ID A0A1F8NC68_9CHLR Unreviewed; 471 AA.
AC A0A1F8NC68;
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=A2Y61_00130 {ECO:0000313|EMBL:OGO08549.1};
OS Chloroflexi bacterium RBG_13_60_13.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797635 {ECO:0000313|EMBL:OGO08549.1, ECO:0000313|Proteomes:UP000180307};
RN [1] {ECO:0000313|EMBL:OGO08549.1, ECO:0000313|Proteomes:UP000180307}
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:OGO08549.1}.
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; MGNC01000077; OGO08549.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8NC68; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000180307; 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 Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 54..212
FT /note="ATP phosphoribosyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01634"
FT DOMAIN 294..457
FT /note="ATP phosphoribosyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01634"
SQ SEQUENCE 471 AA; 51876 MW; 7A678FAD3B965E9B CRC64;
MQLKLALPKG RLQQPTGAML RQSGLEIDGY DEQSRSYRPQ CGSRPDLAMK IFNERDIPIQ
VAVGNYDLGI CGQDWVEELL ARYPGSALVK VKPLPYGNRD LCLVADASSQ TGTMQELAAS
RGSVRIATEY PNLAESFSLN LRLRRFSIIP VWGAAEAYPP ESADAALISR TDDAPLDPSL
LSLTTILRSS AFLIAHRPSW ESRDMAPLLE RLYAAIGVLQ LAAQVSTTPA TAGAYRSTRP
QSDPTAVWLA LPDGHQQAPV LEFLEQAGIK LIPNPQEPRR PGINLDGVRT KIVRPQDMPL
QVANGYFDLA ITGEDWLSEH LCRFPSSPVK KVLRLGLGKV RIVAVVSKRL PFDSTQDLRS
PLRRHGFATL RIASEYVNIA DRFARDNHLT PYRLLPTWGA SEAFLPEDAD VLIENTQTGR
TIAQHNLKII DTLFESSACL VSNESSANGS ELKRKRIGGI IDLLSMSAHQ N
//