ID A0A0Q0GH93_9GAMM Unreviewed; 269 AA.
AC A0A0Q0GH93;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
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_2 {ECO:0000313|EMBL:KPZ71391.1};
GN Synonyms=cysQ {ECO:0000256|HAMAP-Rule:MF_02095};
GN ORFNames=AN944_01766 {ECO:0000313|EMBL:KPZ71391.1};
OS Shewanella sp. P1-14-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=1723761 {ECO:0000313|EMBL:KPZ71391.1, ECO:0000313|Proteomes:UP000050414};
RN [1] {ECO:0000313|EMBL:KPZ71391.1, ECO:0000313|Proteomes:UP000050414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1-14-1 {ECO:0000313|EMBL:KPZ71391.1,
RC ECO:0000313|Proteomes:UP000050414};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:KPZ71391.1}.
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DR EMBL; LKTL01000009; KPZ71391.1; -; Genomic_DNA.
DR RefSeq; WP_055024210.1; NZ_LKTL01000009.1.
DR AlphaFoldDB; A0A0Q0GH93; -.
DR PATRIC; fig|1723761.3.peg.1805; -.
DR Proteomes; UP000050414; 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; IPR000760; Inositol_monophosphatase-like.
DR NCBIfam; TIGR01331; bisphos_cysQ; 1.
DR PANTHER; PTHR43028; 3'(2'),5'-BISPHOSPHATE NUCLEOTIDASE 1; 1.
DR PANTHER; PTHR43028:SF7; 3'(2'),5'-BISPHOSPHATE NUCLEOTIDASE CYSQ; 1.
DR Pfam; PF00459; Inositol_P; 1.
DR PRINTS; PR00377; IMPHPHTASES.
DR SUPFAM; SSF56655; Carbohydrate phosphatase; 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|HAMAP-Rule:MF_02095, ECO:0000313|EMBL:KPZ71391.1};
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:UP000050414}.
FT BINDING 68
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02095"
FT BINDING 68
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 217
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02095"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02095"
SQ SEQUENCE 269 AA; 29396 MW; 016FAA477E545DD3 CRC64;
MKPEEVIEQV IKIATEAGQK IRDIYVKGDF DREIKSDNTP VTSADLAANE IICAGLAALT
PDIPILSEEA ADIPFEERAE WQRYWLVDPL DGTGEFIAGS GDFSVIIALV EHNRPVMGIV
YVPMTNVCYY AIAGLGAYKR DTKNEVRIMS RQIGDIEQSG LKLAVSRRQD PQSVLKLLSH
PNSCELVVLG GAALKSCLVA EGRADCYVRL GPTGEWDTGA AQIILEEAGG ALMDINLQPM
SYNERETLEN PNFIVVGSPS LAWDDILTK
//
