ID A0A1W1XWN0_9CLOT Unreviewed; 279 AA.
AC A0A1W1XWN0;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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 ORFNames=SAMN02745134_03452 {ECO:0000313|EMBL:SMC28277.1};
OS Clostridium acidisoli DSM 12555.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121291 {ECO:0000313|EMBL:SMC28277.1, ECO:0000313|Proteomes:UP000192468};
RN [1] {ECO:0000313|EMBL:SMC28277.1, ECO:0000313|Proteomes:UP000192468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12555 {ECO:0000313|EMBL:SMC28277.1,
RC ECO:0000313|Proteomes:UP000192468};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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; FWXH01000023; SMC28277.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W1XWN0; -.
DR STRING; 1121291.SAMN02745134_03452; -.
DR OrthoDB; 9775255at2; -.
DR UniPathway; UPA00031; UER00013.
DR Proteomes; UP000192468; Unassembled WGS sequence.
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:UP000192468}.
FT DOMAIN 7..207
FT /note="PHP"
FT /evidence="ECO:0000259|Pfam:PF02811"
SQ SEQUENCE 279 AA; 32568 MW; 35C642149F54AB02 CRC64;
MMSFSNFHTH CYFCDGTDDP EEYVKKAIEF KFSDLGFSSH APLPFPNSWT MGKNNFYEYC
NKINSLKLKY KNEINIYLGL EVDYIENLIS PTDEKFASLD YTIGSVHMLK DIKTGEFLAV
DGDEDEYIKL ITSAFDNDVK KFVHAYYTQI RNMVSNKTPS IVGHLDLIKK HNKNNKYFNE
NEPWYKDEIL NTLKVISENK TILELNTGGK VRGYTDDFYP SNWILTECRH LDIPIILNSD
AHNPQYINAY FSDATILLKN SNYLKQRILH NEVWQDVLL
//
