ID   XEEP_SULDN              Reviewed;         341 AA.
AC   Q30PM2;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=L-amino acid-D/L-Glu epimerase;
DE            EC=5.1.1.-;
DE   AltName: Full=L-Xxx-D/L-Glu epimerase;
GN   OrderedLocusNames=Suden_1785;
OS   Sulfurimonas denitrificans (strain ATCC 33889 / DSM 1251) (Thiomicrospira
OS   denitrificans (strain ATCC 33889 / DSM 1251)).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Thiovulaceae; Sulfurimonas.
OX   NCBI_TaxID=326298;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33889 / DSM 1251;
RX   PubMed=18065616; DOI=10.1128/aem.01844-07;
RA   Sievert S.M., Scott K.M., Klotz M.G., Chain P.S.G., Hauser L.J., Hemp J.,
RA   Huegler M., Land M., Lapidus A., Larimer F.W., Lucas S., Malfatti S.A.,
RA   Meyer F., Paulsen I.T., Ren Q., Simon J., Bailey K., Diaz E.,
RA   Fitzpatrick K.A., Glover B., Gwatney N., Korajkic A., Long A.,
RA   Mobberley J.M., Pantry S.N., Pazder G., Peterson S., Quintanilla J.D.,
RA   Sprinkle R., Stephens J., Thomas P., Vaughn R., Weber M.J., Wooten L.L.;
RT   "Genome of the epsilonproteobacterial chemolithoautotroph Sulfurimonas
RT   denitrificans.";
RL   Appl. Environ. Microbiol. 74:1145-1156(2008).
RN   [2]
RP   FUNCTION, AND COFACTOR.
RC   STRAIN=ATCC 33889 / DSM 1251;
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 dipeptides with L-Glu in the
CC       second position. Has epimerase activity with L-Gly-L-Glu, L-Ala-L-Glu,
CC       L-Ser-L-Glu, L-Pro-L-Glu, L-Val-L-Glu, L-Met-L-Glu, L-Thr-L-Glu and L-
CC       Phe-L-Glu (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 was 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; CP000153; ABB45059.1; -; Genomic_DNA.
DR   RefSeq; WP_011373399.1; NC_007575.1.
DR   AlphaFoldDB; Q30PM2; -.
DR   SMR; Q30PM2; -.
DR   STRING; 326298.Suden_1785; -.
DR   EnsemblBacteria; ABB45059; ABB45059; Suden_1785.
DR   KEGG; tdn:Suden_1785; -.
DR   eggNOG; COG4948; Bacteria.
DR   HOGENOM; CLU_030273_4_0_7; -.
DR   OMA; RQRDICL; -.
DR   OrthoDB; 951991at2; -.
DR   Proteomes; UP000002714; 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; 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   Isomerase; Magnesium; Metal-binding; Reference proteome.
FT   CHAIN           1..341
FT                   /note="L-amino acid-D/L-Glu epimerase"
FT                   /id="PRO_0000429660"
FT   BINDING         132
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         157..159
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         186
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         212
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         261
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         315..317
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   341 AA;  37811 MW;  B425A3F1E1B796E5 CRC64;
     MKIVNITTQV ESIELKTPFK TALRQTSHVE FVRVEVECDN GFVGIGEASA TKVITGEDIY
     IILTSIASVE ELFLNLTCEE ALGALHTKCA IGSSAKASLD IAFVHLLSQE AKKPLYEYFG
     ATDKSALKSD ITISLNEADV MLNDAKKAFS NGMDILKIKV GSDILHAIDI VRKIAKELPE
     CDILVDANQA WSFENTVLFI ENMLNTPIKL IEQPVEAPNL DGLKKITELS HIPILADEAV
     FTLKDAKKVI EEKCADMINI KLMKCGGVSK AIEILEFARN REFKCMLGSM LEGPYSINMA
     LHLAFAYRDV IEFVDLDSPL LYKEMPKELD FVFDGCEIKP L