ID   HIS1_MYCLE              Reviewed;         287 AA.
AC   Q49776;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=ATP phosphoribosyltransferase;
DE            Short=ATP-PRT;
DE            Short=ATP-PRTase;
DE            EC=2.4.2.17;
GN   Name=hisG; OrderedLocusNames=ML1310; ORFNames=B2126_C1_162, MLCB2533.07;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Smith D.R., Robison K.;
RL   Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAC31691.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U00017; AAA17183.1; -; Genomic_DNA.
DR   EMBL; AL035310; CAA22921.1; -; Genomic_DNA.
DR   EMBL; AL583921; CAC31691.1; ALT_INIT; Genomic_DNA.
DR   PIR; H87072; H87072.
DR   PIR; S72843; S72843.
DR   RefSeq; WP_041322695.1; NC_002677.1.
DR   AlphaFoldDB; Q49776; -.
DR   SMR; Q49776; -.
DR   STRING; 272631.ML1310; -.
DR   PRIDE; Q49776; -.
DR   EnsemblBacteria; CAC31691; CAC31691; CAC31691.
DR   KEGG; mle:ML1310; -.
DR   Leproma; ML1310; -.
DR   eggNOG; COG0040; Bacteria.
DR   HOGENOM; CLU_038115_1_1_11; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000000806; 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..287
FT                   /note="ATP phosphoribosyltransferase"
FT                   /id="PRO_0000151855"
SQ   SEQUENCE   287 AA;  30893 MW;  BA4FB1176D016FB0 CRC64;
     MLRVAVPNKG ALSEPATEIL AEAGYRRRTD PKDLTVVDPV NRVEFFFLRP KDIAIYVGSG
     DLDFGITGRD LVHDSDASVC ERLALGFGSS SFRYAGPAGR DWTTSDLAGK RIATAYSNLV
     RKDLVAKGIE ATVIRLDGAV EISVQLGVAD VIADVVGSGR TLSLHDLVAF GEPLCDSEAV
     LIERGDRGSL DHHETVAARD QLVARVQGVV FGQQYLMLDY DCPRSVLDKA TLITSGLESP
     TIAPLAEPGW VAIRALVPRR DINGIMDELA AIGAKAILAS DIRFCRF