ID A0A0A2TZA9_9BACI Unreviewed; 361 AA.
AC A0A0A2TZA9;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Dipeptide epimerase {ECO:0000256|RuleBase:RU366006};
DE EC=5.1.1.- {ECO:0000256|RuleBase:RU366006};
GN ORFNames=N782_00795 {ECO:0000313|EMBL:KGP74610.1};
OS Pontibacillus yanchengensis Y32.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pontibacillus.
OX NCBI_TaxID=1385514 {ECO:0000313|EMBL:KGP74610.1, ECO:0000313|Proteomes:UP000030147};
RN [1] {ECO:0000313|EMBL:KGP74610.1, ECO:0000313|Proteomes:UP000030147}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y32 {ECO:0000313|EMBL:KGP74610.1,
RC ECO:0000313|Proteomes:UP000030147};
RX PubMed=26561516; DOI=10.1186/s40793-015-0085-y;
RA Huang J., Qiao Z.X., Tang J.W., Wang G.;
RT "High quality draft genome sequence of the moderately halophilic bacterium
RT Pontibacillus yanchengensis Y32(T) and comparison among Pontibacillus
RT genomes.";
RL Stand. Genomic Sci. 10:93-93(2015).
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:KGP74610.1}.
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DR EMBL; AVBF01000001; KGP74610.1; -; Genomic_DNA.
DR RefSeq; WP_036815236.1; NZ_AVBF01000001.1.
DR AlphaFoldDB; A0A0A2TZA9; -.
DR STRING; 1385514.N782_00795; -.
DR eggNOG; COG4948; Bacteria.
DR OrthoDB; 9775391at2; -.
DR Proteomes; UP000030147; 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; SFLDG00180; muconate_cycloisomerase; 2.
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:UP000030147}.
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 361 AA; 39480 MW; BEB8496A733FAC9B CRC64;
MKIESIETYP VAIPLNKPFK TALRTVTVAE SIYVKVTCDD GTVGWGEAPP THVITGESLF
SIKETIEHIL KPAILGMTLL ERENVFHTLH KATVGNTSAK AAIDIALHDC FAQKCGLPLF
QLLGGSSSSL ETDYTVSVNS PEEMAEDAAE YIQNGFNVLK IKVGKNDIET DIARIQAIRN
EIGSEATIRL DANQGWTAKE AIYAIRRMEE LFLNVELVEQ PVKAHDIEGL KQVTDNTNTL
IMADESIFSP DDARRVLTTR SADLLNIKLM KAGGIHRAMQ INKLAESFGV ACMVGSMIET
KLGVTAAAHF AASQRNITRV DFDAPLMLSK DLIDGGINYD GRHISFSEGA GLGIEHVYYE
N
//
