ID   B2ICK9_BEII9            Unreviewed;       106 AA.
AC   B2ICK9;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   04-NOV-2026, entry version 93.
DE   RecName: Full=Phosphoribosyl-ATP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01020};
DE            Short=PRA-PH {ECO:0000256|HAMAP-Rule:MF_01020};
DE            EC=3.6.1.31 {ECO:0000256|HAMAP-Rule:MF_01020};
GN   Name=hisE {ECO:0000256|HAMAP-Rule:MF_01020};
GN   OrderedLocusNames=Bind_0242 {ECO:0000313|EMBL:ACB93898.1};
OS   Beijerinckia indica subsp. indica (strain ATCC 9039 / DSM 1715 / NCIMB
OS   8712).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Hyphomicrobiales; Beijerinckiaceae; Beijerinckia.
OX   NCBI_TaxID=395963 {ECO:0000313|EMBL:ACB93898.1, ECO:0000313|Proteomes:UP000001695};
RN   [1] {ECO:0000313|Proteomes:UP000001695}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9039 / DSM 1715 / NCIMB 8712
RC   {ECO:0000313|Proteomes:UP000001695};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., LaButti K., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Mikhailova N., Dunfield P.F., Dedysh S.N.,
RA   Liesack W., Saw J.H., Alam M., Chen Y., Murrell J.C., Richardson P.;
RT   "Complete sequence of chromosome of Beijerinckia indica subsp. indica ATCC
RT   9039.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACB93898.1, ECO:0000313|Proteomes:UP000001695}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9039 / DSM 1715 / NCIMB 8712
RC   {ECO:0000313|Proteomes:UP000001695};
RX   PubMed=20601475; DOI=10.1128/JB.00656-10;
RA   Tamas I., Dedysh S.N., Liesack W., Stott M.B., Alam M., Murrell J.C.,
RA   Dunfield P.F.;
RT   "Complete genome sequence of Beijerinckia indica subsp. indica.";
RL   J. Bacteriol. 192:4532-4533(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         Evidence={ECO:0000256|ARBA:ARBA00001460, ECO:0000256|HAMAP-
CC         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:0000256|ARBA:ARBA00005204, ECO:0000256|HAMAP-Rule:MF_01020}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_01020}.
CC   -!- SIMILARITY: Belongs to the PRA-PH family.
CC       {ECO:0000256|ARBA:ARBA00009392, ECO:0000256|HAMAP-Rule:MF_01020}.
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DR   EMBL; CP001016; ACB93898.1; -; Genomic_DNA.
DR   RefSeq; WP_012383256.1; NC_010581.1.
DR   AlphaFoldDB; B2ICK9; -.
DR   STRING; 395963.Bind_0242; -.
DR   KEGG; bid:Bind_0242; -.
DR   eggNOG; COG0140; Bacteria.
DR   HOGENOM; CLU_123337_1_1_5; -.
DR   OMA; ADLFFHA; -.
DR   OrthoDB; 9814738at2; -.
DR   UniPathway; UPA00031; UER00007.
DR   Proteomes; UP000001695; Chromosome.
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   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 {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_01020};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01020};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01020};
KW   Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102, ECO:0000256|HAMAP-
KW   Rule:MF_01020};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01020};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01020}; Reference proteome {ECO:0000313|Proteomes:UP000001695}.
SQ   SEQUENCE   106 AA;  11477 MW;  4AC518008F2E9840 CRC64;
     MKRFTLEDLA AVIADRAKAT AESSYTKSLL EGGPPRAAKK LGEEAVEVVI AALGTDRAAL
     TAETADLLYH LLVVLHLRDI SLQDVLDELG RRTSRSGHEE KASRAH
//