ID HIS1_BRUMB Reviewed; 231 AA.
AC C0RKC9;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=ATP phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01018};
DE Short=ATP-PRT {ECO:0000255|HAMAP-Rule:MF_01018};
DE Short=ATP-PRTase {ECO:0000255|HAMAP-Rule:MF_01018};
DE EC=2.4.2.17 {ECO:0000255|HAMAP-Rule:MF_01018};
GN Name=hisG {ECO:0000255|HAMAP-Rule:MF_01018}; OrderedLocusNames=BMEA_B0189;
OS Brucella melitensis biotype 2 (strain ATCC 23457).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=546272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23457;
RA Setubal J.C., Boyle S., Crasta O.R., Gillespie J.J., Kenyon R.W., Lu J.,
RA Mane S., Nagrani S., Shallom J.M., Shallom S., Shukla M., Snyder E.E.,
RA Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., Munk C., Tapia R.,
RA Han C., Detter J.C., Bruce D., Brettin T.S.;
RT "Brucella melitensis ATCC 23457 whole genome shotgun sequencing project.";
RL Submitted (MAR-2009) 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:0000255|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; Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_01018}.
CC -!- SUBUNIT: Heteromultimer composed of HisG and HisZ subunits.
CC {ECO:0000255|HAMAP-Rule:MF_01018}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01018}.
CC -!- DOMAIN: Lacks the C-terminal regulatory region which is replaced by
CC HisZ.
CC -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Short
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01018}.
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DR EMBL; CP001489; ACO02062.1; -; Genomic_DNA.
DR RefSeq; WP_004681430.1; NC_012442.1.
DR AlphaFoldDB; C0RKC9; -.
DR SMR; C0RKC9; -.
DR KEGG; bmi:BMEA_B0189; -.
DR HOGENOM; CLU_038115_0_1_5; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000001748; Chromosome II.
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; cd13593; PBP2_HisGL3; 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; ATP-binding; Cytoplasm; Glycosyltransferase;
KW Histidine biosynthesis; Nucleotide-binding; Transferase.
FT CHAIN 1..231
FT /note="ATP phosphoribosyltransferase"
FT /id="PRO_1000213257"
SQ SEQUENCE 231 AA; 25468 MW; AF342B9DD1ED0DA6 CRC64;
MSVTLALPSK GRLKEKTLAV LEKAGYKVVL PDDDRNYRAR VEGEDDLDIL FLSASEIARK
LGYGSVDLGV TGEDLVRETL AHADERVAIE AQLGFGHADV VVAVPEVWRD VTTMADLDDV
AADFRQRHGR RLRIATKYWR LTQQFFSQKH GIQVYRIVES LGATEGAPAA GSADMIVDIT
STGSTLRANR LKVLEDGIIL RSQACLVSAR RSHTSRRVEE IAARIRAGLE I
//
