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P0AES2 (GUDD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glucarate dehydratase
Short name=GDH
Short name=GlucD
EC=4.2.1.40
Gene names
Name:gudD
Synonyms:ygcX
Ordered Locus Names:b2787, JW2758
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length446 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the dehydration of glucarate to 5-keto-4-deoxy-D-glucarate (5-kdGluc). Also acts on L-idarate.

Catalytic activity

D-glucarate = 5-dehydro-4-deoxy-D-glucarate + H2O.

Cofactor

Magnesium. Ref.5

Pathway

Carbohydrate acid metabolism; D-glucarate degradation; 2,5-dioxopentanoate from D-glucarate: step 1/2.

Subunit structure

Homodimer. Ref.5 Ref.6

Sequence similarities

Belongs to the mandelate racemase/muconate lactonizing enzyme family. GlucD subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=16 µM for idarate Ref.4

KM=60 µM for glucarate

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 446445Glucarate dehydratase
PRO_0000171264

Regions

Region235 – 2373Substrate binding
Region339 – 3413Substrate binding

Sites

Active site2071Proton acceptor
Active site3391Proton acceptor
Metal binding2351Magnesium
Metal binding2661Magnesium
Metal binding2891Magnesium
Binding site321Substrate
Binding site1031Substrate
Binding site1501Substrate
Binding site2051Substrate
Binding site2891Substrate
Binding site3681Substrate
Binding site4221Substrate

Experimental info

Mutagenesis1501Y → F: Reduces activity 100-fold. Ref.5
Mutagenesis2071K → Q: Reduces activity 1000-fold. Ref.5
Mutagenesis2071K → R: Reduces activity 10000-fold. Ref.5
Mutagenesis3391H → A: Loss of activity. Ref.5
Mutagenesis3391H → N: Reduces activity 10000-fold. Ref.5
Mutagenesis3391H → Q: Reduces activity 1000-fold. Ref.5
Mutagenesis3661D → A or N: Reduces activity over 100-fold. Ref.5
Sequence conflict310 – 3134PLAD → RWRI in AAB40437. Ref.1

Secondary structure

1 .......................................................................... 446
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0AES2 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: DFB07C9CA33F542C

FASTA44649,141
        10         20         30         40         50         60 
MSSQFTTPVV TEMQVIPVAG HDSMLMNLSG AHAPFFTRNI VIIKDNSGHT GVGEIPGGEK 

        70         80         90        100        110        120 
IRKTLEDAIP LVVGKTLGEY KNVLTLVRNT FADRDAGGRG LQTFDLRTTI HVVTGIEAAM 

       130        140        150        160        170        180 
LDLLGQHLGV NVASLLGDGQ QRSEVEMLGY LFFVGNRKAT PLPYQSQPDD SCDWYRLRHE 

       190        200        210        220        230        240 
EAMTPDAVVR LAEAAYEKYG FNDFKLKGGV LAGEEEAESI VALAQRFPQA RITLDPNGAW 

       250        260        270        280        290        300 
SLNEAIKIGK YLKGSLAYAE DPCGAEQGFS GREVMAEFRR ATGLPTATNM IATDWRQMGH 

       310        320        330        340        350        360 
TLSLQSVDIP LADPHFWTMQ GSVRVAQMCH EFGLTWGSHS NNHFDISLAM FTHVAAAAPG 

       370        380        390        400        410        420 
KITAIDTHWI WQEGNQRLTK EPFEIKGGLV QVPEKPGLGV EIDMDQVMKA HELYQKHGLG 

       430        440 
ARDDAMGMQY LIPGWTFDNK RPCMVR

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[2]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. expand/collapse author list , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 315-446.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"Evolution of enzymatic activities in the enolase superfamily: characterization of the (D)-glucarate/galactarate catabolic pathway in Escherichia coli."
Hubbard B.K., Koch M., Palmer D.R., Babbitt P.C., Gerlt J.A.
Biochemistry 37:14369-14375(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-15, BIOPHYSICOCHEMICAL PROPERTIES.
[5]"Evolution of enzymatic activities in the enolase superfamily: crystallographic and mutagenesis studies of the reaction catalyzed by D-glucarate dehydratase from Escherichia coli."
Gulick A.M., Hubbard B.K., Gerlt J.A., Rayment I.
Biochemistry 39:4590-4602(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND MAGNESIUM IONS, MUTAGENESIS OF TYR-150; LYS-207; HIS-339 AND ASP-366, COFACTOR, SUBUNIT.
[6]"Evolution of enzymatic activities in the enolase superfamily: identification of the general acid catalyst in the active site of D-glucarate dehydratase from Escherichia coli."
Gulick A.M., Hubbard B.K., Gerlt J.A., Rayment I.
Biochemistry 40:10054-10062(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND MAGNESIUM IONS, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U00096 Genomic DNA. Translation: AAC75829.1.
U29581 Genomic DNA. Translation: AAB40437.1.
AP009048 Genomic DNA. Translation: BAA16572.2.
PIRG65060.
RefSeqNP_417267.1. NC_000913.2.
YP_490995.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EC7X-ray1.90A/B/C/D1-446[»]
1EC8X-ray1.90A/B/C/D1-446[»]
1EC9X-ray2.00A/B/C/D1-446[»]
1ECQX-ray2.00A/B/C/D1-446[»]
1JCTX-ray2.75A/B1-446[»]
1JDFX-ray2.00A/B/C/D1-446[»]
3PWGX-ray2.00A/B/C/D1-446[»]
3PWIX-ray2.23A/B1-446[»]
4GYPX-ray2.10A/B1-446[»]
ProteinModelPortalP0AES2.
SMRP0AES2. Positions 5-446.
ModBaseSearch...

Protein-protein interaction databases

IntActP0AES2. 3 interactions.
STRING511145.b2787.

Proteomic databases

PaxDbP0AES2.
PRIDEP0AES2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75829; AAC75829; b2787.
BAA16572; BAA16572; BAA16572.
GeneID12933293.
947258.
KEGGecj:Y75_p2724.
eco:b2787.
PATRIC32120990. VBIEscCol129921_2887.

Organism-specific databases

EchoBASEEB2959.
EcoGeneEG13167. gudD.

Phylogenomic databases

eggNOGCOG4948.
HOGENOMHOG000238021.
KOK01706.
OMAIATDWRE.
ProtClustDBCLSK880490.

Enzyme and pathway databases

BioCycEcoCyc:GLUCARDEHYDRA-MONOMER.
ECOL316407:JW2758-MONOMER.
MetaCyc:GLUCARDEHYDRA-MONOMER.
SABIO-RKP0AES2.
UniPathwayUPA00564; UER00627.

Gene expression databases

GenevestigatorP0AES2.

Family and domain databases

InterProIPR017653. Glucarate_dehydratase.
IPR013342. Mandelate_racemase_C.
IPR001354. MR_MLE.
[Graphical view]
PANTHERPTHR13794. PTHR13794. 1 hit.
PfamPF01188. MR_MLE. 1 hit.
[Graphical view]
SMARTSM00922. MR_MLE. 1 hit.
[Graphical view]
TIGRFAMsTIGR03247. glucar-dehydr. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP0AES2.

Entry information

Entry nameGUDD_ECOLI
AccessionPrimary (citable) accession number: P0AES2
Secondary accession number(s): P76637, P78217, Q46914
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 70 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents