ID   HYEP_FLABM              Reviewed;         349 AA.
AC   C0BK17;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=Hydrophobic dipeptide epimerase;
DE            EC=5.1.1.-;
GN   ORFNames=Flav2ADRAFT_0209;
OS   Flavobacteria bacterium (strain MS024-2A).
OC   Bacteria; Bacteroidetes; Flavobacteriia.
OX   NCBI_TaxID=487796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS024-2A;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Woyke T., Xie G., Copeland A., Gonzalez J., Han C., Kiss H., Saw J.,
RA   Senin P., Chatterji S., Cheng J.-F., Eisen J.A., Sieracki M.E.,
RA   Stepanauskas R.;
RT   "Assembling the metagenome, one cell at a time.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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 a variety of hydrophobic
CC       dipeptides. Epimerase activity is highest with L-Ala-L-Tyr, and lower
CC       with L-Ala-L-Met, L-Ala-L-Phe, L-Tyr-L-Ala, L-Tyr-L-Met and L-Tyr-L-Trp
CC       (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; ABVV01000007; EEG40905.1; -; Genomic_DNA.
DR   RefSeq; WP_008866726.1; NZ_ABVV01000007.1.
DR   AlphaFoldDB; C0BK17; -.
DR   SMR; C0BK17; -.
DR   STRING; 487796.Flav2ADRAFT_0209; -.
DR   EnsemblBacteria; EEG40905; EEG40905; Flav2ADRAFT_0209.
DR   eggNOG; COG4948; Bacteria.
DR   OMA; DIVDHRH; -.
DR   OrthoDB; 951991at2; -.
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   SFLD; SFLDF00010; dipeptide_epimerase; 1.
DR   SMART; SM00922; MR_MLE; 1.
DR   SUPFAM; SSF51604; SSF51604; 1.
DR   SUPFAM; SSF54826; SSF54826; 1.
DR   PROSITE; PS00909; MR_MLE_2; 1.
PE   3: Inferred from homology;
KW   Isomerase; Magnesium; Metal-binding.
FT   CHAIN           1..349
FT                   /note="Hydrophobic dipeptide epimerase"
FT                   /id="PRO_0000429645"
FT   BINDING         127
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         153..155
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         259
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         309..311
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   349 AA;  38267 MW;  FBD6BC76C990716B CRC64;
     MKFTFHKVTL KKRFPLAISR GVRYNSENLF VCYEKDGHIG WGEAAPGNSE GAATAEAVQE
     ALENFIATGI EGFSIQELYD RAREMKIPPC AYVALDTAFW DWTAKKAQLP LRQLLGFSKP
     HTPTSVTIGI NPPEVIKERV PLLLEGTTVQ SLKIKLGSPE GIDADKTMFE QVVESTKKYP
     VKLRVDANGG WDVNQAQHMM QWLADRKVDY IEQPLKEGDE AGLKTLFKSR PLPIYVDESC
     RFSQNIPSFA AHVDGVNMKL MKCGGITEAL RIIGTARAHG LKTMIGCMSE SSVAIAAAAA
     MTGGIDHIDL DSHYNLAPDP AHGAPLINGV TLPPEIPGHG AYLKEEFYA