ID   HIS9_NEIM8              Reviewed;         222 AA.
AC   P0DV34;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   23-FEB-2022, sequence version 1.
DT   03-AUG-2022, entry version 3.
DE   RecName: Full=Histidinol-phosphatase {ECO:0000303|PubMed:33139723};
DE            Short=Hol-Pase {ECO:0000305};
DE            EC=3.1.3.15 {ECO:0000305|PubMed:33139723};
DE   AltName: Full=Histidinol-phosphate phosphatase {ECO:0000305};
GN   OrderedLocusNames=NMV_1317 {ECO:0000312|EMBL:CAX50163.1};
OS   Neisseria meningitidis serogroup C (strain 8013).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=604162;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8013;
RX   PubMed=19818133; DOI=10.1186/gb-2009-10-10-r110;
RA   Rusniok C., Vallenet D., Floquet S., Ewles H., Mouze-Soulama C., Brown D.,
RA   Lajus A., Buchrieser C., Medigue C., Glaser P., Pelicic V.;
RT   "NeMeSys: a biological resource for narrowing the gap between sequence and
RT   function in the human pathogen Neisseria meningitidis.";
RL   Genome Biol. 10:R110.1-R110.13(2009).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=8013;
RX   PubMed=33139723; DOI=10.1038/s41467-020-19347-y;
RA   Muir A., Gurung I., Cehovin A., Bazin A., Vallenet D., Pelicic V.;
RT   "Construction of a complete set of Neisseria meningitidis mutants and its
RT   use for the phenotypic profiling of this human pathogen.";
RL   Nat. Commun. 11:5541-5541(2020).
CC   -!- FUNCTION: Catalyzes the dephosphorylation of histidinol-phosphate to
CC       histidinol, the direct precursor of histidine.
CC       {ECO:0000305|PubMed:33139723}.
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:0000305|PubMed:33139723};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14466;
CC         Evidence={ECO:0000305|PubMed:33139723};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q58989};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q58989};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
CC       {ECO:0000305|PubMed:33139723}.
CC   -!- DISRUPTION PHENOTYPE: Deletion mutant is histidine auxotroph.
CC       Complementation of the mutant with hisB from E.coli restored growth on
CC       M9 without added histidine. {ECO:0000269|PubMed:33139723}.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. SerB family.
CC       {ECO:0000305}.
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DR   EMBL; FM999788; CAX50163.1; -; Genomic_DNA.
DR   SMR; P0DV34; -.
DR   KEGG; nmt:NMV_1317; -.
DR   UniPathway; UPA00031; UER00013.
DR   Proteomes; UP000002076; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006385; HAD_hydro_SerB1.
DR   InterPro; IPR023214; HAD_sf.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01490; HAD-SF-IB-hyp1; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Histidine biosynthesis; Hydrolase; Magnesium;
KW   Metal-binding.
FT   CHAIN           1..222
FT                   /note="Histidinol-phosphatase"
FT                   /id="PRO_0000454767"
FT   ACT_SITE        8
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q58989"
FT   ACT_SITE        10
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q58989"
FT   BINDING         8
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q58989"
FT   BINDING         10
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q58989"
FT   BINDING         184
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q58989"
SQ   SEQUENCE   222 AA;  25327 MW;  9B01A88AA9281100 CRC64;
     MKNLAIFDLD NTLINTDSDH AWPQYLIKKG LVDAAETEAQ NEKFYRDYQN GCLDIDAFLK
     FHLAPLARYS KEELAEFHRE FMAEYIIPHI SPMQRMLVQS HQMAGDETLV ISSTNEFIIT
     PVCHLFGITN IIGTQLETGS DGRYTGNYIG TPSLKEGKIT RLNQWLAERG ETLQSYGKTY
     FYSDSKNDLP LLRLVSEPVA VNPDAELEKE AKEKGWPVLN FK