ID A0A1D9MA17_9RHOB Unreviewed; 234 AA.
AC A0A1D9MA17;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=ATP phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00020998};
DE EC=2.4.2.17 {ECO:0000256|ARBA:ARBA00011946};
GN ORFNames=LPB142_04465 {ECO:0000313|EMBL:AOZ68661.1};
OS Rhodobacter sp. LPB0142.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=1850250 {ECO:0000313|EMBL:AOZ68661.1, ECO:0000313|Proteomes:UP000176562};
RN [1] {ECO:0000313|EMBL:AOZ68661.1, ECO:0000313|Proteomes:UP000176562}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LPB0142 {ECO:0000313|EMBL:AOZ68661.1,
RC ECO:0000313|Proteomes:UP000176562};
RA Kim E., Yi H.;
RT "Rhodobacter sp. LPB0142, isolated from sea water.";
RL Submitted (OCT-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}.
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DR EMBL; CP017781; AOZ68661.1; -; Genomic_DNA.
DR RefSeq; WP_071165641.1; NZ_CP017781.1.
DR AlphaFoldDB; A0A1D9MA17; -.
DR STRING; 1850250.LPB142_04465; -.
DR KEGG; rhp:LPB142_04465; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000176562; Chromosome.
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 CDD; cd13593; PBP2_HisGL3; 1.
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:AOZ68661.1};
KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102};
KW Reference proteome {ECO:0000313|Proteomes:UP000176562};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AOZ68661.1}.
FT DOMAIN 55..211
FT /note="ATP phosphoribosyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01634"
SQ SEQUENCE 234 AA; 25158 MW; 7DA8BCDB9F179CD5 CRC64;
MTIKLGVPSK GRLMEKTFDW FAARGITLRR TGSEREYAGA VEGAEGVELV LLSAGEIPRE
LAAGRIHFGV TGSDLVRDKL ADWESQVAEL APMGFGHADL IIAVPACWSD VDTLEDLDAA
AHAFRADHGF RLRIATKYHR LVRDFLTREG VADYQLVDSQ GATEGTVKNL TAEAIADITS
SGETLRANHL KILSDGLIHQ SQATLFAARG ADWAAEGARP ARLVAQLGLS LPAL
//