ID   HIS1_BUCAP              Reviewed;         299 AA.
AC   Q9ZHE7;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2002, sequence version 2.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=ATP phosphoribosyltransferase;
DE            Short=ATP-PRT;
DE            Short=ATP-PRTase;
DE            EC=2.4.2.17;
GN   Name=hisG; OrderedLocusNames=BUsg_092;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9767718; DOI=10.1007/s002849900392;
RA   Clark M.A., Baumann L., Baumann P.;
RT   "Buchnera aphidicola (Aphid endosymbiont) contains genes encoding enzymes
RT   of histidine biosynthesis.";
RL   Curr. Microbiol. 37:356-358(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Feedback inhibited by histidine. {ECO:0000250}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
CC   -!- SUBUNIT: Equilibrium between an active dimeric form, an inactive
CC       hexameric form and higher aggregates. Interconversion between the
CC       various forms is largely reversible and is influenced by the natural
CC       substrates and inhibitors of the enzyme (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Long
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF067228; AAC97354.1; -; Genomic_DNA.
DR   EMBL; AE013218; AAM67662.1; -; Genomic_DNA.
DR   RefSeq; WP_011053628.1; NC_004061.1.
DR   AlphaFoldDB; Q9ZHE7; -.
DR   SMR; Q9ZHE7; -.
DR   STRING; 198804.BUsg_092; -.
DR   EnsemblBacteria; AAM67662; AAM67662; BUsg_092.
DR   KEGG; bas:BUsg_092; -.
DR   eggNOG; COG0040; Bacteria.
DR   HOGENOM; CLU_038115_1_0_6; -.
DR   OMA; YVMMDYD; -.
DR   OrthoDB; 1419568at2; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000000416; 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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.70.120; -; 1.
DR   HAMAP; MF_00079; HisG_Long; 1.
DR   InterPro; IPR013820; ATP_PRibTrfase_cat.
DR   InterPro; IPR018198; ATP_PRibTrfase_CS.
DR   InterPro; IPR001348; ATP_PRibTrfase_HisG.
DR   InterPro; IPR020621; ATP_PRibTrfase_HisG_long.
DR   InterPro; IPR013115; HisG_C.
DR   InterPro; IPR011322; N-reg_PII-like_a/b.
DR   InterPro; IPR015867; N-reg_PII/ATP_PRibTrfase_C.
DR   PANTHER; PTHR21403; PTHR21403; 1.
DR   Pfam; PF01634; HisG; 1.
DR   Pfam; PF08029; HisG_C; 1.
DR   SUPFAM; SSF54913; SSF54913; 1.
DR   TIGRFAMs; TIGR00070; hisG; 1.
DR   TIGRFAMs; TIGR03455; HisG_C-term; 1.
DR   PROSITE; PS01316; ATP_P_PHORIBOSYLTR; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; ATP-binding; Cytoplasm; Glycosyltransferase;
KW   Histidine biosynthesis; Magnesium; Metal-binding; Nucleotide-binding;
KW   Transferase.
FT   CHAIN           1..299
FT                   /note="ATP phosphoribosyltransferase"
FT                   /id="PRO_0000151834"
FT   CONFLICT        143..145
FT                   /note="NIV -> TL (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        147..148
FT                   /note="KS -> QV (in Ref. 1)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   299 AA;  33349 MW;  8E0858F490DFF1C0 CRC64;
     MFNTNRVRIA MQKTGRLSSE SIKLLTCCGI KINLKQQKLI AFAENMPIDV MLVRDDDIPG
     LVMDGVVDLG IVGENVLQEE LLHRISQNLE NSYITLRRLD FGICRLSLAI PINTPYVDIT
     SLKNFRIATS YPHLLKKYLD SKNIVFKSCM LNGSVEVAPR AGLADAICDL VSTGATLEAN
     GLREVQVVFR SHACLICKTG NINFAKKEVI NKLMTRIKGV IKARESKYIM LHAPVNKLEE
     VISLLHGAEK PTILKLAGDD HRVAMHMVSS ETLFWETMEK LKSLGASSIL VLPIEKMME