ID   BPHF_NOVAR              Reviewed;         262 AA.
AC   O86013;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=4-hydroxy-2-oxovalerate aldolase;
DE            Short=HOA;
DE            EC=4.1.3.39;
GN   Name=bphF;
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   -!- FUNCTION: Catalyzes the reversible retro-aldol cleavage of 4-hydroxy-2-
CC       oxovalerate to pyruvate and acetaldehyde. {ECO:0000250}.
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;
CC   -!- PATHWAY: Xenobiotic degradation; biphenyl degradation.
CC   -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family. {ECO:0000305}.
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DR   EMBL; AF079317; AAD04029.1; -; Genomic_DNA.
DR   PIR; T31305; T31305.
DR   RefSeq; NP_049233.1; NC_002033.1.
DR   RefSeq; WP_010891051.1; NC_002033.1.
DR   AlphaFoldDB; O86013; -.
DR   SMR; O86013; -.
DR   OMA; WNRVDDY; -.
DR   UniPathway; UPA00155; -.
DR   GO; GO:0008701; F:4-hydroxy-2-oxovalerate aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.60; -; 1.
DR   InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   Pfam; PF03328; HpcH_HpaI; 1.
DR   SUPFAM; SSF51621; SSF51621; 1.
PE   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism; Lyase; Magnesium; Metal-binding; Plasmid.
FT   CHAIN           1..262
FT                   /note="4-hydroxy-2-oxovalerate aldolase"
FT                   /id="PRO_0000207098"
FT   ACT_SITE        48
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         149
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         151
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         176
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         177
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         177
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            74
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   SITE            88
FT                   /note="Increases basicity of active site His"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   262 AA;  27341 MW;  0089258869DB547E CRC64;
     MQTPVNSFKA ALREGPVQLG FWLALAHPDI AEICAGQGYD WLLIDGEHGP QTLPGIVAQL
     RAVEATPPCS AIVRVPGHDS VTIKQVLDLG AQTLMVPMVE TAEQAKAIVT ASRYPPAGER
     GLGGARASRW GGYPAYVAEA NAQVCIIAQI ETATAVDNIE AIAAVDGIDA LFLGPADLAA
     TEGLLGASSF DALFKLTGEA LARIVATGKP AGILSRDERL VQQFLDGGAR FIANGIDSFT
     FAKGAGDGLR RWRERIAAQG GV