(data stored in ACNUC7421 zone)

SWISSPROT: A0KFB0_AERHH

ID   A0KFB0_AERHH            Unreviewed;       195 AA.
AC   A0KFB0;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 81.
DE   RecName: Full=dTTP/UTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_00528};
DE            Short=dTTPase/UTPase {ECO:0000256|HAMAP-Rule:MF_00528};
DE            EC=3.6.1.9 {ECO:0000256|HAMAP-Rule:MF_00528};
DE   AltName: Full=Nucleoside triphosphate pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_00528};
DE   AltName: Full=Nucleotide pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_00528};
DE            Short=Nucleotide PPase {ECO:0000256|HAMAP-Rule:MF_00528};
GN   Name=maf-1 {ECO:0000313|EMBL:ABK37586.1};
GN   OrderedLocusNames=AHA_0403 {ECO:0000313|EMBL:ABK37586.1};
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 /
OS   JCM 1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK37586.1, ECO:0000313|Proteomes:UP000000756};
RN   [1] {ECO:0000313|EMBL:ABK37586.1, ECO:0000313|Proteomes:UP000000756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240
RC   {ECO:0000313|Proteomes:UP000000756};
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
CC   -!- FUNCTION: Nucleoside triphosphate pyrophosphatase that hydrolyzes
CC       dTTP and UTP. May have a dual role in cell division arrest and in
CC       preventing the incorporation of modified nucleotides into cellular
CC       nucleic acids. {ECO:0000256|HAMAP-Rule:MF_00528}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + UTP = diphosphate + H(+) + UMP;
CC         Xref=Rhea:RHEA:29395, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:57865;
CC         EC=3.6.1.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00528};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dTTP + H2O = diphosphate + dTMP + H(+);
CC         Xref=Rhea:RHEA:28534, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:63528;
CC         EC=3.6.1.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00528};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00528,
CC         ECO:0000256|SAAS:SAAS01154128};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00528,
CC       ECO:0000256|SAAS:SAAS00965376}.
CC   -!- SIMILARITY: Belongs to the Maf family. YhdE subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00528}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00528}.
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DR   EMBL; CP000462; ABK37586.1; -; Genomic_DNA.
DR   RefSeq; WP_011704377.1; NC_008570.1.
DR   RefSeq; YP_854932.1; NC_008570.1.
DR   STRING; 380703.AHA_0403; -.
DR   EnsemblBacteria; ABK37586; ABK37586; AHA_0403.
DR   GeneID; 4487201; -.
DR   KEGG; aha:AHA_0403; -.
DR   PATRIC; fig|380703.7.peg.392; -.
DR   eggNOG; ENOG4108Z03; Bacteria.
DR   eggNOG; COG0424; LUCA.
DR   HOGENOM; HOG000241745; -.
DR   KO; K06287; -.
DR   OMA; RIDGDFY; -.
DR   BioCyc; AHYD380703:G1G7B-404-MONOMER; -.
DR   Proteomes; UP000000756; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0035529; F:NADH pyrophosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; IEA:InterPro.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00555; Maf; 1.
DR   Gene3D; 3.90.950.10; -; 1.
DR   HAMAP; MF_00528; Maf; 1.
DR   InterPro; IPR029001; ITPase-like_fam.
DR   InterPro; IPR003697; Maf-like.
DR   PANTHER; PTHR43213; PTHR43213; 1.
DR   Pfam; PF02545; Maf; 1.
DR   PIRSF; PIRSF006305; Maf; 1.
DR   SUPFAM; SSF52972; SSF52972; 1.
DR   TIGRFAMs; TIGR00172; maf; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0KFB0.
DR   SWISS-2DPAGE; A0KFB0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000756};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00528,
KW   ECO:0000256|SAAS:SAAS00965379};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00528,
KW   ECO:0000256|SAAS:SAAS01154120};
KW   Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_00528,
KW   ECO:0000256|SAAS:SAAS01154126};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000756}.
FT   ACT_SITE     75     75       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00528}.
FT   SITE         17     17       Important for substrate specificity.
FT                                {ECO:0000256|HAMAP-Rule:MF_00528}.
FT   SITE         76     76       Important for substrate specificity.
FT                                {ECO:0000256|HAMAP-Rule:MF_00528}.
FT   SITE        158    158       Important for substrate specificity.
FT                                {ECO:0000256|HAMAP-Rule:MF_00528}.
SQ   SEQUENCE   195 AA;  21463 MW;  D3F233A9D98AECB8 CRC64;
     MNKHNELQLY LASGSPRRHE LLTQLGYRFE VLKLDVPEQR EEGEKPQDYV CRLARDKATA
     GVAAAPTALP VLGADTIVVL GDRVLEKPSD LLDAKDMLEA LSGKVHQVMT AVALATPERC
     DVRLVTTNVA FRKLDEAEIE AYWRTGEPCD KAGAYAIQGI AGKFVSRIEG SYSAVVGLPL
     LETDLLIKHH LEQSR
//

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