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Protein

4-hydroxy-2-oxovalerate aldolase

Gene

mhpE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

pH dependencei

Optimum pH is 6.25-6.75.1 Publication

Pathway: 3-phenylpropanoate degradation

This protein is involved in the pathway 3-phenylpropanoate degradation, which is part of Aromatic compound metabolism.
View all proteins of this organism that are known to be involved in the pathway 3-phenylpropanoate degradation and in Aromatic compound metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei14 – 141Transition state stabilizerBy similarity
Metal bindingi15 – 151ManganeseBy similarity
Active sitei18 – 181Proton acceptorSequence Analysis
Binding sitei168 – 1681SubstrateBy similarity
Metal bindingi197 – 1971Manganese; via tele nitrogenBy similarity
Binding sitei197 – 1971SubstrateBy similarity
Metal bindingi199 – 1991Manganese; via tele nitrogenBy similarity
Binding sitei288 – 2881SubstrateBy similarity

GO - Molecular functioni

  • 4-hydroxy-2-oxovalerate aldolase activity Source: EcoCyc
  • manganese ion binding Source: UniProtKB-HAMAP

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:MHPELY-MONOMER.
ECOL316407:JW0343-MONOMER.
MetaCyc:MHPELY-MONOMER.
UniPathwayiUPA00714.

Names & Taxonomyi

Protein namesi
Recommended name:
4-hydroxy-2-oxovalerate aldolase (EC:4.1.3.39)
Short name:
HOA
Alternative name(s):
4-hydroxy-2-keto-pentanoic acid aldolase
4-hydroxy-2-oxopentanoate aldolase
Gene namesi
Name:mhpE
Ordered Locus Names:b0352, JW0343
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13292. mhpE.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3373374-hydroxy-2-oxovalerate aldolasePRO_0000096470Add
BLAST

Proteomic databases

PaxDbiP51020.
PRIDEiP51020.

Interactioni

Subunit structurei

Interacts with MhpF.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
mhpFP775801EBI-1116093,EBI-1116083

Protein-protein interaction databases

DIPiDIP-10209N.
IntActiP51020. 11 interactions.
STRINGi511145.b0352.

Structurei

3D structure databases

ProteinModelPortaliP51020.
SMRiP51020. Positions 4-333.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni14 – 152Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0119.
HOGENOMiHOG000048047.
InParanoidiP51020.
KOiK01666.
OMAiDIAWIEA.
OrthoDBiEOG6C2WC0.
PhylomeDBiP51020.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01656. HOA.
InterProiIPR017629. 4OH_2_O-val_aldolase.
IPR013785. Aldolase_TIM.
IPR012425. DmpG_comm.
IPR000891. PYR_CT.
[Graphical view]
PANTHERiPTHR10277:SF3. PTHR10277:SF3. 1 hit.
PfamiPF07836. DmpG_comm. 1 hit.
PF00682. HMGL-like. 1 hit.
[Graphical view]
ProDomiPD005364. DmpG_comm. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsiTIGR03217. 4OH_2_O_val_ald. 1 hit.
PROSITEiPS50991. PYR_CT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P51020-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNGKKLYISD VTLRDGMHAI RHQYSLENVR QIAKALDDAR VDSIEVAHGD
60 70 80 90 100
GLQGSSFNYG FGAHSDLEWI EAAADVVKHA KIATLLLPGI GTIHDLKNAW
110 120 130 140 150
QAGARVVRVA THCTEADVSA QHIQYARELG MDTVGFLMMS HMTTPENLAK
160 170 180 190 200
QAKLMEGYGA TCIYVVDSGG AMNMSDIRDR FRALKAELKP ETQTGMHAHH
210 220 230 240 250
NLSLGVANSI AAVEEGCDRI DASLAGMGAG AGNAPLEVFI AAADKLGWQH
260 270 280 290 300
GTDLYALMDA ADDLVRPLQD RPVRVDRETL ALGYAGVYSS FLRHCETAAA
310 320 330
RYGLSAVDIL VELGKRRMVG GQEDMIVDVA LDLRNNK
Length:337
Mass (Da):36,470
Last modified:November 1, 1997 - v2
Checksum:iEDA263721721212F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiH64762.
RefSeqiNP_414886.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC73455; AAC73455; b0352.
BAE76134; BAE76134; BAE76134.
GeneIDi945012.
KEGGiecj:Y75_p0341.
eco:b0352.
PATRICi32115837. VBIEscCol129921_0360.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiH64762.
RefSeqiNP_414886.1. NC_000913.3.

3D structure databases

ProteinModelPortaliP51020.
SMRiP51020. Positions 4-333.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-10209N.
IntActiP51020. 11 interactions.
STRINGi511145.b0352.

Proteomic databases

PaxDbiP51020.
PRIDEiP51020.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73455; AAC73455; b0352.
BAE76134; BAE76134; BAE76134.
GeneIDi945012.
KEGGiecj:Y75_p0341.
eco:b0352.
PATRICi32115837. VBIEscCol129921_0360.

Organism-specific databases

EchoBASEiEB3077.
EcoGeneiEG13292. mhpE.

Phylogenomic databases

eggNOGiCOG0119.
HOGENOMiHOG000048047.
InParanoidiP51020.
KOiK01666.
OMAiDIAWIEA.
OrthoDBiEOG6C2WC0.
PhylomeDBiP51020.

Enzyme and pathway databases

UniPathwayiUPA00714.
BioCyciEcoCyc:MHPELY-MONOMER.
ECOL316407:JW0343-MONOMER.
MetaCyc:MHPELY-MONOMER.

Miscellaneous databases

PROiP51020.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01656. HOA.
InterProiIPR017629. 4OH_2_O-val_aldolase.
IPR013785. Aldolase_TIM.
IPR012425. DmpG_comm.
IPR000891. PYR_CT.
[Graphical view]
PANTHERiPTHR10277:SF3. PTHR10277:SF3. 1 hit.
PfamiPF07836. DmpG_comm. 1 hit.
PF00682. HMGL-like. 1 hit.
[Graphical view]
ProDomiPD005364. DmpG_comm. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsiTIGR03217. 4OH_2_O_val_ald. 1 hit.
PROSITEiPS50991. PYR_CT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiHOA_ECOLI
AccessioniPrimary (citable) accession number: P51020
Secondary accession number(s): P77787, Q2MC72
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 1, 1997
Last modified: June 24, 2015
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

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. 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.