ID   HIS2_RHOCB              Reviewed;         103 AA.
AC   O30723; D5ARN9;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Phosphoribosyl-ATP pyrophosphatase;
DE            Short=PRA-PH;
DE            EC=3.6.1.31;
GN   Name=hisE; OrderedLocusNames=RCAP_rcc01152;
OS   Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=272942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MT1131;
RX   PubMed=9473054; DOI=10.1128/jb.180.4.969-978.1998;
RA   Koch H.G., Hwang O., Daldal F.;
RT   "Isolation and characterization of Rhodobacter capsulatus mutants affected
RT   in cytochrome cbb3 oxidase activity.";
RL   J. Bacteriol. 180:969-978(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX   PubMed=20418398; DOI=10.1128/jb.00366-10;
RA   Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA   Haselkorn R.;
RT   "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT   Rhodobacter capsulatus SB 1003.";
RL   J. Bacteriol. 192:3545-3546(2010).
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   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PRA-PH family. {ECO:0000305}.
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DR   EMBL; AF016223; AAC46104.1; -; Genomic_DNA.
DR   EMBL; CP001312; ADE84910.1; -; Genomic_DNA.
DR   RefSeq; WP_013066889.1; NC_014034.1.
DR   AlphaFoldDB; O30723; -.
DR   SMR; O30723; -.
DR   STRING; 272942.RCAP_rcc01152; -.
DR   EnsemblBacteria; ADE84910; ADE84910; RCAP_rcc01152.
DR   GeneID; 31490065; -.
DR   KEGG; rcp:RCAP_rcc01152; -.
DR   eggNOG; COG0140; Bacteria.
DR   HOGENOM; CLU_123337_1_1_5; -.
DR   OMA; FTHEKGE; -.
DR   OrthoDB; 2022633at2; -.
DR   UniPathway; UPA00031; UER00007.
DR   Proteomes; UP000002361; 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..103
FT                   /note="Phosphoribosyl-ATP pyrophosphatase"
FT                   /id="PRO_0000136383"
SQ   SEQUENCE   103 AA;  10962 MW;  34EBC0E9A22DECA1 CRC64;
     MTALSRLAAT VEARKGADPE SSWTAKLFAK GPEKCAEKFG EEAVEAIIAA VKNDRANLVY
     EAADVLYHLT VMLAARDVSL DEVLAELDRR AGTSGIAEKA ARG