ID   AXEP_PEDPL              Reviewed;         347 AA.
AC   B9XEK4;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   14-APR-2009, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=L-Ala-D/L-amino acid epimerase;
DE            EC=5.1.1.-;
GN   ORFNames=Cflav_PD4758;
OS   Pedosphaera parvula (strain Ellin514).
OC   Bacteria; Verrucomicrobia; Verrucomicrobiae; Verrucomicrobiales;
OC   Verrucomicrobia subdivision 3; Pedosphaera.
OX   NCBI_TaxID=320771;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ellin514;
RX   PubMed=21460084; DOI=10.1128/jb.00299-11;
RA   Kant R., van Passel M.W., Sangwan P., Palva A., Lucas S., Copeland A.,
RA   Lapidus A., Glavina Del Rio T., Dalin E., Tice H., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Larimer F.W., Land M.L., Hauser L., Brettin T.S.,
RA   Detter J.C., Han S., de Vos W.M., Janssen P.H., Smidt H.;
RT   "Genome sequence of 'Pedosphaera parvula' Ellin514, an aerobic
RT   Verrucomicrobial isolate from pasture soil.";
RL   J. Bacteriol. 193:2900-2901(2011).
RN   [2]
RP   FUNCTION, AND COFACTOR.
RC   STRAIN=Ellin514;
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 broad substrate specificity.
CC       Catalyzes the epimerization of L-Ala-L-Ala, L-Ala-L-Ser, L-Ala-L-Thr,
CC       L-Ala-L-Met, L-Ala-L-Phe, L-Ala-L-Tyr, L-Gly-L-Asp, L-Val-L-Asp, L-Val-
CC       L-Glu and L-Val-L-Phe (in vitro). Can also catalyze the epimerization
CC       of L-Ala-L-Glu, but with lower efficiency.
CC       {ECO:0000269|PubMed:22392983}.
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; ABOX02000008; EEF61718.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9XEK4; -.
DR   SMR; B9XEK4; -.
DR   STRING; 320771.Cflav_PD4758; -.
DR   EnsemblBacteria; EEF61718; EEF61718; Cflav_PD4758.
DR   OMA; HEEFPVT; -.
DR   Proteomes; UP000003688; Unassembled WGS sequence.
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; IEA:InterPro.
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; IPR034593; Mandelate_racemase_DgoD-like.
DR   InterPro; IPR013341; Mandelate_racemase_N_dom.
DR   PANTHER; PTHR48080; PTHR48080; 1.
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   Isomerase; Magnesium; Metal-binding; Reference proteome.
FT   CHAIN           1..347
FT                   /note="L-Ala-D/L-amino acid epimerase"
FT                   /id="PRO_0000429651"
FT   BINDING         156..158
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         183
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         211
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         237
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         259
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         309..311
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   347 AA;  37646 MW;  E69C19B6D827ECC4 CRC64;
     MQIKFWPQDL KLAHTWTIAS SVTSGSDVTS VGIVQLTDRD GTVGLGEAAP ARRYNESTPG
     SLDFIAKVDA TKLSFDNIEA SMKYVESLAS GQFAAKSAIN VALLDGAARK AGKPIYDLLG
     LGFRNNHHVT SFSIGIDKAD VIRKKVLAAE QYPVLKLKVG AADDKANLAA LREAAPQKWV
     RVDANEGWKT KEHALEMIEW LAQDKFIQYI EQPMPADSNP KDIAWLKARS PLPLFGDESY
     HTAKDVDHCA ECYHGVNVKL CKTGGISNAY EALQVARKAG LKTMIGCMIE TSILISAAAH
     LAELCDYLDI DGNLLTTNDP YLGVTAEKGL LSFASAPEKL GLRVRAK