AEEP_ECOLI
ID AEEP_ECOLI Reviewed; 321 AA.
AC P51981; P51982; P76048; P77345;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=L-Ala-D/L-Glu epimerase;
DE Short=AE epimerase;
DE Short=AEE;
DE EC=5.1.1.20 {ECO:0000269|PubMed:11747447};
GN Name=ycjG; Synonyms=ycjH; OrderedLocusNames=b1325, JW1318;
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=7499381; DOI=10.1074/jbc.270.48.28635;
RA Cha M.-K., Kim H.-K., Kim I.-H.;
RT "Thioredoxin-linked 'thiol peroxidase' from periplasmic space of
RT Escherichia coli.";
RL J. Biol. Chem. 270:28635-28641(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [3]
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 [4]
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 [5]
RP IDENTIFICATION.
RA Rudd K.E.;
RL Unpublished observations (MAR-1996).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=11747447; DOI=10.1021/bi011640x;
RA Schmidt D.M.Z., Hubbard B.K., Gerlt J.A.;
RT "Evolution of enzymatic activities in the enolase superfamily: functional
RT assignment of unknown proteins in Bacillus subtilis and Escherichia coli as
RT L-Ala-D/L-Glu epimerases.";
RL Biochemistry 40:15707-15715(2001).
RN [7]
RP FUNCTION IN PEPTIDOGLYCAN RECYCLING, AND REVIEW.
RX PubMed=18535144; DOI=10.1128/mmbr.00027-07;
RA Park J.T., Uehara T.;
RT "How bacteria consume their own exoskeletons (turnover and recycling of
RT cell wall peptidoglycan).";
RL Microbiol. Mol. Biol. Rev. 72:211-227(2008).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), AND SUBUNIT.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=11747448; DOI=10.1021/bi011641p;
RA Gulick A.M., Schmidt D.M.Z., Gerlt J.A., Rayment I.;
RT "Evolution of enzymatic activities in the enolase superfamily: crystal
RT structures of the L-Ala-D/L-Glu epimerases from Escherichia coli and
RT Bacillus subtilis.";
RL Biochemistry 40:15716-15724(2001).
CC -!- FUNCTION: Catalyzes the epimerization of L-Ala-D-Glu to L-Ala-L-Glu and
CC has a role in the recycling of the murein peptide, of which L-Ala-D-Glu
CC is a component. Is also able to catalyze the reverse reaction and the
CC epimerization of all the L-Ala-X dipeptides, except L-Ala-L-Arg, L-Ala-
CC L-Lys and L-Ala-L-Pro. Is also active with L-Gly-L-Glu, L-Phe-L-Glu,
CC and L-Ser-L-Glu, but not with L-Glu-L-Glu, L-Lys-L-Glu, L-Pro-L-Glu, L-
CC Lys-L-Ala, or D-Ala-D-Ala. {ECO:0000269|PubMed:11747447,
CC ECO:0000269|PubMed:18535144}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-alanyl-L-glutamate = L-alanyl-D-glutamate;
CC Xref=Rhea:RHEA:28394, ChEBI:CHEBI:61395, ChEBI:CHEBI:61396;
CC EC=5.1.1.20; Evidence={ECO:0000269|PubMed:11747447};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.13 mM for L-Ala-D-Glu (at pH 8.5) {ECO:0000269|PubMed:11747447};
CC KM=0.19 mM for L-Ala-D-Asp (at pH 8.5) {ECO:0000269|PubMed:11747447};
CC KM=0.69 mM for L-Ala-D-Met (at pH 8.5) {ECO:0000269|PubMed:11747447};
CC KM=1.8 mM for L-Ala-D-Gln (at pH 8.5) {ECO:0000269|PubMed:11747447};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11747448}.
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=U33213; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=U33213; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U33213; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U00096; AAC74407.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA14907.1; -; Genomic_DNA.
DR PIR; H64881; H64881.
DR RefSeq; NP_415841.4; NC_000913.3.
DR RefSeq; WP_001261211.1; NZ_SSZK01000012.1.
DR PDB; 1JPD; X-ray; 2.60 A; X=1-321.
DR PDBsum; 1JPD; -.
DR AlphaFoldDB; P51981; -.
DR SMR; P51981; -.
DR BioGRID; 4260152; 370.
DR IntAct; P51981; 1.
DR STRING; 511145.b1325; -.
DR jPOST; P51981; -.
DR PaxDb; P51981; -.
DR PRIDE; P51981; -.
DR EnsemblBacteria; AAC74407; AAC74407; b1325.
DR EnsemblBacteria; BAA14907; BAA14907; BAA14907.
DR GeneID; 946013; -.
DR KEGG; ecj:JW1318; -.
DR KEGG; eco:b1325; -.
DR PATRIC; fig|1411691.4.peg.953; -.
DR EchoBASE; EB3018; -.
DR eggNOG; COG4948; Bacteria.
DR HOGENOM; CLU_030273_4_3_6; -.
DR InParanoid; P51981; -.
DR OMA; DIVDHRH; -.
DR PhylomeDB; P51981; -.
DR BioCyc; EcoCyc:G6661-MON; -.
DR BioCyc; MetaCyc:G6661-MON; -.
DR BRENDA; 5.1.1.20; 2026.
DR SABIO-RK; P51981; -.
DR UniPathway; UPA00544; -.
DR EvolutionaryTrace; P51981; -.
DR PRO; PR:P51981; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0103031; F:L-Ala-D/L-Glu epimerase activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016855; F:racemase and epimerase activity, acting on amino acids and derivatives; IDA:EcoCyc.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009063; P:cellular amino acid catabolic process; IEA:InterPro.
DR GO; GO:0009254; P:peptidoglycan turnover; IEA:UniProtKB-UniPathway.
DR CDD; cd03319; L-Ala-DL-Glu_epimerase; 1.
DR Gene3D; 3.20.20.120; -; 1.
DR Gene3D; 3.30.390.10; -; 1.
DR InterPro; IPR034603; Dipeptide_epimerase.
DR InterPro; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR029017; Enolase-like_N.
DR InterPro; IPR029065; Enolase_C-like.
DR InterPro; IPR018110; Mandel_Rmase/mucon_lact_enz_CS.
DR InterPro; IPR013342; Mandelate_racemase_C.
DR InterPro; IPR034593; Mandelate_racemase_DgoD-like.
DR InterPro; IPR013341; Mandelate_racemase_N_dom.
DR PANTHER; PTHR48080; PTHR48080; 2.
DR Pfam; PF13378; MR_MLE_C; 1.
DR Pfam; PF02746; MR_MLE_N; 1.
DR SFLD; SFLDF00010; dipeptide_epimerase; 1.
DR SMART; SM00922; MR_MLE; 1.
DR SUPFAM; SSF51604; SSF51604; 1.
DR SUPFAM; SSF54826; SSF54826; 1.
DR PROSITE; PS00908; MR_MLE_1; 1.
DR PROSITE; PS00909; MR_MLE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall biogenesis/degradation; Isomerase; Magnesium;
KW Metal-binding; Reference proteome.
FT CHAIN 1..321
FT /note="L-Ala-D/L-Glu epimerase"
FT /id="PRO_0000171261"
FT ACT_SITE 151
FT /note="Proton acceptor; specific for (R)-substrate
FT epimerization"
FT /evidence="ECO:0000250"
FT ACT_SITE 247
FT /note="Proton acceptor; specific for (S)-substrate
FT epimerization"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 297
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 299
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 236
FT /note="A -> R (in Ref. 1; U33213)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="V -> I (in Ref. 1; U33213)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="Missing (in Ref. 1; U33213)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="A -> G (in Ref. 1; U33213)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="P -> S (in Ref. 1; U33213)"
FT /evidence="ECO:0000305"
FT STRAND 3..14
FT /evidence="ECO:0007829|PDB:1JPD"
FT STRAND 25..36
FT /evidence="ECO:0007829|PDB:1JPD"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:1JPD"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:1JPD"
FT HELIX 55..63
FT /evidence="ECO:0007829|PDB:1JPD"
FT HELIX 66..70
FT /evidence="ECO:0007829|PDB:1JPD"
FT HELIX 75..81
FT /evidence="ECO:0007829|PDB:1JPD"
FT HELIX 86..101
FT /evidence="ECO:0007829|PDB:1JPD"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:1JPD"
FT HELIX 107..111
FT /evidence="ECO:0007829|PDB:1JPD"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:1JPD"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:1JPD"
FT HELIX 130..142
FT /evidence="ECO:0007829|PDB:1JPD"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:1JPD"
FT HELIX 157..167
FT /evidence="ECO:0007829|PDB:1JPD"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:1JPD"
FT HELIX 186..195
FT /evidence="ECO:0007829|PDB:1JPD"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:1JPD"
FT HELIX 211..214
FT /evidence="ECO:0007829|PDB:1JPD"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:1JPD"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:1JPD"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:1JPD"
FT STRAND 241..246
FT /evidence="ECO:0007829|PDB:1JPD"
FT HELIX 248..251
FT /evidence="ECO:0007829|PDB:1JPD"
FT HELIX 254..266
FT /evidence="ECO:0007829|PDB:1JPD"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:1JPD"
FT HELIX 280..286
FT /evidence="ECO:0007829|PDB:1JPD"
FT HELIX 287..292
FT /evidence="ECO:0007829|PDB:1JPD"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:1JPD"
FT HELIX 300..303
FT /evidence="ECO:0007829|PDB:1JPD"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:1JPD"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:1JPD"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:1JPD"
SQ SEQUENCE 321 AA; 34674 MW; B0AA31DD4EC2E2CB CRC64;
MRTVKVFEEA WPLHTPFVIA RGSRSEARVV VVELEEEGIK GTGECTPYPR YGESDASVMA
QIMSVVPQLE KGLTREELQK ILPAGAARNA LDCALWDLAA RRQQQSLADL IGITLPETVI
TAQTVVIGTP DQMANSASTL WQAGAKLLKV KLDNHLISER MVAIRTAVPD ATLIVDANES
WRAEGLAARC QLLADLGVAM LEQPLPAQDD AALENFIHPL PICADESCHT RSNLKALKGR
YEMVNIKLDK TGGLTEALAL ATEARAQGFS LMLGCMLCTS RAISAALPLV PQVSFADLDG
PTWLAVDVEP ALQFTTGELH L
