ID   AEEP_FRATN              Reviewed;         356 AA.
AC   A0Q5S7;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=L-Ala-D/L-Glu epimerase;
DE            Short=AE epimerase;
DE            Short=AEE;
DE            EC=5.1.1.20;
DE   AltName: Full=L-Hydrophobic/Polar-D/L-Glu epimerase;
GN   OrderedLocusNames=FTN_0700;
OS   Francisella tularensis subsp. novicida (strain U112).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=401614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U112;
RX   PubMed=17550600; DOI=10.1186/gb-2007-8-6-r102;
RA   Rohmer L., Fong C., Abmayr S., Wasnick M., Larson Freeman T.J., Radey M.,
RA   Guina T., Svensson K., Hayden H.S., Jacobs M., Gallagher L.A., Manoil C.,
RA   Ernst R.K., Drees B., Buckley D., Haugen E., Bovee D., Zhou Y., Chang J.,
RA   Levy R., Lim R., Gillett W., Guenthener D., Kang A., Shaffer S.A.,
RA   Taylor G., Chen J., Gallis B., D'Argenio D.A., Forsman M., Olson M.V.,
RA   Goodlett D.R., Kaul R., Miller S.I., Brittnacher M.J.;
RT   "Comparison of Francisella tularensis genomes reveals evolutionary events
RT   associated with the emergence of human pathogenic strains.";
RL   Genome Biol. 8:R102.1-R102.16(2007).
RN   [2]
RP   FUNCTION, AND COFACTOR.
RX   PubMed=22392983; DOI=10.1073/pnas.1112081109;
RA   Lukk T., Sakai A., Kalyanaraman C., Brown S.D., Imker H.J., Song L.,
RA   Fedorov A.A., Fedorov E.V., Toro R., Hillerich B., Seidel R.,
RA   Patskovsky Y., Vetting M.W., Nair S.K., Babbitt P.C., Almo S.C.,
RA   Gerlt J.A., Jacobson M.P.;
RT   "Homology models guide discovery of diverse enzyme specificities among
RT   dipeptide epimerases in the enolase superfamily.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:4122-4127(2012).
CC   -!- FUNCTION: Dipeptide epimerase with a preference for substrates
CC       containing a Glu residue in the second position. Catalyzes the
CC       epimerization of L-Ala-L-Glu, L-Ser-L-Glu, L-Thr-L-Glu, L-Val-L-Glu, L-
CC       Gly-L-Glu and L-Thr-L-Glu (in vitro). May play a role in the metabolism
CC       of the murein peptide, of which L-Ala-D-Glu is a component.
CC       {ECO:0000269|PubMed:22392983}.
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;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:22392983};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:22392983};
CC   -!- MISCELLANEOUS: Part of a large, functionally divergent protein family.
CC       Protein modeling and substrate docking were used to predict the
CC       substrate specificity, prior to biochemical analysis.
CC   -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC       enzyme family. {ECO:0000305}.
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DR   EMBL; CP000439; ABK89592.1; -; Genomic_DNA.
DR   RefSeq; WP_003038832.1; NZ_CP009633.1.
DR   AlphaFoldDB; A0Q5S7; -.
DR   SMR; A0Q5S7; -.
DR   EnsemblBacteria; ABK89592; ABK89592; FTN_0700.
DR   KEGG; ftn:FTN_0700; -.
DR   OMA; RQRDICL; -.
DR   OrthoDB; 951991at2; -.
DR   BioCyc; FTUL401614:G1G75-728-MON; -.
DR   Proteomes; UP000000762; Chromosome.
DR   GO; GO:0103031; F:L-Ala-D/L-Glu epimerase activity; IEA:RHEA.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR   GO; GO:0016854; F:racemase and epimerase activity; IDA:UniProtKB.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0006518; P:peptide metabolic process; IDA:UniProtKB.
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; IPR013342; Mandelate_racemase_C.
DR   InterPro; IPR013341; Mandelate_racemase_N_dom.
DR   Pfam; PF13378; MR_MLE_C; 1.
DR   Pfam; PF02746; MR_MLE_N; 1.
DR   SMART; SM00922; MR_MLE; 1.
DR   SUPFAM; SSF51604; SSF51604; 1.
DR   SUPFAM; SSF54826; SSF54826; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Isomerase; Magnesium; Metal-binding.
FT   CHAIN           1..356
FT                   /note="L-Ala-D/L-Glu epimerase"
FT                   /id="PRO_0000429647"
FT   BINDING         161..163
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         191
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         219
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         244
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         268
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         320..322
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   356 AA;  39122 MW;  4EF62A31CFCF3087 CRC64;
     MSKIIDIKTS IVTIPLKRTF VTAVRSTNHI DAVVVELSLD NGNKGYGVAP ATTAITGDTL
     QGMQYIISEI FAPVILSSNL SDYKQTLELA FKKVMFNSAA KMALDLAFHD LLAKQKNISV
     AKLLGAKNNI IETDVSISCG SVAETIQNIQ NGVEANFTTI KVKTGADFNR DIQLLKSLDN
     EFSKNIKFRF DANQGWNISQ TKQFIEELNK YSLNVEIIEQ PVKYYDISAM REITKFSNIP
     IVADESVFDA KDAERVIDEQ ACNMINIKLA KSGGILEAQK IKKLADSVGI PCMVGCMMES
     PAGILATASF ALAEGITVAD LDPLDWVAKD LYSDYITFNE PNIIIKDNLK GFGFSF