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.

A1RZJ5

- A1RZJ5_THEPD

UniProt

A1RZJ5 - A1RZJ5_THEPD

(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
rbcL, Tpen_1227
Organism
Thermofilum pendens (strain Hrk 5)
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 sitei162 – 1621Proton acceptor By similarityUniRule annotation
Binding sitei164 – 1641Substrate By similarityUniRule annotation
Metal bindingi188 – 1881Magnesium; via carbamate group By similarityUniRule annotation
Metal bindingi190 – 1901Magnesium By similarityUniRule annotation
Metal bindingi191 – 1911Magnesium By similarityUniRule annotation
Active sitei280 – 2801Proton acceptor By similarityUniRule annotation
Binding sitei281 – 2811Substrate By similarityUniRule annotation
Binding sitei313 – 3131Substrate By similarityUniRule annotation
Sitei321 – 3211Transition state stabilizer By similarityUniRule annotation

GO - Molecular functioni

  1. magnesium ion binding Source: InterPro
  2. ribulose-bisphosphate carboxylase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbon fixation Source: InterPro
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

BioCyciTPEN368408:GHSG-1282-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:Tpen_1227Imported
OrganismiThermofilum pendens (strain Hrk 5)Imported
Taxonomic identifieri368408 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiThermoprotealesThermofilaceaeThermofilum
ProteomesiUP000000641: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei188 – 1881N6-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

Protein-protein interaction databases

STRINGi368408.Tpen_1227.

Structurei

3D structure databases

ProteinModelPortaliA1RZJ5.
SMRiA1RZJ5. Positions 11-442.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni366 – 3683Substrate binding By similarityUniRule annotation
Regioni388 – 3914Substrate binding By similarityUniRule annotation

Sequence similaritiesi

Belongs to the RuBisCO large chain family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiVIVTFRV.

Family and domain databases

Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
InterProiIPR017712. RuBisCO_III.
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.
TIGRFAMsiTIGR03326. rubisco_III. 1 hit.
PROSITEiPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A1RZJ5-1 [UniParc]FASTAAdd to Basket

« Hide

MPEEFEPYGE FVVKSYLPDP DKDVIVTFRV TPSEGFTIED AAGGVAAESS    50
VGTWTTLYQW YDKSRIDRLK GKAYYMESLG DGSYILRVAY PVELFEEGNM 100
PAFLASVAGN IFGMRRVRSL RVEDIYLPEA FLKHFKGPSQ GVEGVRGKLK 150
IWGRPIIGTV PKPKVGYSPE EVEKLAYEIL VGGMDFVKDD ENLAGPSYCR 200
FEERAKAIMK AIDRAEKETG ERKAWLANIT ADVREMERRL KLVAELGNTH 250
VMVDVVIAGW SSLTYVRDLA ADYKLAIHGH RAFHAAFTRN PYHGVSMFTL 300
AKLYRIIGVD QLHVGTPEVG KLEAKAVDVI RMARLLREQT YKPDIEDGLH 350
MQQPFPGIKP AFPVSSGGLH PGTLPAVIKA MGVDTVIQVG GGVVGHPDGP 400
RAGAAAARQA VEAYLEGVPL QEYAKTHREL ARALEKWGQV IPV 443
Length:443
Mass (Da):48,972
Last modified:February 6, 2007 - v1
Checksum:i64E48C8F1DAF8288
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000505 Genomic DNA. Translation: ABL78625.1.
RefSeqiWP_011752890.1. NC_008698.1.
YP_920628.1. NC_008698.1.

Genome annotation databases

EnsemblBacteriaiABL78625; ABL78625; Tpen_1227.
GeneIDi4601724.
KEGGitpe:Tpen_1227.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000505 Genomic DNA. Translation: ABL78625.1 .
RefSeqi WP_011752890.1. NC_008698.1.
YP_920628.1. NC_008698.1.

3D structure databases

ProteinModelPortali A1RZJ5.
SMRi A1RZJ5. Positions 11-442.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 368408.Tpen_1227.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABL78625 ; ABL78625 ; Tpen_1227 .
GeneIDi 4601724.
KEGGi tpe:Tpen_1227.

Phylogenomic databases

eggNOGi COG1850.
HOGENOMi HOG000230831.
KOi K01601.
OMAi VIVTFRV.

Enzyme and pathway databases

BioCyci TPEN368408:GHSG-1282-MONOMER.

Family and domain databases

Gene3Di 3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
InterProi IPR017712. RuBisCO_III.
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.
TIGRFAMsi TIGR03326. rubisco_III. 1 hit.
PROSITEi PS00157. RUBISCO_LARGE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Hrk 5.

Entry informationi

Entry nameiA1RZJ5_THEPD
AccessioniPrimary (citable) accession number: A1RZJ5
Entry historyi
Integrated into UniProtKB/TrEMBL: February 6, 2007
Last sequence update: February 6, 2007
Last modified: September 3, 2014
This is version 51 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, Reference proteome

External Data

Dasty 3

Similar proteinsi