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.

O84917

- RBL2_THIK1

UniProt

O84917 - RBL2_THIK1

(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, Tint_1655
Organism
Thiomonas intermedia (strain K12) (Thiobacillus intermedius)
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 sitei113 – 1131Substrate; in homodimeric partner By similarity
Active sitei168 – 1681Proton acceptor By similarity
Binding sitei170 – 1701Substrate By similarity
Metal bindingi193 – 1931Magnesium; via carbamate group By similarity
Metal bindingi195 – 1951Magnesium By similarity
Metal bindingi196 – 1961Magnesium By similarity
Active sitei289 – 2891Proton acceptor By similarity
Binding sitei290 – 2901Substrate By similarity
Binding sitei323 – 3231Substrate By similarity
Sitei331 – 3311Transition state stabilizer By similarity
Binding sitei370 – 3701Substrate 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

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciTINT75379:GH6C-1675-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:Tint_1655
OrganismiThiomonas intermedia (strain K12) (Thiobacillus intermedius)
Taxonomic identifieri75379 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesThiomonas
ProteomesiUP000002185: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 461461Ribulose bisphosphate carboxylaseUniRule annotation
PRO_0000062669Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei193 – 1931N6-carboxylysine By similarity

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliO84917.
SMRiO84917. Positions 4-459.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000230831.
KOiK01601.

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.

O84917-1 [UniParc]FASTAAdd to Basket

« Hide

MAHDQSSRYA NLDLKESDLI AGGKHILVAY KMKPKAGYDY LATAAHFAAE    50
SSTGTNVEVS TTDDFTKGVD ALVYFIDEAT EDMRIAYPIE LFDRNVIDGR 100
FMIVSFLTLV IGNNQGMGDV EYGKMIDFYV PERAIQMFDG PATDISNLWR 150
ILGRPIKDGG YIAGTIIKPK LGLRPEPFAQ AAYQFWLGGD FIKNDEPQGN 200
QVFAPVKKVI PLVYDAMKRA QDETGEAKLF SMNITADDYH EMCARADFAL 250
EVFGPDADKL AFLVDGYVGG PGMVTTARRQ YPNQYLHYHR AGHGAITSPS 300
SKRGYTAFVL AKMSRLQGAS GIHVGTMGYG KMEGEGDDRN IAYMIERDEC 350
QGPVYFQKWY GMKPTTPIIS GGMNALRLPG FFENLGHGNV INTAGGGSYG 400
HIDSPAAGAK SLRQAYECWK AGADPIEYAK EHKEFARAFE SFPGDADKLF 450
PGWRDKLGVH K 461
Length:461
Mass (Da):50,818
Last modified:November 1, 1998 - v1
Checksum:iD470D17F356800E2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF012127 Genomic DNA. Translation: AAC24964.1.
CP002021 Genomic DNA. Translation: ADG31025.1.
RefSeqiWP_013123277.1. NC_014153.1.
YP_003643355.1. NC_014153.1.

Genome annotation databases

EnsemblBacteriaiADG31025; ADG31025; Tint_1655.
GeneIDi9152388.
KEGGitin:Tint_1655.
PATRICi38293853. VBIThiInt85915_1685.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF012127 Genomic DNA. Translation: AAC24964.1 .
CP002021 Genomic DNA. Translation: ADG31025.1 .
RefSeqi WP_013123277.1. NC_014153.1.
YP_003643355.1. NC_014153.1.

3D structure databases

ProteinModelPortali O84917.
SMRi O84917. Positions 4-459.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ADG31025 ; ADG31025 ; Tint_1655 .
GeneIDi 9152388.
KEGGi tin:Tint_1655.
PATRICi 38293853. VBIThiInt85915_1685.

Phylogenomic databases

HOGENOMi HOG000230831.
KOi K01601.

Enzyme and pathway databases

BioCyci TINT75379:GH6C-1675-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

« Hide 'large scale' publications
  1. "A form II Rubisco gene and associated genes in Thiobacillus intermedius."
    Shively J.M., Soyer F.
    Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12.
  3. "Cloning and expression of the D-ribulose-1,5-bisphosphate carboxylase/oxygenase form II gene from Thiobacillus intermedius in Escherichia coli."
    Stoner M.T., Shively J.M.
    FEMS Microbiol. Lett. 107:287-292(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: EXPRESSION IN T.INTERMEDIUS.
  4. Shively J.M.
    Unpublished observations (OCT-2005)
    Cited for: PROBABLE EXPRESSION.

Entry informationi

Entry nameiRBL2_THIK1
AccessioniPrimary (citable) accession number: O84917
Secondary accession number(s): D5X1M9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 1, 1998
Last modified: September 3, 2014
This is version 72 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.

Caution

No expression of this protein has been seen during autotrophic and mixotrophic growth, however the protein is probably expressed under other conditions. In a related bacteria (T.neapolitanus) expression has been seen when the form I enzyme has been knocked out.

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi