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Database: UniProt
Entry: D7A4M5_STAND
LinkDB: D7A4M5_STAND
Original site: D7A4M5_STAND 
ID   D7A4M5_STAND            Unreviewed;       275 AA.
AC   D7A4M5;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 61.
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=Snov_2593 {ECO:0000313|EMBL:ADH89888.1};
OS   Starkeya novella (strain ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM
OS   12100 / NBRC 12443 / NCIMB 10456).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Xanthobacteraceae; Starkeya.
OX   NCBI_TaxID=639283 {ECO:0000313|EMBL:ADH89888.1, ECO:0000313|Proteomes:UP000006633};
RN   [1] {ECO:0000313|EMBL:ADH89888.1, ECO:0000313|Proteomes:UP000006633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM 12100 / NBRC
RC   12443 / NCIMB 10456 {ECO:0000313|Proteomes:UP000006633};
RX   PubMed=23450099; DOI=10.4056/sigs.3006378;
RA   Kappler U., Davenport K., Beatson S., Lucas S., Lapidus A., Copeland A.,
RA   Berry K.W., Glavina Del Rio T., Hammon N., Dalin E., Tice H., Pitluck S.,
RA   Richardson P., Bruce D., Goodwin L.A., Han C., Tapia R., Detter J.C.,
RA   Chang Y.J., Jeffries C.D., Land M., Hauser L., Kyrpides N.C., Goker M.,
RA   Ivanova N., Klenk H.P., Woyke T.;
RT   "Complete genome sequence of the facultatively chemolithoautotrophic and
RT   methylotrophic alpha Proteobacterium Starkeya novella type strain (ATCC
RT   8093(T)).";
RL   Stand. Genomic Sci. 7:44-58(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;
CC         Evidence={ECO:0000256|HAMAP-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-Rule:MF_02095}.
CC   -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily. CysQ
CC       family. {ECO:0000256|ARBA:ARBA00005289, ECO:0000256|HAMAP-
CC       Rule:MF_02095}.
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DR   EMBL; CP002026; ADH89888.1; -; Genomic_DNA.
DR   RefSeq; WP_013167392.1; NC_014217.1.
DR   AlphaFoldDB; D7A4M5; -.
DR   STRING; 639283.Snov_2593; -.
DR   KEGG; sno:Snov_2593; -.
DR   eggNOG; COG1218; Bacteria.
DR   HOGENOM; CLU_044118_3_0_5; -.
DR   OMA; IYNRPDP; -.
DR   OrthoDB; 9785695at2; -.
DR   Proteomes; UP000006633; 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 phosphate biosynthetic process; IEA:InterPro.
DR   GO; GO:0006790; P:sulfur compound metabolic process; IEA:InterPro.
DR   CDD; cd01638; CysQ; 1.
DR   Gene3D; 3.40.190.80; -; 1.
DR   Gene3D; 3.30.540.10; Fructose-1,6-Bisphosphatase, subunit A, domain 1; 1.
DR   HAMAP; MF_02095; CysQ; 1.
DR   InterPro; IPR006240; CysQ.
DR   InterPro; IPR000760; Inositol_monophosphatase-like.
DR   InterPro; IPR020550; Inositol_monophosphatase_CS.
DR   PANTHER; PTHR43028; 3'(2'),5'-BISPHOSPHATE NUCLEOTIDASE 1; 1.
DR   PANTHER; PTHR43028:SF5; 3'(2'),5'-BISPHOSPHATE NUCLEOTIDASE 1; 1.
DR   Pfam; PF00459; Inositol_P; 1.
DR   PRINTS; PR00377; IMPHPHTASES.
DR   SUPFAM; SSF56655; Carbohydrate phosphatase; 1.
DR   PROSITE; PS00630; IMP_2; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519, ECO:0000256|HAMAP-
KW   Rule:MF_02095};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_02095}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_02095};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_02095};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02095};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_02095}.
FT   BINDING         74
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02095"
FT   BINDING         74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02095"
FT   BINDING         99
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02095"
FT   BINDING         99
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02095"
FT   BINDING         101..104
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02095"
FT   BINDING         101
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02095"
FT   BINDING         102
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02095"
FT   BINDING         231
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02095"
FT   BINDING         231
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02095"
SQ   SEQUENCE   275 AA;  27737 MW;  53C12573BCC250BF CRC64;
     MSLPSSSAAD LSLLAALAQA SLKAGEVILR IRAEGITVNA KSDQSPVTAA DLAAEELLHA
     ELARILPGVP VIAEEAVAQG KGEALGTGEA PADAFLLVDP LDGTKEFIGA SGEFTVNIGL
     VIGGVPAFGI VLAPAVARLY AGMTTAAGGA AFAAGLEPDA GLWTPIRCRP TPERGLVAVA
     SRSHPDAGTE AILAELDVAE RISCGSALKF GLVAEGRADI YPRLGTVCEW DVAAGHALVR
     AAGGSVCRPD GSPLPYGRTE AAYRVHGFIA RGAAA
//
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