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Database: UniProt
Entry: A0A1T5KT16_9GAMM
LinkDB: A0A1T5KT16_9GAMM
Original site: A0A1T5KT16_9GAMM 
ID   A0A1T5KT16_9GAMM        Unreviewed;       365 AA.
AC   A0A1T5KT16;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Dipeptide epimerase {ECO:0000256|RuleBase:RU366006};
DE            EC=5.1.1.- {ECO:0000256|RuleBase:RU366006};
GN   ORFNames=SAMN06296058_2001 {ECO:0000313|EMBL:SKC66924.1};
OS   Pseudoxanthomonas indica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Pseudoxanthomonas.
OX   NCBI_TaxID=428993 {ECO:0000313|EMBL:SKC66924.1, ECO:0000313|Proteomes:UP000190341};
RN   [1] {ECO:0000313|EMBL:SKC66924.1, ECO:0000313|Proteomes:UP000190341}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P15 {ECO:0000313|EMBL:SKC66924.1,
RC   ECO:0000313|Proteomes:UP000190341};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) 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; FUZV01000001; SKC66924.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T5KT16; -.
DR   STRING; 428993.SAMN06296058_2001; -.
DR   OrthoDB; 9796450at2; -.
DR   Proteomes; UP000190341; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016855; F:racemase and epimerase activity, acting on amino acids and derivatives; IEA:UniProtKB-UniRule.
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; 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; SFLDG00180; muconate_cycloisomerase; 1.
DR   SFLD; SFLDF00009; o-succinylbenzoate_synthase; 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.
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:UP000190341}.
FT   DOMAIN          141..239
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
FT   ACT_SITE        162
FT                   /note="Proton acceptor; specific for (R)-substrate
FT                   epimerization"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-1"
FT   ACT_SITE        267
FT                   /note="Proton acceptor; specific for (S)-substrate
FT                   epimerization"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-1"
FT   BINDING         24
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-2"
FT   BINDING         135
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-2"
FT   BINDING         160
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-2"
FT   BINDING         190
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-3"
FT   BINDING         218
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-3"
FT   BINDING         243
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-3"
FT   BINDING         295
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-2"
FT   BINDING         297
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-2"
FT   BINDING         321
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-2"
FT   BINDING         323
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-2"
SQ   SEQUENCE   365 AA;  39126 MW;  CB68CC4DA8925340 CRC64;
     MKITDIQFGM LRVPLKTPFK TALRTVDTVE DIVVLVHTDT GQVGYGEAPA TAVITGDTHG
     SIIEAIARFI KPRLIGQEIA NLNQITHLIQ TALERNTSAK AAVEIAIYDL WGQLYNAPLY
     KMLGGGDPVI TTDITISVDY IDKMVADSIA AVDRGFESLK IKVGKDIGLD IERVKAIYSA
     VEGRALLRLD ANQGWTAKQA VFAMHNLEDA GVVLELLEQP VKAADIDGLK YVTDRVHTPV
     MADESVFGPT EVIDLIKMRA ADIINIKLMK TGGLSNAIRI ADIASLYGVE CMIGCMLESS
     ISVAAACHVA VAKSQAITKI DLDGPSLSQF NPVEGGVIFN ESEISITDAP GLGIQSIQGL
     ELISV
//
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