ID   HIS1_SHELP              Reviewed;         299 AA.
AC   A3QF15;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=ATP phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00079};
DE            Short=ATP-PRT {ECO:0000255|HAMAP-Rule:MF_00079};
DE            Short=ATP-PRTase {ECO:0000255|HAMAP-Rule:MF_00079};
DE            EC=2.4.2.17 {ECO:0000255|HAMAP-Rule:MF_00079};
GN   Name=hisG {ECO:0000255|HAMAP-Rule:MF_00079}; OrderedLocusNames=Shew_2197;
OS   Shewanella loihica (strain ATCC BAA-1088 / PV-4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=323850;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1088 / PV-4;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Serres G.,
RA   Fredrickson J., Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella loihica PV-4.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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.
CC       {ECO:0000255|HAMAP-Rule:MF_00079}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00079};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00079};
CC   -!- ACTIVITY REGULATION: Feedback inhibited by histidine.
CC       {ECO:0000255|HAMAP-Rule:MF_00079}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
CC       {ECO:0000255|HAMAP-Rule:MF_00079}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00079}.
CC   -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Long
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00079}.
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DR   EMBL; CP000606; ABO24063.1; -; Genomic_DNA.
DR   RefSeq; WP_011865995.1; NC_009092.1.
DR   AlphaFoldDB; A3QF15; -.
DR   SMR; A3QF15; -.
DR   STRING; 323850.Shew_2197; -.
DR   EnsemblBacteria; ABO24063; ABO24063; Shew_2197.
DR   KEGG; slo:Shew_2197; -.
DR   eggNOG; COG0040; Bacteria.
DR   HOGENOM; CLU_038115_1_0_6; -.
DR   OMA; YVMMDYD; -.
DR   OrthoDB; 1419568at2; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000001558; 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   Reference proteome; Transferase.
FT   CHAIN           1..299
FT                   /note="ATP phosphoribosyltransferase"
FT                   /id="PRO_1000004503"
SQ   SEQUENCE   299 AA;  33110 MW;  1DF6F4E7D4AB221D CRC64;
     MSESNRLRIA IQKSGRLSKE SQKLLKSCGI KFNVNEQRLI AHSDNMPIDL LRVRDDDIPG
     LVMDGVVDLG IIGENVLEEE QIERQTLDKP SECIKLRQLD FGACRLSLAV PTEFRYQDAS
     SLEGLRIATS YPNLLRRYMQ EKGISYRDCM LKGSVEVAPR AGLADGICDL VSTGATLEAN
     GLYETEVIYR SMACIIQSTQ EQSEAKQALI DKILSRVNGV VRAKESKYIL LHAPTETLDQ
     IVALLPGAEN PTVLPLNDDT NRVAIHAVSS EDLFWDTMEA LTQLGASSIL VMPIEKMMG