ID   HYEP_ROSLO              Reviewed;         344 AA.
AC   F7ZLS5;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Hydrophobic dipeptide epimerase;
DE            EC=5.1.1.-;
GN   OrderedLocusNames=RLO149_c021500;
OS   Roseobacter litoralis (strain ATCC 49566 / DSM 6996 / JCM 21268 / NBRC
OS   15278 / OCh 149).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseobacter.
OX   NCBI_TaxID=391595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49566 / DSM 6996 / JCM 21268 / NBRC 15278 / OCh 149;
RX   PubMed=21693016; DOI=10.1186/1471-2164-12-324;
RA   Kalhoefer D., Thole S., Voget S., Lehmann R., Liesegang H., Wollher A.,
RA   Daniel R., Simon M., Brinkhoff T.;
RT   "Comparative genome analysis and genome-guided physiological analysis of
RT   Roseobacter litoralis.";
RL   BMC Genomics 12:324-324(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: Dipeptide epimerase with a preference for hydrophobic
CC       substrates. Catalyzes the epimerization of L-Ala-L-Thr, L-Ala-L-Met, L-
CC       Ala-L-His, L-Ala-L-Phe, L-Ala-L-Tyr, L-Ala-L-Trp, L-Ile-L-Ala, L-Ile-L-
CC       Ser, L-Ile-L-Met, L-Ile-L-His, L-Ile-L-Phe, L-Ile-L-Tyr, L-Ile-L-Trp,
CC       L-Phe-L-Met, L-Phe-L-His, L-Phe-L-Phe, L-Phe-L-Tyr, L-Phe-L-Trp, L-Phe-
CC       L-Ser, L-Phe-L-Thr and L-Phe-L-Lys (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 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; CP002623; AEI94126.1; -; Genomic_DNA.
DR   RefSeq; WP_013962050.1; NC_015730.1.
DR   AlphaFoldDB; F7ZLS5; -.
DR   SMR; F7ZLS5; -.
DR   STRING; 391595.RLO149_c021500; -.
DR   EnsemblBacteria; AEI94126; AEI94126; RLO149_c021500.
DR   KEGG; rli:RLO149_c021500; -.
DR   eggNOG; COG4948; Bacteria.
DR   HOGENOM; CLU_030273_4_3_5; -.
DR   OMA; MIGQMNE; -.
DR   OrthoDB; 951991at2; -.
DR   Proteomes; UP000001353; 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:0009063; P:cellular amino acid catabolic process; 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; IPR018110; Mandel_Rmase/mucon_lact_enz_CS.
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.
DR   PROSITE; PS00908; MR_MLE_1; 1.
DR   PROSITE; PS00909; MR_MLE_2; 1.
PE   3: Inferred from homology;
KW   Isomerase; Magnesium; Metal-binding.
FT   CHAIN           1..344
FT                   /note="Hydrophobic dipeptide epimerase"
FT                   /id="PRO_0000429655"
FT   BINDING         126
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         151..153
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         184
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         210
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         235
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         257
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         307..309
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   344 AA;  36436 MW;  CA9558323D5D96F7 CRC64;
     MKVEYHTVYL KKRFPLRISR GVFEGSDNLY ISLTENGHTG WGEMAPGGTE GAETAAAGQA
     MLEQFCATGL SASIHDTWQN AHAAGVAPCA LAALDMALWD LRAKQAGVPL YALLGLARRA
     VVSSVTVGIN PPDVVRERVP LLLARGARAL KIKLGSPEGI EADQAMFAAV FEAAQGSGAV
     LRVDANGGWS LKDARRMMGW LAEHDVEYIE QPLVRGAEDQ LPDLFKDRAM PIFVDESCRM
     SGDIATFFQS VDGVNLKLMK CGGITEALRI VATARAFGLK TMIGCMGESS VSIAAGASIG
     ALFDYIDLDS HLNLDPDPAT GAPFENGITL PADQPGHGGV LSHA