ID S9ZPA0_9RHOO Unreviewed; 214 AA.
AC S9ZPA0;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
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:EPZ15342.1};
GN ORFNames=M622_04210 {ECO:0000313|EMBL:EPZ15342.1};
OS Thauera terpenica 58Eu.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Thauera.
OX NCBI_TaxID=1348657 {ECO:0000313|EMBL:EPZ15342.1, ECO:0000313|Proteomes:UP000015455};
RN [1] {ECO:0000313|EMBL:EPZ15342.1, ECO:0000313|Proteomes:UP000015455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=58Eu {ECO:0000313|EMBL:EPZ15342.1,
RC ECO:0000313|Proteomes:UP000015455};
RA Liu B., Frostegard A.H., Shapleigh J.P.;
RT "Draft genome sequence of Thauera terpenica.";
RL Submitted (JUN-2013) 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:EPZ15342.1}.
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DR EMBL; ATJV01000059; EPZ15342.1; -; Genomic_DNA.
DR RefSeq; WP_021249735.1; NZ_ATJV01000059.1.
DR AlphaFoldDB; S9ZPA0; -.
DR STRING; 1348657.M622_04210; -.
DR PATRIC; fig|1348657.5.peg.2322; -.
DR eggNOG; COG0040; Bacteria.
DR OrthoDB; 9801867at2; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000015455; 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}; Reference proteome {ECO:0000313|Proteomes:UP000015455};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01018}.
FT DOMAIN 53..208
FT /note="ATP phosphoribosyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01634"
SQ SEQUENCE 214 AA; 22641 MW; 8EE65C117633C3B4 CRC64;
MSSITLALSK GRIFEETLPL LAAAGIVPTD NPESSRKLII GTNRPDVRLV IVRATDTPTY
VQYGAADIGI AGKDVLLEHG GAGLYQPLDL NIAACRLCVA VQKGFDYAAA TRPGGRIRIA
TKYINAAKAH FAGKGMHADL IKLYGSMELA PLVGLADAIV DLVSTGGTLR ANNLEEVEDI
MPISARLIVN QASLKLKREL LQPVLDAFAG AVKP
//
