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A1RZJ5

- A1RZJ5_THEPD

UniProt

A1RZJ5 - A1RZJ5_THEPD

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Protein

Ribulose bisphosphate carboxylase

Gene

rbcL

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.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

Note: Binds 1 magnesium ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei162 – 1621Proton acceptorUniRule annotation
Binding sitei164 – 1641SubstrateUniRule annotation
Metal bindingi188 – 1881Magnesium; via carbamate groupUniRule annotation
Metal bindingi190 – 1901MagnesiumUniRule annotation
Metal bindingi191 – 1911MagnesiumUniRule annotation
Active sitei280 – 2801Proton acceptorUniRule annotation
Binding sitei281 – 2811SubstrateUniRule annotation
Binding sitei313 – 3131SubstrateUniRule annotation
Sitei321 – 3211Transition state stabilizerUniRule 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

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-carboxylysineUniRule annotation

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi368408.Tpen_1227.

Structurei

3D structure databases

ProteinModelPortaliA1RZJ5.
SMRiA1RZJ5. Positions 11-442.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni366 – 3683Substrate bindingUniRule annotation
Regioni388 – 3914Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the RuBisCO large chain family.UniRule annotation
Belongs to the RuBisCO large chain family. Type III subfamily.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

        10         20         30         40         50
MPEEFEPYGE FVVKSYLPDP DKDVIVTFRV TPSEGFTIED AAGGVAAESS
60 70 80 90 100
VGTWTTLYQW YDKSRIDRLK GKAYYMESLG DGSYILRVAY PVELFEEGNM
110 120 130 140 150
PAFLASVAGN IFGMRRVRSL RVEDIYLPEA FLKHFKGPSQ GVEGVRGKLK
160 170 180 190 200
IWGRPIIGTV PKPKVGYSPE EVEKLAYEIL VGGMDFVKDD ENLAGPSYCR
210 220 230 240 250
FEERAKAIMK AIDRAEKETG ERKAWLANIT ADVREMERRL KLVAELGNTH
260 270 280 290 300
VMVDVVIAGW SSLTYVRDLA ADYKLAIHGH RAFHAAFTRN PYHGVSMFTL
310 320 330 340 350
AKLYRIIGVD QLHVGTPEVG KLEAKAVDVI RMARLLREQT YKPDIEDGLH
360 370 380 390 400
MQQPFPGIKP AFPVSSGGLH PGTLPAVIKA MGVDTVIQVG GGVVGHPDGP
410 420 430 440
RAGAAAARQA VEAYLEGVPL QEYAKTHREL ARALEKWGQV IPV
Length:443
Mass (Da):48,972
Last modified:February 6, 2007 - v1
Checksum:i64E48C8F1DAF8288
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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 5Imported.

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: November 26, 2014
This is version 54 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.UniRule annotation

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3