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Database: UniProt
Entry: A0A127A2W6_9MICC
LinkDB: A0A127A2W6_9MICC
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ID   A0A127A2W6_9MICC        Unreviewed;       273 AA.
AC   A0A127A2W6;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
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=SA2016_2574 {ECO:0000313|EMBL:AMM33241.1};
OS   Sinomonas atrocyanea.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Sinomonas.
OX   NCBI_TaxID=37927 {ECO:0000313|EMBL:AMM33241.1, ECO:0000313|Proteomes:UP000070134};
RN   [1] {ECO:0000313|EMBL:AMM33241.1, ECO:0000313|Proteomes:UP000070134}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 3377 {ECO:0000313|EMBL:AMM33241.1,
RC   ECO:0000313|Proteomes:UP000070134};
RA   Kim K.M.;
RT   "Complete genome of Sinomonas atrocyanea KCTC 3377.";
RL   Submitted (FEB-2016) 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; CP014518; AMM33241.1; -; Genomic_DNA.
DR   RefSeq; WP_066498640.1; NZ_CP014518.1.
DR   AlphaFoldDB; A0A127A2W6; -.
DR   STRING; 37927.SA2016_2574; -.
DR   KEGG; satk:SA2016_2574; -.
DR   PATRIC; fig|37927.3.peg.2649; -.
DR   OrthoDB; 9772456at2; -.
DR   UniPathway; UPA00031; UER00013.
DR   Proteomes; UP000070134; 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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070134}.
FT   REGION          57..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..71
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   273 AA;  29397 MW;  E1A4ADD5D29B54C3 CRC64;
     MTSVTETSYN DDLRLAHVLA DSVDAQTMER FKALDLKVET KPDLTPVTDA DRAAEEAIRG
     QLSRSRPRDA VVGEEFGTTG HGSRRWIIDP IDGTKNFVRG VPVWASLIAL ADGDEIVVGV
     VSAPALGRRW WAAKGTGAYT GRSLASATRL KVSDVSKLQD ASLSYSSLSG WKERGSLEDF
     LGLTDEVWRT RAYGDFWSYC LVAEGAVDIA TEPELALYDM AALVPIVTEA GGRFTSLDGQ
     DGPWGGNALA TNGILHSEVL GKLNPGRDDL LPD
//
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