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Database: UniProt
Entry: A0A218ZG29_9HELO
LinkDB: A0A218ZG29_9HELO
Original site: A0A218ZG29_9HELO 
ID   A0A218ZG29_9HELO        Unreviewed;       304 AA.
AC   A0A218ZG29;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
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=B2J93_1873 {ECO:0000313|EMBL:OWP06116.1};
OS   Marssonina coronariae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Dermateaceae; Marssonina.
OX   NCBI_TaxID=503106 {ECO:0000313|EMBL:OWP06116.1, ECO:0000313|Proteomes:UP000242519};
RN   [1] {ECO:0000313|EMBL:OWP06116.1, ECO:0000313|Proteomes:UP000242519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NL1 {ECO:0000313|EMBL:OWP06116.1,
RC   ECO:0000313|Proteomes:UP000242519};
RA   Cheng Q.;
RT   "Draft genome sequence of Marssonina coronaria NL1: causal agent of apple
RT   blotch.";
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OWP06116.1}.
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DR   EMBL; MZNU01000058; OWP06116.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A218ZG29; -.
DR   STRING; 503106.A0A218ZG29; -.
DR   InParanoid; A0A218ZG29; -.
DR   OrthoDB; 2904749at2759; -.
DR   UniPathway; UPA00031; UER00013.
DR   Proteomes; UP000242519; 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:UP000242519}.
FT   DOMAIN          5..216
FT                   /note="PHP"
FT                   /evidence="ECO:0000259|Pfam:PF02811"
SQ   SEQUENCE   304 AA;  33846 MW;  59CE7B3E6701443D CRC64;
     MAFSMHSHSG QFCPGHAKDT LEEVVRAAVA RGMRTFALTE HMPRNSASDL YPEEIEAGDT
     VGPLFLRHEA FLAEAVRLRD KYAEQITLLV GFEGEWIRPS YGPLIQELAA HPAVDYFIGS
     VHHVHAIPID YDAALYRQAR DVAGGTDERL FEDYFDAQLE MLRVLHPRVV GHFDLVRLLS
     DAPNASPRRG DGVWERMVRN LRVIVDQGGL LEVNSSALRK GLQEPYPMRC VCEEFLKLGG
     KLTLSDDSHA IGHVGTNYGR SIEYLESLGV DEIFTLNGKD EASGRATVSV RSVSLQSVKE
     TFKP
//
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