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Protein

Mannonate dehydratase

Gene

uxuA

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

Functioni

Catalyzes the dehydration of D-mannonate.1 Publication

Catalytic activityi

D-mannonate = 2-dehydro-3-deoxy-D-gluconate + H2O.1 Publication

Cofactori

Fe2+1 Publication, Mn2+1 PublicationNote: Mn(2+) can substitute for iron, but in higher concentrations. Cannot use Fe(3+), Ni(2+) or Mg2+.1 Publication

Enzyme regulationi

Is inhibited by high concentrations of Fe2+ (> 2 mM), and by EDTA or other iron chelators in vitro.1 Publication

pH dependencei

Optimum pH is about 7.5. The activity at pH 6.5 and 8.6 is only about 20% of the maximal achievable activity at optimum pH.1 Publication

Pathwayi

GO - Molecular functioni

  1. ferrous iron binding Source: EcoCyc
  2. manganese ion binding Source: EcoCyc
  3. mannonate dehydratase activity Source: CACAO

GO - Biological processi

  1. cellular response to DNA damage stimulus Source: EcoliWiki
  2. D-glucuronate catabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Iron, Manganese

Enzyme and pathway databases

BioCyciEcoCyc:MANNONDEHYDRAT-MONOMER.
ECOL316407:JW4285-MONOMER.
MetaCyc:MANNONDEHYDRAT-MONOMER.
UniPathwayiUPA00246.

Names & Taxonomyi

Protein namesi
Recommended name:
Mannonate dehydratase (EC:4.2.1.8)
Alternative name(s):
D-mannonate hydro-lyase
Gene namesi
Name:uxuA
Ordered Locus Names:b4322, JW4285
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG11066. uxuA.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 394394Mannonate dehydratasePRO_0000170670Add
BLAST

Proteomic databases

PaxDbiP24215.
PRIDEiP24215.

Expressioni

Inductioni

By fructuronate. Its expression is subjected to catabolite repression by glucose.

Gene expression databases

GenevestigatoriP24215.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
nadEP188431EBI-1130634,EBI-548960

Protein-protein interaction databases

DIPiDIP-11108N.
IntActiP24215. 2 interactions.
STRINGi511145.b4322.

Structurei

Secondary structure

1
394
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 64Combined sources
Helixi16 – 227Combined sources
Beta strandi26 – 294Combined sources
Helixi42 – 5413Combined sources
Beta strandi58 – 636Combined sources
Helixi69 – 735Combined sources
Helixi78 – 9417Combined sources
Beta strandi99 – 1024Combined sources
Beta strandi113 – 1186Combined sources
Beta strandi124 – 1285Combined sources
Helixi130 – 13910Combined sources
Helixi146 – 1494Combined sources
Helixi152 – 16312Combined sources
Helixi167 – 17812Combined sources
Helixi190 – 1989Combined sources
Turni199 – 2024Combined sources
Helixi205 – 22622Combined sources
Beta strandi229 – 2324Combined sources
Beta strandi236 – 2394Combined sources
Beta strandi248 – 2503Combined sources
Helixi251 – 26010Combined sources
Beta strandi266 – 2716Combined sources
Helixi272 – 2754Combined sources
Helixi283 – 2908Combined sources
Helixi291 – 2933Combined sources
Beta strandi294 – 2985Combined sources
Beta strandi302 – 3043Combined sources
Beta strandi311 – 3133Combined sources
Beta strandi318 – 3214Combined sources
Helixi323 – 33917Combined sources
Helixi357 – 3615Combined sources
Helixi371 – 39121Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4EACX-ray2.30A/B/C/D1-394[»]
4EAYX-ray2.35A/B/C/D1-394[»]
ProteinModelPortaliP24215.
SMRiP24215. Positions 1-394.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the mannonate dehydratase family.Curated

Phylogenomic databases

eggNOGiCOG1312.
HOGENOMiHOG000195381.
InParanoidiP24215.
KOiK01686.
OMAiEGDVDMY.
OrthoDBiEOG6ZSP6Z.
PhylomeDBiP24215.

Family and domain databases

Gene3Di3.20.20.150. 1 hit.
HAMAPiMF_00106. UxuA.
InterProiIPR004628. Man_deHydtase.
IPR013022. Xyl_isomerase-like_TIM-brl.
[Graphical view]
PfamiPF03786. UxuA. 1 hit.
[Graphical view]
PIRSFiPIRSF016049. Man_dehyd. 1 hit.
SUPFAMiSSF51658. SSF51658. 2 hits.
TIGRFAMsiTIGR00695. uxuA. 1 hit.

Sequencei

Sequence statusi: Complete.

P24215-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEQTWRWYGP NDPVSLADVR QAGATGVVTA LHHIPNGEVW SVEEILKRKA
60 70 80 90 100
IIEDAGLVWS VVESVPIHED IKTHTGNYEQ WIANYQQTLR NLAQCGIRTV
110 120 130 140 150
CYNFMPVLDW TRTDLEYVLP DGSKALRFDQ IEFAAFEMHI LKRPGAEADY
160 170 180 190 200
TEEEIAQAAE RFATMSDEDK ARLTRNIIAG LPGAEEGYTL DQFRKHLELY
210 220 230 240 250
KDIDKAKLRE NFAVFLKAII PVAEEVGVRM AVHPDDPPRP ILGLPRIVST
260 270 280 290 300
IEDMQWMVDT VNSMANGFTM CTGSYGVRAD NDLVDMIKQF GPRIYFTHLR
310 320 330 340 350
STMREDNPKT FHEAAHLNGD VDMYEVVKAI VEEEHRRKAE GKEDLIPMRP
360 370 380 390
DHGHQMLDDL KKKTNPGYSA IGRLKGLAEV RGVELAIQRA FFSR
Length:394
Mass (Da):44,838
Last modified:February 1, 1995 - v2
Checksum:i0716A50BD6436679
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti52 – 521I → V in strain: MT78.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13329 Genomic DNA. Translation: BAA02590.1.
U14003 Genomic DNA. Translation: AAA97218.1.
U00096 Genomic DNA. Translation: AAC77278.1.
AP009048 Genomic DNA. Translation: BAE78315.1.
AJ225176 Genomic DNA. Translation: CAA12424.1.
X03411 Genomic DNA. Translation: CAA27147.1. Different termination.
X91735 Genomic DNA. Translation: CAA62860.1.
PIRiI57745.
S56547.
RefSeqiNP_418742.1. NC_000913.3.
YP_492456.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC77278; AAC77278; b4322.
BAE78315; BAE78315; BAE78315.
GeneIDi12932009.
947082.
KEGGiecj:Y75_p4208.
eco:b4322.
PATRICi32124240. VBIEscCol129921_4463.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13329 Genomic DNA. Translation: BAA02590.1.
U14003 Genomic DNA. Translation: AAA97218.1.
U00096 Genomic DNA. Translation: AAC77278.1.
AP009048 Genomic DNA. Translation: BAE78315.1.
AJ225176 Genomic DNA. Translation: CAA12424.1.
X03411 Genomic DNA. Translation: CAA27147.1. Different termination.
X91735 Genomic DNA. Translation: CAA62860.1.
PIRiI57745.
S56547.
RefSeqiNP_418742.1. NC_000913.3.
YP_492456.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4EACX-ray2.30A/B/C/D1-394[»]
4EAYX-ray2.35A/B/C/D1-394[»]
ProteinModelPortaliP24215.
SMRiP24215. Positions 1-394.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-11108N.
IntActiP24215. 2 interactions.
STRINGi511145.b4322.

Proteomic databases

PaxDbiP24215.
PRIDEiP24215.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77278; AAC77278; b4322.
BAE78315; BAE78315; BAE78315.
GeneIDi12932009.
947082.
KEGGiecj:Y75_p4208.
eco:b4322.
PATRICi32124240. VBIEscCol129921_4463.

Organism-specific databases

EchoBASEiEB1059.
EcoGeneiEG11066. uxuA.

Phylogenomic databases

eggNOGiCOG1312.
HOGENOMiHOG000195381.
InParanoidiP24215.
KOiK01686.
OMAiEGDVDMY.
OrthoDBiEOG6ZSP6Z.
PhylomeDBiP24215.

Enzyme and pathway databases

UniPathwayiUPA00246.
BioCyciEcoCyc:MANNONDEHYDRAT-MONOMER.
ECOL316407:JW4285-MONOMER.
MetaCyc:MANNONDEHYDRAT-MONOMER.

Miscellaneous databases

PROiP24215.

Gene expression databases

GenevestigatoriP24215.

Family and domain databases

Gene3Di3.20.20.150. 1 hit.
HAMAPiMF_00106. UxuA.
InterProiIPR004628. Man_deHydtase.
IPR013022. Xyl_isomerase-like_TIM-brl.
[Graphical view]
PfamiPF03786. UxuA. 1 hit.
[Graphical view]
PIRSFiPIRSF016049. Man_dehyd. 1 hit.
SUPFAMiSSF51658. SSF51658. 2 hits.
TIGRFAMsiTIGR00695. uxuA. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Mizobuchi K.
    Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
    Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "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.
  5. "Colonization ability and pathogenic properties of a fim- mutant of an avian strain of Escherichia coli."
    Marc D., Arne P., Bree A., Dho-Moulin M.
    Res. Microbiol. 149:473-485(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-128.
    Strain: O2:K1:H+ / MT78.
  6. "The regulatory region of the uxuAB operon in Escherichia coli K12."
    Blanco C., Ritzenthaler P., Kolb A.
    Mol. Gen. Genet. 202:112-119(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
    Strain: K12.
  7. "The gntP gene of Escherichia coli involved in gluconate uptake."
    Klemm P., Tong S., Nielsen H., Conway T.
    J. Bacteriol. 178:61-67(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
    Strain: K12.
  8. "The role of iron in the activation of mannonic and altronic acid hydratases, two Fe-requiring hydro-lyases."
    Dreyer J.L.
    Eur. J. Biochem. 166:623-630(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PH DEPENDENCE, ENZYME REGULATION.
    Strain: K12.

Entry informationi

Entry nameiUXUA_ECOLI
AccessioniPrimary (citable) accession number: P24215
Secondary accession number(s): O87739, Q2M5Z1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: February 1, 1995
Last modified: January 7, 2015
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.