(data stored in ACNUC7421 zone)

SWISSPROT: Q3ILB4_PSEHT

ID   Q3ILB4_PSEHT            Unreviewed;       267 AA.
AC   Q3ILB4;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   30-AUG-2017, entry version 70.
DE   RecName: Full=Inositol-1-monophosphatase {ECO:0000256|RuleBase:RU364068};
DE            EC=3.1.3.25 {ECO:0000256|RuleBase:RU364068};
GN   Name=suhB {ECO:0000313|EMBL:CAI85422.1};
GN   OrderedLocusNames=PSHAa0323 {ECO:0000313|EMBL:CAI85422.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85422.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85422.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- CATALYTIC ACTIVITY: Myo-inositol phosphate + H(2)O = myo-inositol
CC       + phosphate. {ECO:0000256|RuleBase:RU364068}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU364068};
CC   -!- SIMILARITY: Belongs to the inositol monophosphatase family.
CC       {ECO:0000256|RuleBase:RU364068}.
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DR   EMBL; CR954246; CAI85422.1; -; Genomic_DNA.
DR   RefSeq; WP_011327036.1; NC_007481.1.
DR   ProteinModelPortal; Q3ILB4; -.
DR   STRING; 326442.PSHAa0323; -.
DR   EnsemblBacteria; CAI85422; CAI85422; PSHAa0323.
DR   KEGG; pha:PSHAa0323; -.
DR   PATRIC; fig|326442.8.peg.309; -.
DR   eggNOG; ENOG4105ECY; Bacteria.
DR   eggNOG; COG0483; LUCA.
DR   HOGENOM; HOG000282238; -.
DR   KO; K01092; -.
DR   OMA; FAVNQEL; -.
DR   OrthoDB; POG091H061V; -.
DR   Proteomes; UP000006843; Chromosome I.
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:0046855; P:inositol phosphate dephosphorylation; IEA:InterPro.
DR   GO; GO:0046854; P:phosphatidylinositol phosphorylation; IEA:InterPro.
DR   CDD; cd01639; IMPase; 1.
DR   InterPro; IPR033942; IMPase.
DR   InterPro; IPR020583; Inositol_monoP_metal-BS.
DR   InterPro; IPR000760; Inositol_monophosphatase-like.
DR   InterPro; IPR020550; Inositol_monophosphatase_CS.
DR   InterPro; IPR022337; Inositol_monophosphatase_SuhB.
DR   PANTHER; PTHR20854; PTHR20854; 1.
DR   Pfam; PF00459; Inositol_P; 1.
DR   PRINTS; PR00377; IMPHPHTASES.
DR   PRINTS; PR01959; SBIMPHPHTASE.
DR   PROSITE; PS00629; IMP_1; 1.
DR   PROSITE; PS00630; IMP_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3ILB4.
DR   SWISS-2DPAGE; Q3ILB4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
KW   Hydrolase {ECO:0000256|RuleBase:RU364068,
KW   ECO:0000313|EMBL:CAI85422.1};
KW   Magnesium {ECO:0000256|RuleBase:RU364068};
KW   Metal-binding {ECO:0000256|RuleBase:RU364068};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843}.
SQ   SEQUENCE   267 AA;  29054 MW;  CF762F283EB399AE CRC64;
     MHPMLNIAVR AARNAGKIIL RASEDLSKVE VQQKGTNDLV TNIDKEAEAI IRDTILRSYP
     DHCIVGEELG EHKGKDADYQ WIVDPLDGTT NFIKGIPHFA VSIALKVKGR LDQAVIYDPI
     RGELFTASRG QGAQLNSKRL RVSKTVDLGG SILATGFPFK QKQHLDAYTE AFKALFIHTA
     DIRRAGSAAL DMAYVAAGRV DGFFEIGLKP WDTAAGELLV KEAGGMVVDF AGGVNYNNSG
     NIICGAPKLT QAIIREIRPV LTESLLR
//

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