ID F2LIC3_BURGS Unreviewed; 449 AA.
AC F2LIC3;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=glucarate dehydratase {ECO:0000256|ARBA:ARBA00011973};
DE EC=4.2.1.40 {ECO:0000256|ARBA:ARBA00011973};
GN OrderedLocusNames=bgla_2g00190 {ECO:0000313|EMBL:AEA62502.1};
OS Burkholderia gladioli (strain BSR3).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=999541 {ECO:0000313|EMBL:AEA62502.1, ECO:0000313|Proteomes:UP000008316};
RN [1] {ECO:0000313|EMBL:AEA62502.1, ECO:0000313|Proteomes:UP000008316}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BSR3 {ECO:0000313|EMBL:AEA62502.1,
RC ECO:0000313|Proteomes:UP000008316};
RX PubMed=21478339; DOI=10.1128/JB.00420-11;
RA Seo Y.S., Lim J., Choi B.S., Kim H., Goo E., Lee B., Lim J.S., Choi I.Y.,
RA Moon J.S., Kim J., Hwang I.;
RT "Complete genome sequence of Burkholderia gladioli BSR3.";
RL J. Bacteriol. 193:3149-3149(2011).
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}.
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DR EMBL; CP002600; AEA62502.1; -; Genomic_DNA.
DR RefSeq; WP_013688834.1; NC_015376.1.
DR AlphaFoldDB; F2LIC3; -.
DR STRING; 999541.bgla_2g00190; -.
DR GeneID; 66462358; -.
DR KEGG; bgd:bgla_2g00190; -.
DR eggNOG; COG4948; Bacteria.
DR HOGENOM; CLU_030273_9_0_4; -.
DR UniPathway; UPA00564; UER00627.
DR Proteomes; UP000008316; Chromosome 2.
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};
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 189..289
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
FT ACT_SITE 211
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617653-1"
FT ACT_SITE 343
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617653-1"
FT BINDING 36
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
FT BINDING 209
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
FT BINDING 239..241
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
FT BINDING 239
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR617653-3"
FT BINDING 270
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR617653-3"
FT BINDING 293
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR617653-3"
FT BINDING 293
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
FT BINDING 343..345
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
FT BINDING 372
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
FT BINDING 425
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
SQ SEQUENCE 449 AA; 48913 MW; 394F83E800B5BB28 CRC64;
MSSNSIQANA TPVVTELRVV PVAGRDSMLM NLSGAHGPFF TRNVVILRDS SGHTGVGEVP
GGEAIRKTID DARGIVVGQS IGNLQAMLNR VRSTFADRDA GGRGLQTFDL RTTIHAVTAL
EAALLDLLGQ HLNVPVAALL GEGQQRDEVE MLGYLFYIGD RNKTDLAYAS GADGRDDWER
LRTEVAMTPE AVVRLAEAAQ ARYGFNDFKL KGGVLSGDEE IEAAKALAER FPQARVTLDP
NGAWSLAEAV RLCRDMHGVL AYAEDPCGAE NGYSGREVMA EFRRATGLPT ATNMIATDWR
QMGHAIQLQS VDIPLADPHF WTMQGSVRVA QMCNDWGLTW GSHSNNHFDI SLAMFTHVAA
AAPGKITAID THWIWQDGQF LTRDPLQIVG GKVKVPARPG LGIEVDMDAL ERANALYEQH
GLGARDDGVA MQYLIPNWKF DNKRPCLVR
//
