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Database: UniProt
Entry: A0A0D5YWW1_9FLAO
LinkDB: A0A0D5YWW1_9FLAO
Original site: A0A0D5YWW1_9FLAO 
ID   A0A0D5YWW1_9FLAO        Unreviewed;       345 AA.
AC   A0A0D5YWW1;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Dipeptide epimerase {ECO:0000256|RuleBase:RU366006};
DE            EC=5.1.1.- {ECO:0000256|RuleBase:RU366006};
GN   ORFNames=VC82_2855 {ECO:0000313|EMBL:AKA36401.1};
OS   Allomuricauda lutaonensis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Allomuricauda.
OX   NCBI_TaxID=516051 {ECO:0000313|EMBL:AKA36401.1, ECO:0000313|Proteomes:UP000032726};
RN   [1] {ECO:0000313|EMBL:AKA36401.1, ECO:0000313|Proteomes:UP000032726}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC-HSB-11 {ECO:0000313|EMBL:AKA36401.1,
RC   ECO:0000313|Proteomes:UP000032726};
RA   Kim K.M.;
RT   "Complete genome sequence of Muricauda lutaonensis CC-HSB-11T, isolated
RT   from a coastal hot spring.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR634603-3,
CC         ECO:0000256|RuleBase:RU366006};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR634603-3,
CC       ECO:0000256|RuleBase:RU366006};
CC   -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC       enzyme family. {ECO:0000256|ARBA:ARBA00008031,
CC       ECO:0000256|RuleBase:RU366006}.
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DR   EMBL; CP011071; AKA36401.1; -; Genomic_DNA.
DR   RefSeq; WP_045802934.1; NZ_CP011071.1.
DR   AlphaFoldDB; A0A0D5YWW1; -.
DR   STRING; 516051.VC82_2855; -.
DR   KEGG; mlt:VC82_2855; -.
DR   PATRIC; fig|516051.4.peg.2924; -.
DR   HOGENOM; CLU_030273_4_3_10; -.
DR   OrthoDB; 9775391at2; -.
DR   Proteomes; UP000032726; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR   GO; GO:0016855; F:racemase and epimerase activity, acting on amino acids and derivatives; IEA:UniProtKB-UniRule.
DR   GO; GO:0009063; P:amino acid catabolic process; IEA:InterPro.
DR   CDD; cd03319; L-Ala-DL-Glu_epimerase; 1.
DR   Gene3D; 3.20.20.120; Enolase-like C-terminal domain; 1.
DR   Gene3D; 3.30.390.10; Enolase-like, N-terminal domain; 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; IPR013341; Mandelate_racemase_N_dom.
DR   PANTHER; PTHR48073:SF2; O-SUCCINYLBENZOATE SYNTHASE; 1.
DR   PANTHER; PTHR48073; O-SUCCINYLBENZOATE SYNTHASE-RELATED; 1.
DR   Pfam; PF13378; MR_MLE_C; 1.
DR   Pfam; PF02746; MR_MLE_N; 1.
DR   SFLD; SFLDS00001; Enolase; 1.
DR   SFLD; SFLDG00180; muconate_cycloisomerase; 1.
DR   SMART; SM00922; MR_MLE; 1.
DR   SUPFAM; SSF51604; Enolase C-terminal domain-like; 1.
DR   SUPFAM; SSF54826; Enolase N-terminal domain-like; 1.
DR   PROSITE; PS00908; MR_MLE_1; 1.
DR   PROSITE; PS00909; MR_MLE_2; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU366006};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR634603-3, ECO:0000256|RuleBase:RU366006};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR634603-3,
KW   ECO:0000256|RuleBase:RU366006};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032726}.
FT   DOMAIN          133..233
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
FT   ACT_SITE        155
FT                   /note="Proton acceptor; specific for (R)-substrate
FT                   epimerization"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-1"
FT   ACT_SITE        259
FT                   /note="Proton acceptor; specific for (S)-substrate
FT                   epimerization"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-1"
FT   BINDING         186
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-3"
FT   BINDING         212
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-3"
FT   BINDING         237
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-3"
SQ   SEQUENCE   345 AA;  37755 MW;  27E2393BEF2E6D19 CRC64;
     MQVDYKIRYL KKLFPLRISR GVRDGQHNLF VSVRDGGHTG WGETSPGASE GAETAEEAQS
     QLEAFLKDGT NLQSVFETYD AALEAKVAPC ALAALDMALW DLLAKKADMP LYRLLGFPKP
     SKPTSITLGI MSPEEARGRL PLILENMHIK TLKVKLGSND GIEADKALYE EVLAYHKKYP
     ISIRVDANGG WNLEEAHHMM KWLAERHCEY VEQPLKEGLE NELPFLHKNR PLPIFVDESC
     RFATDIPKWA HSVDGVNMKL MKCGGITGAL RIIATANAFG LKTMIGCMGE TSISIAAGAA
     VSGMLDHIDL DSHLNLNPDP CIGAPLVNGI TMPQEVPGHG GGFKK
//
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