GUDD_ECO57
ID GUDD_ECO57 Reviewed; 446 AA.
AC P0AES3; P76637; P78217; Q46914;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
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; OrderedLocusNames=Z4102, ECs3647;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Catalyzes the dehydration of glucarate to 5-keto-4-deoxy-D-
CC glucarate (5-kdGluc). Also acts on L-idarate (By similarity).
CC {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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. GlucD subfamily. {ECO:0000305}.
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DR EMBL; AE005174; AAG57900.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB37070.1; -; Genomic_DNA.
DR PIR; G91084; G91084.
DR RefSeq; NP_311674.1; NC_002695.1.
DR RefSeq; WP_000098255.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AES3; -.
DR SMR; P0AES3; -.
DR STRING; 155864.EDL933_3965; -.
DR PRIDE; P0AES3; -.
DR EnsemblBacteria; AAG57900; AAG57900; Z4102.
DR EnsemblBacteria; BAB37070; BAB37070; ECs_3647.
DR GeneID; 916552; -.
DR KEGG; ece:Z4102; -.
DR KEGG; ecs:ECs_3647; -.
DR PATRIC; fig|386585.9.peg.3811; -.
DR eggNOG; COG4948; Bacteria.
DR HOGENOM; CLU_030273_9_0_6; -.
DR OMA; MQYLIPN; -.
DR UniPathway; UPA00564; UER00627.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
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 PANTHER; PTHR48080; PTHR48080; 1.
DR Pfam; PF13378; MR_MLE_C; 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 3: Inferred from homology;
KW Lyase; Magnesium; Metal-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..446
FT /note="Glucarate dehydratase"
FT /id="PRO_0000171265"
FT ACT_SITE 207
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 339
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 32
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 235..237
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 289
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 289
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 339..341
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 368
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 422
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 446 AA; 49141 MW; DFB07C9CA33F542C CRC64;
MSSQFTTPVV TEMQVIPVAG HDSMLMNLSG AHAPFFTRNI VIIKDNSGHT GVGEIPGGEK
IRKTLEDAIP LVVGKTLGEY KNVLTLVRNT FADRDAGGRG LQTFDLRTTI HVVTGIEAAM
LDLLGQHLGV NVASLLGDGQ QRSEVEMLGY LFFVGNRKAT PLPYQSQPDD SCDWYRLRHE
EAMTPDAVVR LAEAAYEKYG FNDFKLKGGV LAGEEEAESI VALAQRFPQA RITLDPNGAW
SLNEAIKIGK YLKGSLAYAE DPCGAEQGFS GREVMAEFRR ATGLPTATNM IATDWRQMGH
TLSLQSVDIP LADPHFWTMQ GSVRVAQMCH EFGLTWGSHS NNHFDISLAM FTHVAAAAPG
KITAIDTHWI WQEGNQRLTK EPFEIKGGLV QVPEKPGLGV EIDMDQVMKA HELYQKHGLG
ARDDAMGMQY LIPGWTFDNK RPCMVR
