ID   HOA_NOVAR               Reviewed;         343 AA.
AC   O85977;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=xylK;
OS   Novosphingobium aromaticivorans (Sphingomonas aromaticivorans).
OG   Plasmid pNL1.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=48935;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 700278 / DSM 12444 / F199;
RX   PubMed=10049392; DOI=10.1128/jb.181.5.1585-1602.1999;
RA   Romine M.F., Stillwell L.C., Wong K.-K., Thurston S.J., Sisk E.C.,
RA   Sensen C., Gaasterland T., Fredrickson J.K., Saffer J.D.;
RT   "Complete sequence of a 184-kilobase catabolic plasmid from Sphingomonas
RT   aromaticivorans F199.";
RL   J. Bacteriol. 181:1585-1602(1999).
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; AF079317; AAD03993.1; -; Genomic_DNA.
DR   PIR; T31269; T31269.
DR   RefSeq; NP_049197.1; NC_002033.1.
DR   RefSeq; WP_010891015.1; NC_002033.1.
DR   AlphaFoldDB; O85977; -.
DR   SMR; O85977; -.
DR   OMA; YVGGQED; -.
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; Plasmid.
FT   CHAIN           1..343
FT                   /note="4-hydroxy-2-oxovalerate aldolase"
FT                   /id="PRO_0000387918"
FT   DOMAIN          10..262
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   ACT_SITE        22
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         18..19
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         19
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         172
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         201
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         201
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         203
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         292
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   SITE            18
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
SQ   SEQUENCE   343 AA;  36859 MW;  465022794BBCDCF9 CRC64;
     MTFDPTSDRL YIQDVTLRDG MHAILHMYGT DSVRTIAKAL DEAGVDAIEV SHGDGLNGST
     FNYGFGAHTD WDWIEAAADV IKNAVLTTLL VPGIGTAEEL KRAYSMGVRS VRVATHCTEA
     DVGKQHIGIA RDLGMDVSGF LMMSHMIEPE ALAQQALLME SYGAHCVYVT DSGGALDMDG
     VIARLQAYDR VLKPETQRGI HAHHNLSLGV ANSIVAAQAG AVRIDASLAG MGAGAGNAPL
     EVFIAAANRK GWKHGCDVMA LMDAADDIIR PLQDRPVRVD RETLSLGYAG VYSSFLRHAE
     KAAEQYGIDT REILVELGNR RMVGGQEDMI IDVALDLIKA KAN