ID M1LT97_9PROT Unreviewed; 122 AA.
AC M1LT97;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
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=ST1E_0244 {ECO:0000313|EMBL:AGF48742.1};
OS Candidatus Kinetoplastibacterium galatii TCC219.
OC Bacteria; Pseudomonadota; Betaproteobacteria;
OC Candidatus Kinetoplastibacterium.
OX NCBI_TaxID=1208921 {ECO:0000313|EMBL:AGF48742.1, ECO:0000313|Proteomes:UP000011658};
RN [1] {ECO:0000313|EMBL:AGF48742.1, ECO:0000313|Proteomes:UP000011658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TCC219 {ECO:0000313|EMBL:AGF48742.1,
RC ECO:0000313|Proteomes:UP000011658};
RX PubMed=23345457;
RA Alves J.M., Serrano M.G., Maia da Silva F., Voegtly L.J., Matveyev A.V.,
RA Teixeira M.M., Camargo E.P., Buck G.A.;
RT "Genome evolution and phylogenomic analysis of candidatus
RT kinetoplastibacterium, the betaproteobacterial endosymbionts of strigomonas
RT and angomonas.";
RL Genome Biol. Evol. 5:338-350(2013).
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}.
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DR EMBL; CP003806; AGF48742.1; -; Genomic_DNA.
DR RefSeq; WP_015389227.1; NC_020284.1.
DR AlphaFoldDB; M1LT97; -.
DR STRING; 1208921.ST1E_0244; -.
DR KEGG; kga:ST1E_0244; -.
DR PATRIC; fig|1208921.3.peg.16; -.
DR eggNOG; COG0140; Bacteria.
DR HOGENOM; CLU_123337_1_2_4; -.
DR OrthoDB; 9814738at2; -.
DR UniPathway; UPA00031; UER00007.
DR Proteomes; UP000011658; 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 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 122 AA; 13888 MW; 46E6FE9080A67058 CRC64;
MNTIKNKEQE VLSRLADTLE TRKPNENNEL NNNSYVAKLF TNGPDSFLKK IGEEATELVM
AAKDGQSKFI INETADLWFH CIVLLTYYNL RPEDVLAELA RREGLSGIEE KARRVNKKDS
NG
//
