PUR1_ECOLI
ID PUR1_ECOLI Reviewed; 505 AA.
AC P0AG16; P00496; P78092; P78191; P78192; Q47255; Q59425;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Amidophosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01931, ECO:0000303|PubMed:6443594};
DE Short=ATase {ECO:0000255|HAMAP-Rule:MF_01931};
DE EC=2.4.2.14 {ECO:0000255|HAMAP-Rule:MF_01931, ECO:0000269|PubMed:372191};
DE AltName: Full=Glutamine phosphoribosylpyrophosphate amidotransferase {ECO:0000255|HAMAP-Rule:MF_01931, ECO:0000303|PubMed:372191};
DE Short=GPATase {ECO:0000255|HAMAP-Rule:MF_01931, ECO:0000303|PubMed:9333323};
GN Name=purF {ECO:0000255|HAMAP-Rule:MF_01931};
GN OrderedLocusNames=b2312, JW2309;
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=3047685; DOI=10.1093/nar/16.17.8717;
RA Sampei G., Mizobuchi K.;
RT "Nucleotide sequence of the Escherichia coli purF gene encoding
RT amidophosphoribosyltransferase for de novo purine nucleotide synthesis.";
RL Nucleic Acids Res. 16:8717-8717(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6443594; DOI=10.1016/0065-2571(83)90016-x;
RA Zalkin H.;
RT "Structure, function, and regulation of amidophosphoribosyltransferase from
RT prokaryotes.";
RL Adv. Enzyme Regul. 21:225-237(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6277938; DOI=10.1016/s0021-9258(18)34810-5;
RA Tso J.Y., Zalkin H., van Cleemput M., Yanofsky C., Smith J.M.;
RT "Nucleotide sequence of Escherichia coli purF and deduced amino acid
RT sequence of glutamine phosphoribosylpyrophosphate amidotransferase.";
RL J. Biol. Chem. 257:3525-3531(1982).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31 AND 483-505.
RC STRAIN=K12;
RX PubMed=3040734; DOI=10.1016/s0021-9258(18)45338-0;
RA Nonet M.L., Marvel C.C., Tolan D.R.;
RT "The hisT-purF region of the Escherichia coli K-12 chromosome.
RT Identification of additional genes of the hisT and purF operons.";
RL J. Biol. Chem. 262:12209-12217(1987).
RN [8]
RP PROTEIN SEQUENCE OF 2-24, AND ACTIVE SITE.
RX PubMed=7037784; DOI=10.1016/s0021-9258(18)34811-7;
RA Tso J.Y., Hermodson M.A., Zalkin H.;
RT "Glutamine phosphoribosylpyrophosphate amidotransferase from cloned
RT Escherichia coli purF. NH2-terminal amino acid sequence, identification of
RT the glutamine site, and trace metal analysis.";
RL J. Biol. Chem. 257:3532-3536(1982).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND PATHWAY.
RX PubMed=372191; DOI=10.1016/s0021-9258(18)50771-7;
RA Messenger L.J., Zalkin H.;
RT "Glutamine phosphoribosylpyrophosphate amidotransferase from Escherichia
RT coli. Purification and properties.";
RL J. Biol. Chem. 254:3382-3392(1979).
RN [10]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX PubMed=9333323; DOI=10.1021/bi9714114;
RA Krahn J.M., Kim J.H., Burns M.R., Parry R.J., Zalkin H., Smith J.L.;
RT "Coupled formation of an amidotransferase interdomain ammonia channel and a
RT phosphoribosyltransferase active site.";
RL Biochemistry 36:11061-11068(1997).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND SUBUNIT.
RX PubMed=9514258; DOI=10.1002/pro.5560070104;
RA Muchmore C.R.A., Krahn J.M., Kim J.H., Zalkin H., Smith J.L.;
RT "Crystal structure of glutamine phosphoribosylpyrophosphate
RT amidotransferase from Escherichia coli.";
RL Protein Sci. 7:39-51(1998).
CC -!- FUNCTION: Catalyzes the formation of phosphoribosylamine from
CC phosphoribosylpyrophosphate (PRPP) and glutamine. Can also use NH(3) in
CC place of glutamine. {ECO:0000269|PubMed:372191}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-
CC phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine;
CC Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01931, ECO:0000269|PubMed:372191};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01931};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01931};
CC -!- ACTIVITY REGULATION: Inhibited by iodoacetamide and by the glutamine
CC analogs chloroketone and DON. {ECO:0000269|PubMed:372191}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.067 mM for phosphoribosylpyrophosphate
CC {ECO:0000269|PubMed:372191};
CC KM=1.7 mM for glutamine {ECO:0000269|PubMed:372191};
CC KM=8.8 mM for NH(3) {ECO:0000269|PubMed:372191};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-
CC (5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-
CC diphosphate: step 1/2. {ECO:0000255|HAMAP-Rule:MF_01931,
CC ECO:0000269|PubMed:372191}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:9514258}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the purine/pyrimidine
CC phosphoribosyltransferase family. {ECO:0000255|HAMAP-Rule:MF_01931,
CC ECO:0000305}.
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DR EMBL; X12423; CAA30971.1; -; Genomic_DNA.
DR EMBL; V00322; CAA23613.1; -; Genomic_DNA.
DR EMBL; M26893; AAA24453.1; -; Genomic_DNA.
DR EMBL; J01666; AAA24452.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75372.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16158.1; -; Genomic_DNA.
DR EMBL; M68935; AAA23969.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M68934; AAA23969.1; JOINED; Genomic_DNA.
DR PIR; F65003; XQEC.
DR RefSeq; NP_416815.1; NC_000913.3.
DR RefSeq; WP_000334220.1; NZ_STEB01000008.1.
DR PDB; 1ECB; X-ray; 2.70 A; A/B/C/D=2-505.
DR PDB; 1ECC; X-ray; 2.40 A; A/B=2-505.
DR PDB; 1ECF; X-ray; 2.00 A; A/B=2-505.
DR PDB; 1ECG; X-ray; 2.30 A; A/B=2-505.
DR PDB; 1ECJ; X-ray; 2.50 A; A/B/C/D=2-505.
DR PDB; 6CZF; X-ray; 1.95 A; A/B/C/D=2-499.
DR PDB; 6OTT; X-ray; 2.55 A; A/B=2-505.
DR PDBsum; 1ECB; -.
DR PDBsum; 1ECC; -.
DR PDBsum; 1ECF; -.
DR PDBsum; 1ECG; -.
DR PDBsum; 1ECJ; -.
DR PDBsum; 6CZF; -.
DR PDBsum; 6OTT; -.
DR AlphaFoldDB; P0AG16; -.
DR SMR; P0AG16; -.
DR BioGRID; 4261075; 7.
DR STRING; 511145.b2312; -.
DR DrugBank; DB04296; 5-Oxo-L-Norleucine.
DR DrugBank; DB03942; Carboxylic PRPP.
DR DrugBank; DB01972; Guanosine-5'-Monophosphate.
DR MEROPS; C44.001; -.
DR jPOST; P0AG16; -.
DR PaxDb; P0AG16; -.
DR PRIDE; P0AG16; -.
DR EnsemblBacteria; AAC75372; AAC75372; b2312.
DR EnsemblBacteria; BAA16158; BAA16158; BAA16158.
DR GeneID; 66673805; -.
DR GeneID; 946794; -.
DR KEGG; ecj:JW2309; -.
DR KEGG; eco:b2312; -.
DR PATRIC; fig|1411691.4.peg.4422; -.
DR EchoBASE; EB0787; -.
DR eggNOG; COG0034; Bacteria.
DR InParanoid; P0AG16; -.
DR OMA; ENAQPTF; -.
DR PhylomeDB; P0AG16; -.
DR BioCyc; EcoCyc:PRPPAMIDOTRANS-MON; -.
DR BioCyc; MetaCyc:PRPPAMIDOTRANS-MON; -.
DR BRENDA; 2.4.2.14; 2026.
DR SABIO-RK; P0AG16; -.
DR UniPathway; UPA00074; UER00124.
DR EvolutionaryTrace; P0AG16; -.
DR PRO; PR:P0AG16; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0004044; F:amidophosphoribosyltransferase activity; IDA:EcoCyc.
DR GO; GO:0016757; F:glycosyltransferase activity; IDA:EcoliWiki.
DR GO; GO:0097216; F:guanosine tetraphosphate binding; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006541; P:glutamine metabolic process; IDA:EcoliWiki.
DR GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IDA:EcoliWiki.
DR CDD; cd00715; GPATase_N; 1.
DR CDD; cd06223; PRTases_typeI; 1.
DR DisProt; DP00578; -.
DR Gene3D; 3.40.50.2020; -; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR HAMAP; MF_01931; PurF; 1.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR005854; PurF.
DR InterPro; IPR035584; PurF_N.
DR Pfam; PF00156; Pribosyltran; 1.
DR PIRSF; PIRSF000485; Amd_phspho_trans; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR TIGRFAMs; TIGR01134; purF; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Glutamine amidotransferase;
KW Glycosyltransferase; Magnesium; Metal-binding; Purine biosynthesis;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7037784"
FT CHAIN 2..505
FT /note="Amidophosphoribosyltransferase"
FT /id="PRO_0000139638"
FT DOMAIN 2..236
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931"
FT ACT_SITE 2
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931,
FT ECO:0000269|PubMed:7037784"
FT BINDING 305
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931"
FT BINDING 367
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931"
FT BINDING 368
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931"
FT CONFLICT 45..46
FT /note="LR -> SL (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="G -> A (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 213..230
FT /note="ALDTLGFDFLRDVAPGEA -> GSIRWALISCVTSRRAR (in Ref. 2
FT and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="V -> A (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="L -> V (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="M -> I (in Ref. 2; AAA24453)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="A -> R (in Ref. 1; CAA30971)"
FT /evidence="ECO:0000305"
FT CONFLICT 494
FT /note="N -> S (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:6CZF"
FT HELIX 14..23
FT /evidence="ECO:0007829|PDB:6CZF"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:6CZF"
FT STRAND 30..37
FT /evidence="ECO:0007829|PDB:6CZF"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:6CZF"
FT HELIX 52..55
FT /evidence="ECO:0007829|PDB:6CZF"
FT HELIX 58..63
FT /evidence="ECO:0007829|PDB:6CZF"
FT STRAND 66..74
FT /evidence="ECO:0007829|PDB:6CZF"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:1ECJ"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:1ECC"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:6CZF"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:6CZF"
FT STRAND 97..105
FT /evidence="ECO:0007829|PDB:6CZF"
FT HELIX 108..119
FT /evidence="ECO:0007829|PDB:6CZF"
FT HELIX 128..140
FT /evidence="ECO:0007829|PDB:6CZF"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:6CZF"
FT HELIX 150..163
FT /evidence="ECO:0007829|PDB:6CZF"
FT STRAND 166..174
FT /evidence="ECO:0007829|PDB:6CZF"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:6CZF"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:6CZF"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:6CZF"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:6CZF"
FT STRAND 203..210
FT /evidence="ECO:0007829|PDB:6CZF"
FT HELIX 211..216
FT /evidence="ECO:0007829|PDB:6CZF"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:6CZF"
FT STRAND 229..237
FT /evidence="ECO:0007829|PDB:6CZF"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:6CZF"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:6CZF"
FT HELIX 254..258
FT /evidence="ECO:0007829|PDB:6CZF"
FT HELIX 272..290
FT /evidence="ECO:0007829|PDB:6CZF"
FT TURN 291..293
FT /evidence="ECO:0007829|PDB:1ECF"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:6CZF"
FT TURN 303..306
FT /evidence="ECO:0007829|PDB:6CZF"
FT HELIX 307..317
FT /evidence="ECO:0007829|PDB:6CZF"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:6CZF"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:1ECF"
FT HELIX 346..350
FT /evidence="ECO:0007829|PDB:6CZF"
FT STRAND 351..353
FT /evidence="ECO:0007829|PDB:6CZF"
FT HELIX 355..357
FT /evidence="ECO:0007829|PDB:6CZF"
FT TURN 358..360
FT /evidence="ECO:0007829|PDB:6CZF"
FT STRAND 363..368
FT /evidence="ECO:0007829|PDB:6CZF"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:6CZF"
FT HELIX 374..385
FT /evidence="ECO:0007829|PDB:6CZF"
FT STRAND 389..397
FT /evidence="ECO:0007829|PDB:6CZF"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:6CZF"
FT HELIX 413..415
FT /evidence="ECO:0007829|PDB:6CZF"
FT TURN 417..420
FT /evidence="ECO:0007829|PDB:6CZF"
FT HELIX 423..430
FT /evidence="ECO:0007829|PDB:6CZF"
FT STRAND 433..437
FT /evidence="ECO:0007829|PDB:6CZF"
FT HELIX 440..448
FT /evidence="ECO:0007829|PDB:6CZF"
FT HELIX 460..463
FT /evidence="ECO:0007829|PDB:6CZF"
FT HELIX 473..498
FT /evidence="ECO:0007829|PDB:6CZF"
SQ SEQUENCE 505 AA; 56488 MW; 50FD08EA85E6F2A8 CRC64;
MCGIVGIAGV MPVNQSIYDA LTVLQHRGQD AAGIITIDAN NCFRLRKANG LVSDVFEARH
MQRLQGNMGI GHVRYPTAGS SSASEAQPFY VNSPYGITLA HNGNLTNAHE LRKKLFEEKR
RHINTTSDSE ILLNIFASEL DNFRHYPLEA DNIFAAIAAT NRLIRGAYAC VAMIIGHGMV
AFRDPNGIRP LVLGKRDIDE NRTEYMVASE SVALDTLGFD FLRDVAPGEA IYITEEGQLF
TRQCADNPVS NPCLFEYVYF ARPDSFIDKI SVYSARVNMG TKLGEKIARE WEDLDIDVVI
PIPETSCDIA LEIARILGKP YRQGFVKNRY VGRTFIMPGQ QLRRKSVRRK LNANRAEFRD
KNVLLVDDSI VRGTTSEQII EMAREAGAKK VYLASAAPEI RFPNVYGIDM PSATELIAHG
REVDEIRQII GADGLIFQDL NDLIDAVRAE NPDIQQFECS VFNGVYVTKD VDQGYLDFLD
TLRNDDAKAV QRQNEVENLE MHNEG
