(data stored in ACNUC7421 zone)

SWISSPROT: Q5LWI1_RUEPO

ID   Q5LWI1_RUEPO            Unreviewed;       265 AA.
AC   Q5LWI1;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   08-MAY-2019, entry version 80.
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:AAV93370.1};
GN   OrderedLocusNames=SPO0039 {ECO:0000313|EMBL:AAV93370.1};
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS   (Silicibacter pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV93370.1, ECO:0000313|Proteomes:UP000001023};
RN   [1] {ECO:0000313|EMBL:AAV93370.1, ECO:0000313|Proteomes:UP000001023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E.,
RA   Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., Deboy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
RN   [2] {ECO:0000313|EMBL:AAV93370.1, ECO:0000313|Proteomes:UP000001023}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
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; CP000031; AAV93370.1; -; Genomic_DNA.
DR   RefSeq; WP_011045811.1; NC_003911.12.
DR   STRING; 246200.SPO0039; -.
DR   EnsemblBacteria; AAV93370; AAV93370; SPO0039.
DR   KEGG; sil:SPO0039; -.
DR   eggNOG; ENOG4108RNI; Bacteria.
DR   eggNOG; COG1218; LUCA.
DR   HOGENOM; HOG000282237; -.
DR   KO; K01082; -.
DR   OMA; KDWDMAA; -.
DR   OrthoDB; 1741160at2; -.
DR   BioCyc; RPOM246200:G1G48-39-MONOMER; -.
DR   Proteomes; UP000001023; 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   PRINTS; PR00377; IMPHPHTASES.
DR   TIGRFAMs; TIGR01331; bisphos_cysQ; 1.
DR   PROSITE; PS00630; IMP_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q5LWI1.
DR   SWISS-2DPAGE; Q5LWI1.
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:UP000001023};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_02095,
KW   ECO:0000313|EMBL:AAV93370.1};
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:UP000001023}.
FT   REGION       87     90       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_02095}.
FT   METAL        68     68       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_02095}.
FT   METAL        85     85       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_02095}.
FT   METAL        85     85       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_02095}.
FT   METAL        87     87       Magnesium 1; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_02095}.
FT   METAL        88     88       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_02095}.
FT   METAL       217    217       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_02095}.
FT   BINDING      68     68       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02095}.
FT   BINDING     217    217       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02095}.
SQ   SEQUENCE   265 AA;  28244 MW;  6CA5DDB34F1B59AE CRC64;
     MTYEELIPVI RRLALEAGDV IMSIYNADDF GVKVKSDSSP VTEADEAADA LISAGLRAAF
     PDILLVTEEQ AASHSQTGDT FLIVDPLDGT KEFINRRGDF TVNIALVENG TPTRGVVYAP
     AKGRMFYTLA DGSSVEETGG LDKETPGDLS PIRVAEADNA ALLVVASKSH RDQATEDYIG
     KYAVKDSKSA GSSLKFCLVA TGEADLYPRV GRTMEWDTAA GHAVLAGAGG KVVRFDNHQP
     LTYGKDGYAN PFFIAYAPSV TLKEA
//

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