ID S7Q2N8_MYOBR Unreviewed; 277 AA.
AC S7Q2N8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Inositol-1-monophosphatase {ECO:0000256|RuleBase:RU364068};
DE EC=3.1.3.25 {ECO:0000256|RuleBase:RU364068};
GN ORFNames=D623_10021346 {ECO:0000313|EMBL:EPQ15137.1};
OS Myotis brandtii (Brandt's bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ15137.1, ECO:0000313|Proteomes:UP000052978};
RN [1] {ECO:0000313|Proteomes:UP000052978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23962925; DOI=10.1038/ncomms3212;
RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., Hee Yim S.,
RA Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., Chen G., Kulakova O.I.,
RA Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., Sunyaev S.R., Zhang G.,
RA Krogh A., Wang J., Gladyshev V.N.;
RT "Genome analysis reveals insights into physiology and longevity of the
RT Brandt's bat Myotis brandtii.";
RL Nat. Commun. 4:2212-2212(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a myo-inositol phosphate + H2O = myo-inositol + phosphate;
CC Xref=Rhea:RHEA:24056, ChEBI:CHEBI:15377, ChEBI:CHEBI:17268,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:84139; EC=3.1.3.25;
CC Evidence={ECO:0000256|ARBA:ARBA00001033,
CC ECO:0000256|RuleBase:RU364068};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-galactose 1-phosphate + H2O = D-galactose + phosphate;
CC Xref=Rhea:RHEA:29315, ChEBI:CHEBI:4139, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58336; EC=3.1.3.94;
CC Evidence={ECO:0000256|ARBA:ARBA00035990};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|RuleBase:RU364068};
CC -!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-inositol
CC from D-glucose 6-phosphate: step 2/2. {ECO:0000256|ARBA:ARBA00005152,
CC ECO:0000256|RuleBase:RU364068}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000256|ARBA:ARBA00009759, ECO:0000256|RuleBase:RU364068}.
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DR EMBL; KE164113; EPQ15137.1; -; Genomic_DNA.
DR RefSeq; XP_005878244.1; XM_005878182.2.
DR AlphaFoldDB; S7Q2N8; -.
DR GeneID; 102244869; -.
DR KEGG; myb:102244869; -.
DR CTD; 3612; -.
DR eggNOG; KOG2951; Eukaryota.
DR OrthoDB; 3685586at2759; -.
DR UniPathway; UPA00823; UER00788.
DR Proteomes; UP000052978; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052832; F:inositol monophosphate 3-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052833; F:inositol monophosphate 4-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006021; P:inositol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR CDD; cd01639; IMPase; 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; IPR033942; IMPase.
DR InterPro; IPR020583; Inositol_monoP_metal-BS.
DR InterPro; IPR020552; Inositol_monoPase_Li-sen.
DR InterPro; IPR000760; Inositol_monophosphatase-like.
DR InterPro; IPR020550; Inositol_monophosphatase_CS.
DR PANTHER; PTHR20854; INOSITOL MONOPHOSPHATASE; 1.
DR PANTHER; PTHR20854:SF26; INOSITOL MONOPHOSPHATASE 1; 1.
DR Pfam; PF00459; Inositol_P; 1.
DR PRINTS; PR00377; IMPHPHTASES.
DR PRINTS; PR00378; LIIMPHPHTASE.
DR SUPFAM; SSF56655; Carbohydrate phosphatase; 1.
DR PROSITE; PS00629; IMP_1; 1.
DR PROSITE; PS00630; IMP_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|RuleBase:RU364068};
KW Lithium {ECO:0000256|ARBA:ARBA00022671};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU364068};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU364068};
KW Reference proteome {ECO:0000313|Proteomes:UP000052978}.
SQ SEQUENCE 277 AA; 30294 MW; B3C4D70D5C236668 CRC64;
MADPWEECMD YAVTLARRAG EVVREALKNE MNVMIKSSPA DLVTATDQKV EKMLLSFIKE
KYPSHSFIGE ESVAAGEKSV LTDNPTWIID PIDGTTNFVH RFPFVAVSIG FVVNKEMEFG
VVYSCVEDKM YTGRRGRGAF CNGQKLQVSR QEDVTKALLV TELGSSRTPE TVRTVLANME
KLLCLPIHGI RGVGTAAVNM CLVASGAADA YYEMGIHCWD MAGAGVIVTE AGGVLMDVTG
GPFDLMSRRI IAAGSKTLAE RIAREIQVVP FQRDDED
//
