ID   HOA6_RHOJR              Reviewed;         354 AA.
AC   Q0RXC3;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=4-hydroxy-2-oxovalerate aldolase 6 {ECO:0000255|HAMAP-Rule:MF_01656};
DE            Short=HOA 6 {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 6 {ECO:0000255|HAMAP-Rule:MF_01656};
DE   AltName: Full=4-hydroxy-2-oxopentanoate aldolase 6 {ECO:0000255|HAMAP-Rule:MF_01656};
GN   OrderedLocusNames=RHA1_ro09019;
OS   Rhodococcus jostii (strain RHA1).
OG   Plasmid pRHL1.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=101510;
RN   [1]
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   -!- 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; CP000432; ABH00063.1; -; Genomic_DNA.
DR   RefSeq; WP_011599739.1; NC_008269.1.
DR   AlphaFoldDB; Q0RXC3; -.
DR   SMR; Q0RXC3; -.
DR   PRIDE; Q0RXC3; -.
DR   EnsemblBacteria; ABH00063; ABH00063; RHA1_ro09019.
DR   KEGG; rha:RHA1_ro09019; -.
DR   PATRIC; fig|101510.16.peg.8302; -.
DR   HOGENOM; CLU_049173_0_0_11; -.
DR   OMA; YVGGQED; -.
DR   Proteomes; UP000008710; Plasmid pRHL1.
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;
KW   Reference proteome.
FT   CHAIN           1..354
FT                   /note="4-hydroxy-2-oxovalerate aldolase 6"
FT                   /id="PRO_0000387902"
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   354 AA;  37880 MW;  FEDCF28D05142B8F CRC64;
     MTRPELRDDV RIVDTTLRDG SHAQSHQFTE SQVRDTVRAL DGAGVEVIEV THGDGLGGST
     FNYGFSRISD LELVQVAADT AEQAKIAVLL VPGIGTADDL RKAADRGAEV VRIATHCTEA
     DVSLQHFEIA RDLGMQTCGF LMMAHRTTPE ELARQARLMV DAGCQVPYVT DSAGALLMHE
     AKDRFDALIT EVGDDAWVGY HGHQNMSLGV ANSVIAYEAG VRYIDGSLCA LGAGAGNSPT
     ELLAAIFDRM NIATGLDVMA TLDAAETVVR PYLNRWPKID RNAIVQGWVG VYSSFLLHAE
     TAGARYGVPV HEILRRCGEL GYVGGQEDMI IDVAIQLAKV SGTVSEPSAS LVAG