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Database: UniProt
Entry: A0A1B6YSG2_9RHOB
LinkDB: A0A1B6YSG2_9RHOB
Original site: A0A1B6YSG2_9RHOB 
ID   A0A1B6YSG2_9RHOB        Unreviewed;       231 AA.
AC   A0A1B6YSG2;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=ATP phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00020998};
DE            EC=2.4.2.17 {ECO:0000256|ARBA:ARBA00011946};
GN   ORFNames=A8B83_08825 {ECO:0000313|EMBL:OAN72482.1};
OS   Rhodobacteraceae bacterium EhC02.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=1849170 {ECO:0000313|EMBL:OAN72482.1, ECO:0000313|Proteomes:UP000078223};
RN   [1] {ECO:0000313|EMBL:OAN72482.1, ECO:0000313|Proteomes:UP000078223}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EhC02 {ECO:0000313|EMBL:OAN72482.1,
RC   ECO:0000313|Proteomes:UP000078223};
RA   Lavstsen T., Jespersen J.S.;
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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:OAN72482.1}.
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DR   EMBL; LXYH01000005; OAN72482.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B6YSG2; -.
DR   STRING; 1849170.A8B83_08825; -.
DR   OrthoDB; 9806435at2; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000078223; 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; 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.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000313|EMBL:OAN72482.1};
KW   Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078223};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OAN72482.1}.
FT   DOMAIN          55..229
FT                   /note="ATP phosphoribosyltransferase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01634"
SQ   SEQUENCE   231 AA;  25559 MW;  F33856E8D1C20E06 CRC64;
     MTIKLGVPSK GRLMEKTFEW FAARGITLSR SASEREYAGA VEGIDNVELV LLSAGEIPRE
     LAAGRIHLGV TGTDLVREKL GQWDQQVQEL AELGFGHADL IIAVPAAWVD VDTLDDLDAA
     AAAFRKRRGF RMRIATKYHR LVRDFLRNAG VADYALVDSQ GATEGTVKFE TAEAVADITS
     TGETLRANHL KMLRDGLILR SQATLYRSRA ADMDDMDRDT LKHLCRMIEV D
//
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