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Database: UniProt
Entry: V7EMY1_9RHOB
LinkDB: V7EMY1_9RHOB
Original site: V7EMY1_9RHOB 
ID   V7EMY1_9RHOB            Unreviewed;       320 AA.
AC   V7EMY1;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=Dipeptide epimerase {ECO:0000256|RuleBase:RU366006};
DE            EC=5.1.1.- {ECO:0000256|RuleBase:RU366006};
GN   ORFNames=Q27BPR15_07070 {ECO:0000313|EMBL:ESW61330.1};
OS   Rhodobacter sp. CACIA14H1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Rhodobacter.
OX   NCBI_TaxID=1408890 {ECO:0000313|EMBL:ESW61330.1, ECO:0000313|Proteomes:UP000018503};
RN   [1] {ECO:0000313|EMBL:ESW61330.1, ECO:0000313|Proteomes:UP000018503}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24435858;
RA   Lima A.R., Siqueira A.S., Dos Santos B.G., da Silva F.D., Inada D.T.,
RA   Lima C.P., Cardoso J.F., Vianez-Junior J.L., Nunes M.R., Goncalves E.C.;
RT   "Draft Genome Sequence of Rhodobacter sp. Strain CACIA 14H1, a
RT   Heterotrophic Bacterium Obtained from a Nonaxenic Culture of a Cyanobium
RT   Species.";
RL   Genome Announc. 2:e01116-13(2014).
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:ESW61330.1}.
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DR   EMBL; AYNO01000036; ESW61330.1; -; Genomic_DNA.
DR   AlphaFoldDB; V7EMY1; -.
DR   STRING; 1408890.Q27BPR15_07070; -.
DR   PATRIC; fig|449393.3.peg.1436; -.
DR   Proteomes; UP000018503; 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; 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.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018503}.
FT   DOMAIN          124..215
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
FT   ACT_SITE        143
FT                   /note="Proton acceptor; specific for (R)-substrate
FT                   epimerization"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-1"
FT   ACT_SITE        239
FT                   /note="Proton acceptor; specific for (S)-substrate
FT                   epimerization"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-1"
FT   BINDING         168
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-3"
FT   BINDING         194
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-3"
FT   BINDING         217
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-3"
SQ   SEQUENCE   320 AA;  34056 MW;  66F2D818469ECB8B CRC64;
     MITATLDSFP LARAFTISRG SKTEARVVTA TVTRGGVTGR GECVPYARYG ETPESVLAQI
     ATLPEGITRA ALQEALPPGA ARNAVDCALW DHAAKASGRR VWHLAGLPDP KPRLTAFTLS
     LDRPEAMREQ AAANAHRPLL KIKLGTHDDM PRLEAVRQGA PKSTLIIDAN EGWTAEVYTD
     LAPHLLRLGV ALVEQPLPAG EDGMLAEIPR PVPVCADESA HDRASLAALR GRYDMVNLKL
     DKTGGLTEAL VMAQDARAAG FSLMVGCMVG TSLAMAPAIL PAQLAAFTDL DGPLLLARDR
     DHPLHYDETG VHPPEAALWG
//
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