ID   HOA_BACC1               Reviewed;         341 AA.
AC   Q739I4;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 89.
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   OrderedLocusNames=BCE_2157;
OS   Bacillus cereus (strain ATCC 10987 / NRS 248).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=222523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10987 / NRS 248;
RX   PubMed=14960714; DOI=10.1093/nar/gkh258;
RA   Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA   Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA   Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT   "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT   adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL   Nucleic Acids Res. 32:977-988(2004).
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   -!- SIMILARITY: Belongs to the 4-hydroxy-2-oxovalerate aldolase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01656}.
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DR   EMBL; AE017194; AAS41078.1; -; Genomic_DNA.
DR   RefSeq; WP_001254091.1; NC_003909.8.
DR   AlphaFoldDB; Q739I4; -.
DR   SMR; Q739I4; -.
DR   PRIDE; Q739I4; -.
DR   EnsemblBacteria; AAS41078; AAS41078; BCE_2157.
DR   GeneID; 59157720; -.
DR   KEGG; bca:BCE_2157; -.
DR   HOGENOM; CLU_049173_0_0_9; -.
DR   OMA; DLYKMMD; -.
DR   Proteomes; UP000002527; 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:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-UniRule.
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..341
FT                   /note="4-hydroxy-2-oxovalerate aldolase"
FT                   /id="PRO_0000387788"
FT   DOMAIN          9..259
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   ACT_SITE        21
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         17..18
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         18
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         171
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         198
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         198
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         200
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         289
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   SITE            17
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
SQ   SEQUENCE   341 AA;  37139 MW;  863D222844BA22C7 CRC64;
     MRRNSERPVR ITEVCLRDGS HVMKHQFTEE QVRSVTRTLD EAGMHYIEVS HGDGLGGSTL
     QYGKSLVNEM KLIEAAVDEC KQAKVAVLLI PGIGTIHELK QAANIGAKLV RVATHVTEAD
     VSAQHIQFAR ELGMEVCGFL MMAHSASVEK LVEQAKLMES YGAEAVYVTD SAGALLPHEV
     RERIRALRQS LNIEIGFHGH NNLSVAVANT ITAIEEGATR IDGSVRCLGA GAGNAQTEVL
     LAVLDRMGYK LDIDLYKMMD VAEEGVAPLL PVPQEIQKGS LVMGYAGVYS SFLLHAERAA
     QRFNVDARDI LIELGKRKVV GGQEDMILDV AAELAKIKME V