HIS9_PSEAE
ID HIS9_PSEAE Reviewed; 217 AA.
AC Q9I6F6;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Histidinol-phosphatase {ECO:0000305};
DE Short=Hol-Pase {ECO:0000303|PubMed:31862725};
DE EC=3.1.3.15 {ECO:0000305|PubMed:31862725};
DE AltName: Full=Histidinol-phosphate phosphatase {ECO:0000303|PubMed:31862725};
GN OrderedLocusNames=PA0335 {ECO:0000312|EMBL:AAG03724.1};
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION AS A PHOSPHATASE, CATALYTIC ACTIVITY, PATHWAY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=31862725; DOI=10.1128/aem.02593-19;
RA Wang Y., Wang L., Zhang J., Duan X., Feng Y., Wang S., Shen L.;
RT "PA0335, a gene encoding histidinol phosphate phosphatase, mediates
RT histidine auxotrophy in Pseudomonas aeruginosa.";
RL Appl. Environ. Microbiol. 86:0-0(2020).
CC -!- FUNCTION: Catalyzes the dephosphorylation of histidinol-phosphate to
CC histidinol, the direct precursor of histidine.
CC {ECO:0000305|PubMed:31862725}.
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:0000305|PubMed:31862725};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14466;
CC Evidence={ECO:0000305|PubMed:31862725};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q58989};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q58989};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
CC {ECO:0000305|PubMed:31862725}.
CC -!- DISRUPTION PHENOTYPE: Inactivation of the gene results in growth
CC defects and incomplete auxotrophy of the mutant due to a deficiency in
CC histidine synthesis. The growth defect of the mutant is rescued by
CC expressing hisN from C.glutamicum. {ECO:0000269|PubMed:31862725}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. SerB family.
CC {ECO:0000305}.
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DR EMBL; AE004091; AAG03724.1; -; Genomic_DNA.
DR PIR; B83604; B83604.
DR RefSeq; NP_249026.1; NC_002516.2.
DR RefSeq; WP_003110585.1; NZ_QZGE01000016.1.
DR AlphaFoldDB; Q9I6F6; -.
DR SMR; Q9I6F6; -.
DR STRING; 287.DR97_3301; -.
DR PaxDb; Q9I6F6; -.
DR PRIDE; Q9I6F6; -.
DR DNASU; 882191; -.
DR EnsemblBacteria; AAG03724; AAG03724; PA0335.
DR GeneID; 882191; -.
DR KEGG; pae:PA0335; -.
DR PATRIC; fig|208964.12.peg.353; -.
DR PseudoCAP; PA0335; -.
DR HOGENOM; CLU_052657_1_1_6; -.
DR InParanoid; Q9I6F6; -.
DR OMA; DHDQMER; -.
DR PhylomeDB; Q9I6F6; -.
DR BioCyc; PAER208964:G1FZ6-338-MON; -.
DR UniPathway; UPA00031; UER00013.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006385; HAD_hydro_SerB1.
DR InterPro; IPR023214; HAD_sf.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01490; HAD-SF-IB-hyp1; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Histidine biosynthesis; Hydrolase; Magnesium;
KW Metal-binding; Reference proteome.
FT CHAIN 1..217
FT /note="Histidinol-phosphatase"
FT /id="PRO_0000454768"
FT ACT_SITE 7
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT ACT_SITE 9
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 7
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 179
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
SQ SEQUENCE 217 AA; 24386 MW; 1F5A7188F2775F5D CRC64;
MRLALFDLDN TLLAGDSDHS WGEWLCQRGL VDAAEYQARN DAFYADYVAG KLDVLAYQAF
TQAILGRTEM AQLETWHRQF MQEVIEPIVL AKGEALLAEH RAAGDRLVII TATNRFVTGP
IAERLGVETL IATECEMRDG RYTGQTFDVP CFQGGKVVRL QRWLDENGLD LEGASFYSDS
LNDLPLLEKV SRPVAVDPDP RLRAEAEKRG WPIISLR
