HIS2_STRCO
ID HIS2_STRCO Reviewed; 90 AA.
AC Q9EWK0;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Phosphoribosyl-ATP pyrophosphatase;
DE Short=PRA-PH;
DE EC=3.6.1.31;
GN Name=hisE; OrderedLocusNames=SCO1439; ORFNames=SC6D7A.02c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
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; AL939108; CAC17557.1; -; Genomic_DNA.
DR RefSeq; NP_625720.1; NC_003888.3.
DR RefSeq; WP_011027788.1; NZ_VNID01000029.1.
DR PDB; 1YXB; X-ray; 2.60 A; A/B/C/D/E/F/G/H=1-90.
DR PDBsum; 1YXB; -.
DR AlphaFoldDB; Q9EWK0; -.
DR SMR; Q9EWK0; -.
DR STRING; 100226.SCO1439; -.
DR GeneID; 1096865; -.
DR KEGG; sco:SCO1439; -.
DR PATRIC; fig|100226.15.peg.1449; -.
DR eggNOG; COG0140; Bacteria.
DR HOGENOM; CLU_123337_2_1_11; -.
DR InParanoid; Q9EWK0; -.
DR OMA; WMAAEYQ; -.
DR PhylomeDB; Q9EWK0; -.
DR UniPathway; UPA00031; UER00007.
DR EvolutionaryTrace; Q9EWK0; -.
DR Proteomes; UP000001973; 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 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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; ATP-binding; Cytoplasm;
KW Histidine biosynthesis; Hydrolase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..90
FT /note="Phosphoribosyl-ATP pyrophosphatase"
FT /id="PRO_0000136388"
FT HELIX 6..16
FT /evidence="ECO:0007829|PDB:1YXB"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:1YXB"
FT HELIX 35..55
FT /evidence="ECO:0007829|PDB:1YXB"
FT HELIX 58..78
FT /evidence="ECO:0007829|PDB:1YXB"
FT HELIX 83..89
FT /evidence="ECO:0007829|PDB:1YXB"
SQ SEQUENCE 90 AA; 9919 MW; 50CACC42A8D97F55 CRC64;
MSKKTFEELF TELQHKAANG DPATSRTAEL VDKGVHAIGK KVVEEAAEVW MAAEYEGKDA
AAEEISQLLY HVQVMMVARG ISLDDVYAHL
