ID A0A1M5VRD8_9FIRM Unreviewed; 271 AA.
AC A0A1M5VRD8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=SAMN02745823_00966 {ECO:0000313|EMBL:SHH77534.1};
OS Sporobacter termitidis DSM 10068.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Sporobacter.
OX NCBI_TaxID=1123282 {ECO:0000313|EMBL:SHH77534.1, ECO:0000313|Proteomes:UP000183995};
RN [1] {ECO:0000313|EMBL:SHH77534.1, ECO:0000313|Proteomes:UP000183995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10068 {ECO:0000313|EMBL:SHH77534.1,
RC ECO:0000313|Proteomes:UP000183995};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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 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; FQXV01000002; SHH77534.1; -; Genomic_DNA.
DR RefSeq; WP_073076516.1; NZ_FQXV01000002.1.
DR AlphaFoldDB; A0A1M5VRD8; -.
DR STRING; 1123282.SAMN02745823_00966; -.
DR OrthoDB; 9775255at2; -.
DR UniPathway; UPA00031; UER00013.
DR Proteomes; UP000183995; 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 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:UP000183995}.
FT DOMAIN 7..199
FT /note="PHP"
FT /evidence="ECO:0000259|Pfam:PF02811"
SQ SEQUENCE 271 AA; 29635 MW; D0613FEFDD4A8D38 CRC64;
MTLLTNFHAH STFCDGTETP EDMVRAAIGK GCAAFGISGH APMAFDTDWC MTAAGERDFV
REMDRLKAVY GGRLTLMTGV ERDYYSPEPA GVYDYVIGSV HYIKKDGAML TVDESEDAQR
RDAARYYAGD FYTYARDYFR TVAGVAPATK PDFIGHFDLV AKFNDGGRLF DEADPRYTGP
ALEALAAVAE TCGLFEINTG AMYRVGRSVP YPAPFLLRAL RERGGEIILS SDSHDGASIG
YRFAEAAELA KACGFEYAKT LTPSGAETYK L
//
