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-MAR-2018, entry version 3. DE RecName: Full=ATP phosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_00079, ECO:0000256|SAAS:SAAS00046302}; 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|HAMAP-Rule:MF_00079, ECO:0000256|SAAS:SAAS00046302}; GN Name=hisG {ECO:0000256|HAMAP-Rule:MF_00079}; GN ORFNames=BFP75_18105 {ECO:0000313|EMBL:PIB38121.1}; OS Maribacter sp. 4G9. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Maribacter. OX NCBI_TaxID=1889777 {ECO:0000313|EMBL:PIB38121.1}; RN [1] {ECO:0000313|EMBL:PIB38121.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=4G9 {ECO:0000313|EMBL:PIB38121.1}; 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 -!- CATALYTIC ACTIVITY: 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate CC = ATP + 5-phospho-alpha-D-ribose 1-diphosphate. CC {ECO:0000256|HAMAP-Rule:MF_00079, ECO:0000256|SAAS:SAAS00046298}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00079}; CC -!- ENZYME REGULATION: Feedback inhibited by histidine. CC {ECO:0000256|HAMAP-Rule:MF_00079}. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9. CC {ECO:0000256|HAMAP-Rule:MF_00079, ECO:0000256|SAAS:SAAS00046315}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00079}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 UniPathway; UPA00031; UER00006. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule. 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 HAMAP; MF_00079; HisG_Long; 1. DR InterPro; IPR013820; ATP_PRibTrfase_cat. DR InterPro; IPR018198; ATP_PRibTrfase_CS. DR InterPro; IPR001348; ATP_PRibTrfase_HisG. DR InterPro; IPR020621; ATP_PRibTrfase_HisG_long. 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; PTHR21403; 1. DR Pfam; PF01634; HisG; 1. DR Pfam; PF08029; HisG_C; 1. DR SUPFAM; SSF54913; SSF54913; 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|HAMAP-Rule:MF_00079, KW ECO:0000256|SAAS:SAAS00046310}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00079}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00079}; KW Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_00079, KW ECO:0000256|SAAS:SAAS00021142, ECO:0000313|EMBL:PIB38121.1}; KW Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00079, KW ECO:0000256|SAAS:SAAS00046316}; KW 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|HAMAP-Rule:MF_00079, KW ECO:0000256|SAAS:SAAS00046311, ECO:0000313|EMBL:PIB38121.1}. FT DOMAIN 51 205 HisG. {ECO:0000259|Pfam:PF01634}. FT DOMAIN 210 282 HisG_C. {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 //