ID X4QW95_9ACTO Unreviewed; 281 AA.
AC X4QW95;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=ATP phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00020998, ECO:0000256|HAMAP-Rule:MF_00079};
DE Short=ATP-PRT {ECO:0000256|HAMAP-Rule:MF_00079};
DE Short=ATP-PRTase {ECO:0000256|HAMAP-Rule:MF_00079};
DE EC=2.4.2.17 {ECO:0000256|ARBA:ARBA00011946, ECO:0000256|HAMAP-Rule:MF_00079};
GN Name=hisG {ECO:0000256|HAMAP-Rule:MF_00079,
GN ECO:0000313|EMBL:UVJ60662.1};
GN ORFNames=B1R42_00575 {ECO:0000313|EMBL:OQD40359.1}, B1R42_00995
GN {ECO:0000313|EMBL:OQD40066.1}, EBQ10_01270
GN {ECO:0000313|EMBL:AZR06058.1}, M5C92_04895
GN {ECO:0000313|EMBL:UVJ60662.1};
OS Trueperella pyogenes.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Trueperella.
OX NCBI_TaxID=1661 {ECO:0000313|EMBL:AZR06058.1, ECO:0000313|Proteomes:UP000275951};
RN [1] {ECO:0000313|EMBL:OQD40066.1, ECO:0000313|Proteomes:UP000191477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UFV1 {ECO:0000313|EMBL:OQD40066.1,
RC ECO:0000313|Proteomes:UP000191477};
RA Duarte V.S., Treu L., Campanaro S., Dias R.S., Da Silva C., Giacomini A.,
RA Corich V., De Paula S.O.;
RT "The complete genome sequence of Trueperella pyogenes UFV1 reveals an AI-2
RT transporter and processing system involved in quorum sensing signal-
RT response.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AZR06058.1, ECO:0000313|Proteomes:UP000275951}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TP4 {ECO:0000313|EMBL:AZR06058.1,
RC ECO:0000313|Proteomes:UP000275951};
RA Dong W.;
RT "Multidrug-resistant genes are associated with an 42-kb island TGI1
RT carrying a complex class 1 integron in a Trueperella pyogenes.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:UVJ60662.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=22/KM0800 {ECO:0000313|EMBL:UVJ60662.1};
RA Marchionatti E., Perreten V.;
RT "Complete Genome Sequences of Trueperella pyogenes (tetW) from cattle in
RT Switzerland.";
RL Submitted (MAY-2022) 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_00079}.
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_00079};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00079};
CC -!- ACTIVITY REGULATION: Feedback inhibited by histidine.
CC {ECO:0000256|HAMAP-Rule:MF_00079}.
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_00079}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00079}.
CC -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Long
CC subfamily. {ECO:0000256|ARBA:ARBA00007955, ECO:0000256|HAMAP-
CC Rule:MF_00079}.
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DR EMBL; CP033905; AZR06058.1; -; Genomic_DNA.
DR EMBL; MVGS01000004; OQD40066.1; -; Genomic_DNA.
DR EMBL; MVGS01000003; OQD40359.1; -; Genomic_DNA.
DR EMBL; CP097247; UVJ60662.1; -; Genomic_DNA.
DR RefSeq; WP_024964116.1; NZ_RWKU01000001.1.
DR AlphaFoldDB; X4QW95; -.
DR STRING; 1661.CQ11_00580; -.
DR GeneID; 41086138; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000191477; Unassembled WGS sequence.
DR Proteomes; UP000275951; Chromosome.
DR Proteomes; UP001058955; Chromosome.
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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd13591; PBP2_HisGL1; 1.
DR Gene3D; 3.30.70.120; -; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR HAMAP; MF_00079; HisG_Long; 1.
DR InterPro; IPR020621; ATP-PRT_HisG_long.
DR InterPro; IPR013820; ATP_PRibTrfase_cat.
DR InterPro; IPR018198; ATP_PRibTrfase_CS.
DR InterPro; IPR001348; ATP_PRibTrfase_HisG.
DR InterPro; IPR013115; HisG_C.
DR InterPro; IPR011322; N-reg_PII-like_a/b.
DR InterPro; IPR015867; N-reg_PII/ATP_PRibTrfase_C.
DR NCBIfam; TIGR00070; hisG; 1.
DR NCBIfam; TIGR03455; HisG_C-term; 1.
DR PANTHER; PTHR21403:SF8; ATP PHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR21403; ATP PHOSPHORIBOSYLTRANSFERASE ATP-PRTASE; 1.
DR Pfam; PF01634; HisG; 1.
DR Pfam; PF08029; HisG_C; 1.
DR SUPFAM; SSF54913; GlnB-like; 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_00079}; ATP-binding {ECO:0000256|HAMAP-Rule:MF_00079};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00079};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW Rule:MF_00079};
KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102, ECO:0000256|HAMAP-
KW Rule:MF_00079}; Magnesium {ECO:0000256|HAMAP-Rule:MF_00079};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00079};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00079};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00079}.
FT DOMAIN 49..188
FT /note="ATP phosphoribosyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01634"
FT DOMAIN 206..276
FT /note="Histidine biosynthesis HisG C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08029"
SQ SEQUENCE 281 AA; 30852 MW; 447F00DD8BB8FAC6 CRC64;
MLRIAVPNKG SLSDPASRML AEAGYRQRRE SRELVLVDAE NDVEFFYIRP RDVAVYVGAG
TVDVGITGRD LLLDSQAPAI EHRGLGFARA TFRFAAPGGE QMSIDDLQGK RIATSYDSLV
SNYLAKHGID ATVVHLDGAV ESSVRLGVAD AIADVVETGT TLRAAGMAVF GEPLLRSEAI
LIRRADQEVS HDVQILDGRL EGVIMARNYV LMDYDIQRDL LEHAVRLTPG YQSPTISPLH
DDEWVAVRAM VERKRMNKVM DDLHDAGARG ILVTPILTSR M
//