(data stored in ACNUC7421 zone)

SWISSPROT: Q3KJM7_PSEPF

ID   Q3KJM7_PSEPF            Unreviewed;       275 AA.
AC   Q3KJM7;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   08-MAY-2019, entry version 89.
DE   RecName: Full=3'(2'),5'-bisphosphate nucleotidase CysQ {ECO:0000256|HAMAP-Rule:MF_02095};
DE            EC=3.1.3.7 {ECO:0000256|HAMAP-Rule:MF_02095};
DE   AltName: Full=3'(2'),5-bisphosphonucleoside 3'(2')-phosphohydrolase {ECO:0000256|HAMAP-Rule:MF_02095};
DE   AltName: Full=3'-phosphoadenosine 5'-phosphate phosphatase {ECO:0000256|HAMAP-Rule:MF_02095};
DE            Short=PAP phosphatase {ECO:0000256|HAMAP-Rule:MF_02095};
GN   Name=cysQ {ECO:0000256|HAMAP-Rule:MF_02095,
GN   ECO:0000313|EMBL:ABA72029.1};
GN   OrderedLocusNames=Pfl01_0285 {ECO:0000313|EMBL:ABA72029.1};
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922 {ECO:0000313|EMBL:ABA72029.1, ECO:0000313|Proteomes:UP000002704};
RN   [1] {ECO:0000313|EMBL:ABA72029.1, ECO:0000313|Proteomes:UP000002704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1 {ECO:0000313|EMBL:ABA72029.1,
RC   ECO:0000313|Proteomes:UP000002704};
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
CC   -!- FUNCTION: Converts adenosine-3',5'-bisphosphate (PAP) to AMP.
CC       {ECO:0000256|HAMAP-Rule:MF_02095}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine 3',5'-bisphosphate + H2O = AMP + phosphate;
CC         Xref=Rhea:RHEA:10040, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58343, ChEBI:CHEBI:456215; EC=3.1.3.7;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02095};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_02095};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_02095}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_02095}; Cytoplasmic side {ECO:0000256|HAMAP-
CC       Rule:MF_02095}.
CC   -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC       CysQ family. {ECO:0000256|HAMAP-Rule:MF_02095}.
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DR   EMBL; CP000094; ABA72029.1; -; Genomic_DNA.
DR   STRING; 205922.Pfl01_0285; -.
DR   EnsemblBacteria; ABA72029; ABA72029; Pfl01_0285.
DR   KEGG; pfo:Pfl01_0285; -.
DR   eggNOG; ENOG4108RNI; Bacteria.
DR   eggNOG; COG1218; LUCA.
DR   HOGENOM; HOG000282237; -.
DR   KO; K01082; -.
DR   OMA; KDWDMAA; -.
DR   Proteomes; UP000002704; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046854; P:phosphatidylinositol phosphorylation; IEA:InterPro.
DR   GO; GO:0006790; P:sulfur compound metabolic process; IEA:InterPro.
DR   HAMAP; MF_02095; CysQ; 1.
DR   InterPro; IPR006240; CysQ.
DR   InterPro; IPR020583; Inositol_monoP_metal-BS.
DR   InterPro; IPR000760; Inositol_monophosphatase-like.
DR   Pfam; PF00459; Inositol_P; 1.
DR   PRINTS; PR00377; IMPHPHTASES.
DR   TIGRFAMs; TIGR01331; bisphos_cysQ; 1.
DR   PROSITE; PS00629; IMP_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3KJM7.
DR   SWISS-2DPAGE; Q3KJM7.
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_02095};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_02095};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002704};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_02095,
KW   ECO:0000313|EMBL:ABA72029.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_02095};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_02095};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_02095}.
FT   REGION       90     93       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_02095}.
FT   METAL        68     68       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_02095}.
FT   METAL        88     88       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_02095}.
FT   METAL        88     88       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_02095}.
FT   METAL        90     90       Magnesium 1; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_02095}.
FT   METAL        91     91       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_02095}.
FT   METAL       220    220       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_02095}.
FT   BINDING      68     68       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02095}.
FT   BINDING     220    220       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02095}.
SQ   SEQUENCE   275 AA;  29097 MW;  7301A08F545EA561 CRC64;
     MNFPHPLMAP VVELALRAGE AILPFWRADV AVTAKSDDSP VTAADMAAHH VIVAGLTALD
     PSIPVLSEED ADIPQSVRAG WQRWWLVDPL DGTKEFISGS EEFTVNIALI ENGRVVFGVV
     SMPTNGRFYV GGAGLGAWRG DTGGTPVAIQ VRDVPGPGEA FTVVASRRHS SPEQERLLAG
     LSASLGELQL ANIGSSLKFC LLAEGAADCY PRLAPTSQWD TAAAQGVLEG AGGEVLDLNG
     DAFCYPPRDS LRNAFFLALP AKAAWRSKLL ELAHS
//

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