ID   HOA_BACPJ               Reviewed;         337 AA.
AC   Q764S0;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 2.
DT   03-AUG-2022, entry version 54.
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=nahM;
OS   Bacillus sp. (strain JF8).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1921421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15073308; DOI=10.1099/mic.0.26858-0;
RA   Miyazawa D., Mukerjee-Dhar G., Shimura M., Hatta T., Kimbara K.;
RT   "Genes for Mn(II)-dependent NahC and Fe(II)-dependent NahH located in close
RT   proximity in the thermophilic naphthalene and PCB degrader, Bacillus sp.
RT   JF8: cloning and characterization.";
RL   Microbiology 150:993-1004(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD08311.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB116258; BAD08311.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q764S0; -.
DR   SMR; Q764S0; -.
DR   STRING; 1921421.M493_12195; -.
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..337
FT                   /note="4-hydroxy-2-oxovalerate aldolase"
FT                   /id="PRO_0000387789"
FT   DOMAIN          6..256
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         195
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         195
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         286
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;  36279 MW;  79A943DDAA31EB4F CRC64;
     MPKQAIRIMD TTLRDGSHAI RHRFTKENVR QIVQALDEAG VPVIEVSHGD GLGGSSLQYG
     MSLVEEMELI EEAAKTSRRA KIAALLLPGI GTKKELQQAK DCGIQMVRIA TQCSEADVSE
     QHFGLAKELG LETVGFLMMA HMLSPEELAQ QAKLMESYGA DIVYIVDSAG TMLPQDVIDR
     VIALKKVLNV PIGFHAHNNL GLAIGNSLAA IQAGATNIDA STRGLGAGSG NTQTEVLVAV
     LSRMGIETGI DLFQIMDAAE YIVDPLMDSP MIVNRDALTI GFTGVYSTFL WHAKQAGEKF
     GVDPREILIE LGRRKAVAGQ EDWILDVASD LSSAKGR