ID   AXEP_MARSH              Reviewed;         337 AA.
AC   A4AQI7;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=L-Ala-D/L-amino acid epimerase;
DE            EC=5.1.1.-;
GN   OrderedLocusNames=FB2170_14398;
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371;
RX   PubMed=21037013; DOI=10.1128/jb.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the genus
RT   Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
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: Broad specificity dipeptide epimerase. Catalyzes the
CC       epimerization of L-Ala-L-Ala, L-Ala-L-Glu, L-Ala-L-Ser, L-Ala-L-Thr and
CC       L-Ala-L-Met (in vitro). {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; CP002157; EAR01726.1; -; Genomic_DNA.
DR   RefSeq; WP_013307499.1; NC_014472.1.
DR   AlphaFoldDB; A4AQI7; -.
DR   SMR; A4AQI7; -.
DR   STRING; 313603.FB2170_14398; -.
DR   EnsemblBacteria; EAR01726; EAR01726; FB2170_14398.
DR   KEGG; fbc:FB2170_14398; -.
DR   eggNOG; COG4948; Bacteria.
DR   HOGENOM; CLU_030273_4_3_10; -.
DR   OMA; DIVDHRH; -.
DR   OrthoDB; 951991at2; -.
DR   Proteomes; UP000001602; 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; Reference proteome.
FT   CHAIN           1..337
FT                   /note="L-Ala-D/L-amino acid epimerase"
FT                   /id="PRO_0000429652"
FT   BINDING         129
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         151..153
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         177
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         203
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         228
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         250
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         300..302
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   337 AA;  37265 MW;  69B72BEAA4CFCC93 CRC64;
     MQISLKKYTL ELKHTFSISR ESHDFQDTLI AGLTLNGKTG YGEATSNPYY KITAESMIKE
     IEGIKNEIES FEFTTPESFH SFLEEKELSN FAICALDLAA HDLYGKLLGK PLYEIWGTNN
     DQYPTTNYTI GIAELDTMVA KMKEKPWPIY KIKLGTDNDV AIIRELRKHT TATFRIDANC
     AWSAEETIAN APQLKELGVE FLEQPLQADD WAGMEKVMHQ CVLPVIADES CIVESDVEKC
     GLHFNGINIK LTKCGGLTPA LRMIKKAKLM GLKVMVGCMT ESSVGISAIA QLLPQLDYVD
     MDGAILLKRD IANGVRIGED GSVVFPTLGG SGVTLNQ