(data stored in ACNUC7421 zone)

SWISSPROT: C5BF85_EDWI9

ID   C5BF85_EDWI9            Unreviewed;       246 AA.
AC   C5BF85;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   08-MAY-2019, entry version 57.
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   OrderedLocusNames=NT01EI_0433 {ECO:0000313|EMBL:ACR67671.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67671.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACR67671.1, ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|EMBL:ACR67671.1,
RC   ECO:0000313|Proteomes:UP000001485};
RX   PubMed=22247535; DOI=10.1128/JB.06522-11;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Banes M.M.,
RA   Lawrence M.L.;
RT   "Genome Sequence of Edwardsiella ictaluri 93-146, a Strain Associated
RT   with a Natural Channel Catfish Outbreak of Enteric Septicemia of
RT   Catfish.";
RL   J. Bacteriol. 194:740-741(2012).
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; CP001600; ACR67671.1; -; Genomic_DNA.
DR   RefSeq; WP_015869874.1; NC_012779.2.
DR   EnsemblBacteria; ACR67671; ACR67671; NT01EI_0433.
DR   GeneID; 7961258; -.
DR   KEGG; eic:NT01EI_0433; -.
DR   PATRIC; fig|634503.3.peg.392; -.
DR   eggNOG; ENOG4108RNI; Bacteria.
DR   eggNOG; COG1218; LUCA.
DR   HOGENOM; HOG000282237; -.
DR   KO; K01082; -.
DR   OMA; KDWDMAA; -.
DR   OrthoDB; 1741160at2; -.
DR   BioCyc; EICT634503:G1GVC-404-MONOMER; -.
DR   Proteomes; UP000001485; 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; IPR000760; Inositol_monophosphatase-like.
DR   InterPro; IPR020550; Inositol_monophosphatase_CS.
DR   Pfam; PF00459; Inositol_P; 1.
DR   TIGRFAMs; TIGR01331; bisphos_cysQ; 1.
DR   PROSITE; PS00630; IMP_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5BF85.
DR   SWISS-2DPAGE; C5BF85.
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:UP000001485};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_02095,
KW   ECO:0000313|EMBL:ACR67671.1};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485}.
FT   REGION       85     88       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_02095}.
FT   METAL        64     64       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_02095}.
FT   METAL        83     83       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_02095}.
FT   METAL        83     83       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_02095}.
FT   METAL        85     85       Magnesium 1; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_02095}.
FT   METAL        86     86       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_02095}.
FT   METAL       205    205       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_02095}.
FT   BINDING      64     64       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02095}.
FT   BINDING     205    205       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02095}.
SQ   SEQUENCE   246 AA;  26911 MW;  93AF8DD08CD7F0A5 CRC64;
     MLEQICQLAR DAGATIMAVY QGDQPLALAY KGDESPVTAA DLAAHEIIKA GLLRVTPLIP
     LLSEEEPPAW PQRRDWQRYW LVDPLDGTKE FLQRNGEFTV NIALIEQGIP TLGVVYVPTS
     GVLYCACGGK AWKEQDGVRM EIGVRNAIPP LVVISRSHGD AELTDYLQQL GEHQTMMVGS
     SLKFCLVAEG VAQLYPRFGP THIWDTAAGH AIALAAGAQV RDWQGKTLSY IPAESLLNPG
     FRVSLY
//

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