ID A0A0D8XD15_DICVI Unreviewed; 1062 AA.
AC A0A0D8XD15;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Phosphatidylinositol-3,5-bisphosphate 3-phosphatase {ECO:0000256|ARBA:ARBA00032571};
DE EC=2.7.1.105 {ECO:0000256|ARBA:ARBA00012130};
DE EC=3.1.3.46 {ECO:0000256|ARBA:ARBA00013067};
DE EC=3.1.3.95 {ECO:0000256|ARBA:ARBA00012903};
DE AltName: Full=Phosphatidylinositol-3-phosphate phosphatase {ECO:0000256|ARBA:ARBA00031219};
GN ORFNames=DICVIV_11490 {ECO:0000313|EMBL:KJH42515.1};
OS Dictyocaulus viviparus (Bovine lungworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae; Dictyocaulus.
OX NCBI_TaxID=29172 {ECO:0000313|EMBL:KJH42515.1, ECO:0000313|Proteomes:UP000053766};
RN [1] {ECO:0000313|EMBL:KJH42515.1, ECO:0000313|Proteomes:UP000053766}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HannoverDv2000 {ECO:0000313|EMBL:KJH42515.1,
RC ECO:0000313|Proteomes:UP000053766};
RA Mitreva M.;
RT "Draft genome of the bovine lungworm Dictyocaulus viviparus.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053766}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HannoverDv2000 {ECO:0000313|Proteomes:UP000053766};
RX PubMed=26856411; DOI=10.1038/srep20316;
RA McNulty S.N., Strube C., Rosa B.A., Martin J.C., Tyagi R., Choi Y.J.,
RA Wang Q., Hallsworth Pepin K., Zhang X., Ozersky P., Wilson R.K.,
RA Sternberg P.W., Gasser R.B., Mitreva M.;
RT "Dictyocaulus viviparus genome, variome and transcriptome elucidate
RT lungworm biology and support future intervention.";
RL Sci. Rep. 6:20316-20316(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-
CC bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-5-phosphate) + phosphate; Xref=Rhea:RHEA:39019,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57795,
CC ChEBI:CHEBI:57923; EC=3.1.3.95;
CC Evidence={ECO:0000256|ARBA:ARBA00001669};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-
CC phosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol) + phosphate; Xref=Rhea:RHEA:12316, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57880, ChEBI:CHEBI:58088; EC=3.1.3.64;
CC Evidence={ECO:0000256|ARBA:ARBA00001291};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class myotubularin subfamily. {ECO:0000256|ARBA:ARBA00007471}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the phosphoglycerate
CC mutase family. {ECO:0000256|ARBA:ARBA00008408}.
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DR EMBL; KN716656; KJH42515.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D8XD15; -.
DR STRING; 29172.A0A0D8XD15; -.
DR Proteomes; UP000053766; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003873; F:6-phosphofructo-2-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004331; F:fructose-2,6-bisphosphate 2-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052629; F:phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR GO; GO:0006003; P:fructose 2,6-bisphosphate metabolic process; IEA:InterPro.
DR GO; GO:0006000; P:fructose metabolic process; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR CDD; cd07067; HP_PGM_like; 1.
DR CDD; cd13223; PH-GRAM_MTM-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR003094; 6Pfruct_kin.
DR InterPro; IPR013079; 6Phosfructo_kin.
DR InterPro; IPR004182; GRAM.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR010569; Myotubularin-like_Pase_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR PANTHER; PTHR10606:SF70; 6-PHOSPHOFRUCTO-2-KINASE; 1.
DR PANTHER; PTHR10606; 6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE; 1.
DR Pfam; PF01591; 6PF2K; 1.
DR Pfam; PF02893; GRAM; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR Pfam; PF06602; Myotub-related; 1.
DR PRINTS; PR00991; 6PFRUCTKNASE.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000053766}.
FT DOMAIN 643..1023
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT DOMAIN 841..882
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT ACT_SITE 238
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 310
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 237..244
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 287
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 1062 AA; 121980 MW; 873399819E019797 CRC64;
MIDDDCNEQV GVPNVIALVG LPARGKTYIS HKLCRYLNWI GIKTKAFNVG DYRRKAINYE
VEGELDFFSP YNAIGTSIRN ECARLAIEDM GRYLEAKEGE VAILDATNTT RARRRFLMDY
CRRAELAPAF RVFFIESVCD DPDIINSNIT EVKINSPDYK GKMSEEEAKE DFMKRIENYK
LQYEPIDQEI DDDLSFIKVM NAGKSFFVHN VKGHIQSRVV YFLMNIHLLP RSIYLTRHGE
SEYNQIGRLG GDSPLSENGL RYAERLKEYF MKESLEDLRV WSSQKIRAVQ TASRIQELAT
NVEYWKVLDE IDAGICEGLT YEDFEARYPK QFAERDKDKY HYRYPSGESY EDLVARLEPV
IMELERQSDV LVVSHQAVLR CILAYFTNKN REELPYLKVP LHTVIKLTPK AYSCEVEMFK
FDVDAVNTYR EKPGHPVFLV NFVLSSEFNG NKLGRGQWGG LLSLTMSSVY DVPNLGAKDY
KMSDEWGMVQ IAALRSGPTE KQFSGQFPGE RIEVIDRNIG YLSPIGKISG RVLITRYRLR
FEGSDNACHF EVPLGCICKV EKVGHSTVSR SEHSYGVLIG CKDMRNIRFT CQPATHSRRP
LYDALLRYAF PVTNKLPLYA FLYAQALQES SPPPHSSKPM INGWTLYDAK IELNRLGVPN
EQWALSQLNH DYEFADTYPR LLAIPSAVEG KGRDFIEKVG EYRSRQRIPI IIRVQCLKVL
SWLHPVTQAS ITRCSQPKSG MTNRKCAEDE WFLKQIVLAN ANAHQLLIFD ARPIVNAKVN
KAKGGGYEES YEECALLFLN IHNIHVVRES LRKLKDCLFP RVDEKNYLKL VDESKWLNHI
QSIIEGAAQI VSEVERNRNS VLVHCSDGWD RTAQLTSLAM VQLDPYYRTI KGFAVLIEKE
WCSFGHKFAH RIEPRCMIGH GEDKPSDGER SPVFHGCHFE FNSFLLVTIL DELYACRFGT
FLFNSEKQRL VDNKCIKNTV SLWTYVLENK ALFLNPLYNK GDQRTVLSMN SSMRVLRVWT
EYYARYNPHV IAPGSLAAKR YALQRACGKR ALVEELVSLS QA
//
