ID A0A1H1DDM5_9MICC Unreviewed; 443 AA.
AC A0A1H1DDM5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=glucarate dehydratase {ECO:0000256|ARBA:ARBA00011973};
DE EC=4.2.1.40 {ECO:0000256|ARBA:ARBA00011973};
GN ORFNames=SAMN04489742_2394 {ECO:0000313|EMBL:SDQ74591.1};
OS Arthrobacter crystallopoietes.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=37928 {ECO:0000313|EMBL:SDQ74591.1, ECO:0000313|Proteomes:UP000181917};
RN [1] {ECO:0000313|EMBL:SDQ74591.1, ECO:0000313|Proteomes:UP000181917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20117 {ECO:0000313|EMBL:SDQ74591.1,
RC ECO:0000313|Proteomes:UP000181917};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNKH01000002; SDQ74591.1; -; Genomic_DNA.
DR RefSeq; WP_074700603.1; NZ_FNKH01000002.1.
DR AlphaFoldDB; A0A1H1DDM5; -.
DR STRING; 37928.SAMN04489742_2394; -.
DR KEGG; acry:AC20117_05455; -.
DR OrthoDB; 9774531at2; -.
DR Proteomes; UP000181917; 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 PANTHER; PTHR48080; D-GALACTONATE DEHYDRATASE-RELATED; 1.
DR PANTHER; PTHR48080:SF4; GLUCARATE DEHYDRATASE; 1.
DR Pfam; PF13378; MR_MLE_C; 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 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:UP000181917}.
FT DOMAIN 183..283
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
FT ACT_SITE 205
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-1"
FT ACT_SITE 337
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 101
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT BINDING 233..235
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT BINDING 233
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-3"
FT BINDING 264
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-3"
FT BINDING 287
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-3"
FT BINDING 287
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT BINDING 337..339
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT BINDING 366
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT BINDING 419
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
SQ SEQUENCE 443 AA; 47935 MW; 67AD589FBE9C7BFC CRC64;
MASNTPTIVS VEAVPVAGHD SMLLNLSGAH GPFFTRNIAI ITDSNGNTGL GEVPGGEAIR
STIEEAGSIL VGQPISLYRQ LLRKVSVAFA DRDAGGRGAQ TFDLRTTIHA VTALESGLLD
LMGQHLGVPV AELLGEGQQR DKVQMLGYLF YVADRTKTDL PYLAEDNPAD DWERLRREEA
MTPEAIVALA EAAQQRYGFQ DFKLKGGVLP GKEEVAAVTA LAKRFPEARI TLDPNGGWLL
QEAIELCSGL GDVLAYAEDP CGPEGTYSGR ETMAEFRRAT GLPTATNMIA TDWRQMAHAI
RTNAVDIPLA DPHFWTMQGS VRVAQLCNDF GLTWGSHSNN HFDISLAMFT QVGAAAPGKI
TALDTHWIWQ DGQGLTTEPL QIKGGYIEVP ARPGLGVELD RKALEAAHQL YLEHGLGARD
DAAAMQYLVP GWEFNPKRPA LVR
//
