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Database: UniProt
Entry: A0A0M2KDU5_9GAMM
LinkDB: A0A0M2KDU5_9GAMM
Original site: A0A0M2KDU5_9GAMM 
ID   A0A0M2KDU5_9GAMM        Unreviewed;       445 AA.
AC   A0A0M2KDU5;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Glucarate dehydratase {ECO:0000313|EMBL:KKF35383.1};
GN   ORFNames=SY86_08055 {ECO:0000313|EMBL:KKF35383.1};
OS   Erwinia tracheiphila.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=65700 {ECO:0000313|EMBL:KKF35383.1, ECO:0000313|Proteomes:UP000033924};
RN   [1] {ECO:0000313|EMBL:KKF35383.1, ECO:0000313|Proteomes:UP000033924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BuffGH {ECO:0000313|EMBL:KKF35383.1,
RC   ECO:0000313|Proteomes:UP000033924};
RA   Shapiro L.R.;
RT   "Erwinia tracheiphila.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR634598-3};
CC   -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC       enzyme family. GlucD subfamily. {ECO:0000256|ARBA:ARBA00009938}.
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:KKF35383.1}.
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DR   EMBL; JXNU01000003; KKF35383.1; -; Genomic_DNA.
DR   RefSeq; WP_040465316.1; NZ_JXNU01000003.1.
DR   AlphaFoldDB; A0A0M2KDU5; -.
DR   STRING; 65700.SY86_08055; -.
DR   PATRIC; fig|65700.7.peg.2042; -.
DR   Proteomes; UP000033924; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009063; P:amino acid catabolic process; IEA:InterPro.
DR   CDD; cd03323; D-glucarate_dehydratase; 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; IPR034593; DgoD-like.
DR   InterPro; IPR036849; Enolase-like_C_sf.
DR   InterPro; IPR029017; Enolase-like_N.
DR   InterPro; IPR029065; Enolase_C-like.
DR   InterPro; IPR034598; GlucD-like.
DR   InterPro; IPR018110; Mandel_Rmase/mucon_lact_enz_CS.
DR   InterPro; IPR013342; Mandelate_racemase_C.
DR   InterPro; IPR013341; Mandelate_racemase_N_dom.
DR   PANTHER; PTHR48080; D-GALACTONATE DEHYDRATASE-RELATED; 1.
DR   PANTHER; PTHR48080:SF1; GLUCARATE DEHYDRATASE-RELATED PROTEIN; 1.
DR   Pfam; PF13378; MR_MLE_C; 1.
DR   Pfam; PF02746; MR_MLE_N; 1.
DR   SFLD; SFLDF00005; glucarate_dehydratase; 1.
DR   SFLD; SFLDG00055; glucarate_dehydratase; 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.
DR   PROSITE; PS00908; MR_MLE_1; 1.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|PIRSR:PIRSR634598-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR634598-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033924}.
FT   DOMAIN          184..284
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
FT   ACT_SITE        206
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634598-1"
FT   ACT_SITE        338
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634598-1"
FT   BINDING         31
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT   BINDING         104
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT   BINDING         149
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT   BINDING         204
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT   BINDING         234..236
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT   BINDING         234
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634598-3"
FT   BINDING         265
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634598-3"
FT   BINDING         288
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634598-3"
FT   BINDING         288
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT   BINDING         338..340
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT   BINDING         367
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT   BINDING         421
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
SQ   SEQUENCE   445 AA;  48719 MW;  526B737434B5BE4C CRC64;
     MSTQSTPVIT DMKVIPVAGY DSMLLNIGGA HSAYFTRNIV VLTDSAGHTG VGEAPGGETI
     FQTLLAAVPQ VIGNEIARMN SLVQQVHKGN QSADFDTFGK GAWTFELRVN AVAGLEAALL
     DLLGQYLQVP VAELLGPGKQ RDAVAVLGYL FYIGDRRKTD LPYLAGEQAD HAWYHLRHQP
     AMDSAAMLLL AEAAQDKYGF KDFKLKGGVL PGEQEIETLK TLKKRFTDAR ITVDPNGAWG
     LDEAISLCKD LRGILAYAED PCGAEQGYSG REVMAEFRRA TSLPVATNMI ATNWREMNHA
     VMLNAVDIPL ADPHFWTLSG AVRVAQLCDD WGLTWGCHSN NHFDISLAMF THVGAAAPGQ
     PTAIDTHWIW QEGNQRLTRE PLQIRGGKIA VPDAPGLGVE LDWERLEQAH ALYKTLPCGA
     RNDALAMQYL IPGWTFDRKR PVFGR
//
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