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Database: UniProt
Entry: E6UI95_RUMA7
LinkDB: E6UI95_RUMA7
Original site: E6UI95_RUMA7 
ID   E6UI95_RUMA7            Unreviewed;       282 AA.
AC   E6UI95;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 57.
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   OrderedLocusNames=Rumal_1656 {ECO:0000313|EMBL:ADU22156.1};
OS   Ruminococcus albus (strain ATCC 27210 / DSM 20455 / JCM 14654 / NCDO 2250 /
OS   7).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=697329 {ECO:0000313|EMBL:ADU22156.1, ECO:0000313|Proteomes:UP000006919};
RN   [1] {ECO:0000313|EMBL:ADU22156.1, ECO:0000313|Proteomes:UP000006919}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27210 / DSM 20455 / JCM 14654 / NCDO 2250 / 7
RC   {ECO:0000313|Proteomes:UP000006919};
RX   PubMed=21914885; DOI=10.1128/JB.05621-11;
RA   Suen G., Stevenson D.M., Bruce D.C., Chertkov O., Copeland A., Cheng J.F.,
RA   Detter C., Detter J.C., Goodwin L.A., Han C.S., Hauser L.J., Ivanova N.N.,
RA   Kyrpides N.C., Land M.L., Lapidus A., Lucas S., Ovchinnikova G.,
RA   Pitluck S., Tapia R., Woyke T., Boyum J., Mead D., Weimer P.J.;
RT   "Complete genome of the cellulolytic ruminal bacterium Ruminococcus albus
RT   7.";
RL   J. Bacteriol. 193:5574-5575(2011).
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; CP002403; ADU22156.1; -; Genomic_DNA.
DR   RefSeq; WP_013498321.1; NZ_JHYT01000011.1.
DR   AlphaFoldDB; E6UI95; -.
DR   STRING; 697329.Rumal_1656; -.
DR   KEGG; ral:Rumal_1656; -.
DR   eggNOG; COG1387; Bacteria.
DR   HOGENOM; CLU_054611_3_0_9; -.
DR   OrthoDB; 9775255at2; -.
DR   UniPathway; UPA00031; UER00013.
DR   Proteomes; UP000006919; Chromosome.
DR   GO; GO:0004401; F:histidinol-phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
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}.
FT   DOMAIN          7..211
FT                   /note="PHP"
FT                   /evidence="ECO:0000259|Pfam:PF02811"
SQ   SEQUENCE   282 AA;  32102 MW;  94BDCEBCCC93FE9F CRC64;
     MDRILLDMHT HSSYSPDAED SAEAMCLKAA ELGMSVYALT DHCDVNFWEE APSPDTVDAM
     MYGAGKYALS SITEQTELRE RFRGRLDIIV GIELGQPMQN TEKAELIVND PRLDFIIGSH
     HMNKGVDDFY YLDYGKMSDD EIQSLLKDCF EQTLEMCRSA DIDVLGHLTY PLRYICGEYG
     RQVDISGYEE MIREIFRTLI SRGKGIEINT SGLRQKYGRT FPDFEILKLY RELGGEILTV
     GSDAHRTSDL GKGIPEGIEL ARAAGFEKIT YFKRHEPYFL KL
//
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