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Database: UniProt
Entry: A0A3Q3NFK0_9TELE
LinkDB: A0A3Q3NFK0_9TELE
Original site: A0A3Q3NFK0_9TELE 
ID   A0A3Q3NFK0_9TELE        Unreviewed;       459 AA.
AC   A0A3Q3NFK0;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Multiple inositol polyphosphate phosphatase 1 {ECO:0000256|ARBA:ARBA00018097};
DE            EC=3.1.3.62 {ECO:0000256|ARBA:ARBA00013040};
DE            EC=3.1.3.80 {ECO:0000256|ARBA:ARBA00012976};
DE   AltName: Full=2,3-bisphosphoglycerate 3-phosphatase {ECO:0000256|ARBA:ARBA00031642};
OS   Mastacembelus armatus (zig-zag eel).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX   NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000031289.1, ECO:0000313|Proteomes:UP000261640};
RN   [1] {ECO:0000313|Ensembl:ENSMAMP00000031289.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-2,3-bisphosphoglycerate + H2O = (2R)-2-phosphoglycerate +
CC         phosphate; Xref=Rhea:RHEA:27381, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58248, ChEBI:CHEBI:58289; EC=3.1.3.80;
CC         Evidence={ECO:0000256|ARBA:ARBA00043832};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27382;
CC         Evidence={ECO:0000256|ARBA:ARBA00043832};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol 1,2,4,5,6-pentakisphosphate + H2O = 1D-myo-
CC         inositol 1,2,5,6-tetrakisphosphate + phosphate; Xref=Rhea:RHEA:77115,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57798,
CC         ChEBI:CHEBI:195535; EC=3.1.3.62;
CC         Evidence={ECO:0000256|ARBA:ARBA00043671};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77116;
CC         Evidence={ECO:0000256|ARBA:ARBA00043671};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol 1,2,5,6-tetrakisphosphate + H2O = 1D-myo-
CC         inositol 1,2,6-trisphosphate + phosphate; Xref=Rhea:RHEA:77119,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:195535,
CC         ChEBI:CHEBI:195537; EC=3.1.3.62;
CC         Evidence={ECO:0000256|ARBA:ARBA00043668};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77120;
CC         Evidence={ECO:0000256|ARBA:ARBA00043668};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol hexakisphosphate + H2O = 1D-myo-inositol
CC         1,2,4,5,6-pentakisphosphate + phosphate; Xref=Rhea:RHEA:16989,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57798,
CC         ChEBI:CHEBI:58130; EC=3.1.3.62;
CC         Evidence={ECO:0000256|ARBA:ARBA00043691};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16990;
CC         Evidence={ECO:0000256|ARBA:ARBA00043691};
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family. MINPP1
CC       subfamily. {ECO:0000256|ARBA:ARBA00008422}.
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DR   AlphaFoldDB; A0A3Q3NFK0; -.
DR   STRING; 205130.ENSMAMP00000031290; -.
DR   Ensembl; ENSMAMT00000032107.2; ENSMAMP00000031289.1; ENSMAMG00000021071.2.
DR   GeneTree; ENSGT00390000018409; -.
DR   Proteomes; UP000261640; Unplaced.
DR   GO; GO:0034417; F:bisphosphoglycerate 3-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052826; F:inositol hexakisphosphate 2-phosphatase activity; IEA:UniProtKB-EC.
DR   CDD; cd07061; HP_HAP_like; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR000560; His_Pase_clade-2.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR016274; Histidine_acid_Pase_euk.
DR   PANTHER; PTHR20963:SF41; MULTIPLE INOSITOL POLYPHOSPHATE PHOSPHATASE 1; 1.
DR   PANTHER; PTHR20963; MULTIPLE INOSITOL POLYPHOSPHATE PHOSPHATASE-RELATED; 1.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   PIRSF; PIRSF000894; Acid_phosphatase; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR000894-2};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261640};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..459
FT                   /note="Multiple inositol polyphosphate phosphatase 1"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5030081794"
FT   DISULFID        70..401
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT   DISULFID        267..281
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
SQ   SEQUENCE   459 AA;  53007 MW;  415D5CBE86765E1C CRC64;
     MLTFLWKFSV FYFFIIWALF NYVNPEDNLD IPTIAKYFNT KGRYEEVNPY LREDILAVNR
     SILQPPSPQC QEIHLIAIIR HGTRYPTTKN IKDMQQLYNI VMHNASGEAS FLREIQTQWA
     MWYTEDMDGR LVQKGVNELK HLAVRLSKLF PSLVSEENLR GGRVKFITSS KHRCVNSTLS
     FKAGLTELWA IKDQEFDHEV NDALMRFFDK CARIVQEVDN SPLALVEINN FKKGPEMRRV
     QEKIAVRLRV SYSLITHDMA EAAFYLCAYE FAIKAVNSPW CQLFDEDDAK VMEYASDLRE
     FWKRGYGYDI NSKSSCILFH DVFSRLNKAA SENKSGQQVT EAVTVQVGHA DTLLPLLTLL
     GFFKDSEALT STNYATQTQR SFRTSHMLPY AANLLLVLYD CGAGDLRLQP LLNERPVTFP
     GLADQQVSMP LYEDVKEHYR ELLQGCDFEN ECQLFKHPA
//
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