ID A0A0J1HE78_9GAMM Unreviewed; 256 AA.
AC A0A0J1HE78;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Inositol-1-monophosphatase {ECO:0000256|RuleBase:RU364068};
DE EC=3.1.3.25 {ECO:0000256|RuleBase:RU364068};
GN ORFNames=ABT57_09755 {ECO:0000313|EMBL:KLV09945.1};
OS Photobacterium ganghwense.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=320778 {ECO:0000313|EMBL:KLV09945.1, ECO:0000313|Proteomes:UP000035909};
RN [1] {ECO:0000313|EMBL:KLV09945.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22954 {ECO:0000313|EMBL:KLV09945.1};
RA Machado H., Gram L.;
RT "Photobacterium galathea sp. nov.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|RuleBase:RU364068};
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000256|ARBA:ARBA00009759, ECO:0000256|RuleBase:RU364068}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KLV09945.1}.
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DR EMBL; LDOU01000007; KLV09945.1; -; Genomic_DNA.
DR RefSeq; WP_047885034.1; NZ_PYMI01000002.1.
DR AlphaFoldDB; A0A0J1HE78; -.
DR STRING; 320778.ABT57_09755; -.
DR PATRIC; fig|320778.3.peg.2127; -.
DR OrthoDB; 9785695at2; -.
DR Proteomes; UP000035909; Unassembled WGS sequence.
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:0031564; P:transcription antitermination; IEA:UniProtKB-KW.
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; IPR000760; Inositol_monophosphatase-like.
DR PANTHER; PTHR20854; INOSITOL MONOPHOSPHATASE; 1.
DR PANTHER; PTHR20854:SF50; NUS FACTOR SUHB; 1.
DR Pfam; PF00459; Inositol_P; 1.
DR PRINTS; PR00377; IMPHPHTASES.
DR SUPFAM; SSF56655; Carbohydrate phosphatase; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU364068};
KW Magnesium {ECO:0000256|RuleBase:RU364068};
KW Metal-binding {ECO:0000256|RuleBase:RU364068};
KW Reference proteome {ECO:0000313|Proteomes:UP000035909};
KW Transcription {ECO:0000256|ARBA:ARBA00022814};
KW Transcription antitermination {ECO:0000256|ARBA:ARBA00022814};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00022814}.
SQ SEQUENCE 256 AA; 28288 MW; D33BE9421E85B04A CRC64;
MKAAEKLEAL ENAIRIAGDK ALSFRKQGLT IEVKGKNDFV TQVDREVETE IKSVISHLFP
EDGFLGEESG ISAGEEGIWV IDPIDGTTNY IQGMDYWCIS VAYVNNDQIE LGYIYAPERD
EFFAARKGQG AWLNGRCLKM ENEAEGQSII GLGHSNRRPL SDVINLLTIL DENNVDHRRF
GAGALMLAHV ASGLVHGYFE AHLNSWDALA GLLLVEEAGG CVPDFLANDG LINGNPVWVS
TQRLWPVLNT YMEQFS
//
