GUDD_PSEPU
ID GUDD_PSEPU Reviewed; 451 AA.
AC P42206;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Glucarate dehydratase;
DE Short=GDH;
DE Short=GlucD;
DE EC=4.2.1.40;
GN Name=gudD;
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=pp3;
RA Burlingame R.P., Lauer G.D., Platz J.G., Rudd E.A., Ally A., Ally D.,
RA Backman K.C.;
RT "Nucleotide sequence of genes for glucarate dehydratase and 5-keto-4-
RT deoxyglucarate dehydratase from Pseudomonas putida pp3.";
RL Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND SUBUNIT.
RX PubMed=9772161; DOI=10.1021/bi981123n;
RA Gulick A.M., Palmer D.R., Babbitt P.C., Gerlt J.A., Rayment I.;
RT "Evolution of enzymatic activities in the enolase superfamily: crystal
RT structure of (D)-glucarate dehydratase from Pseudomonas putida.";
RL Biochemistry 37:14358-14368(1998).
CC -!- FUNCTION: Catalyzes the dehydration of glucarate to 5-keto-4-deoxy-D-
CC glucarate (5-kdGluc).
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 -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:9772161}.
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. GlucD subfamily. {ECO:0000305}.
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DR EMBL; M69160; AAA25868.1; -; Genomic_DNA.
DR PIR; S27617; S27617.
DR PDB; 1BQG; X-ray; 2.30 A; A=1-451.
DR PDBsum; 1BQG; -.
DR AlphaFoldDB; P42206; -.
DR SMR; P42206; -.
DR BioCyc; MetaCyc:MON-15627; -.
DR BRENDA; 4.2.1.40; 5092.
DR SABIO-RK; P42206; -.
DR UniPathway; UPA00564; UER00627.
DR EvolutionaryTrace; P42206; -.
DR GO; GO:0008872; F:glucarate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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; IPR017653; Glucarate_dehydratase.
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 SFLD; SFLDF00005; glucarate_dehydratase; 1.
DR SMART; SM00922; MR_MLE; 1.
DR SUPFAM; SSF51604; SSF51604; 1.
DR SUPFAM; SSF54826; SSF54826; 1.
DR TIGRFAMs; TIGR03247; glucar-dehydr; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lyase; Magnesium; Metal-binding.
FT CHAIN 1..451
FT /note="Glucarate dehydratase"
FT /id="PRO_0000171268"
FT ACT_SITE 213
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 345
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 38
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 211
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 241..243
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 241
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 272
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 345..347
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 374
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 427
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT STRAND 15..27
FT /evidence="ECO:0007829|PDB:1BQG"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:1BQG"
FT STRAND 40..51
FT /evidence="ECO:0007829|PDB:1BQG"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:1BQG"
FT HELIX 65..72
FT /evidence="ECO:0007829|PDB:1BQG"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:1BQG"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:1BQG"
FT HELIX 86..96
FT /evidence="ECO:0007829|PDB:1BQG"
FT HELIX 113..134
FT /evidence="ECO:0007829|PDB:1BQG"
FT HELIX 138..141
FT /evidence="ECO:0007829|PDB:1BQG"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:1BQG"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:1BQG"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:1BQG"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:1BQG"
FT HELIX 179..183
FT /evidence="ECO:0007829|PDB:1BQG"
FT HELIX 191..205
FT /evidence="ECO:0007829|PDB:1BQG"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:1BQG"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:1BQG"
FT HELIX 219..232
FT /evidence="ECO:0007829|PDB:1BQG"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:1BQG"
FT HELIX 248..255
FT /evidence="ECO:0007829|PDB:1BQG"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:1BQG"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:1BQG"
FT HELIX 277..288
FT /evidence="ECO:0007829|PDB:1BQG"
FT STRAND 292..297
FT /evidence="ECO:0007829|PDB:1BQG"
FT HELIX 301..310
FT /evidence="ECO:0007829|PDB:1BQG"
FT STRAND 314..317
FT /evidence="ECO:0007829|PDB:1BQG"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:1BQG"
FT HELIX 325..338
FT /evidence="ECO:0007829|PDB:1BQG"
FT HELIX 351..361
FT /evidence="ECO:0007829|PDB:1BQG"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:1BQG"
FT TURN 378..380
FT /evidence="ECO:0007829|PDB:1BQG"
FT STRAND 383..386
FT /evidence="ECO:0007829|PDB:1BQG"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:1BQG"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:1BQG"
FT HELIX 409..420
FT /evidence="ECO:0007829|PDB:1BQG"
SQ SEQUENCE 451 AA; 49572 MW; 04CCB563BCB1C6EA CRC64;
MEALNQSQAA TGAPVITDLK VVPVAGHDSM LLNLSGAHGP LFTRNILILT DSSGHVGVGE
VPGGEGIRKT LEDARHLLIN QSIGNYQSLL NKVRNAFADR DVGGRGLQTF DLRIAVHAVT
AVESALLDLL GQHLQVPVAA LLGEGQQRDA VEMLGYLFYV GDRNKTDLGY RSEHEADNEW
FRLRNKEALT PESVVALAEA AYDRYGFKDF KLKGGVLRGE DEIAAVTALS ERFPDARITL
DPNGAWSLKE AVALCRDQHH VLAYAEDPCG AENGYSGREV MAEFRRSTGL RTATNMIATD
WRQMGHAIQL QSVDIPLADP HFWTMQGSVR VAQMCNEWGL TWGSHSNNHF DISLAMFTHV
AAAAPGNITA IDTHWIWQDG QRLTKEPLQI KGGLVEVPKK PGLGVELDWD ALMKAHEVYK
SMGLGARDDA TAMRYLVSGW EFNNKRPCMV R
