ID A0A166FEX8_9AGAM Unreviewed; 321 AA.
AC A0A166FEX8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=FIBSPDRAFT_831520 {ECO:0000313|EMBL:KZP16731.1};
OS Fibularhizoctonia sp. CBS 109695.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Atheliales; Atheliaceae; Fibularhizoctonia.
OX NCBI_TaxID=436010 {ECO:0000313|EMBL:KZP16731.1, ECO:0000313|Proteomes:UP000076532};
RN [1] {ECO:0000313|EMBL:KZP16731.1, ECO:0000313|Proteomes:UP000076532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 109695 {ECO:0000313|EMBL:KZP16731.1,
RC ECO:0000313|Proteomes:UP000076532};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV417590; KZP16731.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166FEX8; -.
DR STRING; 436010.A0A166FEX8; -.
DR OrthoDB; 2904749at2759; -.
DR UniPathway; UPA00031; UER00013.
DR Proteomes; UP000076532; 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:UP000076532}.
FT DOMAIN 5..223
FT /note="PHP"
FT /evidence="ECO:0000259|Pfam:PF02811"
SQ SEQUENCE 321 AA; 36304 MW; E7AC82E8E1B20909 CRC64;
MPHSHHSHSG QFCQHASGLL EEVVVEAVKQ GFEMYGLTEH VPRYREEDLY PEEQGAPLDI
LTQQFTDFLQ EAHRLKLKYE SKISLIVGLE TEFITRPDLD RLQELLSIHG SRIEYIVGSV
HHVNGVPIDF DLKTFDKALS SCASAPTAGR ALDTSPMEGL LSAYFDAQYE IILRFKPEII
GHFDLCRLYH PGLRFSDYPL VWEKILRNVQ LAIGYGALFE VNAAAFRKGW QSAYPAEDVL
ELIAAQGGHL ALSDDSHGPQ SVGLNYDRLA RYLRHIGVCE IWRLESSAIL NAAGRPNAAV
KIENEWWNHS FWKERSSAAY V
//
