HOA2_PSEFK
ID HOA2_PSEFK Reviewed; 346 AA.
AC Q52040;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=4-hydroxy-2-oxovalerate aldolase 2 {ECO:0000255|HAMAP-Rule:MF_01656};
DE Short=HOA 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01656};
DE AltName: Full=4-hydroxy-2-oxopentanoate aldolase 2 {ECO:0000255|HAMAP-Rule:MF_01656};
GN Name=bphX3;
OS Pseudomonas furukawaii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas;
OC Pseudomonas oleovorans/pseudoalcaligenes group.
OX NCBI_TaxID=1149133;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 10086 / NBRC 110670 / KF707;
RX PubMed=9190809; DOI=10.1128/jb.179.12.3936-3943.1997;
RA Kimura N., Nishi A., Goto M., Furukawa K.;
RT "Functional analyses of a variety of chimeric dioxygenases constructed from
RT two biphenyl dioxygenases that are similar structurally but different
RT functionally.";
RL J. Bacteriol. 179:3936-3943(1997).
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; D85853; BAA12886.1; -; Genomic_DNA.
DR RefSeq; WP_003450974.1; NZ_AP014862.1.
DR AlphaFoldDB; Q52040; -.
DR SMR; Q52040; -.
DR STRING; 1149133.ppKF707_3396; -.
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..346
FT /note="4-hydroxy-2-oxovalerate aldolase 2"
FT /id="PRO_0000387881"
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; 36798 MW; BD4A951D513C97CE CRC64;
MKLEGKKVTV HDMTLRDGMH PKRHQMTLEQ MKSIACGLDA AGIPLIEVTH GDGLGGSSVN
YGFPAHSDEE YLGAVIPLMK QAKVSALLLP GIGTVEHLKM AKDLGVNTIR VATHCTEADV
SEQHITQSRK LGLDTVGFLM MAHMASPEKL VSQALLMQGY GANCIYVTDS AGYMLPDDVK
ARLSAVRAAL KPETELGFHG HHNLAMGVAN SIAAIEAGAT RIDAAAAGLG AGAGNTPMEV
FIAVCARMGI ETGVDVFKIQ DVAEDLVVPI MDHVIRIDRD SLTLGYAGVY SSFLLFAKRA
SAKYGVPARD ILVELGRRGM VGGQEDMIED TAMTMARERG LTLTAA
