ID   HOA_ECOHS               Reviewed;         337 AA.
AC   A7ZWZ9;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=4-hydroxy-2-oxovalerate aldolase {ECO:0000255|HAMAP-Rule:MF_01656};
DE            Short=HOA {ECO:0000255|HAMAP-Rule:MF_01656};
DE            EC=4.1.3.39 {ECO:0000255|HAMAP-Rule:MF_01656};
DE   AltName: Full=4-hydroxy-2-keto-pentanoic acid aldolase {ECO:0000255|HAMAP-Rule:MF_01656};
DE   AltName: Full=4-hydroxy-2-oxopentanoate aldolase {ECO:0000255|HAMAP-Rule:MF_01656};
GN   Name=mhpE {ECO:0000255|HAMAP-Rule:MF_01656}; OrderedLocusNames=EcHS_A0416;
OS   Escherichia coli O9:H4 (strain HS).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331112;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HS;
RX   PubMed=18676672; DOI=10.1128/jb.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
CC   -!- FUNCTION: Catalyzes the retro-aldol cleavage of 4-hydroxy-2-
CC       oxopentanoate to pyruvate and acetaldehyde. Is involved in the meta-
CC       cleavage pathway for the degradation of aromatic compounds.
CC       {ECO:0000255|HAMAP-Rule:MF_01656}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-4-hydroxy-2-oxopentanoate = acetaldehyde + pyruvate;
CC         Xref=Rhea:RHEA:22624, ChEBI:CHEBI:15343, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:73143; EC=4.1.3.39; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01656};
CC   -!- PATHWAY: Aromatic compound metabolism; 3-phenylpropanoate degradation.
CC       {ECO:0000255|HAMAP-Rule:MF_01656}.
CC   -!- SUBUNIT: Interacts with MhpF. {ECO:0000255|HAMAP-Rule:MF_01656}.
CC   -!- SIMILARITY: Belongs to the 4-hydroxy-2-oxovalerate aldolase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01656}.
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DR   EMBL; CP000802; ABV04803.1; -; Genomic_DNA.
DR   RefSeq; WP_001013492.1; NC_009800.1.
DR   AlphaFoldDB; A7ZWZ9; -.
DR   SMR; A7ZWZ9; -.
DR   KEGG; ecx:EcHS_A0416; -.
DR   HOGENOM; CLU_049173_0_0_6; -.
DR   OMA; DLYKMMD; -.
DR   UniPathway; UPA00714; -.
DR   Proteomes; UP000001123; Chromosome.
DR   GO; GO:0008701; F:4-hydroxy-2-oxovalerate aldolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019380; P:3-phenylpropionate catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd07943; DRE_TIM_HOA; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_01656; HOA; 1.
DR   InterPro; IPR017629; 4OH_2_O-val_aldolase.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR012425; DmpG_comm.
DR   InterPro; IPR035685; DRE_TIM_HOA.
DR   InterPro; IPR000891; PYR_CT.
DR   Pfam; PF07836; DmpG_comm; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   TIGRFAMs; TIGR03217; 4OH_2_O_val_ald; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism; Lyase; Manganese; Metal-binding.
FT   CHAIN           1..337
FT                   /note="4-hydroxy-2-oxovalerate aldolase"
FT                   /id="PRO_0000337806"
FT   DOMAIN          6..258
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   ACT_SITE        18
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         14..15
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         15
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         197
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         197
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         199
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         288
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   SITE            14
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
SQ   SEQUENCE   337 AA;  36479 MW;  1DAC59F891FEFC9B CRC64;
     MNGKKLYISD VTLRDGMHAI RHQYSLENVR HIAKALDDAR VDSIEVAHGD GLQGSSFNYG
     FGAHSDLEWI EAAADVVKHA KIATLLLPGI GTIHDLKNAW QAGARVVRVA THCTEADVSA
     QHIQYARELG MDTVGFLMMS HMTTPENLAK QAKLMEGYGA TCIYVVDSGG AMNMSDIRDR
     FRALKAELKP ETQTGMHAHH NLSLGVANSI AAVEEGCDRI DASLAGMGAG AGNAPLEVFI
     AAADKLGWQH GTDLYALMDA ADDLVRPLQD RPVRVDRETL ALGYAGVYSS FLRHCETAAA
     RYGLSAVDIL VELGKRRMVG GQEDMIVDVA LDLRNNK