ID   HIS1_BIFA0              Reviewed;         283 AA.
AC   B8DUC3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=BLA_1315;
OS   Bifidobacterium animalis subsp. lactis (strain AD011).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=442563;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AD011;
RX   PubMed=19011029; DOI=10.1128/jb.01515-08;
RA   Kim J.F., Jeong H., Yu D.S., Choi S.-H., Hur C.-G., Park M.-S., Yoon S.H.,
RA   Kim D.-W., Ji G.E., Park H.-S., Oh T.K.;
RT   "Genome sequence of the probiotic bacterium Bifidobacterium animalis subsp.
RT   lactis AD011.";
RL   J. Bacteriol. 191:678-679(2009).
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; CP001213; ACL29602.1; -; Genomic_DNA.
DR   RefSeq; WP_004217986.1; NC_011835.1.
DR   AlphaFoldDB; B8DUC3; -.
DR   SMR; B8DUC3; -.
DR   STRING; 442563.BLA_1315; -.
DR   EnsemblBacteria; ACL29602; ACL29602; BLA_1315.
DR   GeneID; 66533140; -.
DR   KEGG; bla:BLA_1315; -.
DR   PATRIC; fig|442563.4.peg.1377; -.
DR   HOGENOM; CLU_038115_1_1_11; -.
DR   OMA; YVMMDYD; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000002456; 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..283
FT                   /note="ATP phosphoribosyltransferase"
FT                   /id="PRO_1000118243"
SQ   SEQUENCE   283 AA;  31023 MW;  EF8481C273C5285B CRC64;
     MLRIAVPNKG MLSEPAWAML SEAGYTLRSN PRQLVVEDPD NDVELFYLRP LDIAVYVGMG
     TIDVGITGHD LLLNSGTDAQ EEMNLGFGGS TFRFAAPQDS PITTLDDVEG KRVGTSFDKL
     VHDYLTEHGI NATPIHLDGA VESSVQLGVA DLIADVVSTG TTLRNAGLRI FGEPILHSEA
     VLIRSPRLDP QDERLERLER RLHGVLTAKR YVLMDFDIPV EKISAAVQIT PGFESPTISP
     LHDKQWAAVR VMVPKAKVNQ LMDQLYEVGA RGIIVTAIQA TRM