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Q10WH6

- RBL_TRIEI

UniProt

Q10WH6 - RBL_TRIEI

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Protein

Ribulose bisphosphate carboxylase large chain

Gene
cbbL, rbcL, Tery_4410
Organism
Trichodesmium erythraeum (strain IMS101)
Status
Reviewed - Annotation score: 4 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 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. photorespiration Source: UniProtKB-KW
  2. reductive pentose-phosphate cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Lyase, Monooxygenase, Oxidoreductase

Keywords - Biological processi

Calvin cycle, Carbon dioxide fixation, Photorespiration, Photosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciTERY203124:GJDR-4456-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
Synonyms:rbcL
Ordered Locus Names:Tery_4410
OrganismiTrichodesmium erythraeum (strain IMS101)
Taxonomic identifieri203124 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeOscillatorialesTrichodesmium
ProteomesiUP000008878: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 476476Ribulose bisphosphate carboxylase large chainUniRule annotationPRO_0000299976Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei202 – 2021N6-carboxylysine By similarity
Disulfide bondi248 – 248Interchain; in linked form By similarity

Post-translational modificationi

The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover By similarity.UniRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiQ10WH6.

Interactioni

Subunit structurei

Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers By similarity.

Protein-protein interaction databases

STRINGi203124.Tery_4410.

Structurei

3D structure databases

ProteinModelPortaliQ10WH6.
SMRiQ10WH6. Positions 13-470.

Family & Domainsi

Sequence similaritiesi

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.

Q10WH6-1 [UniParc]FASTAAdd to Basket

« Hide

MSYAKTQTQS KSGYQAGVKD YKLTYYTPDY IPKDTDLLAA FRMSPQPGVP    50
PEEAGAAVAA ESSTGTWTTV WTDLLTDLDR YKGRCYDIES VPGEDNQYIC 100
YVAYPLDLFE EGSVTNMLTS IVGNVFGFKA LRSLRLEDLR IPVAYLKTFQ 150
GPPHGITVER DKLNKYGRPL LGCTIKPKLG LSAKNYGRAV YECLRGGLDF 200
TKDDENINSQ PFMRWRDRFL FAQEAIEKAQ AETGEIKGHY LNVTAPTCEE 250
MLERADFAKE IGTPIIMHDY LTGGFTANTT LAKWCRRNGV LLHIHRAMHA 300
VIDRQKAHGI HFRVLAKCLR MSGGDHLHSG TVVGKLEGEK GITMGFVDLM 350
REDHVEQDRE RGIYFTQDWA SMPGVMPVAS GGIHVWHMPA LVEIFGDDSC 400
LQFGGGTLGH PWGNAPGATA NRVALEACIQ ARNEGRNLFR EGGDVIREAA 450
KWSPDLAVAC ELWKEIKFEF EAMDTL 476
Length:476
Mass (Da):53,078
Last modified:August 22, 2006 - v1
Checksum:i99344CF2E8D99C19
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000393 Genomic DNA. Translation: ABG53398.1.
RefSeqiYP_723871.1. NC_008312.1.

Genome annotation databases

EnsemblBacteriaiABG53398; ABG53398; Tery_4410.
GeneIDi4246063.
KEGGiter:Tery_4410.
PATRICi23994367. VBITriEry99848_5586.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000393 Genomic DNA. Translation: ABG53398.1 .
RefSeqi YP_723871.1. NC_008312.1.

3D structure databases

ProteinModelPortali Q10WH6.
SMRi Q10WH6. Positions 13-470.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 203124.Tery_4410.

Proteomic databases

PRIDEi Q10WH6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABG53398 ; ABG53398 ; Tery_4410 .
GeneIDi 4246063.
KEGGi ter:Tery_4410.
PATRICi 23994367. VBITriEry99848_5586.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci TERY203124:GJDR-4456-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: IMS101.

Entry informationi

Entry nameiRBL_TRIEI
AccessioniPrimary (citable) accession number: Q10WH6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: August 22, 2006
Last modified: May 14, 2014
This is version 61 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi