ID S5YTB2_PARAH Unreviewed; 261 AA.
AC S5YTB2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=JCM7686_1365 {ECO:0000313|EMBL:AGT08466.1};
OS Paracoccus aminophilus JCM 7686.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1367847 {ECO:0000313|EMBL:AGT08466.1, ECO:0000313|Proteomes:UP000015480};
RN [1] {ECO:0000313|EMBL:AGT08466.1, ECO:0000313|Proteomes:UP000015480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 7686 {ECO:0000313|EMBL:AGT08466.1};
RX PubMed=24517536; DOI=10.1186/1471-2164-15-124;
RA Dziewit L., Czarnecki J., Wibberg D., Radlinska M., Mrozek P., Szymczak M.,
RA Schluter A., Puhler A., Bartosik D.;
RT "Architecture and functions of a multipartite genome of the methylotrophic
RT bacterium Paracoccus aminophilus JCM 7686, containing primary and secondary
RT chromids.";
RL BMC Genomics 15:124-124(2014).
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; CP006650; AGT08466.1; -; Genomic_DNA.
DR RefSeq; WP_020950104.1; NC_022041.1.
DR AlphaFoldDB; S5YTB2; -.
DR STRING; 1367847.JCM7686_1365; -.
DR KEGG; pami:JCM7686_1365; -.
DR PATRIC; fig|1367847.3.peg.1336; -.
DR eggNOG; COG0483; Bacteria.
DR HOGENOM; CLU_044118_4_1_5; -.
DR OrthoDB; 9785695at2; -.
DR UniPathway; UPA00031; UER00013.
DR Proteomes; UP000015480; 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 GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
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 InterPro; IPR020550; Inositol_monophosphatase_CS.
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.
DR PROSITE; PS00630; IMP_2; 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, ECO:0000313|EMBL:AGT08466.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000015480}.
SQ SEQUENCE 261 AA; 27914 MW; EE68B7D5B5675802 CRC64;
MTDAEQIIAT AHRLADAARR ETLGLFRSPS LRPDNKSLQG FDPVTEADRA SERAMRALLD
ELRPEDAILG EEYGPKSGSS GLTWVLDPID GTRAFMSGAP SWGVLIALCD DSGPRYGIID
QPYIGERFEG GFGRARMVGP RGETALGVRK GVALAQATLM STYPEVGSPE EREAFGRVAK
EVRLTRYGLD CYAYALLAAG QIDLVIEAGL QPYDVCAPIA VIEAAGGIVT DWQGGPAHQG
GRILAAATPE LHAEALQFLR S
//
