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Database: UniProt
Entry: A0A0R1K7L8_9LACO
LinkDB: A0A0R1K7L8_9LACO
Original site: A0A0R1K7L8_9LACO 
ID   A0A0R1K7L8_9LACO        Unreviewed;       110 AA.
AC   A0A0R1K7L8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Phosphoribosyl-ATP pyrophosphatase {ECO:0000256|ARBA:ARBA00013336, ECO:0000256|HAMAP-Rule:MF_01020};
DE            Short=PRA-PH {ECO:0000256|HAMAP-Rule:MF_01020};
DE            EC=3.6.1.31 {ECO:0000256|ARBA:ARBA00012414, ECO:0000256|HAMAP-Rule:MF_01020};
GN   Name=hisE {ECO:0000256|HAMAP-Rule:MF_01020};
GN   ORFNames=FD03_GL001638 {ECO:0000313|EMBL:KRK79272.1};
OS   Companilactobacillus nodensis DSM 19682 = JCM 14932 = NBRC 107160.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Companilactobacillus.
OX   NCBI_TaxID=1423775 {ECO:0000313|EMBL:KRK79272.1, ECO:0000313|Proteomes:UP000051248};
RN   [1] {ECO:0000313|EMBL:KRK79272.1, ECO:0000313|Proteomes:UP000051248}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19682 {ECO:0000313|EMBL:KRK79272.1,
RC   ECO:0000313|Proteomes:UP000051248};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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|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:KRK79272.1}.
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DR   EMBL; AZDZ01000019; KRK79272.1; -; Genomic_DNA.
DR   RefSeq; WP_025023166.1; NZ_BCWC01000001.1.
DR   AlphaFoldDB; A0A0R1K7L8; -.
DR   STRING; 1423775.FD03_GL001638; -.
DR   PATRIC; fig|1423775.4.peg.1669; -.
DR   eggNOG; COG0140; Bacteria.
DR   OrthoDB; 9795769at2; -.
DR   UniPathway; UPA00031; UER00007.
DR   Proteomes; UP000051248; 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; PHOSPHORIBOSYL-ATP PYROPHOSPHATASE; 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}.
SQ   SEQUENCE   110 AA;  12715 MW;  EB01747213700DC5 CRC64;
     MQNLDELYEM VKQRKENPKE GSYTDYLFSK GLDKILKKVG EESTEVVVAA KNPDKPRGDG
     ELVYESADLL YHLCVLWVEQ GVTFDQIKTE LAKREGLMSE YKDRPEIKDL
//
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