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Database: UniProt
Entry: A0A0N0M218_9SPHN
LinkDB: A0A0N0M218_9SPHN
Original site: A0A0N0M218_9SPHN 
ID   A0A0N0M218_9SPHN        Unreviewed;       334 AA.
AC   A0A0N0M218;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Dipeptide epimerase {ECO:0000256|RuleBase:RU366006};
DE            EC=5.1.1.- {ECO:0000256|RuleBase:RU366006};
GN   ORFNames=ADT71_09450 {ECO:0000313|EMBL:KPH65878.1};
OS   Novosphingobium sp. ST904.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1684385 {ECO:0000313|EMBL:KPH65878.1, ECO:0000313|Proteomes:UP000037878};
RN   [1] {ECO:0000313|EMBL:KPH65878.1, ECO:0000313|Proteomes:UP000037878}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ST904 {ECO:0000313|EMBL:KPH65878.1,
RC   ECO:0000313|Proteomes:UP000037878};
RA   Thijs S., Bottos E.M., Van Hamme J.D., Gkorezis P., Rineau F.,
RA   Vangronsveld J.;
RT   "Novosphingobium nitrophenolicus strain ST904 degrades p-nitrophenol and
RT   stimulates plant growth.";
RL   Submitted (JUL-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:KPH65878.1}.
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DR   EMBL; LGJH01000135; KPH65878.1; -; Genomic_DNA.
DR   RefSeq; WP_054436406.1; NZ_SLVC01000016.1.
DR   AlphaFoldDB; A0A0N0M218; -.
DR   STRING; 1684385.ADT71_09450; -.
DR   PATRIC; fig|1684385.3.peg.3770; -.
DR   OrthoDB; 9782675at2; -.
DR   Proteomes; UP000037878; 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; SFLDF00010; dipeptide_epimerase; 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; 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:UP000037878}.
FT   DOMAIN          134..228
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
FT   ACT_SITE        156
FT                   /note="Proton acceptor; specific for (R)-substrate
FT                   epimerization"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-1"
FT   ACT_SITE        252
FT                   /note="Proton acceptor; specific for (S)-substrate
FT                   epimerization"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-1"
FT   BINDING         181
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-3"
FT   BINDING         207
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-3"
FT   BINDING         230
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-3"
SQ   SEQUENCE   334 AA;  34773 MW;  4F52C77DFA5EFAFC CRC64;
     MMRRLSARAD RHRLAQPFAI ARGTREAIDL VTVSIGQDGK IGRGEGAPSA RYGEEAQSVL
     AQVQAIRPAI EAGLDRQGLL SVMAPGAALN AVDCALWDLE AKLSGVAVAD RLGPLPGGIV
     TAITVGIDRP EGMAARARFL AGAKEADGPA PLLKIKLDAD DIIDRVQAVR EAAPLAQLIA
     DANESWDMAL LERVLPALAA ARVELLEQPL PAGADEPLEG FASPVPLSAD ESAHVAAEVE
     WLASRYDYVT IKLDKSGGLT GALALAEAAQ AAGMGLMTGC MLCSSLSVAP AWHLAARSRF
     VDLDGPLWLA ADHPGGSVLE EGLLRAPSGL GWGW
//
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