ID   HIS1_PYRFU              Reviewed;         204 AA.
AC   Q8U0D4;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=ATP phosphoribosyltransferase;
DE            Short=ATP-PRT;
DE            Short=ATP-PRTase;
DE            EC=2.4.2.17;
GN   Name=hisG; OrderedLocusNames=PF1658;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
CC   -!- FUNCTION: Catalyzes the condensation of ATP and 5-phosphoribose 1-
CC       diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial
CC       role in the pathway because the rate of histidine biosynthesis seems to
CC       be controlled primarily by regulation of HisG enzymatic activity (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-phospho-
CC         alpha-D-ribose 1-diphosphate + ATP; Xref=Rhea:RHEA:18473,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017,
CC         ChEBI:CHEBI:73183; EC=2.4.2.17;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Short
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AE009950; AAL81782.1; -; Genomic_DNA.
DR   RefSeq; WP_011012804.1; NZ_CP023154.1.
DR   AlphaFoldDB; Q8U0D4; -.
DR   SMR; Q8U0D4; -.
DR   STRING; 186497.PF1658; -.
DR   EnsemblBacteria; AAL81782; AAL81782; PF1658.
DR   GeneID; 41713486; -.
DR   KEGG; pfu:PF1658; -.
DR   PATRIC; fig|186497.12.peg.1724; -.
DR   eggNOG; arCOG02208; Archaea.
DR   HOGENOM; CLU_038115_2_0_2; -.
DR   OMA; VASKFVH; -.
DR   OrthoDB; 67224at2157; -.
DR   PhylomeDB; Q8U0D4; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000001013; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003879; F:ATP phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd13595; PBP2_HisGs; 1.
DR   HAMAP; MF_01018; HisG_Short; 1.
DR   InterPro; IPR013820; ATP_PRibTrfase_cat.
DR   InterPro; IPR018198; ATP_PRibTrfase_CS.
DR   InterPro; IPR001348; ATP_PRibTrfase_HisG.
DR   InterPro; IPR024893; ATP_PRibTrfase_HisG_short.
DR   PANTHER; PTHR21403; PTHR21403; 1.
DR   Pfam; PF01634; HisG; 1.
DR   TIGRFAMs; TIGR00070; hisG; 1.
DR   PROSITE; PS01316; ATP_P_PHORIBOSYLTR; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; ATP-binding; Cytoplasm; Glycosyltransferase;
KW   Histidine biosynthesis; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..204
FT                   /note="ATP phosphoribosyltransferase"
FT                   /id="PRO_0000151949"
SQ   SEQUENCE   204 AA;  22913 MW;  539983612DC591BA CRC64;
     MRFVLPKGRL YQDSIKVLEL AGIKVPKRDE RALIWGDGNN EFLLARAFDV PVYVEHGIDI
     GIAGSDVVEE RGSDVFIPLE LPFGKCRLSI AVPKEKVVDP ENMDGYKIAT KYPNITKRYF
     ENLNIEVEVI KLHGSIELAP RIGIADAIVD IVETGNTLRS NGLVEVAKIM DVSALLLVNR
     ISQKMFFEEI NSFITKIRRS VYGH