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HAMAP rule MF_00528

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General rule information [?]

Accession MF_00528
Dates 18-JAN-2002 (Created)
1-JUN-2023 (Last updated, Version 62)
Name Maf
Scope(s) Bacteria
Archaea
Template(s) P25536 (NTPPA_ECOLI); Q02169 (NTPPA_BACSU); P0A729 (NTPPB_ECOLI); P58627 (NTPPB_SALTY); Q99210 (NTPPA_YEAST); [ Recover all ]
Triggered by HAMAP; MF_00528 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

case <FTGroup:1>
Identifier NTPPA
Protein name RecName: Full=dTTP/UTP pyrophosphatase;
                 Short=dTTPase/UTPase;
                 EC=3.6.1.9;
AltName: Full=Nucleoside triphosphate pyrophosphatase;
AltName: Full=Nucleotide pyrophosphatase;
                 Short=Nucleotide PPase;
else case <FTGroup:2>
Identifier NTPPB
Protein name RecName: Full=7-methyl-GTP pyrophosphatase;
                 Short=m(7)GTP pyrophosphatase;
                 EC=3.6.1.-;
else
Identifier NTPP
Protein name RecName: Full=Nucleoside triphosphate pyrophosphatase;
                 EC=3.6.1.9;
AltName: Full=Nucleotide pyrophosphatase;
                 Short=Nucleotide PPase;
end case

Comments [?]

case <FTGroup:1>
FUNCTIONNucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
CATALYTIC ACTIVITY Reaction=dTTP + H2O = diphosphate + dTMP + H(+); Xref=Rhea:RHEA:28534, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:63528; EC=3.6.1.9;
CATALYTIC ACTIVITY Reaction=H2O + UTP = diphosphate + H(+) + UMP; Xref=Rhea:RHEA:29395, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:57865; EC=3.6.1.9;
else case <FTGroup:2>
FUNCTIONNucleoside triphosphate pyrophosphatase that hydrolyzes 7- methyl-GTP (m(7)GTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
CATALYTIC ACTIVITY Reaction=H2O + N(7)-methyl-GTP = diphosphate + H(+) + N(7)-methyl-GMP; Xref=Rhea:RHEA:58744, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:58285, ChEBI:CHEBI:87133;
else
FUNCTIONNucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
CATALYTIC ACTIVITY Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'- phosphate + diphosphate + H(+); Xref=Rhea:RHEA:23996, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.9;
CATALYTIC ACTIVITY Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + H2O = a 2'- deoxyribonucleoside 5'-phosphate + diphosphate + H(+); Xref=Rhea:RHEA:44644, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:65317; EC=3.6.1.9;
end case
COFACTOR Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
SUBCELLULAR LOCATIONCytoplasm.
case <FTGroup:1>
SIMILARITYBelongs to the Maf family. YhdE subfamily.
else case <FTGroup:2>
SIMILARITYBelongs to the Maf family. YceF subfamily.
else
SIMILARITYBelongs to the Maf family.
end case

Keywords [?]


Gene Ontology [?]

GO:0016462; Molecular function:pyrophosphatase activity
GO:0005737; Cellular component:cytoplasm

Cross-references [?]

Pfam PF02545; Maf; 1;
NCBIfam TIGR00172; maf; 1;
PIRSF PIRSF006305; Maf; 1;

Features [?]

From: NTPPA_ECOLI (P25536)
Key From To Description Tag Condition FTGroup
ACT_SITE 70 70 /note="Proton acceptor" D
SITE 12 12 /note="Important for substrate specificity" R 1
SITE 12 12 /note="Important for substrate specificity" [WYF] 2
SITE 71 71 /note="Important for substrate specificity" [TS] 1
SITE 71 71 /note="Important for substrate specificity" Q 2
SITE 153 153 /note="Important for substrate specificity" Q 1
SITE 153 153 /note="Important for substrate specificity" E 2

Additional information [?]

Size range 160-350 amino acids
Related rules None
Fusion Nter: None Cter: <Nudix hydrolase>
Comments Classification into YhdE and YceF subfamilies was done according to PubMed:24210219. Authors define two subfamily-specific motifs: R-T-Q for YhdE and W-Q-E for YceF (see FT SITE). Fusion with a possible Nudix hydrolase in BIFLO.



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