{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P33644","secondaryAccessions":["Q46989"],"uniProtkbId":"PGEF_ECOLI","entryAudit":{"firstPublicDate":"1994-02-01","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"1994-02-01","entryVersion":163,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Escherichia coli (strain K12)","taxonId":83333,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"28612943"}],"value":"Peptidoglycan editing factor PgeF"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"35164571"}],"value":"PG-editing factor"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35164571"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"40632566"}],"value":"3.5.-.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Adenosine deaminase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31978345"}],"value":"3.5.4.4"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"16740638"}],"value":"Polyphenol oxidase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16740638"}],"value":"1.10.3.-"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"40632566"}],"value":"Proofreading amidase PgeF"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Purine nucleoside phosphorylase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31978345"}],"value":"2.4.2.1"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"S-methyl-5'-thioadenosine phosphorylase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31978345"}],"value":"2.4.2.28"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"28612943"}],"value":"pgeF"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"16740638"},{"evidenceCode":"ECO:0000312","source":"EMBL","id":"AAC75642.1"}],"value":"yfiH"}],"orderedLocusNames":[{"value":"b2593"},{"value":"JW2575"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28612943"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35164571"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"40632566"}],"value":"Proofreading amidase that contributes to the maintenance of cell wall composition and integrity (PubMed:28612943, PubMed:35164571, PubMed:40632566). It prevents the mis-incorporation of both L-serine and glycine containing precursors into the peptidoglycan (PG) sacculi (PubMed:28612943, PubMed:35164571, PubMed:40632566). Acts by hydrolyzing UDP-N-acetylmuramoyl-L-serine (UDP-MurNAc-L-Ser) to release L-serine and UDP-N-acetylmuramoyl-glycine (UDP-MurNAc-Gly) to release glycine, thereby preventing the mis-incorporation of these amino acids into the PG and ensuring that only the correct PG precursor, UDP-MurNAc-L-Ala, is incorporated (PubMed:35164571, PubMed:40632566). It can also use UDP-MurNAc-L-Ala, with 10-fold lower activity compared to UDP-MurNAc-L-Ser, and it exhibits weak activity toward UDP-MurNAc-L-Ala-D-Glu (UMAE) and UDP-MurNAc-L-Ser-D-Glu (UMSE) (PubMed:35164571). It does not exhibit PG hydrolytic activity (PubMed:28612943)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16740638"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31978345"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"40632566"}],"value":"The enzyme also shows purine nucleoside phosphorylase (PNP) activity in vitro (PubMed:31978345). It can catalyze the phosphorolysis of adenosine and inosine nucleosides, yielding D-ribose 1-phosphate and the respective free bases, adenine and hypoxanthine (PubMed:31978345). However, this PNP activity is weak, requires higher protein concentration as compared to the precursor editing activity, and cannot confer growth to a PNP-deficient mutant in vivo, suggesting that it may not be physiologically significant in E.coli (PubMed:40632566). In addition, the enzyme has several other activities in vitro: it can catalyze the phosphorolysis of S-methyl-5'-thioadenosine into adenine and S-methyl-5-thio-alpha-D-ribose 1-phosphate, and it has adenosine deaminase activity (PubMed:31978345). It also shows polyphenol oxidase activity and is able to oxidize syringaldazine and 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) (PubMed:16740638)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine + phosphate = alpha-D-ribose 1-phosphate + adenine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:27642"},{"database":"ChEBI","id":"CHEBI:16335"},{"database":"ChEBI","id":"CHEBI:16708"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57720"}],"ecNumber":"2.4.2.1","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31978345"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"inosine + phosphate = alpha-D-ribose 1-phosphate + hypoxanthine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:27646"},{"database":"ChEBI","id":"CHEBI:17368"},{"database":"ChEBI","id":"CHEBI:17596"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57720"}],"ecNumber":"2.4.2.1","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31978345"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"S-methyl-5'-thioadenosine + phosphate = 5-(methylsulfanyl)-alpha-D-ribose 1-phosphate + adenine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11852"},{"database":"ChEBI","id":"CHEBI:16708"},{"database":"ChEBI","id":"CHEBI:17509"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58533"}],"ecNumber":"2.4.2.28","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31978345"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine + H2O + H(+) = inosine + NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24408"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16335"},{"database":"ChEBI","id":"CHEBI:17596"},{"database":"ChEBI","id":"CHEBI:28938"}],"ecNumber":"3.5.4.4","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31978345"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Cu(2+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16740638"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29036"}},{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P84138"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}]},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":23.0,"unit":"uM","substrate":"2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (at pH 4.5 and 40 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16740638"}]},{"constant":1.1,"unit":"uM","substrate":"syringaldazine (at pH 4.5 and 40 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16740638"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16740638"}],"value":"kcat is 1450 min(-1) with 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) as substrate (PubMed:16740638). kcat is 21720 min(-1) with syringaldazine as substrate (at pH 4.5 and 40 degrees Celsius) (PubMed:16740638)."}]}},"phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16740638"}],"value":"Optimum pH is 5.5-8.4. Maintains 80% activity at pH 5.0-9.0."}]},"temperatureDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16740638"}],"value":"Optimum temperature is 44 degrees Celsius. Maintains more than 80% activity at 50 degrees Celsius."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"40632566"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"28612943"}],"value":"Cell wall biogenesis; peptidoglycan biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16740638"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35164571"}],"value":"Homodimer (PubMed:16740638). The crystal contains four molecules per asymmetric unit (PubMed:35164571)"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28612943"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35164571"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"40632566"}],"value":"Was originally thought to be periplasmic, but the presence of the N-terminal region in the structure indicates that PgeF does not possess a signal peptide and therefore is a cytoplasmic protein (PubMed:28612943, PubMed:35164571). It was subsequently confirmed that it is located in the cytoplasm (PubMed:40632566)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35164571"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"40632566"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20065048"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28612943"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"40632566"}],"value":"The mutant shows incorporation of L-serine or glycine in place of L-alanine in peptidoglycan (PubMed:28612943, PubMed:40632566). It also shows altered cell morphology and reduced peptidoglycan synthesis (PubMed:28612943). Cells lacking this gene are more sensitive to ampicillin, cephradine and cefoxitin than wild-type strain (PubMed:20065048). The deletion mutant is extremely sensitive to cephalexin and ampicillin and weakly susceptible to other classes of beta-lactam antibiotics, which affect cell wall biosynthesis (PubMed:28612943). It is not susceptible to any of the antibiotics affecting other cellular processes or to outer membrane disrupting agents (PubMed:28612943). All phenotypes of the mutant can be suppressed by a decrease in the intracellular pool of L-serine/glycine (PubMed:28612943). The phenotypes of the mutant are fully complemented by homologs from S.enterica, B.subtilis or G.stearothermophilus (PubMed:40632566)"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"40632566"}],"value":"Peptidoglycan editing and PNP activities of PgeF proceed through distinct and independent catalytic mechanisms"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the PgeF/LACC1 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":243,"modifier":"EXACT"}},"description":"Peptidoglycan editing factor PgeF","featureId":"PRO_0000163163"},{"type":"Binding 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