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Database: UniProt
Entry: R7YWF0_CONA1
LinkDB: R7YWF0_CONA1
Original site: R7YWF0_CONA1 
ID   R7YWF0_CONA1            Unreviewed;       309 AA.
AC   R7YWF0;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 37.
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=W97_05406 {ECO:0000313|EMBL:EON66163.1};
OS   Coniosporium apollinis (strain CBS 100218) (Rock-inhabiting black yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Coniosporium.
OX   NCBI_TaxID=1168221 {ECO:0000313|EMBL:EON66163.1, ECO:0000313|Proteomes:UP000016924};
RN   [1] {ECO:0000313|Proteomes:UP000016924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 100218 {ECO:0000313|Proteomes:UP000016924};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Gorbushina A., Noack S., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The genome sequence of Coniosporium apollinis CBS 100218.";
RL   Submitted (JUN-2012) 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; JH767578; EON66163.1; -; Genomic_DNA.
DR   RefSeq; XP_007781480.1; XM_007783290.1.
DR   AlphaFoldDB; R7YWF0; -.
DR   STRING; 1168221.R7YWF0; -.
DR   GeneID; 19902717; -.
DR   eggNOG; ENOG502RXUQ; Eukaryota.
DR   HOGENOM; CLU_054611_0_1_1; -.
DR   OMA; DYDRPMY; -.
DR   OrthoDB; 2904749at2759; -.
DR   UniPathway; UPA00031; UER00013.
DR   Proteomes; UP000016924; 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:UP000016924}.
FT   DOMAIN          5..213
FT                   /note="PHP"
FT                   /evidence="ECO:0000259|Pfam:PF02811"
SQ   SEQUENCE   309 AA;  35406 MW;  5FC13AF824FF9CF3 CRC64;
     MPISSHSHSG QFCGHAKDTL EEVVKTAISL RMETFAMTEH MPRDEEDLYP EEVEIEQTAA
     GLVDLMDRYY AEAVRLRDLY APQIKLLVGF ESEWIRPSSA GLVERLLQQY QFDLFVGSIH
     HLHTIPIDFD KPRYEAARKI SGGTDERVFE DYFDEQYVML QTLKPPVVGH FDLIRLFSND
     PNRSFKLMKG VWRKILRNLE LIAGYGGLVE LNSAAIRKGM SEPYPKVEIC EEFLRLGGRF
     TLSDDSHGVE QIGQNYHRVF EAITRVGIQD IHYFERGSEK ADERFGHVRV RGHSVASLAN
     HPGFAAPHR
//
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