ID HIS1_THET2 Reviewed; 206 AA. AC P62381; DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 02-SEP-2026, entry version 110. DE RecName: Full=ATP phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01018}; DE Short=ATP-PRT {ECO:0000255|HAMAP-Rule:MF_01018}; DE Short=ATP-PRTase {ECO:0000255|HAMAP-Rule:MF_01018}; DE EC=2.4.2.17 {ECO:0000255|HAMAP-Rule:MF_01018}; GN Name=hisG {ECO:0000255|HAMAP-Rule:MF_01018}; GN OrderedLocusNames=TT_C1866; OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27). OC Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales; Thermaceae; OC Thermus. OX NCBI_TaxID=262724; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27; RX PubMed=15064768; DOI=10.1038/nbt956; RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H., RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C., RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P., RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.; RT "The genome sequence of the extreme thermophile Thermus thermophilus."; RL Nat. Biotechnol. 22:547-553(2004). 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_01018}. 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_01018}; 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_01018}. CC -!- SUBUNIT: Heteromultimer composed of HisG and HisZ subunits. CC {ECO:0000255|HAMAP-Rule:MF_01018}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01018}. CC -!- DOMAIN: Lacks the C-terminal regulatory region which is replaced by CC HisZ. CC -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Short CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01018}. 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; AE017221; AAS82208.1; -; Genomic_DNA. DR RefSeq; WP_011174220.1; NC_005835.1. DR PDB; 1VE4; X-ray; 1.20 A; A=1-206. DR AlphaFoldDB; P62381; -. DR SMR; P62381; -. DR GeneID; 3168686; -. DR KEGG; tth:TT_C1866; -. DR eggNOG; COG0040; Bacteria. DR HOGENOM; CLU_038115_2_0_0; -. DR OrthoDB; 9801867at2; -. DR UniPathway; UPA00031; UER00006. DR EvolutionaryTrace; P62381; -. DR Proteomes; UP000000592; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003879; F:ATP phosphoribosyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000105; P:L-histidine biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd13595; PBP2_HisGs; 1. DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2. DR HAMAP; MF_01018; HisG_Short; 1. DR InterPro; IPR013820; ATP_PRibTrfase_cat. DR InterPro; IPR018198; ATP_PRibTrfase_CS. DR InterPro; IPR001348; ATP_PRibTrfase_HisG. DR InterPro; IPR024893; ATP_PRibTrfase_HisG_short. DR NCBIfam; TIGR00070; hisG; 1. 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. DR PROSITE; PS01316; ATP_P_PHORIBOSYLTR; 1. DR PDBsum; 1VE4; -. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; ATP-binding; Cytoplasm; KW Glycosyltransferase; Histidine biosynthesis; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1..206 FT /note="ATP phosphoribosyltransferase" FT /id="PRO_0000151945" FT STRAND 4..11 FT /evidence="ECO:0007829|PDB:1VE4" FT HELIX 16..25 FT /evidence="ECO:0007829|PDB:1VE4" FT HELIX 30..32 FT /evidence="ECO:0007829|PDB:1VE4" FT STRAND 46..52 FT /evidence="ECO:0007829|PDB:1VE4" FT HELIX 54..56 FT /evidence="ECO:0007829|PDB:1VE4" FT HELIX 57..62 FT /evidence="ECO:0007829|PDB:1VE4" FT STRAND 65..72 FT /evidence="ECO:0007829|PDB:1VE4" FT HELIX 73..78 FT /evidence="ECO:0007829|PDB:1VE4" FT STRAND 84..88 FT /evidence="ECO:0007829|PDB:1VE4" FT STRAND 94..100 FT /evidence="ECO:0007829|PDB:1VE4" FT STRAND 110..114 FT /evidence="ECO:0007829|PDB:1VE4" FT HELIX 116..125 FT /evidence="ECO:0007829|PDB:1VE4" FT STRAND 131..134 FT /evidence="ECO:0007829|PDB:1VE4" FT HELIX 140..144 FT /evidence="ECO:0007829|PDB:1VE4" FT STRAND 147..158 FT /evidence="ECO:0007829|PDB:1VE4" FT HELIX 159..163 FT /evidence="ECO:0007829|PDB:1VE4" FT STRAND 167..175 FT /evidence="ECO:0007829|PDB:1VE4" FT STRAND 177..181 FT /evidence="ECO:0007829|PDB:1VE4" FT HELIX 183..188 FT /evidence="ECO:0007829|PDB:1VE4" FT HELIX 190..202 FT /evidence="ECO:0007829|PDB:1VE4" SQ SEQUENCE 206 AA; 22381 MW; A9CC57D7E43069FE CRC64; MRRFALTVAL PKGRMFREAY EVLKRAGLDL PEVEGERTLL HGKEGGVALL ELRNKDVPIY VDLGIAEIGV VGKDVLLDSG RDLFEPVDLG FGACRLSLIR RPGDTGPIRR VATKYPNFTA RLLKERGWAA DVVELSGNIE LAAVTGLADA VVDVVQTGAT LRAAGLVEVE VLAHSTARLV VNRQALKLKR AVLKPLIQRL RELSGS //