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Entry: D5UEU9_CELFN
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Original site: D5UEU9_CELFN 
ID   D5UEU9_CELFN            Unreviewed;        87 AA.
AC   D5UEU9;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 66.
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   OrderedLocusNames=Cfla_1862 {ECO:0000313|EMBL:ADG74759.1};
OS   Cellulomonas flavigena (strain ATCC 482 / DSM 20109 / BCRC 11376 / JCM
OS   18109 / NBRC 3775 / NCIMB 8073 / NRS 134).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=446466 {ECO:0000313|EMBL:ADG74759.1, ECO:0000313|Proteomes:UP000000849};
RN   [1] {ECO:0000313|EMBL:ADG74759.1, ECO:0000313|Proteomes:UP000000849}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 482 / DSM 20109 / BCRC 11376 / JCM 18109 / NBRC 3775 /
RC   NCIMB 8073 / NRS 134 {ECO:0000313|Proteomes:UP000000849};
RX   PubMed=21304688; DOI=10.4056/sigs.1012662;
RA   Abt B., Foster B., Lapidus A., Clum A., Sun H., Pukall R., Lucas S.,
RA   Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Goodwin L., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M.,
RA   Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Cellulomonas flavigena type strain (134).";
RL   Stand. Genomic Sci. 3:15-25(2010).
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; CP001964; ADG74759.1; -; Genomic_DNA.
DR   RefSeq; WP_013117093.1; NC_014151.1.
DR   AlphaFoldDB; D5UEU9; -.
DR   STRING; 446466.Cfla_1862; -.
DR   KEGG; cfl:Cfla_1862; -.
DR   eggNOG; COG0140; Bacteria.
DR   HOGENOM; CLU_123337_2_1_11; -.
DR   OrthoDB; 3212875at2; -.
DR   UniPathway; UPA00031; UER00007.
DR   Proteomes; UP000000849; 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}; Reference proteome {ECO:0000313|Proteomes:UP000000849}.
SQ   SEQUENCE   87 AA;  9535 MW;  A7A59A638A186D9B CRC64;
     MKSFEELFAE LSHKAATRPA GSGTVAELDA GVHAIGKKIV EEAAEVWMAS EHESDERAAE
     EISQLLYHLQ VLMLAKGLSL QDVYTHL
//
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