ID A0A7U8TZS9_MYCTX Unreviewed; 284 AA. AC A0A7U8TZS9; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 29-SEP-2021, entry version 2. DE RecName: Full=ATP phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00020998, ECO:0000256|HAMAP-Rule:MF_00079}; DE Short=ATP-PRT {ECO:0000256|HAMAP-Rule:MF_00079}; DE Short=ATP-PRTase {ECO:0000256|HAMAP-Rule:MF_00079}; DE EC=2.4.2.17 {ECO:0000256|ARBA:ARBA00011946, ECO:0000256|HAMAP-Rule:MF_00079}; GN Name=hisG {ECO:0000256|HAMAP-Rule:MF_00079}; GN ORFNames=TBOG_02644 {ECO:0000313|EMBL:EFD43809.2}; OS Mycobacterium tuberculosis variant africanum K85. OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium tuberculosis complex. OX NCBI_TaxID=611304 {ECO:0000313|EMBL:EFD43809.2}; RN [1] {ECO:0000313|EMBL:EFD43809.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=K85 {ECO:0000313|EMBL:EFD43809.2}; RG The Broad Institute Genome Sequencing Platform; RA Small P., Gagneaux S., Hopewell P., Young S.K., Kodira C.D., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A., Borenstein D., Chen Z., Engels R., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., RA Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., RA Sykes S., Walk T., White J., Yandava C., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Mycobacterium tuberculosis strain K85."; RL Submitted (MAR-2009) 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:ARBA00003858, ECO:0000256|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; CC Evidence={ECO:0000256|ARBA:ARBA00000915, ECO:0000256|HAMAP- CC Rule:MF_00079}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00079}; CC -!- ACTIVITY REGULATION: Feedback inhibited by histidine. CC {ECO:0000256|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:0000256|ARBA:ARBA00004667, ECO:0000256|HAMAP-Rule:MF_00079}. 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. {ECO:0000256|HAMAP- CC Rule:MF_00079}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00079}. CC -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Long CC subfamily. {ECO:0000256|ARBA:ARBA00007955, ECO:0000256|HAMAP- CC Rule:MF_00079}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; GG663503; EFD43809.2; -; Genomic_DNA. DR RefSeq; WP_003910503.1; NZ_KK338483.1. DR UniPathway; UPA00031; UER00006. DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW. 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 {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP- KW Rule:MF_00079}; ATP-binding {ECO:0000256|HAMAP-Rule:MF_00079}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00079}; KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP- KW Rule:MF_00079}; KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102, ECO:0000256|HAMAP- KW Rule:MF_00079}; Magnesium {ECO:0000256|HAMAP-Rule:MF_00079}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00079}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00079}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00079}. FT DOMAIN 49..204 FT /note="HisG" FT /evidence="ECO:0000259|Pfam:PF01634" FT DOMAIN 210..279 FT /note="HisG_C" FT /evidence="ECO:0000259|Pfam:PF08029" SQ SEQUENCE 284 AA; 30491 MW; C24A17A399302829 CRC64; MLRVAVPNKG ALSEPATEIL AEAGYRRRTD SKDLTVIDPV NNVEFFFLRP KDIAIYVGSG ELDFGITGRD LVCDSGAQVR ERLALGFGSS SFRYAAPAGR NWTTADLAGM RIATAYPNLV RKDLATKGIE ATVIRLDGAV EISVQLGVAD AIADVVGSGR TLSQHDLVAF GEPLCDSEAV LIERAGTDGQ DQTEARDQLV ARVQGVVFGQ QYLMLDYDCP RPALKKATAI TPGLESPTIA PLADPDWVAI RALVPRRDVN GIMDELAAIG AKAILASDIR FCRF //