AC   MF_01656;
DC   Protein; auto
TR   HAMAP; MF_01656; -; 1; level=0
XX
Names: HOA
XX
ID   HOA
DE   RecName: Full=4-hydroxy-2-oxovalerate aldolase;
DE            Short=HOA;
DE            EC=4.1.3.39;
DE   AltName: Full=4-hydroxy-2-keto-pentanoic acid aldolase;
DE   AltName: Full=4-hydroxy-2-oxopentanoate aldolase;
case <OC:Enterobacterales>
GN   Name=mhpE;
end case
XX
case <OC:Enterobacterales>
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.
end case
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;
case <OC:Enterobacterales>
CC   -!- PATHWAY: Aromatic compound metabolism; 3-phenylpropanoate degradation.
CC   -!- SUBUNIT: Interacts with MhpF.
end case
CC   -!- SIMILARITY: Belongs to the 4-hydroxy-2-oxovalerate aldolase family.
XX
DR   PROSITE; PS50991; PYR_CT; 1; trigger=yes
DR   Pfam; PF07836; DmpG_comm; 1; trigger=no
DR   Pfam; PF00682; HMGL-like; 1; trigger=no
DR   NCBIfam; TIGR03217; 4OH_2_O_val_ald; 1; trigger=no
XX
KW   Aromatic hydrocarbons catabolism
KW   Lyase
KW   Manganese
KW   Metal-binding
XX
GO   GO:0008701; F:4-hydroxy-2-oxovalerate aldolase activity
GO   GO:0030145; F:manganese ion binding
GO   GO:0019439; P:aromatic compound catabolic process
XX
FT   From: HOA_PSEUF (P51016)
FT   BINDING         17..18
FT                   /ligand="substrate"
FT   Condition: R-D
FT   ACT_SITE        21
FT                   /note="Proton acceptor"
FT   Condition: H
FT   BINDING         18
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT   Condition: D
FT   BINDING         200
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT   Condition: H
FT   BINDING         202
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT   Condition: H
FT   BINDING         171
FT                   /ligand="substrate"
FT   Condition: S
FT   BINDING         200
FT                   /ligand="substrate"
FT   Condition: H
FT   BINDING         291
FT                   /ligand="substrate"
FT   Condition: Y
FT   SITE            17
FT                   /note="Transition state stabilizer"
FT   Condition: R
XX
Size: 333-377;
Related: None;
Template: P51020; P51015; Q9KWS0; P51014; Q51983; P51016; P51018; P51019; Q53WI0;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: in AZOSB, AZOVD, BURCJ, PARP8, BURL3, BURVG, PARXL, COMTE, DECAR,
 FRASN, METPP, MYCA9, MYCMM, MYCS2, MYCSJ, MYCSK, MYCSS, MYCUA, MYCVP, NOCFA,
 NOCSJ, NOVAD, PSEP1, PSEFK, PSEPW, CUPNH, CUPMC, RHOE4, RHOOB, RHOJR, SALAI,
 RHIWR
Plasmid: in GEOSE, BURVG, MYCSK, MYCSS, NOVAD, POLNA, POLSJ, PSEPU, PSEUF,
 CUPMC, RALN1, RHOOB, RHOJR, SPHAR, RHIWR, STRCO, THET8
Comments: This protein is present in multiple copies in some organisms, each one
 being located in a cluster involved in the degragation of a different aromatic compound.
 The E.coli protein showed no observable dependence on divalent metal ions (and no loss of enzyme
 activity by treatment with EDTA) unlike the purified Pseudomonas sp. strain CF600 and Burkholderia
 xenovorans aldolases.
XX
# Revision 1.38 2023/11/28
//