HIS2_PSEF5
ID HIS2_PSEF5 Reviewed; 110 AA.
AC Q4KJL6;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Phosphoribosyl-ATP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01020};
DE Short=PRA-PH {ECO:0000255|HAMAP-Rule:MF_01020};
DE EC=3.6.1.31 {ECO:0000255|HAMAP-Rule:MF_01020};
GN Name=hisE {ECO:0000255|HAMAP-Rule:MF_01020}; OrderedLocusNames=PFL_0423;
OS Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=220664;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5;
RX PubMed=15980861; DOI=10.1038/nbt1110;
RA Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A.,
RA Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S. III,
RA Thomashow L.S., Loper J.E.;
RT "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT Pf-5.";
RL Nat. Biotechnol. 23:873-878(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-
CC ribosyl)-5'-AMP + diphosphate + H(+); Xref=Rhea:RHEA:22828,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:59457, ChEBI:CHEBI:73183; EC=3.6.1.31;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01020};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
CC {ECO:0000255|HAMAP-Rule:MF_01020}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01020}.
CC -!- SIMILARITY: Belongs to the PRA-PH family. {ECO:0000255|HAMAP-
CC Rule:MF_01020}.
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DR EMBL; CP000076; AAY95832.1; -; Genomic_DNA.
DR RefSeq; WP_011058798.1; NC_004129.6.
DR AlphaFoldDB; Q4KJL6; -.
DR SMR; Q4KJL6; -.
DR STRING; 220664.PFL_0423; -.
DR EnsemblBacteria; AAY95832; AAY95832; PFL_0423.
DR KEGG; pfl:PFL_0423; -.
DR PATRIC; fig|220664.5.peg.432; -.
DR eggNOG; COG0140; Bacteria.
DR HOGENOM; CLU_123337_1_2_6; -.
DR OMA; FTHEKGE; -.
DR OrthoDB; 2022633at2; -.
DR UniPathway; UPA00031; UER00007.
DR Proteomes; UP000008540; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004636; F:phosphoribosyl-ATP diphosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd11534; NTP-PPase_HisIE_like; 1.
DR HAMAP; MF_01020; HisE; 1.
DR InterPro; IPR008179; HisE.
DR InterPro; IPR021130; PRib-ATP_PPHydrolase-like.
DR Pfam; PF01503; PRA-PH; 1.
DR TIGRFAMs; TIGR03188; histidine_hisI; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; ATP-binding; Cytoplasm; Histidine biosynthesis;
KW Hydrolase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..110
FT /note="Phosphoribosyl-ATP pyrophosphatase"
FT /id="PRO_0000230185"
SQ SEQUENCE 110 AA; 11986 MW; A15CD2100E293892 CRC64;
MSDTLTRLAQ VLEERKDAAA DSSYVASLYH KGLNKILEKV GEESVETIIA AKDAAISGDC
SDVIYETADL WFHTLVMLAQ LGQHPQAVLD ELDRRFGLSG HAEKASRPSA