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O28635

- RBL_ARCFU

UniProt

O28635 - RBL_ARCFU

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Protein
Ribulose bisphosphate carboxylase
Gene
rbcL, AF_1638
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 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

Enzyme regulationi

Reversibly inhibited by O2.UniRule annotation

Temperature dependencei

Active over a broad temperature range.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei160 – 1601Proton acceptor By similarity
Binding sitei162 – 1621Substrate By similarity
Metal bindingi186 – 1861Magnesium; via carbamate group By similarity
Metal bindingi188 – 1881Magnesium By similarity
Metal bindingi189 – 1891Magnesium By similarity
Active sitei278 – 2781Proton acceptor By similarity
Binding sitei279 – 2791Substrate By similarity
Binding sitei311 – 3111Substrate By similarity
Sitei319 – 3191Transition state stabilizer By similarity

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 carboxylase (EC:4.1.1.39)
Short name:
RuBisCO
Gene namesi
Name:rbcL
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 carboxylaseUniRule annotation
PRO_0000062671Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei186 – 1861N6-carboxylysine By similarity

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi224325.AF1638.

Structurei

3D structure databases

ProteinModelPortaliO28635.
SMRiO28635. Positions 10-440.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni364 – 3663Substrate binding By similarity
Regioni386 – 3894Substrate binding By similarity

Sequence similaritiesi

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

MAEFEIYREY VDKSYEPQKD DIVAVFRITP AEGFTIEDAA GAVAAESSTG    50
TWTSLHPWYD EERVKGLSAK AYDFVDLGDG SSIVRIAYPS ELFEPHNMPG 100
LLASIAGNVF GMKRVKGLRL EDLQLPKSFL KDFKGPSKGK EGVKKIFGVA 150
DRPIVGTVPK PKVGYSAEEV EKLAYELLSG GMDYIKDDEN LTSPAYCRFE 200
ERAERIMKVI EKVEAETGEK KSWFANITAD VREMERRLKL VAELGNPHVM 250
VDVVITGWGA LEYIRDLAED YDLAIHGHRA MHAAFTRNAK HGISMFVLAK 300
LYRIIGIDQL HIGTAGAGKL EGQKWDTVQN ARIFSEVEYT PDEGDAFHLS 350
QNFHHIKPAM PVSSGGLHPG NLEPVIDALG KEIVIQVGGG VLGHPMGAKA 400
GAKAVRQALD AIISAIPLEE HAKQHPELQA ALEKWGRVTP I 441
Length:441
Mass (Da):48,557
Last modified:January 1, 1998 - v1
Checksum:iF191B4A83F36F3FD
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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: September 3, 2014
This is version 99 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 By similarity.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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