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P51020 (HOA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 107. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
4-hydroxy-2-oxovalerate aldolase

Short name=HOA
EC=4.1.3.39
Alternative name(s):
4-hydroxy-2-keto-pentanoic acid aldolase
4-hydroxy-2-oxopentanoate aldolase
Gene names
Name:mhpE
Ordered Locus Names:b0352, JW0343
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length337 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the retro-aldol cleavage of 4-hydroxy-2-oxopentanoate to pyruvate and acetaldehyde. Is involved in the meta-cleavage pathway for the degradation of 3-phenylpropanoate. Ref.6

Catalytic activity

(S)-4-hydroxy-2-oxopentanoate = acetaldehyde + pyruvate. HAMAP-Rule MF_01656

Pathway

Aromatic compound metabolism; 3-phenylpropanoate degradation. HAMAP-Rule MF_01656

Subunit structure

Interacts with MhpF. Ref.7

Miscellaneous

Presumably stereoselective for the 4S-enantiomer of 4-hydroxy-2-ketovalerate.

Sequence similarities

Belongs to the 4-hydroxy-2-oxovalerate aldolase family.

Biophysicochemical properties

pH dependence:

Optimum pH is 6.25-6.75. Ref.6

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

mhpFP775801EBI-1116093,EBI-1116083

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3373374-hydroxy-2-oxovalerate aldolase HAMAP-Rule MF_01656
PRO_0000096470

Regions

Region14 – 152Substrate binding By similarity

Sites

Active site181Proton acceptor Potential
Metal binding151Manganese By similarity
Metal binding1971Manganese; via tele nitrogen By similarity
Metal binding1991Manganese; via tele nitrogen By similarity
Binding site1681Substrate By similarity
Binding site1971Substrate By similarity
Binding site2881Substrate By similarity
Site141Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
P51020 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: EDA263721721212F

FASTA33736,470
        10         20         30         40         50         60 
MNGKKLYISD VTLRDGMHAI RHQYSLENVR QIAKALDDAR VDSIEVAHGD GLQGSSFNYG 

        70         80         90        100        110        120 
FGAHSDLEWI EAAADVVKHA KIATLLLPGI GTIHDLKNAW QAGARVVRVA THCTEADVSA 

       130        140        150        160        170        180 
QHIQYARELG MDTVGFLMMS HMTTPENLAK QAKLMEGYGA TCIYVVDSGG AMNMSDIRDR 

       190        200        210        220        230        240 
FRALKAELKP ETQTGMHAHH NLSLGVANSI AAVEEGCDRI DASLAGMGAG AGNAPLEVFI 

       250        260        270        280        290        300 
AAADKLGWQH GTDLYALMDA ADDLVRPLQD RPVRVDRETL ALGYAGVYSS FLRHCETAAA 

       310        320        330 
RYGLSAVDIL VELGKRRMVG GQEDMIVDVA LDLRNNK 

« Hide

References

« Hide 'large scale' references
[1]"Complete sequence of the mhp operon."
Kawamukai M.
Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]"Sequence of minutes 4-25 of Escherichia coli."
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"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 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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]Nashimoto H., Saito N.
Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 95-337.
Strain: K12.
[6]"Substrate selectivity and biochemical properties of 4-hydroxy-2-keto-pentanoic acid aldolase from Escherichia coli."
Pollard J.R., Rialland D., Bugg T.D.
Appl. Environ. Microbiol. 64:4093-4094(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, SUBSTRATE SPECIFICITY.
[7]"Coupled expression of MhpE aldolase and MhpF dehydrogenase in Escherichia coli."
Lee S.J., Ko J.H., Kang H.Y., Lee Y.
Biochem. Biophys. Res. Commun. 346:1009-1015(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MHPF.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D86239 Genomic DNA. Translation: BAA13057.1.
U73857 Genomic DNA. Translation: AAB18076.1.
U00096 Genomic DNA. Translation: AAC73455.1.
AP009048 Genomic DNA. Translation: BAE76134.1.
D85613 Genomic DNA. No translation available.
PIRH64762.
RefSeqNP_414886.1. NC_000913.3.
YP_488646.1. NC_007779.1.

3D structure databases

ProteinModelPortalP51020.
SMRP51020. Positions 4-333.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10209N.
IntActP51020. 11 interactions.
STRING511145.b0352.

Proteomic databases

PaxDbP51020.
PRIDEP51020.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73455; AAC73455; b0352.
BAE76134; BAE76134; BAE76134.
GeneID12932630.
945012.
KEGGecj:Y75_p0341.
eco:b0352.
PATRIC32115837. VBIEscCol129921_0360.

Organism-specific databases

EchoBASEEB3077.
EcoGeneEG13292. mhpE.

Phylogenomic databases

eggNOGCOG0119.
HOGENOMHOG000048047.
KOK01666.
OMAHEPDMIY.
OrthoDBEOG6C2WC0.
PhylomeDBP51020.

Enzyme and pathway databases

BioCycEcoCyc:MHPELY-MONOMER.
ECOL316407:JW0343-MONOMER.
MetaCyc:MHPELY-MONOMER.
UniPathwayUPA00714.

Gene expression databases

GenevestigatorP51020.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01656. HOA.
InterProIPR017629. 4OH_2_O-val_aldolase.
IPR013785. Aldolase_TIM.
IPR012425. DmpG_comm.
IPR000891. PYR_CT.
[Graphical view]
PANTHERPTHR10277:SF3. PTHR10277:SF3. 1 hit.
PfamPF07836. DmpG_comm. 1 hit.
PF00682. HMGL-like. 1 hit.
[Graphical view]
ProDomPD005364. DmpG_comm. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR03217. 4OH_2_O_val_ald. 1 hit.
PROSITEPS50991. PYR_CT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP51020.

Entry information

Entry nameHOA_ECOLI
AccessionPrimary (citable) accession number: P51020
Secondary accession number(s): P77787, Q2MC72
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 1, 1997
Last modified: July 9, 2014
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

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