ID   HIS1_NITHX              Reviewed;         325 AA.
AC   Q1QIM4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 89.
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=Nham_3188;
OS   Nitrobacter hamburgensis (strain DSM 10229 / NCIMB 13809 / X14).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Nitrobacter.
OX   NCBI_TaxID=323097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10229 / NCIMB 13809 / X14;
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., Ivanova N., Ward B., Arp D., Klotz M., Stein L.,
RA   O'Mullan G., Starkenburg S., Sayavedra L., Poret-Peterson A.T.,
RA   Gentry M.E., Bruce D., Richardson P.;
RT   "Complete sequence of chromosome of Nitrobacter hamburgensis X14.";
RL   Submitted (MAR-2006) 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; CP000319; ABE63923.1; -; Genomic_DNA.
DR   RefSeq; WP_011511579.1; NC_007964.1.
DR   AlphaFoldDB; Q1QIM4; -.
DR   SMR; Q1QIM4; -.
DR   STRING; 323097.Nham_3188; -.
DR   EnsemblBacteria; ABE63923; ABE63923; Nham_3188.
DR   KEGG; nha:Nham_3188; -.
DR   eggNOG; COG0040; Bacteria.
DR   HOGENOM; CLU_038115_0_1_5; -.
DR   OMA; LDIHNTR; -.
DR   OrthoDB; 1419568at2; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000001953; 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   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   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; Magnesium; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..325
FT                   /note="ATP phosphoribosyltransferase"
FT                   /id="PRO_1000004481"
SQ   SEQUENCE   325 AA;  35153 MW;  3AC978199B7570C1 CRC64;
     MTAPLVLAVP SKGRLQENAE AFFARAGLTL AKPRGVRDYR GTIAELDNVE IAYLSASEIA
     SQLARGMVHL GVTGEDLIRE SIVDADKRVA LIDGLGFGSA NVVVAVPQSW IDVRTMADLD
     DVTIGFRAQH NRRMRVATKY INLTRVFFAS HGVVDYRIVE SAGATEGAPA VGTAEMIVDI
     TTTGATLAAN GLKVLDDGVI LRSQANLVAS RDADWSNGAR ETARIILDHI AARARANQYR
     EVRTRFTGCD TTLLAEAHDR FGVVSPFGGP TSSGMVTLHC PPDRLYALGS FLRQHGAETV
     SIASLDYVFD RENPLFVRLE AFLRP