Ribulose bisphosphate carboxylase - Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)

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O28635 (RBL_ARCFU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 94. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Ribulose bisphosphate carboxylase
Short name=RuBisCO
EC=4.1.1.39

Gene names

Name:	rbcL
Ordered Locus Names:	AF_1638

Organism

Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) [Reference proteome] [HAMAP]

Taxonomic identifier

224325 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Archaeoglobi › Archaeoglobales › Archaeoglobaceae › Archaeoglobus ›

Protein attributes

Sequence length	441 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	2 3-phospho-D-glycerate + 2 H⁺ = D-ribulose 1,5-bisphosphate + CO₂ + H₂O. HAMAP-Rule MF_01133 3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O₂. HAMAP-Rule MF_01133
Cofactor	Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_01133
Enzyme regulation	Reversibly inhibited by O₂. HAMAP-Rule MF_01133
Subunit structure	Homodimer.
Miscellaneous	The basic functional RuBisCO is composed of a large chain homodimer in a "head-to-tail" conformation By similarity. HAMAP-Rule MF_01133
Sequence similarities	Belongs to the RuBisCO large chain family. Type III subfamily.
Biophysicochemical properties	Temperature dependence: Active over a broad temperature range. HAMAP-Rule MF_01133

Ontologies

Keywords
Biological process	Carbon dioxide fixation
Ligand	Magnesium Metal-binding
Molecular function	Lyase Monooxygenase Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	carbon fixation Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	magnesium ion binding Inferred from electronic annotation. Source: HAMAP monooxygenase activity Inferred from electronic annotation. Source: UniProtKB-KW ribulose-bisphosphate carboxylase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 441

441

Ribulose bisphosphate carboxylase HAMAP-Rule MF_01133

PRO_0000062671

Sites

Active site

160

Proton acceptor By similarity

Active site

278

Proton acceptor By similarity

Metal binding

186

Magnesium; via carbamate group By similarity

Metal binding

188

Magnesium By similarity

Metal binding

189

Magnesium By similarity

Binding site

108

Substrate; in homodimeric partner By similarity

Binding site

162

Substrate By similarity

Binding site

279

Substrate By similarity

Binding site

311

Substrate By similarity

Binding site

364

Substrate By similarity

Site

319

Transition state stabilizer By similarity

Amino acid modifications

Modified residue

186

N6-carboxylysine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

O28635 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: F191B4A83F36F3FD
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FASTA

441

48,557

        10         20         30         40         50         60 
MAEFEIYREY VDKSYEPQKD DIVAVFRITP AEGFTIEDAA GAVAAESSTG TWTSLHPWYD 

        70         80         90        100        110        120 
EERVKGLSAK AYDFVDLGDG SSIVRIAYPS ELFEPHNMPG LLASIAGNVF GMKRVKGLRL 

       130        140        150        160        170        180 
EDLQLPKSFL KDFKGPSKGK EGVKKIFGVA DRPIVGTVPK PKVGYSAEEV EKLAYELLSG 

       190        200        210        220        230        240 
GMDYIKDDEN LTSPAYCRFE ERAERIMKVI EKVEAETGEK KSWFANITAD VREMERRLKL 

       250        260        270        280        290        300 
VAELGNPHVM VDVVITGWGA LEYIRDLAED YDLAIHGHRA MHAAFTRNAK HGISMFVLAK 

       310        320        330        340        350        360 
LYRIIGIDQL HIGTAGAGKL EGQKWDTVQN ARIFSEVEYT PDEGDAFHLS QNFHHIKPAM 

       370        380        390        400        410        420 
PVSSGGLHPG NLEPVIDALG KEIVIQVGGG VLGHPMGAKA GAKAVRQALD AIISAIPLEE 

       430        440 
HAKQHPELQA ALEKWGRVTP I

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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. 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: CHARACTERIZATION. Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000782 Genomic DNA. Translation: AAB89603.1.
PIR	E69454.
RefSeq	NP_070466.1. NC_000917.1.
3D structure databases
ProteinModelPortal	O28635.
SMR	O28635. Positions 10-440.
ModBase	Search...
Protein-protein interaction databases
STRING	224325.AF1638.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAB89603; AAB89603; AF_1638.
GeneID	1484861.
KEGG	afu:AF1638.
Phylogenomic databases
eggNOG	COG1850.
KO	K01601.
OMA	HRAMHAA.
ProtClustDB	PRK04208.
Enzyme and pathway databases
BioCyc	AFUL224325:GJBC-1672-MONOMER.
Family and domain databases
Gene3D	3.20.20.110. 1 hit. 3.30.70.150. 1 hit.
HAMAP	MF_01133. RuBisCO_L_type3.
InterPro	IPR017712. RuBisCO_III. IPR000685. RuBisCO_lsu_C. IPR017443. RuBisCO_lsu_fd_N. IPR017444. RuBisCO_lsu_N. [Graphical view]
Pfam	PF00016. RuBisCO_large. 1 hit. PF02788. RuBisCO_large_N. 1 hit. [Graphical view]
SUPFAM	SSF51649. RuBisCO_large. 1 hit. SSF54966. RuBisCO_large. 1 hit.
TIGRFAMs	TIGR03326. rubisco_III. 1 hit.
ProtoNet	Search...

Entry information

Entry name

RBL_ARCFU

Accession

Primary (citable) accession number: O28635

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2003
Last sequence update:	January 1, 1998
Last modified:	May 1, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents