ID HIS2_LEPIN Reviewed; 92 AA.
AC Q8EXX8;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 100.
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=LB_079;
OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS 56601).
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=189518;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=56601;
RX PubMed=12712204; DOI=10.1038/nature01597;
RA Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT "Unique physiological and pathogenic features of Leptospira interrogans
RT revealed by whole-genome sequencing.";
RL Nature 422:888-893(2003).
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; AE010301; AAN51638.1; -; Genomic_DNA.
DR RefSeq; NP_714623.1; NC_004343.2.
DR RefSeq; WP_000394955.1; NC_004343.2.
DR AlphaFoldDB; Q8EXX8; -.
DR SMR; Q8EXX8; -.
DR STRING; 189518.LB_079; -.
DR PaxDb; 189518-LB_079; -.
DR EnsemblBacteria; AAN51638; AAN51638; LB_079.
DR GeneID; 61141257; -.
DR KEGG; lil:LB_079; -.
DR PATRIC; fig|189518.3.peg.4407; -.
DR HOGENOM; CLU_123337_1_2_12; -.
DR InParanoid; Q8EXX8; -.
DR OrthoDB; 9795769at2; -.
DR UniPathway; UPA00031; UER00007.
DR PRO; PR:Q8EXX8; -.
DR Proteomes; UP000001408; Chromosome II.
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; ATP-binding; Cytoplasm; Histidine biosynthesis;
KW Hydrolase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..92
FT /note="Phosphoribosyl-ATP pyrophosphatase"
FT /id="PRO_0000136365"
SQ SEQUENCE 92 AA; 10547 MW; 563DFF26B1937CC4 CRC64;
MEFLLQLENI LKKRKQDLPD KSYTADLFRG GVDRILKKVG EEAGEVIIAA KNSDKKELTH
EVADLLFHLQ VLLVEQGLSL QEIVEELHKR HS
//
