ID N0B4U2_9BACI Unreviewed; 263 AA.
AC N0B4U2;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=B1NLA3E_17355 {ECO:0000313|EMBL:AGK55215.1};
OS Bacillus sp. 1NLA3E.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=666686 {ECO:0000313|EMBL:AGK55215.1, ECO:0000313|Proteomes:UP000013300};
RN [1] {ECO:0000313|EMBL:AGK55215.1, ECO:0000313|Proteomes:UP000013300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1NLA3E {ECO:0000313|EMBL:AGK55215.1};
RX PubMed=23833140;
RA Venkatramanan R., Prakash O., Woyke T., Chain P., Goodwin L.A., Watson D.,
RA Brooks S., Kostka J.E., Green S.J.;
RT "Genome sequences for three denitrifying bacterial strains isolated from a
RT uranium- and nitrate-contaminated subsurface environment.";
RL Genome Announc. 1:e00449-13(2013).
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; CP005586; AGK55215.1; -; Genomic_DNA.
DR RefSeq; WP_015595262.1; NC_021171.1.
DR AlphaFoldDB; N0B4U2; -.
DR STRING; 666686.B1NLA3E_17355; -.
DR KEGG; baci:B1NLA3E_17355; -.
DR eggNOG; COG1387; Bacteria.
DR HOGENOM; CLU_054611_2_1_9; -.
DR OrthoDB; 9775255at2; -.
DR UniPathway; UPA00031; UER00013.
DR Proteomes; UP000013300; Chromosome.
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:UP000013300}.
FT DOMAIN 4..213
FT /note="PHP"
FT /evidence="ECO:0000259|Pfam:PF02811"
SQ SEQUENCE 263 AA; 30156 MW; 921053A975CA4086 CRC64;
MRKDGHIHTP YCPHGTKDSF KEYVENAIFL GFDEISFTEH APLPVGFLDP TPAKDSGMPA
NKIETYLHDI EMIKKEYCSQ IKINSGLEVD FIEGYEEETR EFLTIFGPNL DDAILSVHFL
KHDNEYDCMD YSPQVFGEMV KKYGSVEAVY KKYYETVMKS VNADLGHYKP KRIGHITLVH
KFQKKFPVLS SFESEINELF ITIKRNGYEL DYNGAGTAKP LCQEPYPPDW VVDKAIAMGI
PLIYGSDAHQ KKEMGQGRQF MKI
//
