HIS9_DEIRA
ID HIS9_DEIRA Reviewed; 260 AA.
AC Q9RX45;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Probable histidinol-phosphatase;
DE Short=HolPase;
DE EC=3.1.3.15;
GN Name=hisK; OrderedLocusNames=DR_0470;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(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; AE000513; AAF10049.1; -; Genomic_DNA.
DR PIR; F75515; F75515.
DR RefSeq; NP_294193.1; NC_001263.1.
DR RefSeq; WP_010887115.1; NZ_CP015081.1.
DR AlphaFoldDB; Q9RX45; -.
DR SMR; Q9RX45; -.
DR STRING; 243230.DR_0470; -.
DR EnsemblBacteria; AAF10049; AAF10049; DR_0470.
DR KEGG; dra:DR_0470; -.
DR PATRIC; fig|243230.17.peg.648; -.
DR eggNOG; COG1387; Bacteria.
DR HOGENOM; CLU_054611_2_0_0; -.
DR InParanoid; Q9RX45; -.
DR OMA; DYDRPMY; -.
DR OrthoDB; 1615112at2; -.
DR UniPathway; UPA00031; UER00013.
DR Proteomes; UP000002524; Chromosome I.
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 3: Inferred from homology;
KW Amino-acid biosynthesis; Histidine biosynthesis; Hydrolase;
KW Reference proteome.
FT CHAIN 1..260
FT /note="Probable histidinol-phosphatase"
FT /id="PRO_0000122318"
SQ SEQUENCE 260 AA; 28874 MW; 9CB176BB000EDEA3 CRC64;
MTGLCDSHLH TPLCGHATGT PREYAQAALD AGLSGLCFTD HMPMPRWYDA PWRMKLEQLP
EYIAEIQAVQ QEFAGRLDVR LGLEADFHPG TEKFVEKVLG MFDWDYVIGS VHYLGAWGFD
NPEFVAEYEE RDLGGLYRDY YALVEGAARS GLFDAIGHLD LPKKFGHLDP DPVYALHALD
VVAGQGLALD FNTAGWRKPV AEAYPAPDLV RAAAERGIPF VLGSDAHQPG EVGFRFADAV
KEIRDVGGRT VTFRHRKMQP