ID A0A099D497_9ACTN Unreviewed; 87 AA.
AC A0A099D497;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
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 ECO:0000313|EMBL:KGI80766.1};
GN ORFNames=CDG81_14240 {ECO:0000313|EMBL:ASU79258.1}, IL38_15540
GN {ECO:0000313|EMBL:KGI80766.1};
OS Actinopolyspora erythraea.
OC Bacteria; Actinomycetota; Actinomycetes; Actinopolysporales;
OC Actinopolysporaceae; Actinopolyspora.
OX NCBI_TaxID=414996 {ECO:0000313|EMBL:ASU79258.1, ECO:0000313|Proteomes:UP000215043};
RN [1] {ECO:0000313|EMBL:KGI80766.1, ECO:0000313|Proteomes:UP000029737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM90600 {ECO:0000313|EMBL:KGI80766.1,
RC ECO:0000313|Proteomes:UP000029737};
RX PubMed=25250723;
RA Chen D., Feng J., Huang L., Zhang Q., Wu J., Zhu X., Duan Y., Xu Z.;
RT "Identification and Characterization of a New Erythromycin Biosynthetic
RT Gene Cluster in Actinopolyspora erythraea YIM90600, a Novel Erythronolide-
RT Producing Halophilic Actinomycete Isolated from Salt Field.";
RL PLoS ONE 9:E108129-E108129(2014).
RN [2] {ECO:0000313|EMBL:ASU79258.1, ECO:0000313|Proteomes:UP000215043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 90600 {ECO:0000313|EMBL:ASU79258.1,
RC ECO:0000313|Proteomes:UP000215043};
RA Yin M., Tang S.;
RT "The complete genome sequence of moderately halophilic actinomycete
RT Actinopolyspora erythraea YIM 90600, the producer of novel erythromycin,
RT novel actinopolysporins A-C and tubercidin.";
RL Submitted (AUG-2017) 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|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; CP022752; ASU79258.1; -; Genomic_DNA.
DR EMBL; JPMV01000027; KGI80766.1; -; Genomic_DNA.
DR RefSeq; WP_043574816.1; NZ_CP022752.1.
DR AlphaFoldDB; A0A099D497; -.
DR KEGG; aey:CDG81_14240; -.
DR eggNOG; COG0140; Bacteria.
DR HOGENOM; CLU_123337_2_1_11; -.
DR OrthoDB; 3212875at2; -.
DR UniPathway; UPA00031; UER00007.
DR Proteomes; UP000029737; Unassembled WGS sequence.
DR Proteomes; UP000215043; 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; cd11547; NTP-PPase_HisE; 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:SF1; HISTIDINE BIOSYNTHESIS BIFUNCTIONAL PROTEIN HIS7; 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}; Cytoplasm {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 87 AA; 9754 MW; 69FDFCC5A61A847F CRC64;
MKTFDELFSQ LQQRAHSRPE GSATVDALDA GIHAQGKKVL EEAGEVWLAA EHESDEQLAE
EASQLLYRLQ VILLARGLSP DDVYRYL
//
