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Information on EC 3.1.12.1 - 5' to 3' exodeoxyribonuclease (nucleoside 3'-phosphate-forming) and Organism(s) Saccharolobus solfataricus and UniProt Accession Q97TX9

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Saccharolobus solfataricus
UNIPROT: Q97TX9 not found.
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The taxonomic range for the selected organisms is: Saccharolobus solfataricus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 3'-phosphates
Synonyms
sso0001, pcal_0546, cas4 nuclease, cas4-1, cas4-2, type i-c cas4, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5' to 3' single stranded DNA exonuclease
-
CRISPR-associated exonuclease Cas4
-
SSO0001
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
poly-dC10 + H2O
cytidine 3'-phosphate + ?
show the reaction diagram
-
-
-
?
single-stranded oligodeoxyribonucleotide + H2O
nucleoside 3'-phosphate + ?
show the reaction diagram
ssDNA + H2O
nucleoside 3'-phosphate + ?
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
iron-sulfur centre
K+
nuclease activity of the enzyme is maximal in the presence of 20-200 mM KCl
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
Cas4 proteins exhibit low sequence similarity among themselves and are currently classified into 2 main classes: DUF83 and DUF911. The genome of Sulfolobus solfataricus encodes five Cas4 like protein comprising low sequence similarity (below 30%). Out of them, SSO0001, SSO1392, and SSO1449 belong to DUF83 class, and SSO1391 and SSO1451 belong to DUF911 class. SSO1391 has been reported to show broad range cleavage specificity for cleaving ssDNA in both the directions (5'-3') and (3'-5') (DUF911). By contrast, members of DUF83 class cleave the ssDNA substrate only in the direction 5'-3'. The overall three-dimensional structural fold of DUF83Ss and DUF83Pc appears to be conserved. The separation of Cas4 proteins of DUF83 class into 2 separate branches hints at the possibility of specific sites which guide the evolutionary divergence between Cas4 proteins of the 2 clades, prediction of discriminative motifs among the two subclasses of DUF83 Cas4 proteins through motif analysis, overview. Divergence type I analyses of two clusters and their intra molecular hydrogen bonding with other residues
physiological function
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
170000
gel filtration
23239
x * 23239, calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 23239, calculated from sequence
decamer
crystallized at room temperature using the sitting drop vapour diffusion method. The crystal structure reveals a decameric toroid with a large 55 A diameter central channel formed by five tightly packed dimers
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the crystal structure reveals a decameric toroid with a large 55 A diameter central channel formed by five tightly packed dimers
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C188A
the mutant protein is inactive in both binding and cleavage of ssDNA. It forms various protein aggregates
C191A
the mutant protein is inactive in both binding and cleavage of ssDNA. It forms various protein aggregates
C32A
the mutant protein is inactive in both binding and cleavage of ssDNA. It forms various protein aggregates
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, enzyme loses colour and activity over several days
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli Posetta DE3
gene SSO0001, phylogenetic analysis and tree
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lemak, S.; Beloglazova, N.; Nocek, B.; Skarina, T.; Flick, R.; Brown, G.; Popovic, A.; Joachimiak, A.; Savchenko, A.; Yakunin, A.F.
Toroidal structure and DNA cleavage by the CRISPR-associated [4Fe-4S]-cluster containing Cas4 nuclease SSO0001 from Sulfolobus solfataricus
J. Am. Chem. Soc.
135
17476-17487
2013
Saccharolobus solfataricus (Q97TX9), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q97TX9)
Manually annotated by BRENDA team
Zhang, J.; Kasciukovic, T.; White, M.F.
The CRISPR associated protein Cas4 Is a 5' to 3' DNA exonuclease with an iron-sulfur cluster
PLoS One
7
e47232
2012
Saccharolobus solfataricus (Q97TX9), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q97TX9)
Manually annotated by BRENDA team
Kaushik, V.; Verma, V.V.; Goel, M.
Functional divergence and comparative in-silico study of Cas4 proteins of DUF83 class
J. Mol. Recognit.
31
e2694
2018
Pyrobaculum calidifontis (A3MTK6), Pyrobaculum calidifontis VA1 (A3MTK6), Saccharolobus solfataricus (Q97TX9), Saccharolobus solfataricus ATCC 35092 (Q97TX9), Saccharolobus solfataricus DSM 1617 (Q97TX9), Saccharolobus solfataricus JCM 11322 (Q97TX9), Saccharolobus solfataricus P2 (Q97TX9)
Manually annotated by BRENDA team