ID A0A069IAE1_9BURK Unreviewed; 350 AA.
AC A0A069IAE1;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=4-hydroxy-2-oxovalerate aldolase {ECO:0000256|HAMAP-Rule:MF_01656};
DE Short=HOA {ECO:0000256|HAMAP-Rule:MF_01656};
DE EC=4.1.3.39 {ECO:0000256|HAMAP-Rule:MF_01656};
DE AltName: Full=4-hydroxy-2-keto-pentanoic acid aldolase {ECO:0000256|HAMAP-Rule:MF_01656};
DE AltName: Full=4-hydroxy-2-oxopentanoate aldolase {ECO:0000256|HAMAP-Rule:MF_01656};
GN ORFNames=CF70_007295 {ECO:0000313|EMBL:KDP86473.1};
OS Cupriavidus sp. SK-3.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=1470558 {ECO:0000313|EMBL:KDP86473.1, ECO:0000313|Proteomes:UP000023560};
RN [1] {ECO:0000313|EMBL:KDP86473.1, ECO:0000313|Proteomes:UP000023560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK-3 {ECO:0000313|EMBL:KDP86473.1,
RC ECO:0000313|Proteomes:UP000023560};
RA Vilo C., Benedik M.J., Ilori M., Dong Q.;
RT "Cupriavidus sp. strain SK-3.";
RL Submitted (MAY-2014) 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:0000256|HAMAP-
CC Rule:MF_01656};
CC -!- SIMILARITY: Belongs to the 4-hydroxy-2-oxovalerate aldolase family.
CC {ECO:0000256|ARBA:ARBA00008944, ECO:0000256|HAMAP-Rule:MF_01656}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KDP86473.1}.
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DR EMBL; JFJV02000159; KDP86473.1; -; Genomic_DNA.
DR RefSeq; WP_035866694.1; NZ_JFJV02000159.1.
DR AlphaFoldDB; A0A069IAE1; -.
DR OrthoDB; 9803573at2; -.
DR Proteomes; UP000023560; Unassembled WGS sequence.
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; 1.10.8.60; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 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 NCBIfam; TIGR03217; 4OH_2_O_val_ald; 1.
DR PANTHER; PTHR10277:SF9; 2-ISOPROPYLMALATE SYNTHASE 1, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR10277; HOMOCITRATE SYNTHASE-RELATED; 1.
DR Pfam; PF07836; DmpG_comm; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF89000; post-HMGL domain-like; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Aromatic hydrocarbons catabolism {ECO:0000256|ARBA:ARBA00022797,
KW ECO:0000256|HAMAP-Rule:MF_01656};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01656};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01656};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01656}.
FT DOMAIN 10..262
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT ACT_SITE 22
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT BINDING 18..19
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT BINDING 19
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT BINDING 201
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT BINDING 201
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT BINDING 203
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT BINDING 292
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT SITE 18
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
SQ SEQUENCE 350 AA; 37661 MW; 792821CA46DFE006 CRC64;
MTQQATQKKL YISDVTLRDG SHAIRHQYSL DDVRRIAAAL DAARVDSIEV AHGDGLAGSS
FNYGFGAHTD LEWIAAAAET VRHAKVATLL LPGVGTVHDL RAAYDAGARV VRVATHCTEA
DVSRQHIEYA RELGMDTVGF LMMSHMTTPA ALAQQARLME SFGAQTVYVV DSGGALNMND
VRDRFRAFKD VLKPETQTGM HAHHNLSLGV ANSIVAVEEG CDRVDASLAG MGAGAGNAPL
EVFIAAASRL GWHHGCDLYT LMDAADEIVR PLQDRPVRVD RETLALGYAG VYSSFLRHAE
AAAARYALKT VDILVELGKR RMVGGQEDMI VDVALDLVAR REAGATRIAA
//
