ID A0A0D8I8W8_9CLOT Unreviewed; 447 AA.
AC A0A0D8I8W8;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=glucarate dehydratase {ECO:0000256|ARBA:ARBA00011973};
DE EC=4.2.1.40 {ECO:0000256|ARBA:ARBA00011973};
GN Name=gudD1 {ECO:0000313|EMBL:AKL94605.1};
GN ORFNames=CACET_c11400 {ECO:0000313|EMBL:AKL94605.1}, TZ02_13255
GN {ECO:0000313|EMBL:KJF26489.1};
OS Clostridium aceticum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=84022 {ECO:0000313|EMBL:AKL94605.1, ECO:0000313|Proteomes:UP000035704};
RN [1] {ECO:0000313|EMBL:AKL94605.1, ECO:0000313|Proteomes:UP000035704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1496 {ECO:0000313|EMBL:AKL94605.1,
RC ECO:0000313|Proteomes:UP000035704};
RA Poehlein A., Schiel-Bengelsdorf B., Gottschalk G., Duerre P., Daniel R.;
RT "Genome sequence of Clostridium aceticum DSM 1496.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KJF26489.1, ECO:0000313|Proteomes:UP000032372}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1496 {ECO:0000313|EMBL:KJF26489.1,
RC ECO:0000313|Proteomes:UP000032372};
RA Song Y., Hwang S., Cho B.-K.;
RT "Draft genome sequence of Clostridium aceticum DSM 1496, a potential
RT butanol broducer through syngas fermentation.";
RL Submitted (FEB-2015) 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:PIRSR634598-3};
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; CP009687; AKL94605.1; -; Genomic_DNA.
DR EMBL; JYHU01000015; KJF26489.1; -; Genomic_DNA.
DR RefSeq; WP_044825448.1; NZ_JYHU01000015.1.
DR AlphaFoldDB; A0A0D8I8W8; -.
DR STRING; 84022.CACET_c11400; -.
DR KEGG; cace:CACET_c11400; -.
DR PATRIC; fig|84022.5.peg.924; -.
DR OrthoDB; 193563at2; -.
DR Proteomes; UP000032372; Unassembled WGS sequence.
DR Proteomes; UP000035704; Chromosome.
DR GO; GO:0008872; F:glucarate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR013342; Mandelate_racemase_C.
DR InterPro; IPR013341; Mandelate_racemase_N_dom.
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:0000313|EMBL:AKL94605.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR634598-3};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634598-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000035704}.
FT DOMAIN 187..281
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
FT ACT_SITE 209
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-1"
FT ACT_SITE 341
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-1"
FT BINDING 237
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-3"
FT BINDING 268
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-3"
FT BINDING 291
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-3"
SQ SEQUENCE 447 AA; 49310 MW; 5B6A6715CB6A5B22 CRC64;
MKTQGTPIVT DMKVIPVAGY DSALLTLSGC HGPFFTRNIV ILTDNSGNVG LGEVHGGDDI
TKALEDYKPF VVGQEIGNYK NIINVLRNGN STADDSGEGL QGLDLKNLKF VVHAETAVEC
ALLDLLGQFM NLPVAALLGD GMQRDKILIL GYLFYIADKN KINLPYLDES NSSDRWFRTR
RNVALTPEAI VEQAHAAKER YGFKDFKLKA GVLEGEKEID AIVALSKAFP DARINIDPNA
AWSLKEAINL CKGLKGVLSY AEDPCGPEKG YSGREIMSEF KMATGLQTAT NMIATDWRQF
HHCIVSKAVD IPLADPHFWT MSGSVRVAQV CNDWGMTWGS HSNNHFDISL AIFAHCAAAA
PGEITAMDTH WIWQDGQYLT KEPMEIKGGY LAMPKKPGLG LELDMDKVMK ANELYKKLDS
GDRNDAIAMQ HLIPNWKFDS KKPCLVR
//
