ID A0AAE3CBH9_9ARCH Unreviewed; 328 AA. AC A0AAE3CBH9; DT 29-MAY-2024, integrated into UniProtKB/TrEMBL. DT 29-MAY-2024, sequence version 1. DT 02-OCT-2024, entry version 3. 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 ECO:0000313|EMBL:MBS7270362.1}; GN ORFNames=KIH08_15580 {ECO:0000313|EMBL:MBS7251993.1}, KIH09_07710 GN {ECO:0000313|EMBL:MBS7279710.1}, KIH10_16190 GN {ECO:0000313|EMBL:MBS7270362.1}; OS Candidatus Jordarchaeia archaeon. OC Archaea; Asgard group; Asgard group incertae sedis; OC Candidatus Jordarchaeia. OX NCBI_TaxID=3067279 {ECO:0000313|EMBL:MBS7270362.1, ECO:0000313|Proteomes:UP001166607}; RN [1] {ECO:0000313|EMBL:MBS7270362.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=QZM_A2 {ECO:0000313|EMBL:MBS7279710.1}, QZM_A2_3 RC {ECO:0000313|EMBL:MBS7251993.1}, and QZM_A3 RC {ECO:0000313|EMBL:MBS7270362.1}; RA Chen L., Banfield J.F., Hua Z., Li W.; RL Submitted (MAY-2021) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP001166607, ECO:0000313|Proteomes:UP001166664} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=QZM_A2 {ECO:0000313|EMBL:MBS7279710.1}, QZM_A2_3 RC {ECO:0000313|EMBL:MBS7251993.1}, and QZM_A3 RC {ECO:0000313|EMBL:MBS7270362.1}; RX PubMed=37316666; RA Eme L., Tamarit D., Caceres E.F., Stairs C.W., De Anda V., Schon M.E., RA Seitz K.W., Dombrowski N., Lewis W.H., Homa F., Saw J.H., Lombard J., RA Nunoura T., Li W.J., Hua Z.S., Chen L.X., Banfield J.F., John E.S., RA Reysenbach A.L., Stott M.B., Schramm A., Kjeldsen K.U., Teske A.P., RA Baker B.J., Ettema T.J.G.; RT "Inference and reconstruction of the heimdallarchaeial ancestry of RT eukaryotes."; RL Nature 0:0-0(2023). 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, 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|HAMAP-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:MBS7270362.1}. 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; JAHAWS010000238; MBS7251993.1; -; Genomic_DNA. DR EMBL; JAHAWU010000156; MBS7270362.1; -; Genomic_DNA. DR EMBL; JAHAWT010000044; MBS7279710.1; -; Genomic_DNA. DR Proteomes; UP001166607; Unassembled WGS sequence. DR Proteomes; UP001166664; Unassembled WGS sequence. DR Proteomes; UP001166680; Unassembled WGS sequence. 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:L-histidine biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd13593; PBP2_HisGL3; 1. 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 52..238 FT /note="ATP phosphoribosyltransferase catalytic" FT /evidence="ECO:0000259|Pfam:PF01634" FT DOMAIN 244..315 FT /note="Histidine biosynthesis HisG C-terminal" FT /evidence="ECO:0000259|Pfam:PF08029" SQ SEQUENCE 328 AA; 36960 MW; 5216D11B172F1459 CRC64; MSATKLKFVI PKGSLQDATL QLLEQAGYSI KAVERSYRPW INDPEISLKL LRPQEIPTLI QEGAHELGIA GIDWVNETGA DVKLLSELDY GKVSIVMAVP NSWEKINNLS ELIREFSSNG KTIRIATEYI NITSRYIMEN REYQKLYGNK TPEVITPWSR YGQNPNVKIM LSFGATEAKP PEDADAIVDN TETGTTLKSN ELKIIEVLYQ SQAVLIANKK ALKEKWKEEK IRDVMTLILG AVEARKKLHI FMNVKEENVE ALLEQLPALK RPTISPLAGA EGWFALNTVI AKEDLIKLIP ILRKLAQGIV VHPVRQVLPL EEIENKKI //