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Database: UniProt
Entry: F0C2H4_9XANT
LinkDB: F0C2H4_9XANT
Original site: F0C2H4_9XANT 
ID   F0C2H4_9XANT            Unreviewed;       365 AA.
AC   F0C2H4;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   RecName: Full=Dipeptide epimerase {ECO:0000256|RuleBase:RU366006};
DE            EC=5.1.1.- {ECO:0000256|RuleBase:RU366006};
GN   ORFNames=XGA_1039 {ECO:0000313|EMBL:EGD20290.1};
OS   Xanthomonas hortorum ATCC 19865.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas; Xanthomonas hortorum pv. gardneri.
OX   NCBI_TaxID=925777 {ECO:0000313|EMBL:EGD20290.1, ECO:0000313|Proteomes:UP000005023};
RN   [1] {ECO:0000313|EMBL:EGD20290.1, ECO:0000313|Proteomes:UP000005023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19865 {ECO:0000313|EMBL:EGD20290.1,
RC   ECO:0000313|Proteomes:UP000005023};
RX   PubMed=21396108; DOI=10.1186/1471-2164-12-146;
RA   Potnis N., Krasileva K., Chow V., Almeida N.F., Patil P.B., Ryan R.P.,
RA   Sharlach M., Behlau F., Dow J.M., Momol M.T., White F.F., Preston J.F.,
RA   Vinatzer B.A., Koebnik R., Setubal J.C., Norman D.J., Staskawicz B.J.,
RA   Jones J.B.;
RT   "Comparative genomics reveals diversity among xanthomonads infecting tomato
RT   and pepper.";
RL   BMC Genomics 12:146-146(2011).
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:EGD20290.1}.
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DR   EMBL; AEQX01000098; EGD20290.1; -; Genomic_DNA.
DR   RefSeq; WP_006449383.1; NZ_AEQX01000098.1.
DR   AlphaFoldDB; F0C2H4; -.
DR   PATRIC; fig|925777.8.peg.4696; -.
DR   Proteomes; UP000005023; 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|PIRSR:PIRSR634603-3,
KW   ECO:0000256|RuleBase:RU366006}.
FT   DOMAIN          141..239
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        267
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         190
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-3"
FT   BINDING         218
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-3"
FT   BINDING         243
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-3"
FT   BINDING         295
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-2"
FT   BINDING         297
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;  38609 MW;  4189C1F0F6AA45AD CRC64;
     MKITGFRLGM LRVPLKTPFK TAVRTVQAIE DVVVLLQTDS GHIGYGAAPA TAPITGDTHG
     SIIAAIQQCI APKLIGQDVA DLNRLCTLVQ HALERNTNAK AAVEIALYDL WAQALSTPLY
     QALGGGTPHI TTDITISVDA IDTMVADALS ALARGYGSLK IKVGKDSDSD VERVKAIHAA
     VAGRASLRLD ANQGWTPKQA VRTMRTLEDA DIVMELVEQP VKAADIDGLA FVTARIDTPV
     MADESVFSPI QAIELIQRRA ADIVNIKLMK TGGLSNAIRI ADIAALYGVP CMIGCMIESS
     ISVAAAVHLA VTKADSITLA DLDAPALGQF DPTEGGVHFD EAQLHIDDSP GLGIRRIRGL
     ELLSD
//
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