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Database: UniProt
Entry: A0A2T0WHD3_9RHOB
LinkDB: A0A2T0WHD3_9RHOB
Original site: A0A2T0WHD3_9RHOB 
ID   A0A2T0WHD3_9RHOB        Unreviewed;       387 AA.
AC   A0A2T0WHD3;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=L-alanine-DL-glutamate epimerase-like enolase superfamily enzyme {ECO:0000313|EMBL:PRY86096.1};
GN   ORFNames=CLV74_11371 {ECO:0000313|EMBL:PRY86096.1};
OS   Donghicola tyrosinivorans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Donghicola.
OX   NCBI_TaxID=1652492 {ECO:0000313|EMBL:PRY86096.1, ECO:0000313|Proteomes:UP000238392};
RN   [1] {ECO:0000313|EMBL:PRY86096.1, ECO:0000313|Proteomes:UP000238392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 100212 {ECO:0000313|EMBL:PRY86096.1,
RC   ECO:0000313|Proteomes:UP000238392};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR634611-3};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR634611-3};
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:PRY86096.1}.
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DR   EMBL; PVTQ01000013; PRY86096.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T0WHD3; -.
DR   OrthoDB; 9802699at2; -.
DR   Proteomes; UP000238392; Unassembled WGS sequence.
DR   GO; GO:0047808; F:D(-)-tartrate dehydratase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd03326; MR_like_1; 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; IPR034611; D-tartrate_dehydratase.
DR   InterPro; IPR034593; DgoD-like.
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:SF5; D(-)-TARTRATE DEHYDRATASE; 1.
DR   PANTHER; PTHR48080; D-GALACTONATE DEHYDRATASE-RELATED; 1.
DR   Pfam; PF13378; MR_MLE_C; 1.
DR   Pfam; PF02746; MR_MLE_N; 1.
DR   SFLD; SFLDF00118; D-tartrate_dehydratase; 1.
DR   SFLD; SFLDG00179; mandelate_racemase; 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   4: Predicted;
KW   Magnesium {ECO:0000256|PIRSR:PIRSR634611-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR634611-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000238392}.
FT   DOMAIN          161..258
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
FT   ACT_SITE        182
FT                   /note="acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634611-1"
FT   ACT_SITE        320
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634611-1"
FT   BINDING         19
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634611-2"
FT   BINDING         53
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634611-2"
FT   BINDING         100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634611-2"
FT   BINDING         154
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634611-2"
FT   BINDING         180
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634611-2"
FT   BINDING         211
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634611-3"
FT   BINDING         237
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634611-3"
FT   BINDING         237
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634611-2"
FT   BINDING         263
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634611-3"
FT   BINDING         263
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634611-2"
FT   BINDING         320
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634611-2"
FT   SITE            53
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634611-4"
FT   SITE            180
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634611-4"
FT   SITE            290
FT                   /note="Increases basicity of active site His"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634611-4"
FT   SITE            339
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634611-4"
SQ   SEQUENCE   387 AA;  42848 MW;  1045A956BFAE276A CRC64;
     MRIIDIVEVT KPIASPIRNA YIDFSKMTAS LVAVVTDQVR DGRRVVGYGF NSNGRYGQGG
     LIRERFRDRI LEADPASLLN EDGSNLDAHK IWAAMMQNEK PGGHGERSVA VGTIDMAVWD
     AIAKIAERPL FRMLADMKGL EANPRVFVYA AGGYYYPGKD DGALRAEMRG YLDRGYNVVK
     MKIGGASLAE DQRRIEAVLD EIGSEAQLAV DANGRFDLET AIAYAKMLRQ YPLFWYEEIG
     DPLDYQLQAA MAEFYPAPMA TGENLFSHQD ARNLIRYGGM RPDRDWLQFD CALSYGLVEY
     LRTLDVLDQA GWSPKRCIPH GGHQMSLNIA AGLGLGGNES YPDLFQPYGG FPDGVQVIDG
     HITMPELPGI GFEGKSDLIS VMRDLAE
//
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