HIS1_AERS4
ID HIS1_AERS4 Reviewed; 298 AA.
AC A4SMP5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=ATP phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00079};
DE Short=ATP-PRT {ECO:0000255|HAMAP-Rule:MF_00079};
DE Short=ATP-PRTase {ECO:0000255|HAMAP-Rule:MF_00079};
DE EC=2.4.2.17 {ECO:0000255|HAMAP-Rule:MF_00079};
GN Name=hisG {ECO:0000255|HAMAP-Rule:MF_00079}; OrderedLocusNames=ASA_2101;
OS Aeromonas salmonicida (strain A449).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=382245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A449;
RX PubMed=18801193; DOI=10.1186/1471-2164-9-427;
RA Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J.,
RA Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C.,
RA Brown L.L.;
RT "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into
RT the evolution of a fish pathogen.";
RL BMC Genomics 9:427-427(2008).
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_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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00079};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00079};
CC -!- ACTIVITY REGULATION: Feedback inhibited by histidine.
CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_00079}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00079}.
CC -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Long
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00079}.
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DR EMBL; CP000644; ABO90167.1; -; Genomic_DNA.
DR RefSeq; WP_005311391.1; NC_009348.1.
DR AlphaFoldDB; A4SMP5; -.
DR SMR; A4SMP5; -.
DR STRING; 382245.ASA_2101; -.
DR EnsemblBacteria; ABO90167; ABO90167; ASA_2101.
DR GeneID; 60848448; -.
DR KEGG; asa:ASA_2101; -.
DR eggNOG; COG0040; Bacteria.
DR HOGENOM; CLU_038115_1_0_6; -.
DR OMA; YVMMDYD; -.
DR OrthoDB; 1419568at2; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000000225; 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 Gene3D; 3.30.70.120; -; 1.
DR HAMAP; MF_00079; HisG_Long; 1.
DR InterPro; IPR013820; ATP_PRibTrfase_cat.
DR InterPro; IPR018198; ATP_PRibTrfase_CS.
DR InterPro; IPR001348; ATP_PRibTrfase_HisG.
DR InterPro; IPR020621; ATP_PRibTrfase_HisG_long.
DR InterPro; IPR013115; HisG_C.
DR InterPro; IPR011322; N-reg_PII-like_a/b.
DR InterPro; IPR015867; N-reg_PII/ATP_PRibTrfase_C.
DR PANTHER; PTHR21403; PTHR21403; 1.
DR Pfam; PF01634; HisG; 1.
DR Pfam; PF08029; HisG_C; 1.
DR SUPFAM; SSF54913; SSF54913; 1.
DR TIGRFAMs; TIGR00070; hisG; 1.
DR TIGRFAMs; TIGR03455; HisG_C-term; 1.
DR PROSITE; PS01316; ATP_P_PHORIBOSYLTR; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; ATP-binding; Cytoplasm; Glycosyltransferase;
KW Histidine biosynthesis; Magnesium; Metal-binding; Nucleotide-binding;
KW Transferase.
FT CHAIN 1..298
FT /note="ATP phosphoribosyltransferase"
FT /id="PRO_1000004439"
SQ SEQUENCE 298 AA; 32595 MW; E8570F7DB39FFA15 CRC64;
METQRLRIAM QKSGRLSQDS QALFKSCGLK INLREQRLIA HVENMPIDIL RVRDDDIPGL
VMEGVVDLGI IGENVLEEAQ LIRASQGLPA QVKTLKQLDF GGCRLSLAVP DDVAYTGPES
LAGKRIATSY PGLLKRFFDE KGLNFKSVML GGSVEVAPRA GLADAICDLV STGATLEANG
LKEVEVIYRS KAVLVQAPNP LNEAKQKLID KLLPRIQGMQ QARESKYIML HAPKDKLDAI
TDLLPGAERP TIMQLAGDTN QVALHVVSSE TLFWETMEQL KALGASSILV LPIEKMME
