SubmitCancel

Skip Header

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

Q2RRP5

- RBL2_RHORT

UniProt

Q2RRP5 - RBL2_RHORT

(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, Rru_A2400
Organism
Rhodospirillum rubrum (strain ATCC 11170 / NCIB 8255)
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 By similarity.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

Binds 1 magnesium ion per subunit By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei111 – 1111Substrate; in homodimeric partner By similarity
Active sitei166 – 1661Proton acceptor By similarity
Binding sitei168 – 1681Substrate By similarity
Metal bindingi191 – 1911Magnesium; via carbamate group By similarity
Metal bindingi193 – 1931Magnesium By similarity
Metal bindingi194 – 1941Magnesium By similarity
Active sitei287 – 2871Proton acceptor By similarity
Binding sitei288 – 2881Substrate By similarity
Binding sitei321 – 3211Substrate By similarity
Sitei329 – 3291Transition state stabilizer By similarity
Binding sitei368 – 3681Substrate By similarity

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

BioCyciRRUB269796:GCN1-2442-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase (EC:4.1.1.39)
Short name:
RuBisCO
Gene namesi
Name:cbbM
Ordered Locus Names:Rru_A2400
OrganismiRhodospirillum rubrum (strain ATCC 11170 / NCIB 8255)
Taxonomic identifieri269796 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeRhodospirillum
ProteomesiUP000001929: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 466466Ribulose bisphosphate carboxylaseUniRule annotation
PRO_0000251412Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei191 – 1911N6-carboxylysine By similarity

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi269796.Rru_A2400.

Structurei

3D structure databases

ProteinModelPortaliQ2RRP5.
SMRiQ2RRP5. Positions 2-460.

Family & Domainsi

Sequence similaritiesi

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.

Q2RRP5-1 [UniParc]FASTAAdd to Basket

« Hide

MDQSSRYVNL ALKEEDLIAG GEHVLCAYIM KPKAGYGYVA TAAHFAAESS    50
TGTNVEVCTT DDFTRGVDAL VYEVDEAREL TKIAYPVALF DRNITDGKAM 100
IASFLTLTMG NNQGMGDVEY AKMHDFYVPE AYRALFDGPS VNISALWKVL 150
GRPEVDGGLV VGTIIKPKLG LRPKPFAEAC HAFWLGGDFI KNDEPQGNQP 200
FAPLRDTIAL VADAMRRAQD ETGEAKLFSA NITADDPFEI IARGEYVLET 250
FGENASHVAL LVDGYVAGAA AITTARRRFP DNFLHYHRAG HGAVTSPQSK 300
RGYTAFVHCK MARLQGASGI HTGTMGFGKM EGESSDRAIA YMLTQDEAQG 350
PFYRQSWGGM KACTPIISGG MNALRMPGFF ENLGNANVIL TAGGGAFGHI 400
DGPVAGARSL RQAWQAWRDG VPVLDYAREH KELARAFESF PGDADQIYPG 450
WRKALGVEDT RSALPA 466
Length:466
Mass (Da):50,482
Last modified:January 24, 2006 - v1
Checksum:i4D9F800450AB0155
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000230 Genomic DNA. Translation: ABC23200.1.
RefSeqiYP_427487.1. NC_007643.1.

Genome annotation databases

EnsemblBacteriaiABC23200; ABC23200; Rru_A2400.
GeneIDi3835834.
KEGGirru:Rru_A2400.
PATRICi23328526. VBIRhoRub82919_2502.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000230 Genomic DNA. Translation: ABC23200.1 .
RefSeqi YP_427487.1. NC_007643.1.

3D structure databases

ProteinModelPortali Q2RRP5.
SMRi Q2RRP5. Positions 2-460.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 269796.Rru_A2400.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABC23200 ; ABC23200 ; Rru_A2400 .
GeneIDi 3835834.
KEGGi rru:Rru_A2400.
PATRICi 23328526. VBIRhoRub82919_2502.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci RRUB269796:GCN1-2442-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. "Complete sequence of the chromosome of Rhodospirillum rubrum ATCC 11170."
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.
    , Kyrpides N., Mavrommatis K., Richardson P., Zhang Y., Roberts G., Reslewic S., Zhou S., Schwartz D.C.
    Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S.1.

Entry informationi

Entry nameiRBL2_RHORT
AccessioniPrimary (citable) accession number: Q2RRP5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: January 24, 2006
Last modified: May 14, 2014
This is version 57 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 By similarity.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi