ID D1BCP7_SANKS Unreviewed; 266 AA.
AC D1BCP7;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=histidinol-phosphatase {ECO:0000256|ARBA:ARBA00013085};
DE EC=3.1.3.15 {ECO:0000256|ARBA:ARBA00013085};
DE AltName: Full=Histidinol-phosphate phosphatase {ECO:0000256|ARBA:ARBA00033209};
GN OrderedLocusNames=Sked_09450 {ECO:0000313|EMBL:ACZ20895.1};
OS Sanguibacter keddieii (strain ATCC 51767 / DSM 10542 / NCFB 3025 / ST-74).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Sanguibacteraceae;
OC Sanguibacter.
OX NCBI_TaxID=446469 {ECO:0000313|EMBL:ACZ20895.1, ECO:0000313|Proteomes:UP000000322};
RN [1] {ECO:0000313|EMBL:ACZ20895.1, ECO:0000313|Proteomes:UP000000322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51767 / DSM 10542 / NCFB 3025 / ST-74
RC {ECO:0000313|Proteomes:UP000000322};
RX PubMed=21304646;
RA Ivanova N., Sikorski J., Sims D., Brettin T., Detter J.C., Han C.,
RA Lapidus A., Copeland A., Glavina Del Rio T., Nolan M., Chen F., Lucas S.,
RA Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Pati A.,
RA Mavromatis K., Chen A., Palaniappan K., D'haeseleer P., Chain P.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Goker M., Pukall R.,
RA Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Sanguibacter keddieii type strain (ST-74).";
RL Stand. Genomic Sci. 1:110-118(2009).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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}.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000256|ARBA:ARBA00009759}.
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DR EMBL; CP001819; ACZ20895.1; -; Genomic_DNA.
DR RefSeq; WP_012865964.1; NC_013521.1.
DR AlphaFoldDB; D1BCP7; -.
DR STRING; 446469.Sked_09450; -.
DR KEGG; ske:Sked_09450; -.
DR eggNOG; COG0483; Bacteria.
DR HOGENOM; CLU_044118_4_0_11; -.
DR OrthoDB; 9772456at2; -.
DR UniPathway; UPA00031; UER00013.
DR Proteomes; UP000000322; Chromosome.
DR GO; GO:0004401; F:histidinol-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.190.80; -; 1.
DR Gene3D; 3.30.540.10; Fructose-1,6-Bisphosphatase, subunit A, domain 1; 1.
DR InterPro; IPR011809; His_9_proposed.
DR InterPro; IPR020583; Inositol_monoP_metal-BS.
DR InterPro; IPR000760; Inositol_monophosphatase-like.
DR NCBIfam; TIGR02067; his_9_HisN; 1.
DR PANTHER; PTHR43200:SF26; BIFUNCTIONAL PHOSPHATASE IMPL2, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43200; PHOSPHATASE; 1.
DR Pfam; PF00459; Inositol_P; 1.
DR PRINTS; PR00377; IMPHPHTASES.
DR SUPFAM; SSF56655; Carbohydrate phosphatase; 1.
DR PROSITE; PS00629; IMP_1; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
SQ SEQUENCE 266 AA; 28772 MW; 8F90BF34659D9D2F CRC64;
MIARPHYDDD LRLALVIADQ VDAQTMARFK ALDLHVESKP DHTPVTDADR SAEEIIRGQL
SRSRGRDAVL GEEFGATGHG SRRWIVDPID GTKNFVRGVP VWATLIALAE GDEIVVGVVS
APALGRRWWA AQGTGAWTGR SLSSATRLQV SGVRDIADAS MSYSSLSGWE ERGRLPHFLD
LSRQTWRTRA YGDFWSYMLV AEGAVDIAVE PELELYDMAA LVPIVTEAGG RFTSLAGVDG
PFGGNAAVTN GHLHDHVLAT VGFGAH
//
