ID E6BG04_ECOLX Unreviewed; 454 AA.
AC E6BG04;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=glucarate dehydratase {ECO:0000256|ARBA:ARBA00011973};
DE EC=4.2.1.40 {ECO:0000256|ARBA:ARBA00011973};
GN Name=gudD {ECO:0000313|EMBL:EFU36614.1};
GN ORFNames=HMPREF9350_01264 {ECO:0000313|EMBL:EFU36614.1};
OS Escherichia coli MS 85-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=679202 {ECO:0000313|EMBL:EFU36614.1, ECO:0000313|Proteomes:UP000005056};
RN [1] {ECO:0000313|EMBL:EFU36614.1, ECO:0000313|Proteomes:UP000005056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS 85-1 {ECO:0000313|EMBL:EFU36614.1,
RC ECO:0000313|Proteomes:UP000005056};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucarate = 5-dehydro-4-deoxy-D-glucarate + H2O;
CC Xref=Rhea:RHEA:14573, ChEBI:CHEBI:15377, ChEBI:CHEBI:30612,
CC ChEBI:CHEBI:42819; EC=4.2.1.40;
CC Evidence={ECO:0000256|ARBA:ARBA00001426};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRSR:PIRSR617653-3};
CC -!- PATHWAY: Carbohydrate acid metabolism; D-glucarate degradation; 2,5-
CC dioxopentanoate from D-glucarate: step 1/2.
CC {ECO:0000256|ARBA:ARBA00005183}.
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:EFU36614.1}.
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DR EMBL; ADWQ01000004; EFU36614.1; -; Genomic_DNA.
DR AlphaFoldDB; E6BG04; -.
DR PATRIC; fig|679202.3.peg.1176; -.
DR UniPathway; UPA00564; UER00627.
DR Proteomes; UP000005056; Unassembled WGS sequence.
DR GO; GO:0008872; F:glucarate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0042838; P:D-glucarate catabolic process; IEA:UniProtKB-UniPathway.
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; IPR017653; Glucarate_dehydratase.
DR InterPro; IPR034598; GlucD-like.
DR InterPro; IPR013342; Mandelate_racemase_C.
DR NCBIfam; TIGR03247; glucar-dehydr; 1.
DR PANTHER; PTHR48080; D-GALACTONATE DEHYDRATASE-RELATED; 1.
DR PANTHER; PTHR48080:SF4; GLUCARATE DEHYDRATASE; 1.
DR Pfam; PF13378; MR_MLE_C; 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.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:EFU36614.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR617653-3};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR617653-3}.
FT DOMAIN 193..293
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
FT ACT_SITE 215
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617653-1"
FT ACT_SITE 347
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617653-1"
FT BINDING 40
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
FT BINDING 243..245
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
FT BINDING 243
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR617653-3"
FT BINDING 274
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR617653-3"
FT BINDING 297
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR617653-3"
FT BINDING 297
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
FT BINDING 347..349
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
FT BINDING 376
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
FT BINDING 430
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
SQ SEQUENCE 454 AA; 50097 MW; 21C79C10C2AC5429 CRC64;
MILKKDINMS SQFTTPVVTE MQVIPVAGHD SMLMNLSGAH APFFTRNIVI IKDNSGHTGV
GEIPGGEKIR KTLEDAIPLV VGKTLGEYKN VLTLVRNTFA DRDAGGRGLQ TFDLRTTIHV
VTGIEAAMLD LLGQHLGVNV ASLLGDGQQR SEVEMLGYLF FVGNRKATPL PYQSQPDDSC
DWYRLRHEEA MTPDAVVRLA EAAYEKYGFN DFKLKGGVLA GEEEAESIVA LAKRFPQARI
TLDPNGAWSL NEAIKIGKYL KGSLAYAEDP CGAEQGFSGR EVMAEFRRAT GLPTATNMIA
TDWRQMGHTL SLQSVDIPLA DPHFWTMQGS VRVAQMCHEF GLTWGSHSNN HFDISLAMFT
HVAAAAPGKI TAIDTHWIWQ EGNQRLTKEP FEIKGGLVQV PEKPGLGVEI DMDQVMKAHE
LYQKHGLGAR DDAMGMQYLI PGWTFDNKRP CMVR
//
