ID W5WGB0_9PSEU Unreviewed; 419 AA.
AC W5WGB0;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=glucarate dehydratase {ECO:0000256|ARBA:ARBA00011973};
DE EC=4.2.1.40 {ECO:0000256|ARBA:ARBA00011973};
GN ORFNames=KALB_6870 {ECO:0000313|EMBL:AHI00229.1};
OS Kutzneria albida DSM 43870.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Kutzneria.
OX NCBI_TaxID=1449976 {ECO:0000313|EMBL:AHI00229.1, ECO:0000313|Proteomes:UP000019225};
RN [1] {ECO:0000313|EMBL:AHI00229.1, ECO:0000313|Proteomes:UP000019225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43870 {ECO:0000313|EMBL:AHI00229.1};
RX PubMed=25301375; DOI=10.1186/1471-2164-15-885;
RA Rebets Y., Tokovenko B., Lushchyk I., Ruckert C., Zaburannyi N.,
RA Bechthold A., Kalinowski J., Luzhetskyy A.;
RT "Complete genome sequence of producer of the glycopeptide antibiotic
RT Aculeximycin Kutzneria albida DSM 43870T, a representative of minor genus
RT of Pseudonocardiaceae.";
RL BMC Genomics 15:885-885(2014).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP007155; AHI00229.1; -; Genomic_DNA.
DR RefSeq; WP_025360092.1; NZ_CP007155.1.
DR AlphaFoldDB; W5WGB0; -.
DR STRING; 1449976.KALB_6870; -.
DR KEGG; kal:KALB_6870; -.
DR PATRIC; fig|1449976.3.peg.6898; -.
DR eggNOG; COG4948; Bacteria.
DR HOGENOM; CLU_030273_9_0_11; -.
DR OrthoDB; 193563at2; -.
DR Proteomes; UP000019225; Chromosome.
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:UP000019225}.
FT DOMAIN 167..261
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
FT ACT_SITE 189
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-1"
FT ACT_SITE 316
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-1"
FT BINDING 25
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT BINDING 145
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT BINDING 217..219
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT BINDING 265
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT BINDING 316..318
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT BINDING 345
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT BINDING 399
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
SQ SEQUENCE 419 AA; 45301 MW; F9A92BB7F191A5AB CRC64;
MKITDIELTP IAFRDPPLLN SVGVHEPWAL RTIIQVHTDE GLTGLGETYG DSGHLERMRK
VVPALLGLDV YALNAMHAAV ADALGGVTGS DRHGLTGTIS SGGTVDRVFS GFEVACLDIQ
GKHLGRPVSD LLGGAIRDRV PYSAYLFYKW AGHPGHEPDE WGEAIDPIGI VDQARALIDR
YGFGSIKLKG GVFPPEQEIA AIRALREAFP AHPLRLDPNA AWSVDTSVKV AEELGGLLEY
LEDPTAEIAG MAQVSERVRI PLATNMCVVS YEHLAPAVAR DAIQVLLSDH HYWGGLTRSR
QLAAICQTFG IGLSMHSNSH LGISLAAMTH LAAATPNLDY ACDTHYPWNA ADDVVLPGAL
SFVDGAVPVP TTPGLGVELD PDALALAHQR YLDCGLRDRD DTGYMQRFDP SYERKLPRW
//
