HOA1_PSEPU
ID HOA1_PSEPU Reviewed; 346 AA.
AC P51017;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=nahM;
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OG Plasmid pWW60-22.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 8368 / NCIMB 9816 / PG;
RX PubMed=7496535; DOI=10.1099/13500872-141-9-2223;
RA Platt A., Shingler V., Taylor S.C., Williams P.A.;
RT "The 4-hydroxy-2-oxovalerate aldolase and acetaldehyde dehydrogenase
RT (acylating) encoded by the nahM and nahO genes of the naphthalene catabolic
RT plasmid pWW60-22 provide further evidence of conservation of meta-cleavage
RT pathway gene sequences.";
RL Microbiology 141:2223-2233(1995).
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 -!- PATHWAY: Aromatic compound metabolism; naphthalene degradation.
CC -!- SIMILARITY: Belongs to the 4-hydroxy-2-oxovalerate aldolase family.
CC {ECO:0000255|HAMAP-Rule:MF_01656, ECO:0000305}.
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DR EMBL; U13232; AAA89107.1; -; Genomic_DNA.
DR RefSeq; NP_863098.1; NC_004999.1.
DR RefSeq; WP_011117426.1; NC_004999.1.
DR AlphaFoldDB; P51017; -.
DR SMR; P51017; -.
DR BRENDA; 4.1.3.39; 5092.
DR UniPathway; UPA00082; -.
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..346
FT /note="4-hydroxy-2-oxovalerate aldolase"
FT /id="PRO_0000096706"
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 346 AA; 37102 MW; 65963EE93E4BAB7F CRC64;
MNLHGKSVIL HDMSLRDGMH AKRHQISLEQ MVAVATGLDQ AGMPLIEITH GDGLGGRSIN
YGFPAHSDEE YLRAVIPQLK QAKVSALLLP GIGTVDHLKM ALDCGVSTIR VATHCTEADV
SEQHIGMARK LGVDTVGFLM MAHMISAEKV LEQAKLMESY GANCIYCTDS AGYMLPDEVS
EKIGLLRAEL NPATEVGFHG HHNMGMAIAN SLAAIEAGAA RIDGSVAGLG AGAGNTPLEV
FVAVCKRMGV ETGIDLYKIM DVAEDLVVPM MDQPIRVDRD ALTLGYAGVY SSFLLFAQRA
EKKYGVSARD ILVELGRRGT VGGQEDMIED LALDMARARQ QQKVSA
