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Protein

Glucarate dehydratase-related protein

Gene

gudX

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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

Cofactori

Kineticsi

  1. KM=170 µM for idarate1 Publication
  2. KM=320 µM for glucarate1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei31 – 311SubstrateBy similarity
Binding sitei104 – 1041SubstrateBy similarity
Binding sitei149 – 1491SubstrateBy similarity
Binding sitei204 – 2041SubstrateBy similarity
Active sitei206 – 2061Proton acceptorSequence Analysis
Metal bindingi234 – 2341MagnesiumSequence Analysis
Metal bindingi265 – 2651MagnesiumSequence Analysis
Metal bindingi288 – 2881MagnesiumSequence Analysis
Binding sitei288 – 2881SubstrateBy similarity
Active sitei338 – 3381Proton acceptorSequence Analysis
Binding sitei367 – 3671SubstrateBy similarity
Binding sitei421 – 4211SubstrateBy similarity

GO - Molecular functioni

  1. lyase activity Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. cellular amino acid catabolic process Source: InterPro
  2. cellular catabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:G7446-MONOMER.
ECOL316407:JW2759-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucarate dehydratase-related protein (EC:4.2.1.-)
Short name:
GDH-RP
Short name:
GlucDRP
Gene namesi
Name:gudX
Synonyms:ygcY
Ordered Locus Names:b2788, JW2759
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13168. gudX.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 446446Glucarate dehydratase-related proteinPRO_0000171266Add
BLAST

Proteomic databases

PRIDEiQ46915.

Expressioni

Gene expression databases

GenevestigatoriQ46915.

Interactioni

Protein-protein interaction databases

IntActiQ46915. 3 interactions.
STRINGi511145.b2788.

Structurei

Secondary structure

1
446
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 2013Combined sources
Beta strandi24 – 263Combined sources
Beta strandi33 – 4412Combined sources
Beta strandi49 – 557Combined sources
Helixi58 – 669Combined sources
Helixi68 – 714Combined sources
Helixi76 – 783Combined sources
Helixi79 – 9012Combined sources
Helixi91 – 988Combined sources
Turni99 – 1013Combined sources
Helixi104 – 1063Combined sources
Helixi107 – 12721Combined sources
Helixi131 – 1344Combined sources
Beta strandi142 – 1465Combined sources
Beta strandi148 – 1503Combined sources
Helixi156 – 1583Combined sources
Beta strandi169 – 1713Combined sources
Helixi173 – 1764Combined sources
Helixi184 – 19815Combined sources
Beta strandi201 – 2066Combined sources
Beta strandi208 – 2103Combined sources
Helixi212 – 22514Combined sources
Beta strandi229 – 2346Combined sources
Helixi241 – 2477Combined sources
Turni248 – 2503Combined sources
Turni252 – 2543Combined sources
Beta strandi256 – 2605Combined sources
Helixi270 – 28112Combined sources
Beta strandi285 – 2906Combined sources
Helixi294 – 3029Combined sources
Beta strandi307 – 3104Combined sources
Helixi313 – 3164Combined sources
Helixi318 – 33013Combined sources
Helixi344 – 35512Combined sources
Helixi368 – 3714Combined sources
Turni372 – 3743Combined sources
Beta strandi378 – 3803Combined sources
Beta strandi388 – 3903Combined sources
Beta strandi394 – 3963Combined sources
Helixi403 – 41412Combined sources
Helixi424 – 4307Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GYPX-ray2.10C/D2-446[»]
4IL0X-ray2.80A/B/C/D/E/F/G/H1-446[»]
ProteinModelPortaliQ46915.
SMRiQ46915. Positions 6-445.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni234 – 2363Substrate bindingBy similarity
Regioni338 – 3403Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG4948.
HOGENOMiHOG000238021.
InParanoidiQ46915.
KOiK13918.
OMAiREMNHAL.
OrthoDBiEOG6V7BH9.
PhylomeDBiQ46915.

Family and domain databases

Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
InterProiIPR029065. Enolase_C-like.
IPR029017. Enolase_N_like.
IPR018110. Mandel_Rmase/mucon_lact_enz_CS.
IPR013342. Mandelate_racemase_C.
IPR013341. Mandelate_racemase_N_dom.
IPR001354. MR/MLE/MAL.
[Graphical view]
PANTHERiPTHR13794. PTHR13794. 1 hit.
PfamiPF01188. MR_MLE. 1 hit.
PF02746. MR_MLE_N. 1 hit.
[Graphical view]
SMARTiSM00922. MR_MLE. 1 hit.
[Graphical view]
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
PROSITEiPS00908. MR_MLE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q46915-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATQSSPVIT DMKVIPVAGH DSMLLNIGGA HNAYFTRNIV VLTDNAGHTG
60 70 80 90 100
IGEAPGGDVI YQTLVDAIPM VLGQEVARLN KVVQQVHKGN QAADFDTFGK
110 120 130 140 150
GAWTFELRVN AVAALEAALL DLLGKALNVP VCELLGPGKQ REAITVLGYL
160 170 180 190 200
FYIGDRTKTD LPYVENTPGN HEWYQLRHQK AMNSEAVVRL AEASQDRYGF
210 220 230 240 250
KDFKLKGGVL PGEQEIDTVR ALKKRFPDAR ITVDPNGAWL LDEAISLCKG
260 270 280 290 300
LNDVLTYAED PCGAEQGFSG REVMAEFRRA TGLPVATNMI ATNWREMGHA
310 320 330 340 350
VMLNAVDIPL ADPHFWTLSG AVRVAQLCDD WGLTWGCHSN NHFDISLAMF
360 370 380 390 400
THVGAAAPGN PTAIDTHWIW QEGDCRLTQN PLEIKNGKIA VPDAPGLGVE
410 420 430 440
LDWEQVQKAH EAYKRLPGGA RNDAGPMQYL IPGWTFDRKR PVFGRH
Length:446
Mass (Da):48,850
Last modified:November 1, 1996 - v1
Checksum:i9010C7FAAE4FBE49
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U29581 Genomic DNA. Translation: AAB40438.1.
U00096 Genomic DNA. Translation: AAC75830.1.
AP009048 Genomic DNA. Translation: BAE76860.1.
PIRiH65060.
RefSeqiNP_417268.1. NC_000913.3.
YP_490996.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75830; AAC75830; b2788.
BAE76860; BAE76860; BAE76860.
GeneIDi12931905.
947261.
KEGGiecj:Y75_p2725.
eco:b2788.
PATRICi32120992. VBIEscCol129921_2888.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U29581 Genomic DNA. Translation: AAB40438.1.
U00096 Genomic DNA. Translation: AAC75830.1.
AP009048 Genomic DNA. Translation: BAE76860.1.
PIRiH65060.
RefSeqiNP_417268.1. NC_000913.3.
YP_490996.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GYPX-ray2.10C/D2-446[»]
4IL0X-ray2.80A/B/C/D/E/F/G/H1-446[»]
ProteinModelPortaliQ46915.
SMRiQ46915. Positions 6-445.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ46915. 3 interactions.
STRINGi511145.b2788.

Proteomic databases

PRIDEiQ46915.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75830; AAC75830; b2788.
BAE76860; BAE76860; BAE76860.
GeneIDi12931905.
947261.
KEGGiecj:Y75_p2725.
eco:b2788.
PATRICi32120992. VBIEscCol129921_2888.

Organism-specific databases

EchoBASEiEB2960.
EcoGeneiEG13168. gudX.

Phylogenomic databases

eggNOGiCOG4948.
HOGENOMiHOG000238021.
InParanoidiQ46915.
KOiK13918.
OMAiREMNHAL.
OrthoDBiEOG6V7BH9.
PhylomeDBiQ46915.

Enzyme and pathway databases

BioCyciEcoCyc:G7446-MONOMER.
ECOL316407:JW2759-MONOMER.

Miscellaneous databases

PROiQ46915.

Gene expression databases

GenevestigatoriQ46915.

Family and domain databases

Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
InterProiIPR029065. Enolase_C-like.
IPR029017. Enolase_N_like.
IPR018110. Mandel_Rmase/mucon_lact_enz_CS.
IPR013342. Mandelate_racemase_C.
IPR013341. Mandelate_racemase_N_dom.
IPR001354. MR/MLE/MAL.
[Graphical view]
PANTHERiPTHR13794. PTHR13794. 1 hit.
PfamiPF01188. MR_MLE. 1 hit.
PF02746. MR_MLE_N. 1 hit.
[Graphical view]
SMARTiSM00922. MR_MLE. 1 hit.
[Graphical view]
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
PROSITEiPS00908. MR_MLE_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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(2005) [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(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-15, BIOPHYSICOCHEMICAL PROPERTIES.

Entry informationi

Entry nameiGUDX_ECOLI
AccessioniPrimary (citable) accession number: Q46915
Secondary accession number(s): Q2MA46
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: January 7, 2015
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.