ID   AXEP_FLAJ1              Reviewed;         336 AA.
AC   A5FHW9;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=L-Ala-D/L-amino acid epimerase;
DE            EC=5.1.1.-;
DE   AltName: Full=L-Ala-L-Xxx epimerase;
GN   OrderedLocusNames=Fjoh_2168;
OS   Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / NBRC
OS   14942 / NCIMB 11054 / UW101) (Cytophaga johnsonae).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=376686;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17061 / DSM 2064 / JCM 8514 / NBRC 14942 / NCIMB 11054 / UW101;
RX   PubMed=19717629; DOI=10.1128/aem.01495-09;
RA   McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., Rhodes R.G.,
RA   Goltsman E., Wang W., Xu J., Hunnicutt D.W., Staroscik A.M., Hoover T.R.,
RA   Cheng Y.Q., Stein J.L.;
RT   "Novel features of the polysaccharide-digesting gliding bacterium
RT   Flavobacterium johnsoniae as revealed by genome sequence analysis.";
RL   Appl. Environ. Microbiol. 75:6864-6875(2009).
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: Catalyzes the epimerization of D-Ala-D-Ala to D-Ala-L-Ala.
CC       Has broad substrate specificity and catalyzes the epimerization of a
CC       variety of dipeptides containing an N-terminal Ala followed by Ser,
CC       Thr, Val, Met, His, Phe or Trp (in vitro).
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; CP000685; ABQ05196.1; -; Genomic_DNA.
DR   RefSeq; WP_012024235.1; NZ_MUGZ01000022.1.
DR   AlphaFoldDB; A5FHW9; -.
DR   SMR; A5FHW9; -.
DR   STRING; 376686.Fjoh_2168; -.
DR   EnsemblBacteria; ABQ05196; ABQ05196; Fjoh_2168.
DR   KEGG; fjo:Fjoh_2168; -.
DR   eggNOG; COG4948; Bacteria.
DR   HOGENOM; CLU_030273_4_3_10; -.
DR   OMA; DIVDHRH; -.
DR   OrthoDB; 951991at2; -.
DR   Proteomes; UP000006694; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR   GO; GO:0016854; F:racemase and epimerase activity; IDA:UniProtKB.
DR   GO; GO:0016855; F:racemase and epimerase activity, acting on amino acids and derivatives; IEA:InterPro.
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; 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.
FT   CHAIN           1..336
FT                   /note="L-Ala-D/L-amino acid epimerase"
FT                   /id="PRO_0000429649"
FT   BINDING         130
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         152..154
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         178
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         204
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         229
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         251
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         301..303
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   336 AA;  37996 MW;  1B3B54877B884A4A CRC64;
     MKLILREYNL KLKHTFTISR ESIDFQPSLI VELQSEGFSG FGEATSNPYY NITVPMMMQD
     LEKIRSIIED TENETPDVFW AKIHPYLKND MFALCALDLA YNDLYARKKG KKLYELWNYT
     TERNPMTDYT IGIASIDKMV SKMQELPWPI YKIKLGTKED IEIVKELRKH TNAVFRIDAN
     CGWGVEETIN NSVELKKLGV EFLEQPMKAD NWEGHKEVFK HSVLPVIADE SCIIEEDVAK
     CFNHFHGVNV KLVKCGGLTP GKRMIEEAKK LGLRTMVGCM TESTVGISAI AHLLPQLDYV
     DMDGALLLAE DIATGVTIKD GVVSYSNLNG TGVTLL