ID L9U6P8_9GAMM Unreviewed; 257 AA.
AC L9U6P8;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
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 ORFNames=HALTITAN_2827 {ECO:0000313|EMBL:ELY20472.1};
OS Halomonas titanicae BH1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1204738 {ECO:0000313|EMBL:ELY20472.1, ECO:0000313|Proteomes:UP000011651};
RN [1] {ECO:0000313|EMBL:ELY20472.1, ECO:0000313|Proteomes:UP000011651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BH1 {ECO:0000313|EMBL:ELY20472.1,
RC ECO:0000313|Proteomes:UP000011651};
RX PubMed=23516210;
RA Sanchez-Porro C., de la Haba R.R., Cruz-Hernandez N., Gonzalez J.M.,
RA Reyes-Guirao C., Navarro-Sampedro L., Carballo M., Ventosa A.;
RT "Draft Genome of the Marine Gammaproteobacterium Halomonas titanicae.";
RL Genome Announc. 1:E0008313-E0008313(2013).
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|HAMAP-Rule:MF_02095}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELY20472.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AOPO01000017; ELY20472.1; -; Genomic_DNA.
DR RefSeq; WP_009288294.1; NZ_AOPO01000017.1.
DR AlphaFoldDB; L9U6P8; -.
DR PATRIC; fig|1204738.3.peg.4260; -.
DR Proteomes; UP000011651; Unassembled WGS sequence.
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: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; IPR020583; Inositol_monoP_metal-BS.
DR InterPro; IPR000760; Inositol_monophosphatase-like.
DR NCBIfam; TIGR01331; bisphos_cysQ; 1.
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; PS00629; IMP_1; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_02095};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_02095};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_02095};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_02095};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_02095};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_02095}.
FT BINDING 69
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02095"
FT BINDING 69
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02095"
FT BINDING 88
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02095"
FT BINDING 88
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02095"
FT BINDING 90..93
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02095"
FT BINDING 90
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02095"
FT BINDING 91
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02095"
FT BINDING 216
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02095"
FT BINDING 216
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02095"
SQ SEQUENCE 257 AA; 27452 MW; 5DC9A9152F1AF0AD CRC64;
MALIDQALLD AVEGIAREAG DAIMSVYARE FSVEEKEDKS PLTEADKAAH NVIVRSLQAL
PVQIPILSEE DIEGFSGADA EGRYWLVDPL DGTKEFIKRN GEFTVNIALI ENGKPVLGVV
TAPALEVGYV AARGLGAFKV EADGSRKAIS VAGKPKEGVT WRVVGSRSHP SPDLAAWLEQ
LGEHTMLPMG SSLKLCIIAE GFADAYPRLG PTCLWDTGAA HAVVLEAGGR VETLEGTALS
YANPSEKLNP YFVVWGH
//
