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Database: UniProt
Entry: A0LS96_ACIC1
LinkDB: A0LS96_ACIC1
Original site: A0LS96_ACIC1 
ID   A0LS96_ACIC1            Unreviewed;       265 AA.
AC   A0LS96;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   SubName: Full=Histidinol-phosphate phosphatase {ECO:0000313|EMBL:ABK52306.1};
DE            EC=3.1.3.15 {ECO:0000313|EMBL:ABK52306.1};
GN   OrderedLocusNames=Acel_0533 {ECO:0000313|EMBL:ABK52306.1};
OS   Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC   Bacteria; Actinomycetota; Actinomycetes; Acidothermales; Acidothermaceae;
OC   Acidothermus.
OX   NCBI_TaxID=351607 {ECO:0000313|EMBL:ABK52306.1, ECO:0000313|Proteomes:UP000008221};
RN   [1] {ECO:0000313|EMBL:ABK52306.1, ECO:0000313|Proteomes:UP000008221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43068 / DSM 8971 / 11B
RC   {ECO:0000313|Proteomes:UP000008221};
RX   PubMed=19270083; DOI=10.1101/gr.084848.108;
RA   Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V.,
RA   Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C.,
RA   Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.;
RT   "Complete genome of the cellulolytic thermophile Acidothermus
RT   cellulolyticus 11B provides insights into its ecophysiological and
RT   evolutionary adaptations.";
RL   Genome Res. 19:1033-1043(2009).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC       {ECO:0000256|ARBA:ARBA00009759}.
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DR   EMBL; CP000481; ABK52306.1; -; Genomic_DNA.
DR   RefSeq; WP_011719369.1; NC_008578.1.
DR   AlphaFoldDB; A0LS96; -.
DR   STRING; 351607.Acel_0533; -.
DR   KEGG; ace:Acel_0533; -.
DR   eggNOG; COG0483; Bacteria.
DR   HOGENOM; CLU_044118_4_0_11; -.
DR   InParanoid; A0LS96; -.
DR   OrthoDB; 9772456at2; -.
DR   Proteomes; UP000008221; Chromosome.
DR   GO; GO:0004401; F:histidinol-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.190.80; -; 1.
DR   Gene3D; 3.30.540.10; Fructose-1,6-Bisphosphatase, subunit A, domain 1; 1.
DR   InterPro; IPR000760; Inositol_monophosphatase-like.
DR   PANTHER; PTHR43200:SF26; BIFUNCTIONAL PHOSPHATASE IMPL2, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR43200; PHOSPHATASE; 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|ARBA:ARBA00022801, ECO:0000313|EMBL:ABK52306.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008221}.
SQ   SEQUENCE   265 AA;  27925 MW;  235681B7D25907FC CRC64;
     MSDPTAADLA LALRLADLAD EISLSRFQAM DFRVETKPDL TPVSDVDLSV EREVRRVLAA
     DRPGDAVLGE EFGGEPVDGR VWVIDPIDAT KNFVRGVPIW ATLIALLDAG EPVIGVVSAP
     ALASRWWAGR GLGSWTARLG AAPRRNQVSA VRNLSDASLS YSGLGGWGTR VSDFLNLTKA
     VWRTRAYGDF FSHVLVAEGA VDISAEPEVS LWDTAALVVI VTEAGGRVTG VDGGPSPAAS
     SILCTNAWLH DAALSHLAGS ARRGG
//
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