ID   HIS9_BACSU              Reviewed;         268 AA.
AC   O34411;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Histidinol-phosphatase;
DE            Short=HolPase;
DE            EC=3.1.3.15;
GN   Name=hisK; Synonyms=hisJ; OrderedLocusNames=BSU29620;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA   Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT   "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT   200 kb rrnB-dnaB region.";
RL   Microbiology 143:3431-3441(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   CHARACTERIZATION.
RX   PubMed=10322033; DOI=10.1128/jb.181.10.3277-3280.1999;
RA   Le Coq D., Fillinger S., Aymerich S.;
RT   "Histidinol phosphate phosphatase, catalyzing the penultimate step of the
RT   histidine biosynthesis pathway, is encoded by ytvP (hisJ) in Bacillus
RT   subtilis.";
RL   J. Bacteriol. 181:3277-3280(1999).
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   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
CC   -!- SIMILARITY: Belongs to the PHP hydrolase family. HisK subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF008220; AAC00399.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14940.1; -; Genomic_DNA.
DR   PIR; D70002; D70002.
DR   RefSeq; NP_390840.1; NC_000964.3.
DR   RefSeq; WP_003229318.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; O34411; -.
DR   SMR; O34411; -.
DR   STRING; 224308.BSU29620; -.
DR   PaxDb; O34411; -.
DR   EnsemblBacteria; CAB14940; CAB14940; BSU_29620.
DR   GeneID; 937924; -.
DR   KEGG; bsu:BSU29620; -.
DR   PATRIC; fig|224308.179.peg.3218; -.
DR   eggNOG; COG1387; Bacteria.
DR   InParanoid; O34411; -.
DR   OMA; KRIGHIT; -.
DR   PhylomeDB; O34411; -.
DR   BioCyc; BSUB:BSU29620-MON; -.
DR   UniPathway; UPA00031; UER00013.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0004401; F:histidinol-phosphatase activity; IBA:GO_Central.
DR   GO; GO:0000105; P:histidine biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR010140; Histidinol_P_phosphatase_HisJ.
DR   InterPro; IPR004013; PHP_dom.
DR   InterPro; IPR016195; Pol/histidinol_Pase-like.
DR   PANTHER; PTHR21039; PTHR21039; 1.
DR   Pfam; PF02811; PHP; 1.
DR   SUPFAM; SSF89550; SSF89550; 1.
DR   TIGRFAMs; TIGR01856; hisJ_fam; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Histidine biosynthesis; Hydrolase;
KW   Reference proteome.
FT   CHAIN           1..268
FT                   /note="Histidinol-phosphatase"
FT                   /id="PRO_0000122316"
SQ   SEQUENCE   268 AA;  30476 MW;  5F948F4CB9E0DC6F CRC64;
     MQKRDGHIHT PFCPHGSNDT LRQYAEEALK KGFESITFTE HAPLPPSFTD PTPLKDSAMA
     QASLERYIHE ISGLKKEYRG QLSIRTGLEV DYIAEFEDEI TLFLDTYGPY LDDSILSVHF
     LRTDSSYLCL DYDEHTFKEL ISACGSIEAV YEQYYRSIYS SIVASLGVYK PKRVGHITLV
     QKFIKLFPYS MSEHIRGLVS LCLNAIEENG MELDFNTSGL RKTYAGGIYI EDWMLNEAKQ
     KKIPLVFGSD AHQAGDVGYA YEAFLERC