ID   HIS1_ZYMMO              Reviewed;         222 AA.
AC   Q9RH04; Q5NM86;
DT   03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 2.
DT   25-MAY-2022, entry version 113.
DE   RecName: Full=ATP phosphoribosyltransferase;
DE            Short=ATP-PRT;
DE            Short=ATP-PRTase;
DE            EC=2.4.2.17;
GN   Name=hisG; OrderedLocusNames=ZMO1550;
OS   Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Zymomonadaceae; Zymomonas.
OX   NCBI_TaxID=264203;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RA   Lee J.S., Kang H.S.;
RT   "Sequence analysis of 65G3 cosmid clone of Zymomonas mobilis ZM4 containing
RT   rrnA operon.";
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RX   PubMed=15592456; DOI=10.1038/nbt1045;
RA   Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA   Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA   Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA   Kang H.S.;
RT   "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT   ZM4.";
RL   Nat. Biotechnol. 23:63-68(2005).
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   -!- SUBUNIT: Heteromultimer composed of HisG and HisZ subunits.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DOMAIN: Lacks the C-terminal regulatory region which is replaced by
CC       HisZ.
CC   -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Short
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF088897; AAF18282.1; -; Genomic_DNA.
DR   EMBL; AE008692; AAV90174.1; -; Genomic_DNA.
DR   RefSeq; WP_011241315.1; NZ_CP035711.1.
DR   AlphaFoldDB; Q9RH04; -.
DR   SMR; Q9RH04; -.
DR   STRING; 264203.ZMO1550; -.
DR   EnsemblBacteria; AAV90174; AAV90174; ZMO1550.
DR   GeneID; 58027272; -.
DR   KEGG; zmo:ZMO1550; -.
DR   eggNOG; COG0040; Bacteria.
DR   HOGENOM; CLU_038115_2_0_5; -.
DR   OMA; YVMMDYD; -.
DR   OrthoDB; 1419568at2; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000001173; 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..222
FT                   /note="ATP phosphoribosyltransferase"
FT                   /id="PRO_0000151948"
FT   CONFLICT        116
FT                   /note="E -> G (in Ref. 1; AAF18282)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        131
FT                   /note="H -> D (in Ref. 1; AAF18282)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   222 AA;  24536 MW;  F3EF436F25B7D7AE CRC64;
     MTKPLVFAIP KGRILKEALP MLEAAGIIPE PAFLDKESRL LRFKTNRPDI EIIRVRAFDV
     ATFVAHGAAQ MGIVGSDVIE EFSYPELYAP VDLDIGHCRL SIAEPKRLAK DDDPREWSHV
     RVATKYPHLT HRHFEARGVQ AECIKLNGAM EIAPALGLAG RIVDLVSSGR TLEENGLVEV
     EKIMPISARL IVNRAAFKMR AGDIAPLVEN FRRLVGVADN VA