HOA5_RHOOB
ID HOA5_RHOOB Reviewed; 352 AA.
AC C1AYB4;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=4-hydroxy-2-oxovalerate aldolase 5 {ECO:0000255|HAMAP-Rule:MF_01656};
DE Short=HOA 5 {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 5 {ECO:0000255|HAMAP-Rule:MF_01656};
DE AltName: Full=4-hydroxy-2-oxopentanoate aldolase 5 {ECO:0000255|HAMAP-Rule:MF_01656};
GN OrderedLocusNames=ROP_58620;
OS Rhodococcus opacus (strain B4).
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; AP011115; BAH54109.1; -; Genomic_DNA.
DR RefSeq; WP_015889603.1; NC_012522.1.
DR AlphaFoldDB; C1AYB4; -.
DR SMR; C1AYB4; -.
DR STRING; 632772.ROP_58620; -.
DR EnsemblBacteria; BAH54109; BAH54109; ROP_58620.
DR KEGG; rop:ROP_58620; -.
DR PATRIC; fig|632772.20.peg.6125; -.
DR HOGENOM; CLU_049173_0_0_11; -.
DR OMA; TVNIMAI; -.
DR OrthoDB; 840579at2; -.
DR Proteomes; UP000002212; Chromosome.
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.
FT CHAIN 1..352
FT /note="4-hydroxy-2-oxovalerate aldolase 5"
FT /id="PRO_0000387896"
FT DOMAIN 9..261
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT ACT_SITE 21
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 17..18
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 18
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 200
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 202
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 291
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT SITE 17
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
SQ SEQUENCE 352 AA; 36903 MW; 2EF12C5AFAC85F59 CRC64;
MPYSADLDIR VTDSSLRDGS HAKRHQFTVE HVRSIVGALD AAGVPVIEVT HGDGLGGSSF
NYGFSHTPEQ ELIKAAVETA EQAKIAFLML PGLGVRSDIR EAADNGASIC RIATHCTEAD
ISVQHFGLAR DLGLETVGFL MMSHSQPPEV LAKQARIMAD AGCQCVYVVD SAGALILNAV
SDRVSALVAE LGDDAQVGFH GHENLGLGVA NSVLAVEAGA LQIDGSTRRF GAGAGNTPVE
AFAAVTEKLG IRTGIDTLKI IDAAEDVVRP IMDGDCLLDR LSLTMGYAGV YSSFLKHADS
HASRYGVSGA EILIEAGRRK LVGGQEDQLI EIALGLADRK SAETAVAEKK SA
