HIS2_NATPD
ID HIS2_NATPD Reviewed; 101 AA.
AC Q3IU57;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, 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=NP_0470A;
OS Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS 8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Natronomonas.
OX NCBI_TaxID=348780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB
RC 2260 / Gabara;
RX PubMed=16169924; DOI=10.1101/gr.3952905;
RA Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA Oesterhelt D.;
RT "Living with two extremes: conclusions from the genome sequence of
RT Natronomonas pharaonis.";
RL Genome Res. 15:1336-1343(2005).
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; CR936257; CAI48326.1; -; Genomic_DNA.
DR RefSeq; WP_011321962.1; NC_007426.1.
DR AlphaFoldDB; Q3IU57; -.
DR SMR; Q3IU57; -.
DR STRING; 348780.NP_0470A; -.
DR EnsemblBacteria; CAI48326; CAI48326; NP_0470A.
DR GeneID; 3702818; -.
DR KEGG; nph:NP_0470A; -.
DR eggNOG; arCOG02677; Archaea.
DR HOGENOM; CLU_123337_0_0_2; -.
DR OMA; FTHEKGE; -.
DR OrthoDB; 110768at2157; -.
DR UniPathway; UPA00031; UER00007.
DR Proteomes; UP000002698; 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..101
FT /note="Phosphoribosyl-ATP pyrophosphatase"
FT /id="PRO_0000230198"
SQ SEQUENCE 101 AA; 11386 MW; 7C9DE5CF9BF812DD CRC64;
MSGDGHDGDE VLDELFEVIE SRKEELPDGS YTASLFTHEK GENAVLEKLG EETTELLLAA
KDDDDEELAH EAADIVYHLL VLLSMKDMEL ADLRAELRKR R