HAMAP rule MF_00528

General rule information [?]

Accession	MF_00528
Dates	18-JAN-2002 (Created) 3-SEP-2024 (Last updated, Version 67)
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>
FUNCTION	Nucleoside 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 = dTMP + diphosphate + 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=UTP + H2O = UMP + diphosphate + H(+); 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>
FUNCTION	Nucleoside 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=N(7)-methyl-GTP + H2O = N(7)-methyl-GMP + diphosphate + H(+); Xref=Rhea:RHEA:58744, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:58285, ChEBI:CHEBI:87133;
else
FUNCTION	Nucleoside 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 LOCATION	Cytoplasm.
case <FTGroup:1>
SIMILARITY	Belongs to the Maf family. YhdE subfamily.
else case <FTGroup:2>
SIMILARITY	Belongs to the Maf family. YceF subfamily.
else
SIMILARITY	Belongs to the Maf family.
end case

Keywords [?]

Cytoplasm

Hydrolase

Nucleotide metabolism

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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