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