HOA_PSESP
ID HOA_PSESP Reviewed; 343 AA.
AC Q9KWS0;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=4-hydroxy-2-oxovalerate aldolase {ECO:0000255|HAMAP-Rule:MF_01656};
DE Short=HOA {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 {ECO:0000255|HAMAP-Rule:MF_01656};
DE AltName: Full=4-hydroxy-2-oxopentanoate aldolase {ECO:0000255|HAMAP-Rule:MF_01656};
GN Name=amnG;
OS Pseudomonas sp.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=306;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=AP-3;
RX PubMed=9169437; DOI=10.1074/jbc.272.23.14727;
RA Takenaka S., Murakami S., Shinke R., Hatakeyama K., Yukawa H., Aoki K.;
RT "Novel genes encoding 2-aminophenol 1,6-dioxygenase from Pseudomonas
RT species AP-3 growing on 2-aminophenol and catalytic properties of the
RT purified enzyme.";
RL J. Biol. Chem. 272:14727-14732(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AP-3;
RX PubMed=11081795; DOI=10.1007/s002030000203;
RA Takenaka S., Murakami S., Kim Y.J., Aoki K.;
RT "Complete nucleotide sequence and functional analysis of the genes for 2-
RT aminophenol metabolism from Pseudomonas sp. AP-3.";
RL Arch. Microbiol. 174:265-272(2000).
CC -!- FUNCTION: Catalyzes the retro-aldol cleavage of 4-hydroxy-2-
CC oxopentanoate to pyruvate and acetaldehyde. Is involved in the meta-
CC cleavage pathway for the degradation of 2-aminophenol.
CC {ECO:0000269|PubMed:9169437}.
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, ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB020521; BAB03538.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9KWS0; -.
DR SMR; Q9KWS0; -.
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..343
FT /note="4-hydroxy-2-oxovalerate aldolase"
FT /id="PRO_0000383026"
FT DOMAIN 8..260
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT ACT_SITE 20
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 16..17
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 17
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 199
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 199
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 290
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT SITE 16
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
SQ SEQUENCE 343 AA; 37065 MW; CC41F08DD42D9ADE CRC64;
MIDQAKKIYI SDVTLRDGMH AIRHRYTLNH VSQIARALDE AGVDSIEVAH GDGLKGSSFN
YGFGAYSDLE WISAAAEAVK QAKIATLLLP GIGTVHDLRE AYDAGARVVR VATHCTEADV
SRQHIEYARG LGMDTVGFLM MSHMQTPVGL AQQAKLMENY GAQCIYVVDS GGAMNMWDIA
ERFKALKDVL DPATQTGMHA HHNLSLGVAN SLVALENGCD RVDASLTGMG AGAGNAPLEV
FIAAAERMGL NHGCDVKKLI NAAEDIVRPL QERPVRVDRE TLALGYAGVY SSFLRHAETA
AKKYNLSAFD ILVELGKRRM IGGQEDMIVD VALDMAKGRV LPT
