KEGG ENZYME: 5.6.1.7

ENZYME: 5.6.1.7

Entry

EC 5.6.1.7                  Enzyme

Name

chaperonin ATPase;
chaperonin

Class

Isomerases;
Isomerases altering macromolecular conformation;
Enzymes altering polypeptide conformation or assembly

Sysname

ATP phosphohydrolase (polypeptide-unfolding)

Reaction(IUBMB)

ATP + H2O + an unfolded polypeptide = ADP + phosphate + a folded polypeptide

Substrate

ATP [CPD:C00002];
H2O [CPD:C00001];
unfolded polypeptide

Product

ADP [CPD:C00008];
phosphate [CPD:C00009];
folded polypeptide

Comment

Multisubunit proteins with 2x7 (Type I, in most cells) or 2x8 (Type II, in Archaea) ATP-binding sites involved in maintaining an unfolded polypeptide structure before folding or entry into mitochondria and chloroplasts. Molecular masses of subunits ranges from 10-90 kDa. They are a subclass of molecular chaperones that are related to EC 5.6.1.5 (proteasome ATPase).

History

EC 5.6.1.7 created 2000 as EC 3.6.4.9, transferred 2018 to EC 5.6.1.7

Reference

1 [PMID:2897629]

Authors

Hemmingsen SM, Woolford C, van der Vies SM, Tilly K, Dennis DT, Georgopoulos CP, Hendrix RW, Ellis RJ.

Title

Homologous plant and bacterial proteins chaperone oligomeric protein assembly.

Journal

Nature 333:330-4 (1988)
DOI:10.1038/333330a0

Reference

2 [PMID:2577724]

Authors

Lubben TH, Donaldson GK, Viitanen PV, Gatenby AA

Title

Several proteins imported into chloroplasts form stable complexes with the GroEL-related chloroplast molecular chaperone.

Journal

Plant Cell 1:1223-30 (1989)
DOI:10.1105/tpc.1.12.1223

Reference

Authors

In: Ellis, R.J. (Ed.), The Chaperonins, Academic Press, San Diego, 1996

Reference

4 [PMID:9657960]

Authors

Ranson NA, White HE, Saibil HR.

Title

Chaperonins.

Journal

Biochem J 333 ( Pt 2):233-42 (1998)
DOI:10.1042/bj3330233

Other DBs

ExplorEnz - The Enzyme Database:

5.6.1.7

IUBMB Enzyme Nomenclature:

5.6.1.7

ExPASy - ENZYME nomenclature database:

5.6.1.7

BRENDA, the Enzyme Database:

5.6.1.7

All links

Protein sequence (48680)   
   UniProt (47561)   
   SWISS-PROT (1060)   
   RefSeq(pep) (16)   
   PDBSTR (43)   
DNA sequence (30)   
   RefSeq(nuc) (17)   
   GenBank (9)   
   EMBL (4)   
3D Structure (3)   
   PDB (3)   
Protein domain (8)   
   InterPro (8)   
All databases (48721)   

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