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O28635

- RBL_ARCFU

UniProt

O28635 - RBL_ARCFU

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Protein

Ribulose bisphosphate carboxylase

Gene

rbcL

Organism
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

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.1 PublicationUniRule annotation
3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2.1 PublicationUniRule annotation

Cofactori

Mg2+UniRule annotationNote: Binds 1 Mg(2+) ion per subunit.UniRule annotation

Enzyme regulationi

Reversibly inhibited by O2.1 Publication

Temperature dependencei

Active over a broad temperature range.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei160 – 1601Proton acceptorUniRule annotation
Binding sitei162 – 1621SubstrateUniRule annotation
Metal bindingi186 – 1861Magnesium; via carbamate groupUniRule annotation
Metal bindingi188 – 1881MagnesiumUniRule annotation
Metal bindingi189 – 1891MagnesiumUniRule annotation
Active sitei278 – 2781Proton acceptorUniRule annotation
Binding sitei279 – 2791SubstrateUniRule annotation
Binding sitei311 – 3111SubstrateUniRule annotation
Sitei319 – 3191Transition 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

Lyase, Oxidoreductase

Keywords - Biological processi

Carbon dioxide fixation

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciAFUL224325:GJBC-1672-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:AF_1638
OrganismiArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Taxonomic identifieri224325 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus
ProteomesiUP000002199: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 441441Ribulose bisphosphate carboxylasePRO_0000062671Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei186 – 1861N6-carboxylysineUniRule annotation

Interactioni

Subunit structurei

Homodimer. In contrast to form I RuBisCO, the form III RuBisCO is composed solely of large subunits.1 Publication

Protein-protein interaction databases

STRINGi224325.AF1638.

Structurei

3D structure databases

ProteinModelPortaliO28635.
SMRiO28635. Positions 10-440.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni364 – 3663Substrate bindingUniRule annotation
Regioni386 – 3894Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1850.
KOiK01601.
OMAiFTQDWAS.

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.

O28635-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAEFEIYREY VDKSYEPQKD DIVAVFRITP AEGFTIEDAA GAVAAESSTG
60 70 80 90 100
TWTSLHPWYD EERVKGLSAK AYDFVDLGDG SSIVRIAYPS ELFEPHNMPG
110 120 130 140 150
LLASIAGNVF GMKRVKGLRL EDLQLPKSFL KDFKGPSKGK EGVKKIFGVA
160 170 180 190 200
DRPIVGTVPK PKVGYSAEEV EKLAYELLSG GMDYIKDDEN LTSPAYCRFE
210 220 230 240 250
ERAERIMKVI EKVEAETGEK KSWFANITAD VREMERRLKL VAELGNPHVM
260 270 280 290 300
VDVVITGWGA LEYIRDLAED YDLAIHGHRA MHAAFTRNAK HGISMFVLAK
310 320 330 340 350
LYRIIGIDQL HIGTAGAGKL EGQKWDTVQN ARIFSEVEYT PDEGDAFHLS
360 370 380 390 400
QNFHHIKPAM PVSSGGLHPG NLEPVIDALG KEIVIQVGGG VLGHPMGAKA
410 420 430 440
GAKAVRQALD AIISAIPLEE HAKQHPELQA ALEKWGRVTP I
Length:441
Mass (Da):48,557
Last modified:January 1, 1998 - v1
Checksum:iF191B4A83F36F3FD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000782 Genomic DNA. Translation: AAB89603.1.
PIRiE69454.
RefSeqiNP_070466.1. NC_000917.1.
WP_010879134.1. NC_000917.1.

Genome annotation databases

EnsemblBacteriaiAAB89603; AAB89603; AF_1638.
GeneIDi1484861.
KEGGiafu:AF1638.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000782 Genomic DNA. Translation: AAB89603.1 .
PIRi E69454.
RefSeqi NP_070466.1. NC_000917.1.
WP_010879134.1. NC_000917.1.

3D structure databases

ProteinModelPortali O28635.
SMRi O28635. Positions 10-440.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224325.AF1638.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAB89603 ; AAB89603 ; AF_1638 .
GeneIDi 1484861.
KEGGi afu:AF1638.

Phylogenomic databases

eggNOGi COG1850.
KOi K01601.
OMAi FTQDWAS.

Enzyme and pathway databases

BioCyci AFUL224325:GJBC-1672-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. "The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus."
    Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G.
    , Gill S.R., Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.
    Nature 390:364-370(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.
  2. "Synthesis of catalytically active form III ribulose 1,5-bisphosphate carboxylase/oxygenase in archaea."
    Finn M.W., Tabita F.R.
    J. Bacteriol. 185:3049-3059(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.

Entry informationi

Entry nameiRBL_ARCFU
AccessioniPrimary (citable) accession number: O28635
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: January 1, 1998
Last modified: November 26, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

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 proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3