ID A0A212RDT4_9PROT Unreviewed; 328 AA.
AC A0A212RDT4;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Dipeptide epimerase {ECO:0000256|RuleBase:RU366006};
DE EC=5.1.1.- {ECO:0000256|RuleBase:RU366006};
GN ORFNames=SAMN07250955_107190 {ECO:0000313|EMBL:SNB70407.1};
OS Arboricoccus pini.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Geminicoccales;
OC Geminicoccaceae; Arboricoccus.
OX NCBI_TaxID=1963835 {ECO:0000313|EMBL:SNB70407.1, ECO:0000313|Proteomes:UP000197065};
RN [1] {ECO:0000313|EMBL:SNB70407.1, ECO:0000313|Proteomes:UP000197065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B29T1 {ECO:0000313|EMBL:SNB70407.1,
RC ECO:0000313|Proteomes:UP000197065};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-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; FYEH01000007; SNB70407.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A212RDT4; -.
DR OrthoDB; 9782675at2; -.
DR Proteomes; UP000197065; 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 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:UP000197065}.
FT DOMAIN 132..223
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
FT BINDING 176
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR634603-3"
FT BINDING 202
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR634603-3"
FT BINDING 225
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR634603-3"
SQ SEQUENCE 328 AA; 34875 MW; B4B6BF4608DE79C6 CRC64;
MAGRRLTVRH ERFPLKEPAP FARSARTHAE TVTVVIEADG QVGRGESVPC RRRGETIESV
MALIRGQKGT IEDGASRLEL DVALPFGAAR NALDCALWDL EAKLAGLPVW ELAGLNRPGP
VVTSHTIAPG PPAIMAAAAA AAADRAILRL RLCGDGDLER LAAVREAAPR CRLVVDAEES
WTQGRLEPYL AAMAAANVEL VEQPLPVGQD AVLADILHPV PIAADESVQT SEDLEGLTRR
YDVATVTLDK VGGLTEALRF AMKARDVGLG LAVAGGCGSS LGAAPAMLVA QRARFVDLDG
LRQLAQDRSV PLRFEHSTLY PAARELWG
//
