ID Q1ASY9_RUBXD Unreviewed; 270 AA.
AC Q1ASY9;
DT 11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Histidinol-phosphatase {ECO:0000256|ARBA:ARBA00013085, ECO:0000256|RuleBase:RU366003};
DE Short=HolPase {ECO:0000256|RuleBase:RU366003};
DE EC=3.1.3.15 {ECO:0000256|ARBA:ARBA00013085, ECO:0000256|RuleBase:RU366003};
GN OrderedLocusNames=Rxyl_2572 {ECO:0000313|EMBL:ABG05489.1};
OS Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129 / PRD-1).
OC Bacteria; Actinomycetota; Rubrobacteria; Rubrobacterales; Rubrobacteraceae;
OC Rubrobacter.
OX NCBI_TaxID=266117 {ECO:0000313|EMBL:ABG05489.1, ECO:0000313|Proteomes:UP000006637};
RN [1] {ECO:0000313|EMBL:ABG05489.1, ECO:0000313|Proteomes:UP000006637}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9941 / NBRC 16129 / PRD-1
RC {ECO:0000313|Proteomes:UP000006637};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., da Costa M.S.,
RA Rainey F.A., Empadinhas N., Jolivet E., Battista J.R., Richardson P.;
RT "Complete sequence of Rubrobacter xylanophilus DSM 9941.";
RL Submitted (JUN-2006) 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 ECO:0000256|RuleBase:RU366003};
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, ECO:0000256|RuleBase:RU366003}.
CC -!- SIMILARITY: Belongs to the PHP hydrolase family. HisK subfamily.
CC {ECO:0000256|ARBA:ARBA00009152, ECO:0000256|RuleBase:RU366003}.
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DR EMBL; CP000386; ABG05489.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1ASY9; -.
DR STRING; 266117.Rxyl_2572; -.
DR KEGG; rxy:Rxyl_2572; -.
DR eggNOG; COG1387; Bacteria.
DR HOGENOM; CLU_054611_2_0_11; -.
DR OrthoDB; 6637113at2; -.
DR PhylomeDB; Q1ASY9; -.
DR UniPathway; UPA00031; UER00013.
DR Proteomes; UP000006637; Chromosome.
DR GO; GO:0004401; F:histidinol-phosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd12110; PHP_HisPPase_Hisj_like; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR InterPro; IPR010140; Histidinol_P_phosphatase_HisJ.
DR InterPro; IPR004013; PHP_dom.
DR InterPro; IPR016195; Pol/histidinol_Pase-like.
DR NCBIfam; TIGR01856; hisJ_fam; 1.
DR PANTHER; PTHR21039; HISTIDINOL PHOSPHATASE-RELATED; 1.
DR PANTHER; PTHR21039:SF0; HISTIDINOL-PHOSPHATASE; 1.
DR Pfam; PF02811; PHP; 1.
DR SUPFAM; SSF89550; PHP domain-like; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|RuleBase:RU366003};
KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102,
KW ECO:0000256|RuleBase:RU366003};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366003};
KW Reference proteome {ECO:0000313|Proteomes:UP000006637}.
FT DOMAIN 36..199
FT /note="PHP"
FT /evidence="ECO:0000259|Pfam:PF02811"
SQ SEQUENCE 270 AA; 30399 MW; 8300DD294CF13970 CRC64;
MISLRRPSRR RGTEASGGCL IDYHLHVVAH DDRPMTVENI LEYCRVAREK GIRQLGITEH
DRYLEKVDLA AFQEARERSR EVELRLGIEI DYVPGNEEEM ERVATALPYD YVIGSVHRVD
GEEIDIDPGA GIYERDTYEL YAAYFANVRA AARSGLFDVI GHPDLIKIFR RFPQRDVTPL
LEETAEAVAA SGVVVDVNSA GLRKPVGEIY PSRAFLEMFY ERGVPIILSS DAHAPGQVGA
GYEESLRMVR EVGYREVTTF RNGERGSLPL
//
