Ribulose bisphosphate carboxylase - Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)

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Q8THG2 (RBL_METAC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 79. 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:	MA_4555

Organism

Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A) [Reference proteome] [HAMAP]

Taxonomic identifier

188937 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanosarcina ›

Protein attributes

Sequence length	428 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.
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 from 25 to 40 degrees Celsius. 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 – 428

428

Ribulose bisphosphate carboxylase HAMAP-Rule MF_01133

PRO_0000062672

Sites

Active site

151

Proton acceptor By similarity

Active site

270

Proton acceptor By similarity

Metal binding

177

Magnesium; via carbamate group By similarity

Metal binding

179

Magnesium By similarity

Metal binding

180

Magnesium By similarity

Binding site

Substrate; in homodimeric partner By similarity

Binding site

153

Substrate By similarity

Binding site

271

Substrate By similarity

Binding site

303

Substrate By similarity

Binding site

354

Substrate By similarity

Site

310

Transition state stabilizer By similarity

Amino acid modifications

Modified residue

177

N6-carboxylysine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q8THG2 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: B03BFCBD9E8AFED5
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FASTA

428

46,787

        10         20         30         40         50         60 
MRRDYVDPGY SPKDTDLICE FHIEPAAGIS FEEASTHMAG ESSIDSWTEI STLSPELAAR 

        70         80         90        100        110        120 
LKPHVFYLDA DTQTVRVAYS EDLFELGSVP QVLSAVAGNI FSMKIVDNLR LQDITFPKSM 

       130        140        150        160        170        180 
LREFEGPNFG LPGVRDIVGV KDRPLVGTIV KPKVGLTSEM HAEVAYNAFA GGCDLVKDDE 

       190        200        210        220        230        240 
NLTDQKFNGF EKRAELTLKI AEKAEAETGE RKMYLCNITA PTCEEMIRRL HVLKDLGASY 

       250        260        270        280        290        300 
AMIDIVPTGW TALQTLREAA ADEGLALHAH RCMHSAFTRN PRHGVSMLLV AKLCRLIGLD 

       310        320        330        340        350        360 
QLHIGTVVGK MHGDKDEVLS IRDECVLDTV PADPEQHVLA QDWGGLKPMF PVASGGLAPT 

       370        380        390        400        410        420 
MIPDLYSIFG KEVIMQFGGG IHAHPMGTAA GAAACRQALE ASLEGISLQD YAKDHKELEA 


ALGKWLEK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity." Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W., Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J., Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P. Birren B. Genome Res. 12:532-542(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35395 / DSM 2834 / JCM 12185 / C2A.
[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 35395 / DSM 2834 / JCM 12185 / C2A.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE010299 Genomic DNA. Translation: AAM07894.1.
RefSeq	NP_619414.1. NC_003552.1.
3D structure databases
ProteinModelPortal	Q8THG2.
ModBase	Search...
Protein-protein interaction databases
STRING	188937.MA4555.
Proteomic databases
PRIDE	Q8THG2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAM07894; AAM07894; MA_4555.
GeneID	1476449.
KEGG	mac:MA4555.
Phylogenomic databases
eggNOG	COG1850.
KO	K01601.
OMA	HRAMHAA.
ProtClustDB	PRK04208.
Enzyme and pathway databases
BioCyc	MACE188937:GI2O-4620-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_METAC

Accession

Primary (citable) accession number: Q8THG2

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2003
Last sequence update:	June 1, 2002
Last modified:	May 1, 2013
This is version 79 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

Proteomic databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents