ID   HIS2_DECAR              Reviewed;         108 AA.
AC   Q47AM5;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   02-SEP-2026, entry version 90.
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};
GN   OrderedLocusNames=Daro_3377;
OS   Dechloromonas aromatica (strain RCB).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Rhodocyclales; Azonexaceae; Dechloromonas.
OX   NCBI_TaxID=159087;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCB;
RX   PubMed=19650930; DOI=10.1186/1471-2164-10-351;
RA   Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G.,
RA   Lapidus A.;
RT   "Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB:
RT   indications of a surprisingly complex life-style and cryptic anaerobic
RT   pathways for aromatic degradation.";
RL   BMC Genomics 10:351-351(2009).
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; CP000089; AAZ48106.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q47AM5; -.
DR   SMR; Q47AM5; -.
DR   STRING; 159087.Daro_3377; -.
DR   KEGG; dar:Daro_3377; -.
DR   eggNOG; COG0140; Bacteria.
DR   HOGENOM; CLU_123337_1_2_4; -.
DR   OrthoDB; 9814738at2; -.
DR   UniPathway; UPA00031; UER00007.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004636; F:phosphoribosyl-ATP diphosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000105; P:L-histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd11534; NTP-PPase_HisIE_like; 1.
DR   FunFam; 1.10.287.1080:FF:000002; Histidine biosynthesis bifunctional protein HisIE; 1.
DR   Gene3D; 1.10.287.1080; MazG-like; 1.
DR   HAMAP; MF_01020; HisE; 1.
DR   InterPro; IPR008179; HisE.
DR   InterPro; IPR021130; PRib-ATP_PPHydrolase-like.
DR   NCBIfam; TIGR03188; histidine_hisI; 1.
DR   NCBIfam; NF001611; PRK00400.1-3; 1.
DR   NCBIfam; NF001613; PRK00400.1-5; 1.
DR   PANTHER; PTHR42945; HISTIDINE BIOSYNTHESIS BIFUNCTIONAL PROTEIN; 1.
DR   PANTHER; PTHR42945:SF9; HISTIDINE BIOSYNTHESIS BIFUNCTIONAL PROTEIN HISIE; 1.
DR   Pfam; PF01503; PRA-PH; 1.
DR   SUPFAM; SSF101386; all-alpha NTP pyrophosphatases; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; ATP-binding; Cytoplasm; Histidine biosynthesis;
KW   Hydrolase; Nucleotide-binding.
FT   CHAIN           1..108
FT                   /note="Phosphoribosyl-ATP pyrophosphatase"
FT                   /id="PRO_0000230174"
SQ   SEQUENCE   108 AA;  12161 MW;  A8609C77F60CE6BC CRC64;
     MSTHDILHRL SETLASRRHA DPEKSYTAKL FSEGPDSILK KIGEECAELI MAAKDGKRLN
     IVWESTDVIY HVLVLLAFYG LSIEDVSQEM RRREGISGID EKASRGTK
//