ID D2PMB8_KRIFD Unreviewed; 281 AA. AC D2PMB8; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 02-SEP-2026, entry version 80. 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 OrderedLocusNames=Kfla_5475 {ECO:0000313|EMBL:ADB34486.1}; OS Kribbella flavida (strain DSM 17836 / JCM 10339 / NBRC 14399). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Propionibacteriales; OC Kribbellaceae; Kribbella. OX NCBI_TaxID=479435 {ECO:0000313|EMBL:ADB34486.1, ECO:0000313|Proteomes:UP000007967}; RN [1] {ECO:0000313|Proteomes:UP000007967} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17836 / JCM 10339 / NBRC 14399 RC {ECO:0000313|Proteomes:UP000007967}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N., RA Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M., RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., RA Pukall R., Klenk H.-P., Eisen J.A.; RT "The complete genome of Kribbella flavida DSM 17836."; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADB34486.1, ECO:0000313|Proteomes:UP000007967} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17836 / JCM 10339 / NBRC 14399 RC {ECO:0000313|Proteomes:UP000007967}; RX PubMed=21304701; RA Pukall R., Lapidus A., Glavina Del Rio T., Copeland A., Tice H., RA Cheng J.-F., Lucas S., Chen F., Nolan M., LaButti K., Pati A., Ivanova N., RA Mavrommatis K., Mikhailova N., Pitluck S., Bruce D., Goodwin L., Land M., RA Hauser L., Chang Y.-J., Jeffries C.D., Chen A., Palaniappan K., Chain P., RA Rohde M., Goeker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Kyrpides N.C., Klenk H.-P., Brettin T.; RT "Complete genome sequence of Kribbella flavida type strain (IFO 14399)."; RL Stand. Genomic Sci. 2:186-193(2010). 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; Evidence={ECO:0000256|HAMAP- CC 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|ARBA:ARBA00004496, CC 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; CP001736; ADB34486.1; -; Genomic_DNA. DR RefSeq; WP_012923040.1; NC_013729.1. DR AlphaFoldDB; D2PMB8; -. DR STRING; 479435.Kfla_5475; -. DR KEGG; kfl:Kfla_5475; -. DR eggNOG; COG0040; Bacteria. DR HOGENOM; CLU_038115_1_1_11; -. DR OrthoDB; 9801867at2; -. DR UniPathway; UPA00031; UER00006. DR Proteomes; UP000007967; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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; cd13591; PBP2_HisGL1; 1. DR FunFam; 3.30.70.120:FF:000003; ATP phosphoribosyltransferase; 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; 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 NCBIfam; TIGR00070; hisG; 1. DR NCBIfam; TIGR03455; HisG_C-term; 1. 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 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}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00079}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00079}; Reference proteome {ECO:0000313|Proteomes:UP000007967}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00079}. FT DOMAIN 49..202 FT /note="ATP phosphoribosyltransferase catalytic" FT /evidence="ECO:0000259|Pfam:PF01634" FT DOMAIN 206..277 FT /note="Histidine biosynthesis HisG C-terminal" FT /evidence="ECO:0000259|Pfam:PF08029" SQ SEQUENCE 281 AA; 30053 MW; B2E5A49BD2D3EE68 CRC64; MLRVAVPNKG SLSEAATAIL IEAGYKQRRT TKDLSLTDPD NGVEFYYLRP RDIAVYVGEG TLDVGISGRD LVLDSHADAD TIIELGFGGS TFRFAGRPGV ADSVKDLAGK RIATSFAGIL SDHLAEHGVE ASVVKLDGAV ESAVQLGVAD VIADVVETGT TLRQAGLEVF GEPILTSEAV LIKRHGVEQP AGLEQLVRRL QGVLVARNYV MMDYDIRAEA VEAANAVAPG LESPTVSPLH REGWVAVRVM VLRSEAQNIM DQLWDVGARA ILTTDIHACR I //