ID   HYEP_CITBB              Reviewed;         368 AA.
AC   B5EFW2;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Hydrophobic dipeptide epimerase;
DE            EC=5.1.1.-;
DE   AltName: Full=L-Hydrophobic-D/L-Hydrophobic epimerase;
GN   OrderedLocusNames=Gbem_2417;
OS   Citrifermentans bemidjiense (strain ATCC BAA-1014 / DSM 16622 / JCM 12645 /
OS   Bem) (Geobacter bemidjiensis).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Citrifermentans.
OX   NCBI_TaxID=404380;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1014 / DSM 16622 / JCM 12645 / Bem;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Lovley D., Richardson P.;
RT   "Complete sequence of Geobacter bemidjiensis BEM.";
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, AND COFACTOR.
RC   STRAIN=ATCC BAA-1014 / DSM 16622 / JCM 12645 / Bem;
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 various hydrophobic
CC       dipeptides, such as L-Ala-L-Phe. Has epimerase activity with L-Ala-L-
CC       Thr, L-Ala-L-Met, L-Ala-L-Tyr, as well as L-Phe-L-Met, L-Phe-L-Ser and
CC       L-Phe-L-Thr (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; CP001124; ACH39427.1; -; Genomic_DNA.
DR   RefSeq; WP_012530849.1; NC_011146.1.
DR   AlphaFoldDB; B5EFW2; -.
DR   SMR; B5EFW2; -.
DR   STRING; 404380.Gbem_2417; -.
DR   EnsemblBacteria; ACH39427; ACH39427; Gbem_2417.
DR   KEGG; gbm:Gbem_2417; -.
DR   eggNOG; COG4948; Bacteria.
DR   HOGENOM; CLU_030273_4_1_7; -.
DR   OMA; RQRDICL; -.
DR   OrthoDB; 951991at2; -.
DR   Proteomes; UP000008825; 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..368
FT                   /note="Hydrophobic dipeptide epimerase"
FT                   /id="PRO_0000429654"
FT   BINDING         143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         168..170
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         197
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         225
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         253
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         277
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         329..331
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   368 AA;  38981 MW;  6310D29D49546165 CRC64;
     MDISFQIQDA VASVIRAPLA SPFRIATGQH DELENVFLKL TTRDGVSGYG EAAVASHITG
     ETVPGTLANL QNAAAALRGQ TVDDAESACR QFAAAFAGNH AGLAALEMAL LDLSSRVRGI
     PFYRLFAPVA ALEPRLAFST DITVVIGSLD EARATAREFA SRGFKAFKIK IGRDEQLDLA
     RVLAVHEIAP DSQIILDANM GFSAGSMLAF LDRLAAKGVR PVLLEQPVPK MDWDGLSEIT
     AALTGSETLV CADESVGSLA DARRAIDSNA VSAINVKFMK SGILEGAEIA RLAASRGIRL
     MLGAMMESAL AVTASAHFAA GLACFDYLDM DTTFFLKGEL AHSPYLDEHG RFDLHDAGPG
     IGVEPRFS