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Database: UniProt
Entry: H0G768_RHIML
LinkDB: H0G768_RHIML
Original site: H0G768_RHIML 
ID   H0G768_RHIML            Unreviewed;       327 AA.
AC   H0G768;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   RecName: Full=Dipeptide epimerase {ECO:0000256|RuleBase:RU366006};
DE            EC=5.1.1.- {ECO:0000256|RuleBase:RU366006};
GN   ORFNames=SM0020_26741 {ECO:0000313|EMBL:EHK74847.1};
OS   Sinorhizobium meliloti CCNWSX0020.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=1107881 {ECO:0000313|EMBL:EHK74847.1, ECO:0000313|Proteomes:UP000004038};
RN   [1] {ECO:0000313|EMBL:EHK74847.1, ECO:0000313|Proteomes:UP000004038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCNWSX0020 {ECO:0000313|EMBL:EHK74847.1,
RC   ECO:0000313|Proteomes:UP000004038};
RX   PubMed=22328762; DOI=10.1128/JB.06682-11;
RA   Li Z., Ma Z., Hao X., Wei G.;
RT   "Draft Genome Sequence of Sinorhizobium meliloti CCNWSX0020, a Nitrogen-
RT   Fixing Symbiont with Copper Tolerance Capability Isolated from Lead-Zinc
RT   Mine Tailings.";
RL   J. Bacteriol. 194:1267-1268(2012).
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; AGVV01000075; EHK74847.1; -; Genomic_DNA.
DR   RefSeq; WP_003534117.1; NZ_AGVV01000075.1.
DR   AlphaFoldDB; H0G768; -.
DR   PATRIC; fig|1107881.3.peg.5418; -.
DR   Proteomes; UP000004038; 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; IPR034593; DgoD-like.
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; PTHR48080; D-GALACTONATE DEHYDRATASE-RELATED; 1.
DR   PANTHER; PTHR48080:SF3; ENOLASE SUPERFAMILY MEMBER DDB_G0284701; 1.
DR   Pfam; PF13378; MR_MLE_C; 1.
DR   Pfam; PF02746; MR_MLE_N; 1.
DR   SFLD; SFLDF00010; dipeptide_epimerase; 1.
DR   SFLD; SFLDS00001; Enolase; 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|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}.
FT   DOMAIN          131..222
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
FT   ACT_SITE        150
FT                   /note="Proton acceptor; specific for (R)-substrate
FT                   epimerization"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-1"
FT   ACT_SITE        246
FT                   /note="Proton acceptor; specific for (S)-substrate
FT                   epimerization"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-1"
FT   BINDING         175
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-3"
FT   BINDING         201
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-3"
FT   BINDING         224
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-3"
SQ   SEQUENCE   327 AA;  34376 MW;  7747856B5660FB9B CRC64;
     MPITLTATVE HFPIAGAFTI SRGSKTTASV VTCRITDGEL SGWGECVPYA RYGESVESVL
     SAIETVRPLI EEDMTRTDLQ TAMKAGAARN AVDCALWDLE AKRSGSSAAA LAGIAGPTPL
     TTAYTLSLAE PEEMRAQAAK HAHRALLKVK VGTSDDTARI RAVRSGAPAS RIILDANEGW
     TEANIAAHFA ACAENGISLI EQPLPAGRDE ILASLPRPVP VCADESVHAT EDLERLVGRY
     DAVNIKLDKT GGLTEALRMR AAAEALGLKI MVGCMVGSSL AMAPAVLVAQ GADFVDLDGP
     LLLSKDRSPG LRYEASLVFP PEASLWG
//
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