HIS1_ECOLI
ID HIS1_ECOLI Reviewed; 299 AA.
AC P60757; P10366;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=ATP phosphoribosyltransferase;
DE Short=ATP-PRT;
DE Short=ATP-PRTase;
DE EC=2.4.2.17;
GN Name=hisG; OrderedLocusNames=b2019, JW2001;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3062174; DOI=10.1016/0022-2836(88)90194-5;
RA Carlomagno M.S., Chiariotti L., Alifano P., Nappo A.G., Bruni C.B.;
RT "Structure and function of the Salmonella typhimurium and Escherichia coli
RT K-12 histidine operons.";
RL J. Mol. Biol. 203:585-606(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION.
RC STRAIN=K12;
RX PubMed=8201624; DOI=10.1006/jmbi.1994.1384;
RA Jovanovic G., Kostic T., Jankovic M., Savic D.J.;
RT "Nucleotide sequence of the Escherichia coli K12 histidine operon
RT revisited.";
RL J. Mol. Biol. 239:433-435(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RX PubMed=6170941; DOI=10.1093/nar/9.9.2075;
RA Verde P., Frunzio R., di Nocera P.P., Blasi F., Bruni C.B.;
RT "Identification, nucleotide sequence and expression of the regulatory
RT region of the histidine operon of Escherichia coli K-12.";
RL Nucleic Acids Res. 9:2075-2086(1981).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND PATHWAY.
RX PubMed=4909873; DOI=10.1021/bi00811a025;
RA Klungsoyr L., Atkinson D.E.;
RT "Regulatory properties of phosphoribosyladenosine triphosphate synthetase.
RT Synergism between adenosine monophosphate, phosphoribosyladenosine
RT triphosphate, and histidine.";
RL Biochemistry 9:2021-2027(1970).
RN [8]
RP SUBUNIT.
RX PubMed=4927808; DOI=10.1016/0005-2744(71)90064-7;
RA Klungsoeyr L., Kryvi H.;
RT "Sedimentation behaviour of phosphoribosyladenosine triphosphate
RT synthetase. Effects of substrates and modifiers.";
RL Biochim. Biophys. Acta 227:327-336(1971).
RN [9]
RP SUBUNIT.
RC STRAIN=K12;
RX PubMed=4358959; DOI=10.1007/bf01943865;
RA Tebar A.R., Fernandez V.M., Martin Del Rio R., Ballesteros A.O.;
RT "Studies on the quaternary structure of the first enzyme for histidine
RT biosynthesis.";
RL Experientia 29:1477-1479(1973).
RN [10]
RP CRYSTALLIZATION.
RX PubMed=11185885; DOI=10.1107/s0907444900011306;
RA Lohkamp B., Coggins J.R., Lapthorn A.J.;
RT "Purification, crystallization and preliminary X-ray crystallographic
RT analysis of ATP-phosphoribosyltransferase from Escherichia coli.";
RL Acta Crystallogr. D 56:1488-1491(2000).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH AMP AND PR-ATP, AND
RP ACTIVITY REGULATION.
RX PubMed=14741209; DOI=10.1016/j.jmb.2003.12.020;
RA Lohkamp B., McDermott G., Campbell S.A., Coggins J.R., Lapthorn A.J.;
RT "The structure of Escherichia coli ATP-phosphoribosyltransferase:
RT identification of substrate binding sites and mode of AMP inhibition.";
RL J. Mol. Biol. 336:131-144(2004).
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:0000269|PubMed:4909873}.
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:0000269|PubMed:4909873};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:4909873};
CC -!- ACTIVITY REGULATION: Feedback inhibited by histidine. Also inhibited by
CC AMP and PR-ATP. {ECO:0000269|PubMed:14741209,
CC ECO:0000269|PubMed:4909873}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
CC {ECO:0000269|PubMed:4909873}.
CC -!- SUBUNIT: Equilibrium between an active dimeric form, an inactive
CC hexameric form and higher aggregates. Interconversion between the
CC various forms is largely reversible and is influenced by the natural
CC substrates and inhibitors of the enzyme. {ECO:0000269|PubMed:14741209,
CC ECO:0000269|PubMed:4358959, ECO:0000269|PubMed:4927808}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Long
CC subfamily. {ECO:0000305}.
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DR EMBL; X13462; CAA31811.1; -; Genomic_DNA.
DR EMBL; X63697; CAA45224.1; -; Genomic_DNA.
DR EMBL; U02070; AAA19742.1; -; Unassigned_DNA.
DR EMBL; U00096; AAC75080.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15850.1; -; Genomic_DNA.
DR EMBL; V00284; CAA23549.1; -; Genomic_DNA.
DR PIR; B64967; XREC.
DR RefSeq; NP_416523.1; NC_000913.3.
DR RefSeq; WP_000131782.1; NZ_STEB01000048.1.
DR PDB; 1H3D; X-ray; 2.70 A; A=1-299.
DR PDB; 1Q1K; X-ray; 2.90 A; A=1-299.
DR PDBsum; 1H3D; -.
DR PDBsum; 1Q1K; -.
DR AlphaFoldDB; P60757; -.
DR SMR; P60757; -.
DR BioGRID; 4263530; 24.
DR IntAct; P60757; 1.
DR STRING; 511145.b2019; -.
DR DrugBank; DB01661; 1-(5-phospho-D-ribosyl)-ATP.
DR SWISS-2DPAGE; P60757; -.
DR jPOST; P60757; -.
DR PaxDb; P60757; -.
DR PRIDE; P60757; -.
DR EnsemblBacteria; AAC75080; AAC75080; b2019.
DR EnsemblBacteria; BAA15850; BAA15850; BAA15850.
DR GeneID; 66674083; -.
DR GeneID; 946549; -.
DR KEGG; ecj:JW2001; -.
DR KEGG; eco:b2019; -.
DR PATRIC; fig|1411691.4.peg.233; -.
DR EchoBASE; EB0444; -.
DR eggNOG; COG0040; Bacteria.
DR HOGENOM; CLU_038115_1_0_6; -.
DR InParanoid; P60757; -.
DR OMA; YVMMDYD; -.
DR PhylomeDB; P60757; -.
DR BioCyc; EcoCyc:ATPPHOSRIBOSTRANS-MON; -.
DR BioCyc; MetaCyc:ATPPHOSRIBOSTRANS-MON; -.
DR BRENDA; 2.4.2.17; 2026.
DR UniPathway; UPA00031; UER00006.
DR EvolutionaryTrace; P60757; -.
DR PRO; PR:P60757; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003879; F:ATP phosphoribosyltransferase activity; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000105; P:histidine biosynthetic process; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; ATP-binding; Cytoplasm;
KW Glycosyltransferase; Histidine biosynthesis; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..299
FT /note="ATP phosphoribosyltransferase"
FT /id="PRO_0000151848"
FT CONFLICT 6
FT /note="R -> P (in Ref. 6; CAA23549)"
FT /evidence="ECO:0000305"
FT CONFLICT 49..50
FT /note="DI -> GV (in Ref. 1; CAA31811)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="V -> A (in Ref. 1; CAA31811)"
FT /evidence="ECO:0000305"
FT STRAND 7..15
FT /evidence="ECO:0007829|PDB:1H3D"
FT HELIX 18..27
FT /evidence="ECO:0007829|PDB:1H3D"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:1H3D"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:1H3D"
FT STRAND 44..53
FT /evidence="ECO:0007829|PDB:1H3D"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:1H3D"
FT HELIX 58..63
FT /evidence="ECO:0007829|PDB:1H3D"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:1H3D"
FT HELIX 74..86
FT /evidence="ECO:0007829|PDB:1H3D"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:1H3D"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:1H3D"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:1H3D"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:1H3D"
FT HELIX 132..142
FT /evidence="ECO:0007829|PDB:1H3D"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:1H3D"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:1H3D"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:1H3D"
FT STRAND 165..173
FT /evidence="ECO:0007829|PDB:1H3D"
FT HELIX 175..179
FT /evidence="ECO:0007829|PDB:1H3D"
FT STRAND 182..191
FT /evidence="ECO:0007829|PDB:1H3D"
FT STRAND 193..200
FT /evidence="ECO:0007829|PDB:1H3D"
FT HELIX 204..225
FT /evidence="ECO:0007829|PDB:1H3D"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:1H3D"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:1H3D"
FT HELIX 238..244
FT /evidence="ECO:0007829|PDB:1H3D"
FT STRAND 265..271
FT /evidence="ECO:0007829|PDB:1H3D"
FT HELIX 275..283
FT /evidence="ECO:0007829|PDB:1H3D"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:1H3D"
SQ SEQUENCE 299 AA; 33367 MW; 716B2A8F4538A724 CRC64;
MTDNTRLRIA MQKSGRLSDD SRELLARCGI KINLHTQRLI AMAENMPIDI LRVRDDDIPG
LVMDGVVDLG IIGENVLEEE LLNRRAQGED PRYFTLRRLD FGGCRLSLAT PVDEAWDGPL
SLNGKRIATS YPHLLKRYLD QKGISFKSCL LNGSVEVAPR AGLADAICDL VSTGATLEAN
GLREVEVIYR SKACLIQRDG EMEESKQQLI DKLLTRIQGV IQARESKYIM MHAPTERLDE
VIALLPGAER PTILPLAGDQ QRVAMHMVSS ETLFWETMEK LKALGASSIL VLPIEKMME
