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B3Q7E1

- RBL_RHOPT

UniProt

B3Q7E1 - RBL_RHOPT

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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Rhodopseudomonas palustris (strain TIE-1)
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

Binds 1 magnesium ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei124 – 1241Substrate; in homodimeric partnerUniRule annotation
Binding sitei174 – 1741SubstrateUniRule annotation
Active sitei176 – 1761Proton acceptorUniRule annotation
Binding sitei178 – 1781SubstrateUniRule annotation
Metal bindingi202 – 2021Magnesium; via carbamate groupUniRule annotation
Metal bindingi204 – 2041MagnesiumUniRule annotation
Metal bindingi205 – 2051MagnesiumUniRule annotation
Active sitei294 – 2941Proton acceptorUniRule annotation
Binding sitei295 – 2951SubstrateUniRule annotation
Binding sitei327 – 3271SubstrateUniRule annotation
Sitei334 – 3341Transition state stabilizerUniRule annotation
Binding sitei379 – 3791SubstrateUniRule 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

BioCyciRPAL395960:GHPC-1762-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase large chainUniRule annotation (EC:4.1.1.39UniRule annotation)
Short name:
RuBisCO large subunitUniRule annotation
Gene namesi
Name:cbbLUniRule annotation
Ordered Locus Names:Rpal_1747
OrganismiRhodopseudomonas palustris (strain TIE-1)
Taxonomic identifieri395960 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeRhodopseudomonas
ProteomesiUP000001725: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 485485Ribulose bisphosphate carboxylase large chainPRO_1000142752Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei202 – 2021N6-carboxylysineUniRule annotation

Interactioni

Subunit structurei

Heterohexadecamer of 8 large chains and 8 small chains.UniRule annotation

Protein-protein interaction databases

STRINGi395960.Rpal_1747.

Structurei

3D structure databases

ProteinModelPortaliB3Q7E1.
SMRiB3Q7E1. Positions 12-477.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiFTQDWAS.
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.

B3Q7E1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNEAVTIRGK ERYKSGVMEY KKMGYWEPDY EPKDTDVIAL FRVTPQDGVD
60 70 80 90 100
PIEAAAAVAG ESSTATWTVV WTDRLTAAEK YRAKCYRVDP VPNSPGQYFA
110 120 130 140 150
YIAYDLDLFE PGSISNLTAS IIGNVFGFKP LKALRLEDMR LPIAYVKTFQ
160 170 180 190 200
GPATGIVVER ERMDKFGRPL LGATVKPKLG LSGRNYGRVV YEALKGGLDF
210 220 230 240 250
TKDDENINSQ PFMHWRERFQ YCMEAVNKAQ AQTGEIKGTY LNVTAATMED
260 270 280 290 300
MYERAEYAKE LGSIIVMIDL VIGYTAIQSM AKWARKNDMI LHLHRAGHST
310 320 330 340 350
YTRQRNHGVS FRVIAKWMRL AGVDHIHAGT VVGKLEGDPA TTKGYYDICR
360 370 380 390 400
EDFNPMTLEN GLFFDQNWAS LNKLMPVASG GIHAGQMHQL LHLLGEDVVL
410 420 430 440 450
QFGGGTIGHP MGIAAGATAN RVALEAMILA RNEGRDYLHE GPEILAKAAQ
460 470 480
TCTPLKAALD TWKNVTFNYE STDTPDYAPT PSVSV
Length:485
Mass (Da):53,874
Last modified:September 2, 2008 - v1
Checksum:i50429A1FFD40FDC9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001096 Genomic DNA. Translation: ACF00275.1.
RefSeqiYP_001990750.1. NC_011004.1.

Genome annotation databases

EnsemblBacteriaiACF00275; ACF00275; Rpal_1747.
GeneIDi6409404.
KEGGirpt:Rpal_1747.
PATRICi23307913. VBIRhoPal88240_1774.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001096 Genomic DNA. Translation: ACF00275.1 .
RefSeqi YP_001990750.1. NC_011004.1.

3D structure databases

ProteinModelPortali B3Q7E1.
SMRi B3Q7E1. Positions 12-477.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 395960.Rpal_1747.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACF00275 ; ACF00275 ; Rpal_1747 .
GeneIDi 6409404.
KEGGi rpt:Rpal_1747.
PATRICi 23307913. VBIRhoPal88240_1774.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci RPAL395960:GHPC-1762-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: TIE-1.

Entry informationi

Entry nameiRBL_RHOPT
AccessioniPrimary (citable) accession number: B3Q7E1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 2, 2008
Last modified: October 29, 2014
This is version 37 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 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".UniRule annotation

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3