ID A0A163M7A2_DIDRA Unreviewed; 410 AA.
AC A0A163M7A2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=3'(2'),5'-bisphosphate nucleotidase {ECO:0000256|ARBA:ARBA00012633};
DE EC=3.1.3.7 {ECO:0000256|ARBA:ARBA00012633};
GN ORFNames=EKO05_0006014 {ECO:0000313|EMBL:UPX15570.1}, EKO05_004826
GN {ECO:0000313|EMBL:KAF9708749.1}, ST47_g379
GN {ECO:0000313|EMBL:KZM28462.1};
OS Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS rabiei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX NCBI_TaxID=5454 {ECO:0000313|EMBL:KZM28462.1, ECO:0000313|Proteomes:UP000076837};
RN [1] {ECO:0000313|EMBL:KZM28462.1, ECO:0000313|Proteomes:UP000076837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ArDII {ECO:0000313|EMBL:KZM28462.1,
RC ECO:0000313|Proteomes:UP000076837};
RX PubMed=27091329; DOI=10.1038/srep24638;
RA Verma S., Gazara R.K., Nizam S., Parween S., Chattopadhyay D., Verma P.K.;
RT "Draft genome sequencing and secretome analysis of fungal phytopathogen
RT Ascochyta rabiei provides insight into the necrotrophic effector
RT repertoire.";
RL Sci. Rep. 6:24638-24638(2016).
RN [2] {ECO:0000313|EMBL:KAF9708749.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:KAF9708749.1};
RA Syme R.A., Farfan-Caceres L., Lichtenzveig J.;
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAF9708749.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:KAF9708749.1};
RX PubMed=32345704; DOI=10.1534/g3.120.401265;
RA Shah R.M., Williams A.H., Hane J.K., Lawrence J.A., Farfan-Caceres L.M.,
RA Debler J.W., Oliver R.P., Lee R.C.;
RT "Reference Genome Assembly for Australian Ascochyta rabiei Isolate
RT ArME14.";
RL G3 (Bethesda) 10:2131-2140(2020).
RN [4] {ECO:0000313|EMBL:KAF9708749.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:KAF9708749.1};
RA Shah R.M., Williams A.H., Hane J.K., Lawrence J.A., Farfan-Caceres L.M.,
RA Debler J.W., Oliver R.P., Lee R.C.;
RL Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:UPX15570.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:UPX15570.1};
RA Mobegi F.M., Debler J.W.D., Lee R.C.L.;
RL Submitted (MAR-2022) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00001625};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000256|ARBA:ARBA00009759}.
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DR EMBL; RYYQ01000008; KAF9708749.1; -; Genomic_DNA.
DR EMBL; JYNV01000015; KZM28462.1; -; Genomic_DNA.
DR EMBL; CP095296; UPX15570.1; -; Genomic_DNA.
DR STRING; 5454.A0A163M7A2; -.
DR OrthoDB; 5486961at2759; -.
DR Proteomes; UP000076837; Unassembled WGS sequence.
DR Proteomes; UP000617380; Chromosome 9.
DR GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0006790; P:sulfur compound metabolic process; IEA:InterPro.
DR CDD; cd01517; PAP_phosphatase; 1.
DR Gene3D; 3.40.190.80; -; 1.
DR Gene3D; 3.30.540.10; Fructose-1,6-Bisphosphatase, subunit A, domain 1; 1.
DR InterPro; IPR006239; Bisphos_HAL2.
DR InterPro; IPR020583; Inositol_monoP_metal-BS.
DR InterPro; IPR000760; Inositol_monophosphatase-like.
DR InterPro; IPR020550; Inositol_monophosphatase_CS.
DR NCBIfam; TIGR01330; bisphos_HAL2; 1.
DR PANTHER; PTHR43200:SF6; 3'(2'),5'-BISPHOSPHATE NUCLEOTIDASE; 1.
DR PANTHER; PTHR43200; PHOSPHATASE; 1.
DR Pfam; PF00459; Inositol_P; 1.
DR SUPFAM; SSF56655; Carbohydrate phosphatase; 1.
DR PROSITE; PS00629; IMP_1; 1.
DR PROSITE; PS00630; IMP_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000076837}.
SQ SEQUENCE 410 AA; 43525 MW; E55D3DB8BC6D8308 CRC64;
MPPTAPYRYF FLAALVLASA ILQPTAFFRS AARLFQWKQH LPLSPALDAN RTLHAMAYDR
ELELALLAVQ RASILTKSVY SSHSKGTLTK TDSSPVTIGD FGAQALIIAS IKSAFPDDEV
VGEEDADDLR SNADLKQLVW DLVQQARLSD AASEHKIGGP IKSADDMLTA LDSGASPGGN
KGRIWALDPI DGTKGFLRGG QYAVCLALMV DGVPTVGVIG CPNLPVDDKA PLDSNIGTDA
DDKEGKGVLF GAVKGQGATS RALTAGKLEP PTTIHMSPLP DVAQATFCES VEAAHSSHGD
QADIAKKLGI TKHSVRMDSQ AKYCSIARGA GDLYLRLPTS KTYQEKIWDH AAGVVLVQEA
GGEVTDAWGK TLNFGMGRTL KENKGIIAAP KSVHAQVIEV VKEVLSAKKD
//
