ID A0A2I7N7V6_9NEIS Unreviewed; 366 AA.
AC A0A2I7N7V6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Dipeptide epimerase {ECO:0000256|RuleBase:RU366006};
DE EC=5.1.1.- {ECO:0000256|RuleBase:RU366006};
GN ORFNames=CUN60_09610 {ECO:0000313|EMBL:AUR52543.1};
OS Aquella oligotrophica.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Aquella.
OX NCBI_TaxID=2067065 {ECO:0000313|EMBL:AUR52543.1, ECO:0000313|Proteomes:UP000236655};
RN [1] {ECO:0000313|Proteomes:UP000236655}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100970 {ECO:0000313|Proteomes:UP000236655};
RA Chan K.G., Lee L.S.;
RL Submitted (NOV-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; CP024847; AUR52543.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I7N7V6; -.
DR KEGG; nba:CUN60_09610; -.
DR OrthoDB; 5596677at2; -.
DR Proteomes; UP000236655; Chromosome.
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; SFLDS00001; Enolase; 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|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:UP000236655}.
FT DOMAIN 140..238
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
FT ACT_SITE 161
FT /note="Proton acceptor; specific for (R)-substrate
FT epimerization"
FT /evidence="ECO:0000256|PIRSR:PIRSR634603-1"
FT ACT_SITE 266
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 134
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634603-2"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634603-2"
FT BINDING 189
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"
FT BINDING 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR634603-3"
FT BINDING 294
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634603-2"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634603-2"
FT BINDING 319
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634603-2"
FT BINDING 321
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634603-2"
SQ SEQUENCE 366 AA; 39360 MW; 894211C2574B714D CRC64;
MQITEISIAK LQIPLIRPFI TALRRTEHVE DIVVILKTDT GHIAYGSAAS TPVITGDSQE
SIIGGLQLLA NKFLGASLDN YENILREINI SLVNNNSAKA AFDIAIHDLV AKGMGIPLYK
FLGGGKPEVK ILTTISVKDV SEMVADARLF ISQGFETLKI KVGLNPDEDI IRIKSIRDAV
GDSINIVTDA NQGWDAKSAL NIIEQLVSGK VNIAMVEQPV KAWDYANLKY VRDNSKLPIY
ADESVFGIRD ALKIISENIA DGINIKLMKS AGIYAARGIY DLATSHNIPC MAGCMLESPI
GLAAMASFIV SRANIHFVDL DPITMIKTNP VIGGVILNGA TLSLSESPGL GIEHIDGLQT
VATRAL
//
