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Database: UniProt
Entry: A0A0P7AYR5_9FLAO
LinkDB: A0A0P7AYR5_9FLAO
Original site: A0A0P7AYR5_9FLAO 
ID   A0A0P7AYR5_9FLAO        Unreviewed;       345 AA.
AC   A0A0P7AYR5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Dipeptide epimerase {ECO:0000256|RuleBase:RU366006};
DE            EC=5.1.1.- {ECO:0000256|RuleBase:RU366006};
GN   ORFNames=I595_285 {ECO:0000313|EMBL:KPM33382.1};
OS   Croceitalea dokdonensis DOKDO 023.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Croceitalea.
OX   NCBI_TaxID=1300341 {ECO:0000313|EMBL:KPM33382.1, ECO:0000313|Proteomes:UP000050280};
RN   [1] {ECO:0000313|EMBL:KPM33382.1, ECO:0000313|Proteomes:UP000050280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DOKDO 023 {ECO:0000313|EMBL:KPM33382.1,
RC   ECO:0000313|Proteomes:UP000050280};
RA   Kwon S.-K., Lee H.K., Kwak M.-J., Kim J.F.;
RT   "Genome sequence of the marine flavobacterium Croceitalea dokdonensis DOKDO
RT   023 that contains proton- and sodium-pumping rhodopsins.";
RL   Submitted (SEP-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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPM33382.1}.
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DR   EMBL; LDJX01000001; KPM33382.1; -; Genomic_DNA.
DR   RefSeq; WP_054557585.1; NZ_LDJX01000001.1.
DR   AlphaFoldDB; A0A0P7AYR5; -.
DR   STRING; 1300341.I595_285; -.
DR   PATRIC; fig|1300341.3.peg.286; -.
DR   OrthoDB; 9775391at2; -.
DR   Proteomes; UP000050280; Unassembled WGS sequence.
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:UP000050280}.
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;  37773 MW;  252B214C460D11C5 CRC64;
     MEVSFKQVYL KKLFPLRISR GVRDGQTNLF VQVTDGEHAG IGEVSPGTSE GAATPDEAQQ
     QLALFLTNHK DLSSVQNTYD KALAHGVAPC AMAALDMALW DLKAKKAQMP LYHLLGFAKP
     THPTSITLGI MSPEEAKERL PLILKDMNIR TLKVKLGSNE GIEADKAMYQ EVLNYHKKQP
     IAIRIDANGG WSLDEAKHMM QWLSERHCDY VEQPLKEGQE YDLPQLYKNR PLPIFVDESC
     RFATDIPKWA NAVDGVNMKL MKCGGITGAL RIIATAKAFG LQTMIGCMGE SSISIAAGAA
     VSGALDHIDL DSHLNLNPDP CEGAPLINEI TMPLDVPGHG GRFKD
//
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