ID   B6IWI8_RHOCS            Unreviewed;       111 AA.
AC   B6IWI8;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   02-SEP-2026, entry version 95.
DE   RecName: Full=phosphoribosyl-ATP diphosphatase {ECO:0000256|ARBA:ARBA00012414};
DE            EC=3.6.1.31 {ECO:0000256|ARBA:ARBA00012414};
GN   Name=hisE {ECO:0000313|EMBL:ACJ00662.1};
GN   OrderedLocusNames=RC1_3300 {ECO:0000313|EMBL:ACJ00662.1};
OS   Rhodospirillum centenum (strain ATCC 51521 / SW).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Rhodospirillales; Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=414684 {ECO:0000313|EMBL:ACJ00662.1, ECO:0000313|Proteomes:UP000001591};
RN   [1] {ECO:0000313|EMBL:ACJ00662.1, ECO:0000313|Proteomes:UP000001591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51521 / SW {ECO:0000313|Proteomes:UP000001591};
RX   PubMed=20500872; DOI=10.1186/1471-2164-11-325;
RA   Lu Y.K., Marden J., Han M., Swingley W.D., Mastrian S.D., Chowdhury S.R.,
RA   Hao J., Helmy T., Kim S., Kurdoglu A.A., Matthies H.J., Rollo D.,
RA   Stothard P., Blankenship R.E., Bauer C.E., Touchman J.W.;
RT   "Metabolic flexibility revealed in the genome of the cyst-forming alpha-1
RT   proteobacterium Rhodospirillum centenum.";
RL   BMC Genomics 11:325-325(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};
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}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the PRA-PH family.
CC       {ECO:0000256|ARBA:ARBA00009392}.
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DR   EMBL; CP000613; ACJ00662.1; -; Genomic_DNA.
DR   RefSeq; WP_012568440.1; NC_011420.2.
DR   AlphaFoldDB; B6IWI8; -.
DR   STRING; 414684.RC1_3300; -.
DR   KEGG; rce:RC1_3300; -.
DR   eggNOG; COG0140; Bacteria.
DR   HOGENOM; CLU_123337_1_1_5; -.
DR   UniPathway; UPA00031; UER00007.
DR   Proteomes; UP000001591; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004636; F:phosphoribosyl-ATP diphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000105; P:L-histidine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd11534; NTP-PPase_HisIE_like; 1.
DR   Gene3D; 1.10.287.1080; MazG-like; 1.
DR   InterPro; IPR008179; HisE.
DR   InterPro; IPR021130; PRib-ATP_PPHydrolase-like.
DR   NCBIfam; TIGR03188; histidine_hisI; 1.
DR   NCBIfam; NF001611; PRK00400.1-3; 1.
DR   NCBIfam; NF001613; PRK00400.1-5; 1.
DR   PANTHER; PTHR42945; HISTIDINE BIOSYNTHESIS BIFUNCTIONAL PROTEIN; 1.
DR   PANTHER; PTHR42945:SF9; HISTIDINE BIOSYNTHESIS BIFUNCTIONAL PROTEIN HISIE; 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};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ACJ00662.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001591}.
FT   REGION          92..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   111 AA;  12215 MW;  45C6B1B9A2BD54DC CRC64;
     MLDALHRVIL SRRGADPDQS HTARLFARGR AKIAQKVGEE AVETVIEGIR GDKAKLAEES
     ADLLYHLLVL WADADLEPAR VYAILDGRRG TSGIEEKKNR KPKGKAEEAD A
//