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Entry: A0A0A1HTQ3_9PSED
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ID   A0A0A1HTQ3_9PSED        Unreviewed;       389 AA.
AC   A0A0A1HTQ3;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=Mandelate racemase/muconate lactonizing enzyme family protein {ECO:0000313|EMBL:CDF93630.1};
GN   ORFNames=BN844_0210 {ECO:0000313|EMBL:CDF93630.1};
OS   Pseudomonas sp. SHC52.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=984195 {ECO:0000313|EMBL:CDF93630.1, ECO:0000313|Proteomes:UP000031550};
RN   [1] {ECO:0000313|EMBL:CDF93630.1, ECO:0000313|Proteomes:UP000031550}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SHC52 {ECO:0000313|EMBL:CDF93630.1,
RC   ECO:0000313|Proteomes:UP000031550};
RA   Van der Voort M., Mendes R., Raaijmakers J.M.;
RT   "Genome mining of the rhizosphere bacterium Pseudomonas sp. SH-C52.";
RL   Submitted (MAY-2013) 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:CDF93630.1}.
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DR   EMBL; CBLV010000130; CDF93630.1; -; Genomic_DNA.
DR   RefSeq; WP_041021420.1; NZ_CBLV010000130.1.
DR   AlphaFoldDB; A0A0A1HTQ3; -.
DR   OrthoDB; 9802699at2; -.
DR   Proteomes; UP000031550; 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   PANTHER; PTHR48080:SF5; D(-)-TARTRATE DEHYDRATASE; 1.
DR   PANTHER; PTHR48080; D-GALACTONATE DEHYDRATASE-RELATED; 1.
DR   Pfam; PF13378; MR_MLE_C; 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}.
FT   DOMAIN          162..259
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
FT   ACT_SITE        183
FT                   /note="acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634611-1"
FT   ACT_SITE        321
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         155
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634611-2"
FT   BINDING         181
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634611-2"
FT   BINDING         212
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634611-3"
FT   BINDING         238
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634611-3"
FT   BINDING         238
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634611-2"
FT   BINDING         264
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634611-3"
FT   BINDING         264
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634611-2"
FT   BINDING         321
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            181
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634611-4"
FT   SITE            291
FT                   /note="Increases basicity of active site His"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634611-4"
FT   SITE            340
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634611-4"
SQ   SEQUENCE   389 AA;  43128 MW;  A38343C31150B976 CRC64;
     MRIVDIREQT VSIASPIANA YIDFSKMTCS VVAVITDVIR DGKPVIGYGF NSNGRYGQGA
     LMRDRFLARV TEADPDSLVD HENNNLDPFA IWKTLMTNEK PGGHGERSVA VGTLDMAVWD
     AVAKIEGKPL YRLLADRYRG GVADDKVWVY AAGGYYYPGK DQTKLKAEMQ SYLDRGYDVV
     KMKIGAVPLD EDIRRIEAVL EVVGDGRRLA VDANGRFDLQ TGIAYAEAIK KYNLFWYEEV
     GDPLDYALQA ELANHYELPM ATGENLFSHQ DARNLLRHGG MRPDRDYLQF DCALSYGLVE
     YMRTLKVMEE MGWSSRRVVP HGGHQMSLNI AAGLHLGGNE SYPDVFQPFG GFADGIRVEN
     GYVGLPDIPG VGFEAKSALY AVMRALGEG
//
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