ID A0A6G0AAS5_UNCAC Unreviewed; 291 AA. AC A0A6G0AAS5; DT 12-AUG-2020, integrated into UniProtKB/TrEMBL. DT 12-AUG-2020, sequence version 1. DT 24-JUL-2024, entry version 14. 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=EDR02_00930 {ECO:0000313|EMBL:KAA0236362.1}; OS Actinomycetes bacterium. OC Bacteria; Actinomycetota; Actinomycetes. OX NCBI_TaxID=1883427 {ECO:0000313|EMBL:KAA0236362.1}; RN [1] {ECO:0000313|EMBL:KAA0236362.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATB {ECO:0000313|EMBL:KAA0236362.1}; RX PubMed=31478060; RA Zhao Y., Feng Y., Chen L., Niu Z., Liu S.; RT "Genome-centered omics insight into the competition and niche RT differentiation of Ca. Jettenia and Ca. Brocadia affiliated to anammox RT bacteria."; RL Appl. Microbiol. Biotechnol. 0:0-0(2019). 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|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 -!- 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KAA0236362.1}. 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; RHKU01000001; KAA0236362.1; -; Genomic_DNA. DR AlphaFoldDB; A0A6G0AAS5; -. DR UniPathway; UPA00031; UER00006. 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:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule. DR Gene3D; 3.30.70.120; -; 1. DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2. DR HAMAP; MF_00079; HisG_Long; 1. DR InterPro; IPR020621; ATP-PRT_HisG_long. DR InterPro; IPR013820; ATP_PRibTrfase_cat. DR InterPro; IPR001348; ATP_PRibTrfase_HisG. DR InterPro; IPR013115; HisG_C. DR InterPro; IPR011322; N-reg_PII-like_a/b. DR InterPro; IPR015867; N-reg_PII/ATP_PRibTrfase_C. DR NCBIfam; TIGR00070; hisG; 1. DR NCBIfam; TIGR03455; HisG_C-term; 1. DR PANTHER; PTHR21403:SF10; ATP PHOSPHORIBOSYLTRANSFERASE; 1. DR PANTHER; PTHR21403; ATP PHOSPHORIBOSYLTRANSFERASE ATP-PRTASE; 1. DR Pfam; PF01634; HisG; 1. DR Pfam; PF08029; HisG_C; 1. DR SUPFAM; SSF54913; GlnB-like; 1. DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 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|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00079}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00079}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00079}. FT DOMAIN 50..211 FT /note="ATP phosphoribosyltransferase catalytic" FT /evidence="ECO:0000259|Pfam:PF01634" FT DOMAIN 216..288 FT /note="Histidine biosynthesis HisG C-terminal" FT /evidence="ECO:0000259|Pfam:PF08029" SQ SEQUENCE 291 AA; 31620 MW; E44A8070CAEF9516 CRC64; MLKLVLPKGS LERSTLELFE AADLPVTRSS SVDYRATIDD PRIESVRILR PQEIPIYVAD GLFDVGITGR DWVEETGSVV ESLGELRYSK ATARPVHIVV AVPADSPCEA VSDLPSRVKV SSEYPQLTRR YFEAQGVDAD IRLSYGATEA KVPDIVDCVV DLTETGRALR AAGLKVIDTI LTSHTELIAN PVAYADVERR RAMEQINTLL QGVLEARGKV LVKLNVDDAN LAAVIDLLPA LKTPTVNELY GKSGYAVESV VPKSEINTLI PALSEHGASD IIELPLSKIV H //