ID A0A0B8ZZR0_9SPHN Unreviewed; 343 AA.
AC A0A0B8ZZR0;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
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=NJ75_03643 {ECO:0000313|EMBL:KHS43824.1};
OS Novosphingobium subterraneum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=48936 {ECO:0000313|EMBL:KHS43824.1, ECO:0000313|Proteomes:UP000031338};
RN [1] {ECO:0000313|EMBL:KHS43824.1, ECO:0000313|Proteomes:UP000031338}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12447 {ECO:0000313|EMBL:KHS43824.1,
RC ECO:0000313|Proteomes:UP000031338};
RA Gan H.M., Gan H.Y., Savka M.A.;
RT "Draft genome sequence of Novosphingobium subterraneum DSM 12447.";
RL Submitted (OCT-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:KHS43824.1}.
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DR EMBL; JRVC01000021; KHS43824.1; -; Genomic_DNA.
DR RefSeq; WP_039336977.1; NZ_JRVC01000021.1.
DR AlphaFoldDB; A0A0B8ZZR0; -.
DR STRING; 48936.NJ75_03643; -.
DR PATRIC; fig|48936.3.peg.3675; -.
DR Proteomes; UP000031338; 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|HAMAP-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 343 AA; 36994 MW; D681BCEC3A1F239E CRC64;
MTFNPESDRL YIQDVTLRDG MHAILHMYGT DSVRTIAKAL DDAGVDAIEV SHGDGLNGST
FNYGFGAHTD WDWIEAAADV IKNAVLTTLL VPGIGTAEEL KRAYSMGVRS VRVATHCTEA
DVGKQHIGIA RDLGMDVSGF LMMSHMIEPE ALAQQALLME SYGAQCVYVT DSGGALDMDG
VTARLQAYDR VLKPETQRGI HAHHNLSLGV ANSIVAAQAG AVRIDASLAG MGAGAGNAPL
EVFIAAANRK GWKHRCDVMA LMDAADDIIR PLQDRPVRVD RETLSLGYAG VYSSFLRHAE
KASEQYGIDT REILVELGNR RMVGGQEDMI IDVALDLIKA RAN
//