HIS2_STRSV
ID HIS2_STRSV Reviewed; 104 AA.
AC A3CNS8;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 87.
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=SSA_1440;
OS Streptococcus sanguinis (strain SK36).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=388919;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK36;
RX PubMed=17277061; DOI=10.1128/jb.01808-06;
RA Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL J. Bacteriol. 189:3166-3175(2007).
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; CP000387; ABN44833.1; -; Genomic_DNA.
DR RefSeq; WP_011837137.1; NC_009009.1.
DR RefSeq; YP_001035383.1; NC_009009.1.
DR AlphaFoldDB; A3CNS8; -.
DR SMR; A3CNS8; -.
DR STRING; 388919.SSA_1440; -.
DR EnsemblBacteria; ABN44833; ABN44833; SSA_1440.
DR KEGG; ssa:SSA_1440; -.
DR PATRIC; fig|388919.9.peg.1365; -.
DR eggNOG; COG0140; Bacteria.
DR HOGENOM; CLU_123337_0_0_9; -.
DR OMA; FTHEKGE; -.
DR OrthoDB; 2022633at2; -.
DR UniPathway; UPA00031; UER00007.
DR Proteomes; UP000002148; 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 HAMAP; MF_01020; HisE; 1.
DR InterPro; IPR008179; HisE.
DR InterPro; IPR021130; PRib-ATP_PPHydrolase-like.
DR Pfam; PF01503; PRA-PH; 1.
DR TIGRFAMs; TIGR03188; histidine_hisI; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; ATP-binding; Cytoplasm; Histidine biosynthesis;
KW Hydrolase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..104
FT /note="Phosphoribosyl-ATP pyrophosphatase"
FT /id="PRO_0000319667"
SQ SEQUENCE 104 AA; 11807 MW; 17914109C9AC3BC6 CRC64;
MLETLYQEAL KRKKEPKEGS YTSYLYDKGL DKILKKVGEE ATEVVIAAKN ADKNEMANET
ADLLYHLAVA LVETGVSLEE VETVLQARQG KQSRIHDRPE IDHY