ID A0A1X7CSI0_9ACTN Unreviewed; 432 AA.
AC A0A1X7CSI0;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=glucarate dehydratase {ECO:0000256|ARBA:ARBA00011973};
DE EC=4.2.1.40 {ECO:0000256|ARBA:ARBA00011973};
GN ORFNames=SAMN02745830_01131 {ECO:0000313|EMBL:SMF02301.1};
OS Streptomyces sp. Amel2xC10.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1305826 {ECO:0000313|EMBL:SMF02301.1, ECO:0000313|Proteomes:UP000192930};
RN [1] {ECO:0000313|EMBL:SMF02301.1, ECO:0000313|Proteomes:UP000192930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Amel2xC10 {ECO:0000313|EMBL:SMF02301.1,
RC ECO:0000313|Proteomes:UP000192930};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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 -!- 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; FWZW01000002; SMF02301.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7CSI0; -.
DR OrthoDB; 193563at2; -.
DR Proteomes; UP000192930; Unassembled WGS sequence.
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; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000192930}.
FT DOMAIN 179..273
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
FT ACT_SITE 201
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-1"
FT ACT_SITE 328
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-1"
FT BINDING 30
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT BINDING 229..231
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT BINDING 277
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT BINDING 328..330
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT BINDING 357
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT BINDING 411
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
SQ SEQUENCE 432 AA; 46282 MW; DE39369C3694CC0E CRC64;
MTAAHLTVAD VRLTPILVAD PPLLNTQGVH QPYTPRLIVE VVTADGTTGV GETYGDTKYL
ELARPFAESL KGRQVSDLNG LFTLADELAV DRSRISGQVD VGGLRGVQTA DKLRLSVVSA
FEVACLDALG KALGLPVHAL LGGKVRGSVE YSAYLFYKWA AHPDGVPSEP DDWGAALDPA
GVVAQARRFT ERHGFTSFKL KGGVFPPEQE IAAVRALAAA FPGQPLRLDP NGAWSVPTSL
AVAKELGDVL EYLEDPALGT PAMAEVAAGT DVPLATNMCV TTFAEIPEAF TRGAVQVVLS
DHHYWGGLRN TRQLAAVCAT FGVDVSMHSN THLGISLAAM THVAATVPGL RHACDSHYPW
QPEDVLTERI AFEGGRVTVT DAPGLGVELD HGKLDRLHRR WLDDDGTLRD RDDTAAMRVA
DPDWVTPTVP RW
//
