GUDD_STRCO
ID GUDD_STRCO Reviewed; 431 AA.
AC Q9RDE9;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Probable glucarate dehydratase;
DE Short=GDH;
DE Short=GlucD;
DE EC=4.2.1.40;
GN Name=gudD; OrderedLocusNames=SCO2542; ORFNames=SCC77.09c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
CC -!- FUNCTION: Catalyzes the dehydration of glucarate to 5-keto-4-deoxy-D-
CC glucarate (5-kdGluc). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- PATHWAY: Carbohydrate acid metabolism; D-glucarate degradation; 2,5-
CC dioxopentanoate from D-glucarate: step 1/2.
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. GlucD subfamily. {ECO:0000305}.
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DR EMBL; AL939113; CAB66220.1; -; Genomic_DNA.
DR RefSeq; NP_626780.1; NC_003888.3.
DR RefSeq; WP_011028417.1; NZ_VNID01000001.1.
DR AlphaFoldDB; Q9RDE9; -.
DR SMR; Q9RDE9; -.
DR STRING; 100226.SCO2542; -.
DR GeneID; 1097976; -.
DR KEGG; sco:SCO2542; -.
DR PATRIC; fig|100226.15.peg.2587; -.
DR eggNOG; COG4948; Bacteria.
DR HOGENOM; CLU_030273_9_0_11; -.
DR InParanoid; Q9RDE9; -.
DR OMA; THYPWQE; -.
DR PhylomeDB; Q9RDE9; -.
DR UniPathway; UPA00564; UER00627.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0008872; F:glucarate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042838; P:D-glucarate catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd03323; D-glucarate_dehydratase; 1.
DR Gene3D; 3.20.20.120; -; 1.
DR Gene3D; 3.30.390.10; -; 1.
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; IPR034593; Mandelate_racemase_DgoD-like.
DR InterPro; IPR013341; Mandelate_racemase_N_dom.
DR PANTHER; PTHR48080; PTHR48080; 1.
DR Pfam; PF13378; MR_MLE_C; 1.
DR Pfam; PF02746; MR_MLE_N; 1.
DR SMART; SM00922; MR_MLE; 1.
DR SUPFAM; SSF51604; SSF51604; 1.
DR SUPFAM; SSF54826; SSF54826; 1.
PE 3: Inferred from homology;
KW Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..431
FT /note="Probable glucarate dehydratase"
FT /id="PRO_0000171269"
FT ACT_SITE 200
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 327
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 29
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 108
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 228..230
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 276
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 276
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 327..329
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 356
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 410
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 431 AA; 46196 MW; 2D5C37DA4983224D CRC64;
MTRDLTITAV HLTPILVADP PLLNTQGVHQ PYTPRLIVEV ETADGVTGVG ETYGDAKYLE
LARPFAAKLV GRQVSDLNGL FTLADEVAVD SSRVFGQVDV GGLRGVQTAD KLRLSVVSGF
EVACLDALGK ALGLPVHALL GGKVRDAVEY SAYLFYKWAD HPEGVASEKD DWGAAVDPAG
VVAQARAFTE RYGFTSFKLK GGVFPPEEEI AAVKALAEAF PGHPLRLDPN GAWSVETSLK
VAAELGDVLE YLEDPALGTP AMAEVAAKTG VPLATNMCVT TFAEIQEAFT KGAVQVVLSD
HHYWGGLRNT QQLAAVCRTF GVGVSMHSNT HLGISLAAMT HVAATVPDLH HACDSHYPWQ
SEDVLTERLA FDGGKVAVSD APGLGVALDR ERLAFLHRRW LDDDGTLRDR DDAAAMRVAD
PEWVTPSVPR W
