ID A0A2G5L8S2_9FLAO Unreviewed; 285 AA. AC A0A2G5L8S2; DT 31-JAN-2018, integrated into UniProtKB/TrEMBL. DT 31-JAN-2018, sequence version 1. DT 28-JUN-2023, entry version 17. 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=BFP75_18105 {ECO:0000313|EMBL:PIB38121.1}; OS Maribacter sp. 4G9. OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Maribacter. OX NCBI_TaxID=1889777 {ECO:0000313|EMBL:PIB38121.1, ECO:0000313|Proteomes:UP000229780}; RN [1] {ECO:0000313|EMBL:PIB38121.1, ECO:0000313|Proteomes:UP000229780} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4G9 {ECO:0000313|EMBL:PIB38121.1, RC ECO:0000313|Proteomes:UP000229780}; RA Wong S.-K., Hamasaki K., Yoshizawa S.; RT "Draft genome of Maribacter sp. strain 4G9."; RL Submitted (AUG-2016) 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, 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:PIB38121.1}. 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; MDGL01000053; PIB38121.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2G5L8S2; -. DR EnsemblBacteria; PIB38121; PIB38121; BFP75_18105. DR OrthoDB; 9801867at2; -. DR UniPathway; UPA00031; UER00006. DR Proteomes; UP000229780; 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: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; IPR018198; ATP_PRibTrfase_CS. 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 PANTHER; PTHR21403:SF8; 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. 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 51..205 FT /note="ATP phosphoribosyltransferase catalytic" FT /evidence="ECO:0000259|Pfam:PF01634" FT DOMAIN 210..282 FT /note="Histidine biosynthesis HisG C-terminal" FT /evidence="ECO:0000259|Pfam:PF08029" SQ SEQUENCE 285 AA; 31484 MW; EA8B6652503F5BDA CRC64; MTKIRIAIQK SGRLNEDSLQ ILKDCGISID NGKDQLKASS RNFPMEVFYL RNGDIPQYLR DGVVDVAIIG ENVLIEKGAD ISIAEKLGFS KCKVSLAVPK SVKYKSVEDF EGKRIATSYP NTVTNYLKEK GVNAELHIIN GSVEIAPNIG LADAICDIVS SGSTLFKNNL KEVEVMLTSE AVLAVSPQIS EERTALLKRL QFRIQSVLRA RKSKYVLLNA PNEKLQEILK LLPGMRSPTV LPLAEEGWSS VHTVIDKDTF WEVIDELKKA GAEGILVCPI EKMVL //