ID HIS9_LACLA Reviewed; 269 AA. AC Q02150; Q9CG89; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 26-SEP-2001, sequence version 2. DT 27-MAR-2024, entry version 126. DE RecName: Full=Histidinol-phosphatase; DE Short=HolPase; DE EC=3.1.3.15; GN Name=hisK; OrderedLocusNames=LL1216; ORFNames=L37351; OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Lactococcus. OX NCBI_TaxID=272623; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=NCDO 2118; RX PubMed=1400209; DOI=10.1128/jb.174.20.6571-6579.1992; RA Delorme C., Ehrlich S.D., Renault P.; RT "Histidine biosynthesis genes in Lactococcus lactis subsp. lactis."; RL J. Bacteriol. 174:6571-6579(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IL1403; RX PubMed=11337471; DOI=10.1101/gr.gr-1697r; RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J., RA Ehrlich S.D., Sorokin A.; RT "The complete genome sequence of the lactic acid bacterium Lactococcus RT lactis ssp. lactis IL1403."; RL Genome Res. 11:731-753(2001). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U92974; AAB81911.1; -; Genomic_DNA. DR EMBL; AE005176; AAK05314.1; -; Genomic_DNA. DR PIR; D47754; D47754. DR PIR; H86776; H86776. DR RefSeq; NP_267372.1; NC_002662.1. DR RefSeq; WP_003131121.1; NC_002662.1. DR PDB; 4GC3; X-ray; 1.32 A; A=2-269. DR PDB; 4GK8; X-ray; 1.93 A; A=2-269. DR PDB; 4GYF; X-ray; 1.65 A; A=2-269. DR PDBsum; 4GC3; -. DR PDBsum; 4GK8; -. DR PDBsum; 4GYF; -. DR AlphaFoldDB; Q02150; -. DR SMR; Q02150; -. DR PaxDb; 272623-L37351; -. DR EnsemblBacteria; AAK05314; AAK05314; L37351. DR KEGG; lla:L37351; -. DR PATRIC; fig|272623.7.peg.1313; -. DR eggNOG; COG1387; Bacteria. DR HOGENOM; CLU_054611_3_0_9; -. DR OrthoDB; 9775255at2; -. DR BRENDA; 3.1.3.15; 2864. DR UniPathway; UPA00031; UER00013. DR Proteomes; UP000002196; Chromosome. DR GO; GO:0004401; F:histidinol-phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1. DR InterPro; IPR010140; Histidinol_P_phosphatase_HisJ. DR InterPro; IPR004013; PHP_dom. DR InterPro; IPR003141; Pol/His_phosphatase_N. 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 SMART; SM00481; POLIIIAc; 1. DR SUPFAM; SSF89550; PHP domain-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Histidine biosynthesis; Hydrolase; KW Reference proteome. FT CHAIN 1..269 FT /note="Histidinol-phosphatase" FT /id="PRO_0000122319" FT CONFLICT 25 FT /note="T -> I (in Ref. 1; AAB81911)" FT /evidence="ECO:0000305" FT CONFLICT 30 FT /note="H -> Y (in Ref. 1; AAB81911)" FT /evidence="ECO:0000305" FT CONFLICT 71..73 FT /note="KIK -> EIN (in Ref. 1; AAB81911)" FT /evidence="ECO:0000305" FT CONFLICT 125 FT /note="I -> T (in Ref. 1; AAB81911)" FT /evidence="ECO:0000305" FT CONFLICT 146 FT /note="N -> T (in Ref. 1; AAB81911)" FT /evidence="ECO:0000305" FT CONFLICT 168 FT /note="K -> T (in Ref. 1; AAB81911)" FT /evidence="ECO:0000305" FT CONFLICT 187 FT /note="E -> G (in Ref. 1; AAB81911)" FT /evidence="ECO:0000305" FT CONFLICT 203 FT /note="E -> G (in Ref. 1; AAB81911)" FT /evidence="ECO:0000305" FT CONFLICT 215 FT /note="K -> R (in Ref. 1; AAB81911)" FT /evidence="ECO:0000305" FT CONFLICT 250 FT /note="H -> R (in Ref. 1; AAB81911)" FT /evidence="ECO:0000305" FT HELIX 20..29 FT /evidence="ECO:0007829|PDB:4GC3" FT STRAND 33..42 FT /evidence="ECO:0007829|PDB:4GC3" FT HELIX 54..67 FT /evidence="ECO:0007829|PDB:4GC3" FT TURN 68..71 FT /evidence="ECO:0007829|PDB:4GC3" FT STRAND 73..81 FT /evidence="ECO:0007829|PDB:4GC3" FT HELIX 84..86 FT /evidence="ECO:0007829|PDB:4GC3" FT HELIX 87..94 FT /evidence="ECO:0007829|PDB:4GC3" FT STRAND 100..105 FT /evidence="ECO:0007829|PDB:4GC3" FT HELIX 119..121 FT /evidence="ECO:0007829|PDB:4GC3" FT HELIX 126..143 FT /evidence="ECO:0007829|PDB:4GC3" FT STRAND 148..150 FT /evidence="ECO:0007829|PDB:4GC3" FT HELIX 155..158 FT /evidence="ECO:0007829|PDB:4GC3" FT STRAND 159..161 FT /evidence="ECO:0007829|PDB:4GYF" FT HELIX 170..172 FT /evidence="ECO:0007829|PDB:4GC3" FT HELIX 173..185 FT /evidence="ECO:0007829|PDB:4GC3" FT STRAND 189..193 FT /evidence="ECO:0007829|PDB:4GC3" FT TURN 195..198 FT /evidence="ECO:0007829|PDB:4GC3" FT HELIX 200..215 FT /evidence="ECO:0007829|PDB:4GC3" FT STRAND 220..224 FT /evidence="ECO:0007829|PDB:4GC3" FT STRAND 228..230 FT /evidence="ECO:0007829|PDB:4GC3" FT HELIX 234..246 FT /evidence="ECO:0007829|PDB:4GC3" SQ SEQUENCE 269 AA; 31473 MW; CF51601DEDD5B8C2 CRC64; MKKLDYHFHS HFSADSEELP RKHVTEAIAH GLEEICFTEH RDFYFPGMDF SLNLPEYFQE INRLQAEFKD KIKIKIGLEM GIDLRFKSEI NQFIDSAPFD FVIASVHEIG DIEVYDGTEF YLQKIKEEAQ REYLLACLDV VQNFENYNSF GHLDYVARYG PYTDKSIKFA ENREILFEIL RALASKEKAL EINTRLFDDP KTEQFYSDLL INFKKLGGKF ITLGTDSHIA KRDWLSIHKA RTLIKKAGFH ELATFSGMKI DKNKKSIKE //