_011664101.1. NC_008435.1.
YP_781603.1. NC_008435.1.

3D structure databases

ProteinModelPortali Q07N61.
SMRi Q07N61. Positions 2-458.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 316055.RPE_2686.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABJ06623 ; ABJ06623 ; RPE_2686 .
GeneIDi 4360364.
KEGGi rpe:RPE_2686.
PATRICi 23259930. VBIRhoPal93214_2710.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci RPAL316055:GHR9-2711-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: BisA53.

Entry informationi

Entry nameiRBL2_RHOP5
AccessioniPrimary (citable) accession number: Q07N61
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 31, 2006
Last modified: November 26, 2014
This is version 55 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3