DPNPH_ARATH
ID DPNPH_ARATH Reviewed; 373 AA.
AC Q38945; O48892;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=PAP-specific phosphatase HAL2-like;
DE Short=AtAHL {ECO:0000303|PubMed:10205895};
DE AltName: Full=3'(2'),5'-bisphosphate nucleotidase;
DE EC=3.1.3.7 {ECO:0000269|PubMed:10205895};
DE AltName: Full=3'(2'),5-bisphosphonucleoside 3'(2')-phosphohydrolase;
DE AltName: Full=DPNPase;
DE AltName: Full=Halotolerance protein;
GN Name=AHL; OrderedLocusNames=At5g54390; ORFNames=F24B18.1;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Cheong J.-J., Kwon H.-B., Goodman H.M.;
RT "A cDNA clone encoding Arabidopsis HAL2-like (AHL) protein.";
RL (er) Plant Gene Register PGR96-042(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Landsberg erecta;
RA Cheong J.-J., Kwon H.-B., Goodman H.M.;
RT "Arabidopsis Ahl encodes a PAP-specific phosphatase that is sensitive to
RT toxic metal ions.";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Columbia;
RX PubMed=10205895; DOI=10.1046/j.1365-313x.1999.00385.x;
RA Gil-Mascarell R., Lopez-Coronado J.M., Belles J.M., Serrano R.,
RA Rodriguez P.L.;
RT "The Arabidopsis HAL2-like gene family includes a novel sodium-sensitive
RT phosphatase.";
RL Plant J. 17:373-383(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to
CC adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine
CC 5'- phosphate (PAP) to AMP (PubMed:10205895). May regulate the flux of
CC sulfur in the sulfur-activation pathway by converting PAPS to APS (By
CC similarity). Prevents both the toxicity of PAP on RNA processing
CC enzymes as well as the product inhibition by PAP of sulfate
CC conjugation. {ECO:0000250|UniProtKB:Q42546,
CC ECO:0000269|PubMed:10205895}.
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:0000269|PubMed:10205895};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10041;
CC Evidence={ECO:0000269|PubMed:10205895};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q42546};
CC -!- ACTIVITY REGULATION: Inhibited by Li(+) (IC(50)=10 mM), Na(+)
CC (IC(50)=50 mM) and Ca(2+) (IC(50)=0.06 mM).
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=160 uM for PAP {ECO:0000269|PubMed:10205895};
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and
CC siliques.
CC -!- MISCELLANEOUS: Substrate preference is 3'-phosphoadenosine 5'-phosphate
CC (PAP) = adenosine 3'-phosphate 5'-phosphosulfate (PAPS). No activity
CC observed against 3' or 5'-AMP, inositol mono and diphosphates and
CC fructose-1,6-bisphosphate. {ECO:0000269|PubMed:10205895}.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000305}.
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DR EMBL; U55205; AAB52964.1; -; mRNA.
DR EMBL; AF016644; AAB94051.1; -; Genomic_DNA.
DR EMBL; AB026634; BAA97512.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96491.1; -; Genomic_DNA.
DR EMBL; AY045848; AAK76522.1; -; mRNA.
DR EMBL; AY091377; AAM14316.1; -; mRNA.
DR EMBL; AY086488; AAM63490.1; -; mRNA.
DR RefSeq; NP_200250.1; NM_124819.3.
DR AlphaFoldDB; Q38945; -.
DR SMR; Q38945; -.
DR BioGRID; 20771; 5.
DR IntAct; Q38945; 4.
DR STRING; 3702.AT5G54390.1; -.
DR PaxDb; Q38945; -.
DR PRIDE; Q38945; -.
DR ProteomicsDB; 220405; -.
DR EnsemblPlants; AT5G54390.1; AT5G54390.1; AT5G54390.
DR GeneID; 835527; -.
DR Gramene; AT5G54390.1; AT5G54390.1; AT5G54390.
DR KEGG; ath:AT5G54390; -.
DR Araport; AT5G54390; -.
DR TAIR; locus:2147279; AT5G54390.
DR eggNOG; KOG1528; Eukaryota.
DR HOGENOM; CLU_033446_3_0_1; -.
DR InParanoid; Q38945; -.
DR OMA; WPNSARL; -.
DR OrthoDB; 1096950at2759; -.
DR PhylomeDB; Q38945; -.
DR BioCyc; ARA:AT5G54390-MON; -.
DR BRENDA; 3.1.3.7; 399.
DR PRO; PR:Q38945; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q38945; baseline and differential.
DR Genevisible; Q38945; AT.
DR GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042578; F:phosphoric ester hydrolase activity; IBA:GO_Central.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IEA:InterPro.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0000103; P:sulfate assimilation; IBA:GO_Central.
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 Pfam; PF00459; Inositol_P; 1.
DR TIGRFAMs; TIGR01330; bisphos_HAL2; 1.
DR PROSITE; PS00629; IMP_1; 1.
DR PROSITE; PS00630; IMP_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Hydrolase; Lithium; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..373
FT /note="PAP-specific phosphatase HAL2-like"
FT /id="PRO_0000142534"
FT BINDING 77
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 146..149
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 310
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 310
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 107..108
FT /note="QN -> SK (in Ref. 2; AAB94051)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 373 AA; 39374 MW; CC0B3F3487859EC8 CRC64;
MAVDSLETEI DTAVRVVHLA SSLCVKVQEK LHLPNGGHVK SKDDDSPVTV ADFGVQAIVS
WVLAEVFGDQ NLSIVAEEDT ETLSEADSLG LLGAVSNAVN EALSEAQNYG LPKPVKPLGS
SEILKAISRC NSVGGPKGRH WVLDPVDGTL GFVRGDQYAV ALALIENGKV LLGVLGCPNY
PVKKECLSNG CNQAMKTKAV AGSVSKGCVM YAKRGSGQAW MQPLIVGGIP ESATLLKVSS
VDDPVLATVC EPVERANSNH LFTAGLANSM GVRKQPMRVY SMVKYAAIAR GDAEVFMKFA
QSSYKEKIWD HAAGVVIVEE AGGVVTDAGG RNLDFSKGVY LEGLDRGIIA CSGQVLHEKI
IGAVYASWES SSL
