ID A0A2U3AH64_9BACL Unreviewed; 365 AA.
AC A0A2U3AH64;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, 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=DEX24_15340 {ECO:0000313|EMBL:PWI23902.1};
OS Kurthia sibirica.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Kurthia.
OX NCBI_TaxID=202750 {ECO:0000313|EMBL:PWI23902.1, ECO:0000313|Proteomes:UP000245938};
RN [1] {ECO:0000313|EMBL:PWI23902.1, ECO:0000313|Proteomes:UP000245938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49154 {ECO:0000313|EMBL:PWI23902.1,
RC ECO:0000313|Proteomes:UP000245938};
RA Maclea K.S., Goen A.E.;
RT "Kurthia sibirica genome sequence.";
RL Submitted (MAY-2018) 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:PWI23902.1}.
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DR EMBL; QFVR01000029; PWI23902.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U3AH64; -.
DR OrthoDB; 9775391at2; -.
DR Proteomes; UP000245938; 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; SFLDF00010; dipeptide_epimerase; 1.
DR SFLD; SFLDS00001; Enolase; 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|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634603-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000245938}.
FT DOMAIN 141..240
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 268
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 191
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR634603-3"
FT BINDING 219
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR634603-3"
FT BINDING 244
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR634603-3"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634603-2"
FT BINDING 298
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; 40097 MW; 17351C8D999DE78C CRC64;
MKITAIYTEK VAVPLKKPFK TALRTVNIAE SIYITIELEN GRRGFGEAPP TLVITGDSLA
SIDFAIHGVF KPLLVGRHLE EFEDIFVQLH KAIVRNTSAK AAVDMAIYDL LAQQANLPLF
QYLGGAKSEL KTDYTVSVNA ASEMAADAQQ YVQDGFDLLK IKVGIGTIEE DIARIVAIRQ
AIGHQATIRL DANQGWSAKD AVYAIRRMED LELKIELVEQ PVLAHDLEGL KYVTDNTLTP
IMADESVFSA HDAQRVIEMR AADLINIKLM KAGGIHEALK INALAKTHNM KCMTGSMIET
KIGITAAAHF AASQSNIHYY DFDAALMMKE ETTVGGIQYD GSRIRFAKES GLGILAIGRK
IHENI
//
