ID   HIS2_NOCFA              Reviewed;          87 AA.
AC   Q5YUV8;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 91.
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=NFA_31860;
OS   Nocardia farcinica (strain IFM 10152).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX   NCBI_TaxID=247156;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 10152;
RX   PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA   Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA   Shiba T., Hattori M.;
RT   "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004).
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; AP006618; BAD58033.1; -; Genomic_DNA.
DR   RefSeq; WP_011209718.1; NC_006361.1.
DR   AlphaFoldDB; Q5YUV8; -.
DR   SMR; Q5YUV8; -.
DR   STRING; 247156.NFA_31860; -.
DR   EnsemblBacteria; BAD58033; BAD58033; NFA_31860.
DR   GeneID; 61133901; -.
DR   KEGG; nfa:NFA_31860; -.
DR   eggNOG; COG0140; Bacteria.
DR   HOGENOM; CLU_123337_2_1_11; -.
DR   OMA; WMAAEYQ; -.
DR   UniPathway; UPA00031; UER00007.
DR   Proteomes; UP000006820; 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   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..87
FT                   /note="Phosphoribosyl-ATP pyrophosphatase"
FT                   /id="PRO_0000230183"
SQ   SEQUENCE   87 AA;  9640 MW;  92DCA1C0998DE1E3 CRC64;
     MKTFETLFAE LQDRAATRPE GSGTVAALDA GVHAQGKKVL EEAGEVWLAA EHESDESLAE
     EISQLLYWVQ VLMVGRGLKL EDVYRHL