ID Q53743_STRAD Unreviewed; 273 AA.
AC Q53743;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 24-JAN-2024, entry version 73.
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 Name=pur3 {ECO:0000313|EMBL:CAA63164.1};
OS Streptomyces alboniger.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX NCBI_TaxID=132473 {ECO:0000313|EMBL:CAA63164.1};
RN [1] {ECO:0000313|EMBL:CAA63164.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC12461 {ECO:0000313|EMBL:CAA63164.1};
RX PubMed=8576156; DOI=10.1074/jbc.271.3.1579;
RA Tercero J.A., Espinosa J.C., Lacalle R.A., Jimenez A.;
RT "The biosynthetic pathway of the aminonucleoside antibiotic puromycin, as
RT deduced from the molecular analysis of the pur cluster of Streptomyces
RT alboniger.";
RL J. Biol. Chem. 271:1579-1590(1996).
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; X92429; CAA63164.1; -; Genomic_DNA.
DR AlphaFoldDB; Q53743; -.
DR KEGG; ag:CAA63164; -.
DR UniPathway; UPA00031; UER00013.
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; PTHR20854; INOSITOL MONOPHOSPHATASE; 1.
DR PANTHER; PTHR20854:SF4; INOSITOL-1-MONOPHOSPHATASE-RELATED; 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}.
SQ SEQUENCE 273 AA; 29091 MW; C68A5E6240DF38DB CRC64;
MPQQADLELA MRLADTADRI TTRRFQARDC GYARKPDRTP VTDADTTVEA AVRESVRAAR
PDDDFAGEET GGEVTAGRTW IVDPIDGTKN FLRGVPVWAT LIALLEDGRP TVGVVAAPAL
RSRWWAAAGH GAWLRRGSAG AEPLRLHVSG VARLENAYLS TTNTRTWDAF HSRAAYLRLA
DACWEDRAFG DFLQHCMVAE GTVDIAAEPV VSPWDIAALQ ILVEEAGGVC TDLLGGSPQR
GTGALSANPE LHRLAVEALA APAAATTGAA TIP
//