ID A0A0K2RR38_9MICC Unreviewed; 276 AA.
AC A0A0K2RR38;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=histidinol-phosphatase {ECO:0000256|ARBA:ARBA00013085};
DE EC=3.1.3.15 {ECO:0000256|ARBA:ARBA00013085};
DE AltName: Full=Histidinol-phosphate phosphatase {ECO:0000256|ARBA:ARBA00033209};
GN ORFNames=AHiyo8_55910 {ECO:0000313|EMBL:BAS17288.1};
OS Arthrobacter sp. Hiyo8.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1588023 {ECO:0000313|EMBL:BAS17288.1, ECO:0000313|Proteomes:UP000060353};
RN [1] {ECO:0000313|Proteomes:UP000060353}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hiyo8 {ECO:0000313|Proteomes:UP000060353};
RA Hiraoka S., Machiyama A., Iwasaki W.;
RT "Microbial genome analysis of tsunami-affected soil.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-histidinol phosphate = L-histidinol + phosphate;
CC Xref=Rhea:RHEA:14465, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57699, ChEBI:CHEBI:57980; EC=3.1.3.15;
CC Evidence={ECO:0000256|ARBA:ARBA00001216};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
CC {ECO:0000256|ARBA:ARBA00004970}.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000256|ARBA:ARBA00009759}.
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DR EMBL; AP014719; BAS17288.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K2RR38; -.
DR STRING; 1588023.AHiyo8_55910; -.
DR KEGG; arh:AHiyo8_55910; -.
DR PATRIC; fig|1588023.3.peg.5843; -.
DR UniPathway; UPA00031; UER00013.
DR Proteomes; UP000060353; Chromosome.
DR GO; GO:0004401; F:histidinol-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01641; Bacterial_IMPase_like_1; 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; IPR011809; His_9_proposed.
DR InterPro; IPR020583; Inositol_monoP_metal-BS.
DR InterPro; IPR000760; Inositol_monophosphatase-like.
DR NCBIfam; TIGR02067; his_9_HisN; 1.
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.
DR PROSITE; PS00629; IMP_1; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT REGION 44..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 276 AA; 29896 MW; C83386E2166CD1AC CRC64;
MTQPDSSYND DLRLAHVLAD SVDSLTMERF KALDLQVETK PDLSPVTDAD KAAEEAIRGQ
LSRSRPRDAV LGEEFGSTGH GSRRWIIDPI DGTKNFVRGV PVWATLIALV DEGEVVVGLV
SAPALGKRWW AAKGSGAYMG RSLAAATRLK VSNVSRLEDA SLSYSELSEW KQHGKLDNFL
GLENDVWRSR AYGDFWSYCL VAEGAVDIAA EPELQVYDMA ALVPIVTEAG GRFTSLDGAD
GPSAETPSPR TRSSIPRSSR GSTPNSTTFC SPLFTE
//