ID   BPHF_RHOJR              Reviewed;         258 AA.
AC   O05151; Q75WN6;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=4-hydroxy-2-oxovalerate aldolase;
DE            Short=HOA;
DE            EC=4.1.3.39;
GN   Name=bphF; Synonyms=etbF; OrderedLocusNames=RHA1_ro10138;
OS   Rhodococcus jostii (strain RHA1).
OG   Plasmid pRHL2.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=101510;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RX   PubMed=9073078; DOI=10.1016/s0378-1119(96)00748-2;
RA   Masai E., Sugiyama K., Iwashita N., Shimizu S., Hauschild J.E., Hatta T.,
RA   Kimbara K., Yano K., Fukuda M.;
RT   "The bphDEF meta-cleavage pathway genes involved in
RT   biphenyl/polychlorinated biphenyl degradation are located on a linear
RT   plasmid and separated from the initial bphACB genes in Rhodococcus sp.
RT   strain RHA1.";
RL   Gene 187:141-149(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Iwasaki T., Miyauchi K., Masai E., Fukuda M.;
RT   "Diversity and characterization of aromatic ring hydroxylation dioxygenase
RT   genes in Rhodococcus sp. strain RHA1.";
RL   Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1;
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA   Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA   Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA   Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA   Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA   Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
CC   -!- FUNCTION: Catalyzes the reversible retro-aldol cleavage of 4-hydroxy-2-
CC       oxovalerate to pyruvate and acetaldehyde. {ECO:0000305}.
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   -!- INDUCTION: By growth on ethylbenzene or biphenyl.
CC       {ECO:0000269|PubMed:9073078}.
CC   -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family. {ECO:0000305}.
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DR   EMBL; D78322; BAA18937.1; -; Genomic_DNA.
DR   EMBL; AB120955; BAC92717.1; -; Genomic_DNA.
DR   EMBL; CP000433; ABH00331.1; -; Genomic_DNA.
DR   PIR; JC6327; JC6327.
DR   RefSeq; WP_011600000.1; NC_008270.1.
DR   AlphaFoldDB; O05151; -.
DR   SMR; O05151; -.
DR   EnsemblBacteria; ABH00331; ABH00331; RHA1_ro10138.
DR   KEGG; rha:RHA1_ro10138; -.
DR   HOGENOM; CLU_059964_1_0_11; -.
DR   OMA; WNRVDDY; -.
DR   UniPathway; UPA00155; -.
DR   Proteomes; UP000008710; Plasmid pRHL2.
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   2: Evidence at transcript level;
KW   Aromatic hydrocarbons catabolism; Lyase; Magnesium; Metal-binding; Plasmid;
KW   Reference proteome.
FT   CHAIN           1..258
FT                   /note="4-hydroxy-2-oxovalerate aldolase"
FT                   /id="PRO_0000207097"
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   258 AA;  27159 MW;  A539C46C4DA0190F CRC64;
     MQSPINSFKK ALAEGRTQIG FWLALGDAYS AEVCAGAGFD WLLIDGEHAP QDLRSVLAQL
     QVIGAYRDCH AAVRVPSADT TVIKQYLDLG AQSLLVPMVD TADEAAAVVR ACRYPPGGIR
     GVGGARASRW GRYPRYLHEA DEQVCVVVQA ETALALSNLE AIAEVDGIDG VFIGTADLAA
     SLGFPGNPAH PEVQDAILDA LQRVRAAGKA PGVLTPVEDL AQKYLAHGAV FVAVGIDTHL
     LAKQTSALAA RFAQVAYS