ID A0A1F8RAT4_9CHLR Unreviewed; 462 AA.
AC A0A1F8RAT4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=ATP phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00011946};
DE EC=2.4.2.17 {ECO:0000256|ARBA:ARBA00011946};
GN ORFNames=A2Z05_07590 {ECO:0000313|EMBL:OGO44331.1};
OS Chloroflexi bacterium RBG_16_60_22.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797656 {ECO:0000313|EMBL:OGO44331.1, ECO:0000313|Proteomes:UP000179512};
RN [1] {ECO:0000313|EMBL:OGO44331.1, ECO:0000313|Proteomes:UP000179512}
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 -!- 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:OGO44331.1}.
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DR EMBL; MGNX01000055; OGO44331.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8RAT4; -.
DR STRING; 1797656.A2Z05_07590; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000179512; 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; 4.
DR InterPro; IPR013820; ATP_PRibTrfase_cat.
DR InterPro; IPR001348; ATP_PRibTrfase_HisG.
DR NCBIfam; TIGR00070; hisG; 2.
DR PANTHER; PTHR21403:SF10; ATP PHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR21403; ATP PHOSPHORIBOSYLTRANSFERASE ATP-PRTASE; 1.
DR Pfam; PF01634; HisG; 2.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 2.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000313|EMBL:OGO44331.1};
KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OGO44331.1}.
FT DOMAIN 52..203
FT /note="ATP phosphoribosyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01634"
FT DOMAIN 288..456
FT /note="ATP phosphoribosyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01634"
SQ SEQUENCE 462 AA; 51143 MW; A1C74F5C50F14746 CRC64;
MKIALPKGRL LRRTAARLQK AGWGLDEYHS RIGFYRPKSE KFPEVLIRVF HEKDIPIQIA
MGNYDLGICG SDWVEELMAK YPSSGLVRVR GLDYGEGTLF MASASEGQRN GDLVRIASEY
PNLAESFALK QRLSRFSVFP VWGAAEAYPP ENADMVLLPA RTGSELSDYG MTAVSRVLDF
SAFLVANRSS WESKDLDKIV TSICDTLAEV ERKTDSGEAV EPVAVKKSYG RIKITDGTVR
LALPDGHQQP PTVNVLNRAG IEIVDYPSET GNRRPRIKLD GVAVKVIRPQ DMPLQVANGN
FDLAVTGRDW LTEHLYQFPS SPVRELLDLE FSKVRLVAVV HRDMAVEDTG GLREYIAARP
EPFRVASEYV NIADKYARDN HLGHYRVIPT WGATEAFLPE DADLLIENTE TGRTIARHSL
KIIDTLFVST ACLIGNAGAI ADPAKGKRIA AIVNKFKAGV EA
//