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Q3IYC2

- RBL_RHOS4

UniProt

Q3IYC2 - RBL_RHOS4

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Protein
Ribulose bisphosphate carboxylase large chain
Gene
cbbL, RHOS4_28940, RSP_1282
Organism
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
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 sitei125 – 1251Substrate; in homodimeric partner By similarity
Binding sitei175 – 1751Substrate By similarity
Active sitei177 – 1771Proton acceptor By similarity
Binding sitei179 – 1791Substrate By similarity
Metal bindingi203 – 2031Magnesium; via carbamate group By similarity
Metal bindingi205 – 2051Magnesium By similarity
Metal bindingi206 – 2061Magnesium By similarity
Active sitei295 – 2951Proton acceptor By similarity
Binding sitei296 – 2961Substrate By similarity
Binding sitei328 – 3281Substrate By similarity
Sitei335 – 3351Transition state stabilizer By similarity
Binding sitei380 – 3801Substrate 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

BioCyciRSPH272943:GJAS-2963-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:RHOS4_28940
ORF Names:RSP_1282
OrganismiRhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Taxonomic identifieri272943 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter
ProteomesiUP000002703: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 486486Ribulose bisphosphate carboxylase large chainUniRule annotation
PRO_0000251460Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei203 – 2031N6-carboxylysine By similarity

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-59569N.
STRINGi272943.RSP_1282.

Structurei

3D structure databases

ProteinModelPortaliQ3IYC2.
SMRiQ3IYC2. Positions 6-479.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiFTQDWAS.
OrthoDBiEOG6ZKXMS.
PhylomeDBiQ3IYC2.

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.

Q3IYC2-1 [UniParc]FASTAAdd to Basket

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MDTKTTEIKG KERYKAGVLK YAQMGYWDGD YVPKDTDVLA LFRITPQEGV    50
DPVEAAAAVA GESSTATWTV VWTDRLTACD SYRAKAYRVE PVPGTPGQYF 100
CYVAYDLILF EEGSIANLTA SIIGNVFSFK PLKAARLEDM RFPVAYVKTY 150
KGPPTGIVGE RERLDKFGKP LLGATTKPKL GLSGKNYGRV VYEGLKGGLD 200
FMKDDENINS QPFMHWRDRF LYVMEAVNLA SAQTGEVKGH YLNITAGTME 250
EMYRRAEFAK SLGSVIVMVD LIIGYTAIQS ISEWCRQNDM ILHMHRAGHG 300
TYTRQKNHGI SFRVIAKWLR LAGVDHLHCG TAVGKLEGDP LTVQGYYNVC 350
REPFNTVDLP RGIFFEQDWA DLRKVMPVAS GGIHAGQMHQ LLSLFGDDVV 400
LQFGGGTIGH PMGIQAGATA NRVALEAMVL ARNEGRNIDV EGPEILRAAA 450
KWCKPLEAAL DTWGNITFNY TSTDTSDFVP TASVAM 486
Length:486
Mass (Da):53,686
Last modified:November 8, 2005 - v1
Checksum:i82B91D700303C3C0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000143 Genomic DNA. Translation: ABA80462.1.
RefSeqiYP_354363.1. NC_007493.2.

Genome annotation databases

EnsemblBacteriaiABA80462; ABA80462; RSP_1282.
GeneIDi3718196.
KEGGirsp:RSP_1282.
PATRICi23155797. VBIRhoSph57909_3263.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000143 Genomic DNA. Translation: ABA80462.1 .
RefSeqi YP_354363.1. NC_007493.2.

3D structure databases

ProteinModelPortali Q3IYC2.
SMRi Q3IYC2. Positions 6-479.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-59569N.
STRINGi 272943.RSP_1282.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABA80462 ; ABA80462 ; RSP_1282 .
GeneIDi 3718196.
KEGGi rsp:RSP_1282.
PATRICi 23155797. VBIRhoSph57909_3263.

Phylogenomic databases

eggNOGi COG1850.
HOGENOMi HOG000230831.
KOi K01601.
OMAi FTQDWAS.
OrthoDBi EOG6ZKXMS.
PhylomeDBi Q3IYC2.

Enzyme and pathway databases

BioCyci RSPH272943:GJAS-2963-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. "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1."
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C., Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158.

Entry informationi

Entry nameiRBL_RHOS4
AccessioniPrimary (citable) accession number: Q3IYC2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: November 8, 2005
Last modified: July 9, 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 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi