ID A0A1F6DWL1_9BACT Unreviewed; 209 AA.
AC A0A1F6DWL1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=ATP phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00011946};
DE EC=2.4.2.17 {ECO:0000256|ARBA:ARBA00011946};
GN ORFNames=A3D71_01860 {ECO:0000313|EMBL:OGG65793.1};
OS Candidatus Kaiserbacteria bacterium RIFCSPHIGHO2_02_FULL_55_20.
OC Bacteria; Candidatus Kaiserbacteria.
OX NCBI_TaxID=1798497 {ECO:0000313|EMBL:OGG65793.1, ECO:0000313|Proteomes:UP000177652};
RN [1] {ECO:0000313|EMBL:OGG65793.1, ECO:0000313|Proteomes:UP000177652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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}.
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};
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}.
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:OGG65793.1}.
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DR EMBL; MFLK01000030; OGG65793.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6DWL1; -.
DR STRING; 1798497.A3D71_01860; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000177652; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0003879; F:ATP phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR013820; ATP_PRibTrfase_cat.
DR InterPro; IPR018198; ATP_PRibTrfase_CS.
DR InterPro; IPR001348; ATP_PRibTrfase_HisG.
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.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000313|EMBL:OGG65793.1};
KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OGG65793.1}.
FT DOMAIN 54..198
FT /note="ATP phosphoribosyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01634"
SQ SEQUENCE 209 AA; 22860 MW; E0BEBF894F6CB10D CRC64;
MKTQERLKIA VQKSGRLYQS SMDFLTSRGL AFSPDSRSLI RTCQNSNIDI VYLRDDDIPE
YVSRGIADFG IVGQNVLAEK GLTLRIVTRL GFALCRLVIA VPRCSRIRTV EDLQNLRIAT
SYPKLLTDYL GKSNIKASIV VVSGSAEIAP RLGLADAVCD LVQTGATLEA NDLVPLCTVL
GSQAVLVGSP VRKRSKKRLL LDLNIKSLI
//