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D5U228

- D5U228_THEAM

UniProt

D5U228 - D5U228_THEAM

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Protein
Ribulose bisphosphate carboxylase
Gene
rbcL, Tagg_0906
Organism
Thermosphaera aggregans (strain DSM 11486 / M11TL)
Status
Unreviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Catalyzes the addition of molecular CO2 and H2O to ribulose 1,5-bisphosphate (RuBP), generating two molecules of 3-phosphoglycerate (3-PGA). Functions in an archaeal AMP degradation pathway, together with AMP phosphorylase and R15P isomerase 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
Active sitei164 – 1641Proton acceptor By similarityUniRule annotation
Binding sitei166 – 1661Substrate By similarityUniRule annotation
Metal bindingi190 – 1901Magnesium; via carbamate group By similarityUniRule annotation
Metal bindingi192 – 1921Magnesium By similarityUniRule annotation
Metal bindingi193 – 1931Magnesium By similarityUniRule annotation
Active sitei282 – 2821Proton acceptor By similarityUniRule annotation
Binding sitei283 – 2831Substrate By similarityUniRule annotation
Binding sitei315 – 3151Substrate By similarityUniRule annotation
Sitei323 – 3231Transition state stabilizer By similarityUniRule annotation

GO - Molecular functioni

  1. magnesium ion binding Source: UniProtKB-HAMAP
  2. oxidoreductase activity Source: UniProtKB-KW
  3. ribulose-bisphosphate carboxylase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. AMP catabolic process Source: UniProtKB-HAMAP
  2. carbon fixation Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

LyaseUniRule annotationImported, OxidoreductaseUniRule annotation

Keywords - Biological processi

Carbon dioxide fixationUniRule annotation

Keywords - Ligandi

MagnesiumUniRule annotation, Metal-bindingUniRule annotation

Enzyme and pathway databases

BioCyciTAGG633148:GHBI-919-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylaseUniRule annotation (EC:4.1.1.39UniRule annotation)
Short name:
RuBisCOUniRule annotation
Gene namesi
Name:rbcLUniRule annotation
Ordered Locus Names:Tagg_0906Imported
OrganismiThermosphaera aggregans (strain DSM 11486 / M11TL)Imported
Taxonomic identifieri633148 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeThermosphaera
ProteomesiUP000002376: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei190 – 1901N6-carboxylysine By similarityUniRule annotation

Interactioni

Subunit structurei

Homodimer or homodecamer. In contrast to form I RuBisCO, the form III RuBisCO is composed solely of large subunits By similarity.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliD5U228.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni368 – 3703Substrate binding By similarityUniRule annotation
Regioni390 – 3934Substrate binding By similarityUniRule annotation

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000230831.
KOiK01601.
OMAiVIVTFRV.

Family and domain databases

Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01133. RuBisCO_L_type3.
InterProiIPR017712. RuBisCO_III.
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.
TIGRFAMsiTIGR03326. rubisco_III. 1 hit.

Sequencei

Sequence statusi: Complete.

D5U228-1 [UniParc]FASTAAdd to Basket

« Hide

MPEKFDFETY HEYIDRTFKP DPDNHVIAVF RIKPAQGFTI DDAAGGVAAE    50
SSTGTWTTVY NWYDRERVRR LSGRAYEFLD LKDGSWIVKI AYPVELFEEG 100
NIPGLLASIA GNVFGMRRVE GLRLEDIYLP GGFLKDFKGP SKGVEGVREI 150
FKVKDRPIVG TVPKPKVGYS PEEVEKLATE LLMGGLDYIK DDENLTSPKY 200
CSFEARAKAI MKVIDKVEKE TGERKAWFAN ITADVREMEK RLRLVADYGN 250
PYVMVDVVVS GWGVLNYIRD LAEEYGLAVH AHRAMHASFT RNPYHGISMF 300
VLAKLYRVIG VDQLHVGTAG AGKLEGGRLD VIRCAKILRE QSFTPDPEDP 350
FHLPQDMRHI KPAMPVSSGG LHPGNLPPVI DALGPDIVLQ VGGGVVGHPD 400
GPRAGAMAVR QALDAIVKGI PLDKYAESHR ELARALEKWG FVKPI 445
Length:445
Mass (Da):49,428
Last modified:July 13, 2010 - v1
Checksum:i358B529EF1A31E75
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001939 Genomic DNA. Translation: ADG91178.1.
RefSeqiYP_003650130.1. NC_014160.1.

Genome annotation databases

EnsemblBacteriaiADG91178; ADG91178; Tagg_0906.
GeneIDi9165923.
KEGGitag:Tagg_0906.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001939 Genomic DNA. Translation: ADG91178.1 .
RefSeqi YP_003650130.1. NC_014160.1.

3D structure databases

ProteinModelPortali D5U228.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ADG91178 ; ADG91178 ; Tagg_0906 .
GeneIDi 9165923.
KEGGi tag:Tagg_0906.

Phylogenomic databases

HOGENOMi HOG000230831.
KOi K01601.
OMAi VIVTFRV.

Enzyme and pathway databases

BioCyci TAGG633148:GHBI-919-MONOMER.

Family and domain databases

Gene3Di 3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPi MF_01133. RuBisCO_L_type3.
InterProi IPR017712. RuBisCO_III.
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.
TIGRFAMsi TIGR03326. rubisco_III. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 11486 / M11TL.
  2. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: DSM 11486.

Entry informationi

Entry nameiD5U228_THEAM
AccessioniPrimary (citable) accession number: D5U228
Entry historyi
Integrated into UniProtKB/TrEMBL: July 13, 2010
Last sequence update: July 13, 2010
Last modified: September 3, 2014
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Miscellaneous

Because the Archaea possessing a type III RuBisCO are all anaerobic, it is most likely that only the carboxylase activity of RuBisCO, and not the competitive oxygenase activity (by which RuBP reacts with O2 to form one molecule of 3-phosphoglycerate and one molecule of 2-phosphoglycolate), is biologically relevant in these strains By similarity.UniRule annotation

Keywords - Technical termi

Complete proteome

External Data

Dasty 3

Similar proteinsi