AC   MF_00528;
DC   Protein; auto
TR   HAMAP; MF_00528; -; 1; level=0
XX
Names: Maf
XX
case <FTGroup:1>
ID   NTPPA
DE   RecName: Full=dTTP/UTP pyrophosphatase;
DE            Short=dTTPase/UTPase;
DE            EC=3.6.1.9;
DE   AltName: Full=Nucleoside triphosphate pyrophosphatase;
DE   AltName: Full=Nucleotide pyrophosphatase;
DE            Short=Nucleotide PPase;
else case <FTGroup:2>
ID   NTPPB
DE   RecName: Full=7-methyl-GTP pyrophosphatase;
DE            Short=m(7)GTP pyrophosphatase;
DE            EC=3.6.1.-;
else
ID   NTPP
DE   RecName: Full=Nucleoside triphosphate pyrophosphatase;
DE            EC=3.6.1.9;
DE   AltName: Full=Nucleotide pyrophosphatase;
DE            Short=Nucleotide PPase;
end case
XX
case <FTGroup:1>
CC   -!- FUNCTION: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP
CC       and UTP. May have a dual role in cell division arrest and in preventing
CC       the incorporation of modified nucleotides into cellular nucleic acids.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dTTP + H2O = diphosphate + dTMP + H(+); Xref=Rhea:RHEA:28534,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:37568, ChEBI:CHEBI:63528; EC=3.6.1.9;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + UTP = diphosphate + H(+) + UMP; Xref=Rhea:RHEA:29395,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:46398, ChEBI:CHEBI:57865; EC=3.6.1.9;
else case <FTGroup:2>
CC   -!- FUNCTION: Nucleoside triphosphate pyrophosphatase that hydrolyzes 7-
CC       methyl-GTP (m(7)GTP). May have a dual role in cell division arrest and
CC       in preventing the incorporation of modified nucleotides into cellular
CC       nucleic acids.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(7)-methyl-GTP = diphosphate + H(+) + N(7)-methyl-GMP;
CC         Xref=Rhea:RHEA:58744, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58285, ChEBI:CHEBI:87133;
else
CC   -!- FUNCTION: Nucleoside triphosphate pyrophosphatase. May have a dual role
CC       in cell division arrest and in preventing the incorporation of modified
CC       nucleotides into cellular nucleic acids.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC         phosphate + diphosphate + H(+); Xref=Rhea:RHEA:23996,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.9;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + H2O = a 2'-
CC         deoxyribonucleoside 5'-phosphate + diphosphate + H(+);
CC         Xref=Rhea:RHEA:44644, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:65317; EC=3.6.1.9;
end case
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
case <FTGroup:1>
CC   -!- SIMILARITY: Belongs to the Maf family. YhdE subfamily.
else case <FTGroup:2>
CC   -!- SIMILARITY: Belongs to the Maf family. YceF subfamily.
else
CC   -!- SIMILARITY: Belongs to the Maf family.
end case
XX
DR   Pfam; PF02545; Maf; 1; trigger=no
DR   NCBIfam; TIGR00172; maf; 1; trigger=no
DR   PIRSF; PIRSF006305; Maf; 1; trigger=no
XX
KW   Cytoplasm
KW   Hydrolase
KW   Nucleotide metabolism
XX
GO   GO:0016462; F:pyrophosphatase activity
GO   GO:0005737; C:cytoplasm
XX
FT   From: NTPPA_ECOLI (P25536)
FT   ACT_SITE        70
FT                   /note="Proton acceptor"
FT   Condition: D
FT   SITE            12
FT                   /note="Important for substrate specificity"
FT   Optional; Group: 1; Condition: R
FT   SITE            12
FT                   /note="Important for substrate specificity"
FT   Optional; Group: 2; Condition: [WYF]
FT   SITE            71
FT                   /note="Important for substrate specificity"
FT   Optional; Group: 1; Condition: [TS]
FT   SITE            71
FT                   /note="Important for substrate specificity"
FT   Optional; Group: 2; Condition: Q
FT   SITE            153
FT                   /note="Important for substrate specificity"
FT   Optional; Group: 1; Condition: Q
FT   SITE            153
FT                   /note="Important for substrate specificity"
FT   Optional; Group: 2; Condition: E
XX
Size: 160-350;
Related: None;
Template: P25536; Q02169; P0A729; P58627; Q99210;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: <Nudix hydrolase>
Duplicate: in ACIAD, AGRFC, ALCBS, ALKEH, AROAE, BARHE, BARQU, BDEBA, BORA1,
 BORBR, BORPA, BORPE, BRADU, BRUA2, BRUAB, BRUME, BRUSU, BURO1, BURMA, BRUP1,
 BURPS, BURL3, BURTA, PARXL, CAUVC, CHRSD, CHRVO, COLP3, DECAR, ECO57, ECOL5,
 ECOLI, ECOUT, PECAS, GLUOX, GRABC, HAHCH, HYPNA, IDILO, JANSC, MAGSA, MARMM,
 CHESB, METCA, METFK, MYXXD, NEIG1, NEIMA, NEIMB, NITEU, NITHX, NITMU, NITOC,
 NITWN, NOVAD, SYNC1, PHOLL, PHOPR, POLSJ, PSE14, PSEA6, PSEAE, PSEF5, PSET1,
 PSEPF, PSEPK, PSESM, PSEU2, CUPPJ, CUPMC, RALN1, RHIEC, RHIJ3, RHILO, RHIME,
 ALBFT, RHOP2, RHOPA, RHOPB, RHOPS, RHORT, CERS4, ROSDO, SACD2, SALCH, SALPA,
 SALTI, SALTY, SHEDO, SHEFN, SHEON, SHESM, SHESR, SHIBS, SHIFL, SHISS, RUEPO,
 RUEST, SPHAL, HYDCU, THIDA, VIBCH, VIBPA, ALIF1, VIBVU, VIBVY, XANAC, XANC8,
 XANCP, XANOM, XANOR, YERPA, YERPE, YERPN, YERPS, ZYMMO
Plasmid: in RUEPO, RUEST
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.
XX
# Revision 1.66 2023/11/29
//