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HOA6_RHOOB
ID   HOA6_RHOOB              Reviewed;         339 AA.
AC   C1BE28;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=ROP_pROB02-02240;
OS   Rhodococcus opacus (strain B4).
OG   Plasmid pROB02.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=632772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4;
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT   PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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; AP011117; BAH47231.1; -; Genomic_DNA.
DR   RefSeq; WP_012687257.1; NC_012521.1.
DR   AlphaFoldDB; C1BE28; -.
DR   SMR; C1BE28; -.
DR   EnsemblBacteria; BAH47231; BAH47231; ROP_pROB02-02240.
DR   KEGG; rop:ROP_pROB02-02240; -.
DR   PATRIC; fig|632772.20.peg.8608; -.
DR   HOGENOM; CLU_049173_0_0_11; -.
DR   OMA; DVIVPMM; -.
DR   OrthoDB; 840579at2; -.
DR   Proteomes; UP000002212; Plasmid pROB02.
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..339
FT                   /note="4-hydroxy-2-oxovalerate aldolase 6"
FT                   /id="PRO_0000387900"
FT   DOMAIN          5..257
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   ACT_SITE        17
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         13..14
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         14
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         167
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         196
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         196
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         198
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         287
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   SITE            13
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
SQ   SEQUENCE   339 AA;  36113 MW;  874C017DDAC8E034 CRC64;
     MTTRLFIQDV TLRDGMHAVR HRITPDDVGK IVAALDAAGV DGIEVAHGDG LAGGSLNYGP
     GSNTDWEWIE AAAANLTHAR LTTLLLPGIG TIAELEHAFR LGVRSVRVAT HCTEADVAAQ
     HIGKARELGM DVSGFLMMSH MTTAPELAAQ AKLMESYGAH CVYVTDSGGR LTMDGVRDRV
     RAYRDVLDEG TEIGIHAHEN LSLSVANSVV AVEEGVTRVD ASLAGHGAGA GNCPIEPFIA
     VADLQGWKHN SALFALQDAA DDLVRPLQDR PVRVDRETLT LGYAGVYSSF LRHAEAASQR
     YGIDVRTILL EVGRRGLVGG QEDLIVDIAL DLRSRAGGN
 
 
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