Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q46915 (GUDX_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
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-related protein
Short name=GDH-RP
Short name=GlucDRP
EC=4.2.1.-
Gene names
Name:gudX
Synonyms:ygcY
Ordered Locus Names:b2788, JW2759
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length446 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Does not seem to have an in-vivo activity on glucarate or idarate. Its real substrate is unknown.

Cofactor

Divalent metal cations By similarity.

Sequence similarities

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

Biophysicochemical properties

Kinetic parameters:

KM=170 µM for idarate Ref.3

KM=320 µM for glucarate

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 446446Glucarate dehydratase-related protein
PRO_0000171266

Regions

Region234 – 2363Substrate binding By similarity
Region338 – 3403Substrate binding By similarity

Sites

Active site2061Proton acceptor Potential
Active site3381Proton acceptor Potential
Metal binding2341Magnesium Potential
Metal binding2651Magnesium Potential
Metal binding2881Magnesium Potential
Binding site311Substrate By similarity
Binding site1041Substrate By similarity
Binding site1491Substrate By similarity
Binding site2041Substrate By similarity
Binding site2881Substrate By similarity
Binding site3671Substrate By similarity
Binding site4211Substrate By similarity

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Q46915 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 9010C7FAAE4FBE49

FASTA44648,850
        10         20         30         40         50         60 
MATQSSPVIT DMKVIPVAGH DSMLLNIGGA HNAYFTRNIV VLTDNAGHTG IGEAPGGDVI 

        70         80         90        100        110        120 
YQTLVDAIPM VLGQEVARLN KVVQQVHKGN QAADFDTFGK GAWTFELRVN AVAALEAALL 

       130        140        150        160        170        180 
DLLGKALNVP VCELLGPGKQ REAITVLGYL FYIGDRTKTD LPYVENTPGN HEWYQLRHQK 

       190        200        210        220        230        240 
AMNSEAVVRL AEASQDRYGF KDFKLKGGVL PGEQEIDTVR ALKKRFPDAR ITVDPNGAWL 

       250        260        270        280        290        300 
LDEAISLCKG LNDVLTYAED PCGAEQGFSG REVMAEFRRA TGLPVATNMI ATNWREMGHA 

       310        320        330        340        350        360 
VMLNAVDIPL ADPHFWTLSG AVRVAQLCDD WGLTWGCHSN NHFDISLAMF THVGAAAPGN 

       370        380        390        400        410        420 
PTAIDTHWIW QEGDCRLTQN PLEIKNGKIA VPDAPGLGVE LDWEQVQKAH EAYKRLPGGA 

       430        440 
RNDAGPMQYL IPGWTFDRKR PVFGRH

« 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]"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 1-15, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U29581 Genomic DNA. Translation: AAB40438.1.
U00096 Genomic DNA. Translation: AAC75830.1.
AP009048 Genomic DNA. Translation: BAE76860.1.
PIRH65060.
RefSeqNP_417268.1. NC_000913.2.
YP_490996.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4GYPX-ray2.10C/D2-446[»]
4IL0X-ray2.80A/B/C/D/E/F/G/H1-446[»]
ProteinModelPortalQ46915.
SMRQ46915. Positions 6-445.
ModBaseSearch...

Protein-protein interaction databases

IntActQ46915. 3 interactions.
STRING511145.b2788.

Proteomic databases

PRIDEQ46915.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75830; AAC75830; b2788.
BAE76860; BAE76860; BAE76860.
GeneID12931905.
947261.
KEGGecj:Y75_p2725.
eco:b2788.
PATRIC32120992. VBIEscCol129921_2888.

Organism-specific databases

EchoBASEEB2960.
EcoGeneEG13168. gudX.

Phylogenomic databases

eggNOGCOG4948.
HOGENOMHOG000238021.
KOK13918.
OMAWREMNHA.
ProtClustDBCLSK880490.

Enzyme and pathway databases

BioCycEcoCyc:G7446-MONOMER.
ECOL316407:JW2759-MONOMER.

Gene expression databases

GenevestigatorQ46915.

Family and domain databases

InterProIPR018110. Mandel_Rmase/mucon_lact_enz_CS.
IPR013342. Mandelate_racemase_C.
IPR013341. Mandelate_racemase_N.
IPR001354. MR_MLE.
[Graphical view]
PANTHERPTHR13794. PTHR13794. 1 hit.
PfamPF01188. MR_MLE. 1 hit.
PF02746. MR_MLE_N. 1 hit.
[Graphical view]
SMARTSM00922. MR_MLE. 1 hit.
[Graphical view]
PROSITEPS00908. MR_MLE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUDX_ECOLI
AccessionPrimary (citable) accession number: Q46915
Secondary accession number(s): Q2MA46
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: May 1, 2013
This is version 88 of the entry and version 1 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

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