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Database: UniProt
Entry: D7JE61_9BACT
LinkDB: D7JE61_9BACT
Original site: D7JE61_9BACT 
ID   D7JE61_9BACT            Unreviewed;       283 AA.
AC   D7JE61;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=ATP phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00011946};
DE            EC=2.4.2.17 {ECO:0000256|ARBA:ARBA00011946};
GN   ORFNames=HMPREF0156_00770 {ECO:0000313|EMBL:EFI17179.1};
OS   Bacteroidetes oral taxon 274 str. F0058.
OC   Bacteria; Bacteroidota.
OX   NCBI_TaxID=575590 {ECO:0000313|EMBL:EFI17179.1, ECO:0000313|Proteomes:UP000004685};
RN   [1] {ECO:0000313|Proteomes:UP000004685}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0058 {ECO:0000313|Proteomes:UP000004685};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Earl A., Feldgarden M., Gevers D., Young S.K., Zeng Q.,
RA   Koehrsen M., Alvarado L., Berlin A., Bochicchio J., Borenstein D.,
RA   Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D.,
RA   Larson L., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA   Yandava C., Izard J., Baranova O.V., Blanton J.M., Tanner A.C.,
RA   Dewhirst F.E., Haas B., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Bacteroidetes bacterium Oral taxon 274 strain
RT   F0058.";
RL   Submitted (MAR-2010) 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:0000256|ARBA:ARBA00024861}.
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         Evidence={ECO:0000256|ARBA:ARBA00000915};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
CC       {ECO:0000256|ARBA:ARBA00004667}.
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DR   EMBL; GG774889; EFI17179.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7JE61; -.
DR   STRING; 575590.HMPREF0156_00770; -.
DR   eggNOG; COG0040; Bacteria.
DR   HOGENOM; CLU_982307_0_0_10; -.
DR   OrthoDB; 9801867at2; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000004685; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0003879; F:ATP phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR   InterPro; IPR013820; ATP_PRibTrfase_cat.
DR   InterPro; IPR001348; ATP_PRibTrfase_HisG.
DR   PANTHER; PTHR21403:SF8; ATP PHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR21403; ATP PHOSPHORIBOSYLTRANSFERASE ATP-PRTASE; 1.
DR   Pfam; PF01634; HisG; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004685};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          58..201
FT                   /note="ATP phosphoribosyltransferase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01634"
SQ   SEQUENCE   283 AA;  32959 MW;  15A785A21F9D5774 CRC64;
     MLRIAISQDI QILKDFENQL VNSGIDIDFH DNSKQLLFSR DFPAEIRYLN KNHLFFSLTN
     GMQDLAIVHE HFLTDQRKEY ERIYSFDSTK TNLSVFVPSN MRYKDVFSFS NKRIATNVPD
     LVRAYFKEKR LRGINIIADD NPQSAVDVGI ADCFVELLYN VDSKRYQPAE TVLESSLALI
     VSPKISPEKR HVFVDELVLR LDAVQSARHQ IKVEIFCDSK NKSRLISELV KIDENILVIT
     TYNQKKIVIQ ATMDEKQLWD IKHYLKELQA EKIIAYDILK KIV
//
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