ID A0A1G8I2G2_9MICC Unreviewed; 442 AA.
AC A0A1G8I2G2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=glucarate dehydratase {ECO:0000256|ARBA:ARBA00011973};
DE EC=4.2.1.40 {ECO:0000256|ARBA:ARBA00011973};
GN ORFNames=SAMN04488693_106115 {ECO:0000313|EMBL:SDI13165.1};
OS Arthrobacter subterraneus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=335973 {ECO:0000313|EMBL:SDI13165.1, ECO:0000313|Proteomes:UP000199258};
RN [1] {ECO:0000313|EMBL:SDI13165.1, ECO:0000313|Proteomes:UP000199258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NP_1H {ECO:0000313|EMBL:SDI13165.1,
RC ECO:0000313|Proteomes:UP000199258};
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; FNDT01000006; SDI13165.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8I2G2; -.
DR STRING; 335973.SAMN04488693_106115; -.
DR OrthoDB; 9774531at2; -.
DR Proteomes; UP000199258; 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; 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 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:UP000199258}.
FT DOMAIN 182..282
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
FT ACT_SITE 204
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-1"
FT ACT_SITE 336
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-1"
FT BINDING 29
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT BINDING 232..234
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT BINDING 232
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-3"
FT BINDING 263
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-3"
FT BINDING 286
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-3"
FT BINDING 286
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT BINDING 336..338
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT BINDING 365
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT BINDING 418
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
SQ SEQUENCE 442 AA; 47970 MW; 7E0A78AB4FE6B294 CRC64;
MTTQPTVAGV EVVPVAGHDS MLLNLSGAHG PFFTRNIAII TDSDGRTGLG EVPGGEAIRS
TIEEAGRILS GKPVAQFRSL LRSVAATFAD RDAGGRGLQT FDLRTTVHAV TAVESALLDL
HGQFLGIPVA ELLGDGQQRD AVPMLGYLFY VGNPDSTDLP YLREQGSADE WDRVRREEAM
TPAAVVRLAE AAQARYGFAD FKLKGGVHAG DDEVDAVVAL KERFPDARIT LDPNGGWLLA
DAIRLGKRMQ DVVAYAEDPC GAEGRFSGRE VMAEFRRATG LRTATNMIAT DWREMAHAIR
VNAVDIPLAD PHFWTMAGSV RVAQLCNEFG LTWGSHSNNH FDISLAMFTH VGAAAPGEIT
ALDTHWIWQD GQGLTVDPLQ IRGGEIRVPD APGLGIELDR TRLEEAHALY LEHGLGARDD
ATSMQYLIPE WSFDPKRPCL VR
//
