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Database: UniProt
Entry: A0A0Q7LQ56_9BURK
LinkDB: A0A0Q7LQ56_9BURK
Original site: A0A0Q7LQ56_9BURK 
ID   A0A0Q7LQ56_9BURK        Unreviewed;       130 AA.
AC   A0A0Q7LQ56;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
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   ORFNames=ASD34_22720 {ECO:0000313|EMBL:KQX94921.1};
OS   Variovorax sp. Root473.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=1736541 {ECO:0000313|EMBL:KQX94921.1, ECO:0000313|Proteomes:UP000051275};
RN   [1] {ECO:0000313|Proteomes:UP000051275}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root473 {ECO:0000313|Proteomes:UP000051275};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQX94921.1, ECO:0000313|Proteomes:UP000051275}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root473 {ECO:0000313|EMBL:KQX94921.1,
RC   ECO:0000313|Proteomes:UP000051275};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|HAMAP-
CC       Rule:MF_01020}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQX94921.1}.
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DR   EMBL; LMEV01000002; KQX94921.1; -; Genomic_DNA.
DR   RefSeq; WP_056572728.1; NZ_LMEV01000002.1.
DR   AlphaFoldDB; A0A0Q7LQ56; -.
DR   OrthoDB; 9814738at2; -.
DR   UniPathway; UPA00031; UER00007.
DR   Proteomes; UP000051275; Unassembled WGS sequence.
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   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   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:UP000051275}.
SQ   SEQUENCE   130 AA;  13997 MW;  FB0609FFFD5A33CE CRC64;
     MSATVNDAHN TSDALARLAA VLESRLPANG GDPEKSYVAR LLHKGPDAFL KKIGEEATEV
     VMAAKDADHG GDRSKIVNEV ADLWFHTMVA LAHYGFSPAD VVAELERREG TSGIEEKALR
     KVQAREASND
//
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