HIS2_NEIMA
ID HIS2_NEIMA Reviewed; 107 AA.
AC Q9JVJ9; A1IQL9;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Phosphoribosyl-ATP pyrophosphatase;
DE Short=PRA-PH;
DE EC=3.6.1.31;
GN Name=hisE; OrderedLocusNames=NMA0807;
OS Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS Z2491).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122587;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15465 / Z2491;
RX PubMed=10761919; DOI=10.1038/35006655;
RA Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA Barrell B.G.;
RT "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT Z2491.";
RL Nature 404:502-506(2000).
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 -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PRA-PH family. {ECO:0000305}.
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DR EMBL; AL157959; CAM08051.1; -; Genomic_DNA.
DR PIR; G81925; G81925.
DR RefSeq; WP_002217796.1; NC_003116.1.
DR AlphaFoldDB; Q9JVJ9; -.
DR SMR; Q9JVJ9; -.
DR EnsemblBacteria; CAM08051; CAM08051; NMA0807.
DR GeneID; 61280830; -.
DR KEGG; nma:NMA0807; -.
DR HOGENOM; CLU_123337_1_2_4; -.
DR OMA; FTHEKGE; -.
DR BioCyc; NMEN122587:NMA_RS04065-MON; -.
DR UniPathway; UPA00031; UER00007.
DR Proteomes; UP000000626; 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.
FT CHAIN 1..107
FT /note="Phosphoribosyl-ATP pyrophosphatase"
FT /id="PRO_0000136373"
SQ SEQUENCE 107 AA; 11896 MW; D2830C03D8C66EEF CRC64;
MGDSVLSAIQ QTITQRKSAN PSESYVAQLL HKGEDKILKK VIEEAGEVLM ASKDKNPSHL
VYEVADLWFH TMILLTHHDL KAEDVLDELA RRQGLSGLAE KAARTES