ID A0A1A6DZ82_9BURK Unreviewed; 226 AA.
AC A0A1A6DZ82;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=ATP phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00020998, ECO:0000256|HAMAP-Rule:MF_01018};
DE Short=ATP-PRT {ECO:0000256|HAMAP-Rule:MF_01018};
DE Short=ATP-PRTase {ECO:0000256|HAMAP-Rule:MF_01018};
DE EC=2.4.2.17 {ECO:0000256|ARBA:ARBA00011946, ECO:0000256|HAMAP-Rule:MF_01018};
GN Name=hisG {ECO:0000256|HAMAP-Rule:MF_01018,
GN ECO:0000313|EMBL:TSE37042.1};
GN ORFNames=A9O67_00160 {ECO:0000313|EMBL:OBS32089.1}, Tfont_01446
GN {ECO:0000313|EMBL:TSE37042.1};
OS Tepidimonas fonticaldi.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Tepidimonas.
OX NCBI_TaxID=1101373 {ECO:0000313|EMBL:OBS32089.1, ECO:0000313|Proteomes:UP000091969};
RN [1] {ECO:0000313|EMBL:OBS32089.1, ECO:0000313|Proteomes:UP000091969}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PL17 {ECO:0000313|EMBL:OBS32089.1,
RC ECO:0000313|Proteomes:UP000091969};
RA Pinnaka A.K.;
RT "Genome sequence of Tepidimonas fonticaldi PL17.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:TSE37042.1, ECO:0000313|Proteomes:UP000316388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AT-A2 {ECO:0000313|EMBL:TSE37042.1,
RC ECO:0000313|Proteomes:UP000316388};
RA Da Costa M.S., Froufe H.J.C., Egas C., Albuquerque L.;
RT "Tepidimonas fonticaldi AT-A2 draft genome.";
RL Submitted (JUL-2019) 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, ECO:0000256|HAMAP-Rule:MF_01018}.
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, ECO:0000256|HAMAP-
CC Rule:MF_01018};
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, ECO:0000256|HAMAP-Rule:MF_01018}.
CC -!- SUBUNIT: Heteromultimer composed of HisG and HisZ subunits.
CC {ECO:0000256|ARBA:ARBA00011496, ECO:0000256|HAMAP-Rule:MF_01018}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_01018}.
CC -!- DOMAIN: Lacks the C-terminal regulatory region which is replaced by
CC HisZ. {ECO:0000256|HAMAP-Rule:MF_01018}.
CC -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Short
CC subfamily. {ECO:0000256|ARBA:ARBA00009489, ECO:0000256|HAMAP-
CC Rule:MF_01018}.
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:OBS32089.1}.
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; LZDH01000001; OBS32089.1; -; Genomic_DNA.
DR EMBL; VJOO01000011; TSE37042.1; -; Genomic_DNA.
DR RefSeq; WP_068606176.1; NZ_VJOO01000011.1.
DR AlphaFoldDB; A0A1A6DZ82; -.
DR STRING; 1101373.A9O67_00160; -.
DR OrthoDB; 9801867at2; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000091969; Unassembled WGS sequence.
DR Proteomes; UP000316388; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003879; F:ATP phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd13595; PBP2_HisGs; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR HAMAP; MF_01018; HisG_Short; 1.
DR InterPro; IPR013820; ATP_PRibTrfase_cat.
DR InterPro; IPR018198; ATP_PRibTrfase_CS.
DR InterPro; IPR001348; ATP_PRibTrfase_HisG.
DR InterPro; IPR024893; ATP_PRibTrfase_HisG_short.
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 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_01018};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01018};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01018};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW Rule:MF_01018};
KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102, ECO:0000256|HAMAP-
KW Rule:MF_01018};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01018};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01018}.
FT DOMAIN 55..217
FT /note="ATP phosphoribosyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01634"
SQ SEQUENCE 226 AA; 24438 MW; 078FC00301E3B802 CRC64;
MSAETVTLAL SKGRIFEETL PLLRAAGIEV LEDPETSRKL ILPTNRPEVR VVLVRATDVP
TYVEHGGADL GVCGKDTLIE HEAAWGDAAQ VGLYRPLDLG IARCRMSVAV PADFDYVRAV
RQGARLRVAT KYVAIAREFF ASKGVHVDLI KLYGSMELAP LTGLADAIVD LVSTGNTLKA
NRLVEVERIM DISSQLVVRP TSLKLKRALI RPILDAFAQA VAAPAA
//
