ID Q01ZG7_SOLUE Unreviewed; 441 AA.
AC Q01ZG7;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=glucarate dehydratase {ECO:0000256|ARBA:ARBA00011973};
DE EC=4.2.1.40 {ECO:0000256|ARBA:ARBA00011973};
GN OrderedLocusNames=Acid_3981 {ECO:0000313|EMBL:ABJ84948.1};
OS Solibacter usitatus (strain Ellin6076).
OC Bacteria; Acidobacteriota; Terriglobia; Bryobacterales; Solibacteraceae;
OC Solibacter.
OX NCBI_TaxID=234267 {ECO:0000313|EMBL:ABJ84948.1};
RN [1] {ECO:0000313|EMBL:ABJ84948.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Ellin6076 {ECO:0000313|EMBL:ABJ84948.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Janssen P.H., Kuske C.R., Richardson P.;
RT "Complete sequence of Solibacter usitatus Ellin6076.";
RL Submitted (OCT-2006) 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}.
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DR EMBL; CP000473; ABJ84948.1; -; Genomic_DNA.
DR AlphaFoldDB; Q01ZG7; -.
DR STRING; 234267.Acid_3981; -.
DR KEGG; sus:Acid_3981; -.
DR eggNOG; COG4948; Bacteria.
DR HOGENOM; CLU_030273_9_0_0; -.
DR InParanoid; Q01ZG7; -.
DR OrthoDB; 193563at2; -.
DR UniPathway; UPA00564; UER00627.
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 InterPro; IPR013341; Mandelate_racemase_N_dom.
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 Pfam; PF02746; MR_MLE_N; 1.
DR SFLD; SFLDS00001; Enolase; 1.
DR SFLD; SFLDF00005; 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:ABJ84948.1};
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 181..281
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
FT ACT_SITE 203
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617653-1"
FT ACT_SITE 335
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617653-1"
FT BINDING 28
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
FT BINDING 201
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
FT BINDING 231..233
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
FT BINDING 231
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR617653-3"
FT BINDING 262
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR617653-3"
FT BINDING 285
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR617653-3"
FT BINDING 285
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
FT BINDING 335..337
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
FT BINDING 364
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
FT BINDING 417
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
SQ SEQUENCE 441 AA; 47782 MW; CDD80F53B0189BB2 CRC64;
MSAPIVEEMR VIPVAGHDSM LLNLSGAHAP LFTRNLVILK DSAGNTGVGE VPGGEAIRAT
LEEAMPLVAG RSIGAYTNIL DSVSRQFADR DAGGRGLQTF DQRTTIHAVT ALEAALLDLL
GKHLGVPVAA LLGEGQQRKT VDVLGYLFYV GDRGKTDLPY ASEPESIDDW LRLRHEEALS
VDAVVRLAEA AQARYGFRDF KLKGGVRAGG EEMEAIVALA ERFPEARITI DPNGAWSLRQ
AIALCKGRGD VLAYAEDPCG AEGGYSGREV MAEFRRATGL PTASNMIATD WRQLGHAIQL
HSVDIPLADP HFWTMRGSVR VAQLCHEWGL TWGSHSNNHF DVSLAMFTHV AAAAPGKITA
IDTHWIWQDG QRLTKEPFRI EGGKIAVPEA PGLGVELDMV EVGKAHAVYR GMGLGARDDA
QAMQYLIPGW KFDNKRPSLV R
//
