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Q219P7

- RBL_RHOPB

UniProt

Q219P7 - RBL_RHOPB

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Protein
Ribulose bisphosphate carboxylase large chain
Gene
cbbL, RPC_1327
Organism
Rhodopseudomonas palustris (strain BisB18)
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 in the photorespiration process. 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 sitei124 – 1241Substrate; in homodimeric partner By similarity
Binding sitei174 – 1741Substrate By similarity
Active sitei176 – 1761Proton acceptor By similarity
Binding sitei178 – 1781Substrate By similarity
Metal bindingi202 – 2021Magnesium; via carbamate group By similarity
Metal bindingi204 – 2041Magnesium By similarity
Metal bindingi205 – 2051Magnesium By similarity
Active sitei294 – 2941Proton acceptor By similarity
Binding sitei295 – 2951Substrate By similarity
Binding sitei327 – 3271Substrate By similarity
Sitei334 – 3341Transition state stabilizer By similarity
Binding sitei379 – 3791Substrate 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

BioCyciRPAL316056:GH3E-1342-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase large chain (EC:4.1.1.39)
Short name:
RuBisCO large subunit
Gene namesi
Name:cbbL
Ordered Locus Names:RPC_1327
OrganismiRhodopseudomonas palustris (strain BisB18)
Taxonomic identifieri316056 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeRhodopseudomonas
ProteomesiUP000001948: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 485485Ribulose bisphosphate carboxylase large chainUniRule annotation
PRO_0000251457Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei202 – 2021N6-carboxylysine By similarity

Interactioni

Subunit structurei

Heterohexadecamer of 8 large chains and 8 small chains By similarity.

Protein-protein interaction databases

STRINGi316056.RPC_1327.

Structurei

3D structure databases

ProteinModelPortaliQ219P7.
SMRiQ219P7. Positions 22-465.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
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.

Q219P7-1 [UniParc]FASTAAdd to Basket

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MNESVTIRGK DRYKSGVMEY KKMGYWEPDY EPKDTDIIAL FRVTPQDGVD    50
PTEASAAVAG ESSTATWTVV WTDRLTAAEK YRAKCYRVDP VPNSPGQFFA 100
YIAYDLDLFE NGSIANLSAS IIGNVFGFKP LKALRLEDMR LPVAYVKTFQ 150
GPATGIVVER ERMDKFGRPL LGATVKPKLG LSGRNYGRVV YEALKGGLDF 200
TKDDENINSQ PFMHWRERFL YCMEAVNKAQ AASGEIKGTY LNVTAGTMEE 250
MYERAEFAKQ LGSVIIMIDL VIGYTAIQSM AKWARRNDMI LHLHRAGHST 300
YTRQRNHGVS FRVIAKWMRL AGVDHIHAGT VVGKLEGDPA TTKGYYDICR 350
EDYNPMQLEH GIFFEQNWAS LNKLMPVASG GIHAGQMHQL LDHLGEDVVL 400
QFGGGTIGHP MGIQAGATAN RVALEAMIMA RNEGRDYLHE GEEILAKAAL 450
TCTPLKAALE TWKNVTFNYE STDMPDYAPT PSVSM 485
Length:485
Mass (Da):54,027
Last modified:October 3, 2006 - v2
Checksum:iB36E403B136F3FC4
GO

Sequence cautioni

The sequence ABD86889.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000301 Genomic DNA. Translation: ABD86889.1. Different initiation.
RefSeqiYP_531208.1. NC_007925.1.

Genome annotation databases

EnsemblBacteriaiABD86889; ABD86889; RPC_1327.
GeneIDi3974066.
KEGGirpc:RPC_1327.
PATRICi23267326. VBIRhoPal29154_1368.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000301 Genomic DNA. Translation: ABD86889.1 . Different initiation.
RefSeqi YP_531208.1. NC_007925.1.

3D structure databases

ProteinModelPortali Q219P7.
SMRi Q219P7. Positions 22-465.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 316056.RPC_1327.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABD86889 ; ABD86889 ; RPC_1327 .
GeneIDi 3974066.
KEGGi rpc:RPC_1327.
PATRICi 23267326. VBIRhoPal29154_1368.

Phylogenomic databases

eggNOGi COG1850.
HOGENOMi HOG000230831.
KOi K01601.
OrthoDBi EOG6ZKXMS.

Enzyme and pathway databases

BioCyci RPAL316056:GH3E-1342-MONOMER.

Family and domain databases

Gene3Di 3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPi MF_01338. RuBisCO_L_type1.
InterProi IPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
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: BisB18.

Entry informationi

Entry nameiRBL_RHOPB
AccessioniPrimary (citable) accession number: Q219P7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: October 3, 2006
Last modified: May 14, 2014
This is version 49 of the entry and version 2 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" By similarity.

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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