(data stored in SCRATCH zone)

SWISSPROT: D3VIJ7_XENNA

ID   D3VIJ7_XENNA            Unreviewed;       247 AA.
AC   D3VIJ7;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 46.
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:CBJ88547.1};
GN   OrderedLocusNames=XNC1_0473 {ECO:0000313|EMBL:CBJ88547.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS   NCIB 9965 / AN6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88547.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ88547.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
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; FN667742; CBJ88547.1; -; Genomic_DNA.
DR   RefSeq; WP_010845236.1; NC_014228.1.
DR   STRING; 406817.XNC1_0473; -.
DR   EnsemblBacteria; CBJ88547; CBJ88547; XNC1_0473.
DR   KEGG; xne:XNC1_0473; -.
DR   eggNOG; ENOG4108RNI; Bacteria.
DR   eggNOG; COG1218; LUCA.
DR   HOGENOM; HOG000282237; -.
DR   KO; K01082; -.
DR   OMA; KDWDMAA; -.
DR   Proteomes; UP000008075; 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   TIGRFAMs; TIGR01331; bisphos_cysQ; 1.
DR   PROSITE; PS00629; IMP_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3VIJ7.
DR   SWISS-2DPAGE; D3VIJ7.
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:UP000008075};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_02095};
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:UP000008075}.
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       206    206       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_02095}.
FT   BINDING      64     64       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02095}.
FT   BINDING     206    206       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02095}.
SQ   SEQUENCE   247 AA;  27320 MW;  3636FF99A2AB7E08 CRC64;
     MLQQICQLAR EAGAAIMEVY QAEQPLQVEH KTDDSPVTAA DIAAHKIIKA GLLRIAPDIP
     LLSEEDPPVW EERKNWRRYW LVDPLDGTKE FIRRNGEFTV NIALIEDGVP VMGVVYVPVQ
     NVLYSGQGHQ ARKEANGQIL PIKVISAALP VVVVSRSHRD DEELQDYLSQ LGVHNTLSIG
     SSLKFCMVAE GKAQLYPRFG PTNIWDTGAG HAVAIAAGAH VTDWEGKTLN YSPRESFLNP
     GFRVSIF
//

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