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Q3Z554 (HOA_SHISS) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:SSON_0331
OrganismShigella sonnei (strain Ss046) [Complete proteome] [HAMAP]
Taxonomic identifier300269 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

Protein attributes

Sequence length337 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 aromatic compounds By similarity. HAMAP MF_01656

Catalytic activity

4-hydroxy-2-oxopentanoate = acetaldehyde + pyruvate. HAMAP MF_01656

Pathway

Aromatic compound metabolism; 3-phenylpropanoate degradation. HAMAP MF_01656

Subunit structure

Interacts with mhpF By similarity. HAMAP MF_01656

Sequence similarities

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

Ontologies

Keywords
   Biological processAromatic hydrocarbons catabolism
   LigandManganese
Metal-binding
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processaromatic compound catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular function4-hydroxy-2-oxovalerate aldolase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3373374-hydroxy-2-oxovalerate aldolase HAMAP MF_01656
PRO_0000337808

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
Q3Z554 [UniParc].

Last modified September 27, 2005. Version 1.
Checksum: A2B4F6A1598DB91A

FASTA33736,502
        10         20         30         40         50         60 
MNGKKLYISD VTLRDGMHAI RHQYSLENVR QIAKALDDAR VDSIEVAHGD GLQGSSFNYG 

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

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

       190        200        210        220        230        240 
FRALKAVLKP ETQTGMHAHH NLSLGVANSI AAVEEGCDRI DASFAGMGAG AGNAPLEVFI 

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

       310        320        330 
RYGLSAVDIL VELGKRRMVG GQEDMIVDVA LDLRNNK 

« Hide

References

[1]"Genome dynamics and diversity of Shigella species, the etiologic agents of bacillary dysentery."
Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J., Xu J. expand/collapse author list , Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J., Jin Q.
Nucleic Acids Res. 33:6445-6458(2005) [PubMed: 16275786] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ss046.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000038 Genomic DNA. Translation: AAZ87108.1.
RefSeqYP_309343.1. NC_007384.1.

3D structure databases

ProteinModelPortalQ3Z554.
SMRQ3Z554. Positions 4-333.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3Z554.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000099547; EBESCP00000095576; EBESCG00000098591.
GeneID3668930.
GenomeReviewsGene locus SSON_0331 in contig CP000038_GR.
KEGGssn:SSON_0331.
PATRIC18734012. VBIShiSon107113_0379.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0119.
GeneTreeEBGT00050000011169.
HOGENOMHBG300122.
OMAATCVYVV.
ProtClustDBPRK08195.

Enzyme and pathway databases

BioCycSSON300269:SSO_0331-MONOMER.

Family and domain databases

HAMAPMF_01656. HOA.
[Tree]
InterProIPR017629. 4OH_2_O-val_aldolase.
IPR013785. Aldolase_TIM.
IPR012425. DmpG_comm.
IPR000891. PYR_CT.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KOK01666.
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...

Entry information

Entry nameHOA_SHISS
AccessionPrimary (citable) accession number: Q3Z554
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: September 27, 2005
Last modified: January 25, 2012
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families