ID   AREP_HERA2              Reviewed;         356 AA.
AC   A9B055;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Aromatic dipeptide epimerase;
DE            EC=5.1.1.-;
GN   OrderedLocusNames=Haur_1114;
OS   Herpetosiphon aurantiacus (strain ATCC 23779 / DSM 785 / 114-95).
OC   Bacteria; Chloroflexi; Chloroflexia; Herpetosiphonales; Herpetosiphonaceae;
OC   Herpetosiphon.
OX   NCBI_TaxID=316274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23779 / DSM 785 / 114-95;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Bryant D.A., Richardson P.;
RT   "Complete sequence of chromosome of Herpetosiphon aurantiacus ATCC 23779.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 2-355, FUNCTION, COFACTOR, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC 23779 / DSM 785 / 114-95;
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: Has epimerase activity with a variety of hydrophobic
CC       dipeptides (in vitro). Enzyme activity is highest with L-Phe-L-Tyr, but
CC       is still relatively low, suggesting that L-Phe-L-Tyr is not the
CC       physiological substrate. {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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=4.8 mM for L-Phe-L-Tyr {ECO:0000269|PubMed:22392983};
CC         Note=kcat is 4.7 sec(-1) for epimerization of L-Phe-L-Tyr.;
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; CP000875; ABX03762.1; -; Genomic_DNA.
DR   PDB; 3IK4; X-ray; 2.10 A; A/B/C/D=2-355.
DR   PDBsum; 3IK4; -.
DR   AlphaFoldDB; A9B055; -.
DR   SMR; A9B055; -.
DR   STRING; 316274.Haur_1114; -.
DR   EnsemblBacteria; ABX03762; ABX03762; Haur_1114.
DR   KEGG; hau:Haur_1114; -.
DR   eggNOG; COG4948; Bacteria.
DR   HOGENOM; CLU_030273_4_1_0; -.
DR   OMA; MFGCYSD; -.
DR   BioCyc; HAUR316274:GHYA-1135-MON; -.
DR   EvolutionaryTrace; A9B055; -.
DR   Proteomes; UP000000787; 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   1: Evidence at protein level;
KW   3D-structure; Isomerase; Magnesium; Metal-binding; Reference proteome.
FT   CHAIN           1..356
FT                   /note="Aromatic dipeptide epimerase"
FT                   /id="PRO_0000429648"
FT   BINDING         136
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         161..163
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         191
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000305"
FT   BINDING         219
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000305"
FT   BINDING         244
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000305"
FT   BINDING         268
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         320..322
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   STRAND          4..18
FT                   /evidence="ECO:0007829|PDB:3IK4"
FT   STRAND          21..23
FT                   /evidence="ECO:0007829|PDB:3IK4"
FT   STRAND          26..28
FT                   /evidence="ECO:0007829|PDB:3IK4"
FT   STRAND          30..40
FT                   /evidence="ECO:0007829|PDB:3IK4"
FT   STRAND          45..50
FT                   /evidence="ECO:0007829|PDB:3IK4"
FT   TURN            55..57
FT                   /evidence="ECO:0007829|PDB:3IK4"
FT   HELIX           61..71
FT                   /evidence="ECO:0007829|PDB:3IK4"
FT   HELIX           72..74
FT                   /evidence="ECO:0007829|PDB:3IK4"
FT   TURN            75..77
FT                   /evidence="ECO:0007829|PDB:3IK4"
FT   HELIX           80..82
FT                   /evidence="ECO:0007829|PDB:3IK4"
FT   HELIX           83..93
FT                   /evidence="ECO:0007829|PDB:3IK4"
FT   HELIX           98..115
FT                   /evidence="ECO:0007829|PDB:3IK4"
FT   HELIX           120..123
FT                   /evidence="ECO:0007829|PDB:3IK4"
FT   STRAND          129..133
FT                   /evidence="ECO:0007829|PDB:3IK4"
FT   STRAND          135..137
FT                   /evidence="ECO:0007829|PDB:3IK4"
FT   HELIX           142..154
FT                   /evidence="ECO:0007829|PDB:3IK4"
FT   STRAND          160..163
FT                   /evidence="ECO:0007829|PDB:3IK4"
FT   HELIX           169..182
FT                   /evidence="ECO:0007829|PDB:3IK4"
FT   STRAND          183..185
FT                   /evidence="ECO:0007829|PDB:3IK4"
FT   STRAND          188..191
FT                   /evidence="ECO:0007829|PDB:3IK4"
FT   HELIX           198..210
FT                   /evidence="ECO:0007829|PDB:3IK4"
FT   STRAND          215..219
FT                   /evidence="ECO:0007829|PDB:3IK4"
FT   HELIX           227..236
FT                   /evidence="ECO:0007829|PDB:3IK4"
FT   STRAND          237..239
FT                   /evidence="ECO:0007829|PDB:3IK4"
FT   STRAND          241..244
FT                   /evidence="ECO:0007829|PDB:3IK4"
FT   HELIX           250..259
FT                   /evidence="ECO:0007829|PDB:3IK4"
FT   STRAND          263..267
FT                   /evidence="ECO:0007829|PDB:3IK4"
FT   HELIX           269..272
FT                   /evidence="ECO:0007829|PDB:3IK4"
FT   HELIX           274..287
FT                   /evidence="ECO:0007829|PDB:3IK4"
FT   STRAND          290..293
FT                   /evidence="ECO:0007829|PDB:3IK4"
FT   HELIX           300..313
FT                   /evidence="ECO:0007829|PDB:3IK4"
FT   STRAND          316..319
FT                   /evidence="ECO:0007829|PDB:3IK4"
FT   HELIX           323..326
FT                   /evidence="ECO:0007829|PDB:3IK4"
FT   STRAND          331..335
FT                   /evidence="ECO:0007829|PDB:3IK4"
FT   STRAND          337..339
FT                   /evidence="ECO:0007829|PDB:3IK4"
FT   STRAND          342..344
FT                   /evidence="ECO:0007829|PDB:3IK4"
FT   STRAND          353..355
FT                   /evidence="ECO:0007829|PDB:3IK4"
SQ   SEQUENCE   356 AA;  36784 MW;  E9E71AE046B97188 CRC64;
     MPTTIQAISA EAINLPLTEP FAIASGAQAV AANVLVKVQL ADGTLGLGEA APFPAVSGET
     QTGTSAAIER LQSHLLGADV RGWRKLAAML DHAEHEAAAA RCGLEMAMLD ALTRHYHMPL
     HVFFGGVSKQ LETDMTITAG DEVHAAASAK AILARGIKSI KVKTAGVDVA YDLARLRAIH
     QAAPTAPLIV DGNCGYDVER ALAFCAACKA ESIPMVLFEQ PLPREDWAGM AQVTAQSGFA
     VAADESARSA HDVLRIAREG TASVINIKLM KAGVAEGLKM IAIAQAAGLG LMIGGMVESI
     LAMSFSANLA AGNGGFDFID LDTPLFIAEH PFIGGFAQTG GTLQLADVAG HGVNLA