HOA_PSES1
ID HOA_PSES1 Reviewed; 352 AA.
AC P51014;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 65.
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=bphF;
OS Pseudomonas sp. (strain KKS102).
OC Bacteria; Proteobacteria.
OX NCBI_TaxID=307;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8021212; DOI=10.1128/jb.176.14.4269-4276.1994;
RA Kikuchi Y., Yasukochi Y., Nagata Y., Fukuda M., Takagi M.;
RT "Nucleotide sequence and functional analysis of the meta-cleavage pathway
RT involved in biphenyl and polychlorinated biphenyl degradation in
RT Pseudomonas sp. strain KKS102.";
RL J. Bacteriol. 176:4269-4276(1994).
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: Xenobiotic degradation; biphenyl degradation.
CC -!- SIMILARITY: Belongs to the 4-hydroxy-2-oxovalerate aldolase family.
CC {ECO:0000255|HAMAP-Rule:MF_01656}.
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DR EMBL; D16407; BAA03893.1; -; Genomic_DNA.
DR PIR; C55511; C55511.
DR AlphaFoldDB; P51014; -.
DR SMR; P51014; -.
DR PRIDE; P51014; -.
DR UniPathway; UPA00155; -.
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"
FT /id="PRO_0000064977"
FT DOMAIN 6..258
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT ACT_SITE 18
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 14..15
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 15
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 197
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 197
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 288
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT SITE 14
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
SQ SEQUENCE 352 AA; 38264 MW; FE72890E9E6039E2 CRC64;
MTTKKIYISD VTLRDGSHAI RHQYSVEQVR TIAKELDEAK VDSIEVAHGS GLQGSSFNYG
FGAHTDLEWI EAVASVVKHA KIATLLLPGI GTIHDLKAAY DAGARIVRVA THCTEADISK
QHIEYARHLG MEAVGFLMMS HMSTPQGLAQ QAKLMESYGA TCCYVVDSGG ALSMDDVRMR
FRAFKDVLKP ETETGIHAHH NLSLGVANSI VAIEEGCDRV DASLAGMGAG AGNAPLEVFI
AAAERMGWHH GTELYKLMDA ADDIVRPLQD RPVRVDRETL ALGYAGVYSS FLRHSEAAAQ
KYGLKTMDIL VELGRRRMVG GQEDMIVDVA LDLLKSLEHE RIHAQPVSSE AG
