HOA2_CUPMC
ID HOA2_CUPMC Reviewed; 345 AA.
AC Q1LCQ8;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
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 OrderedLocusNames=Rmet_5209;
OS Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS CH34) (Ralstonia metallidurans).
OG Plasmid megaplasmid CH34.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=266264;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT master survivalist in harsh and anthropogenic environments.";
RL PLoS ONE 5:E10433-E10433(2010).
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; CP000353; ABF12068.1; -; Genomic_DNA.
DR RefSeq; WP_011519614.1; NC_007974.2.
DR AlphaFoldDB; Q1LCQ8; -.
DR SMR; Q1LCQ8; -.
DR STRING; 266264.Rmet_5209; -.
DR EnsemblBacteria; ABF12068; ABF12068; Rmet_5209.
DR KEGG; rme:Rmet_5209; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_049173_0_0_4; -.
DR OMA; WARENGM; -.
DR OrthoDB; 840579at2; -.
DR Proteomes; UP000002429; Plasmid megaplasmid CH34.
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;
KW Reference proteome.
FT CHAIN 1..345
FT /note="4-hydroxy-2-oxovalerate aldolase 2"
FT /id="PRO_0000387889"
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 345 AA; 36821 MW; 91591FB626827C6D CRC64;
MTDKKLYISD VTLRDGSHAI RHQYSVPQVR AIARALDAAG VDSIEVAHGD GLAGSSFNYG
FGAHTDVEWI AAVAESVQRA AVATLLLPGI GTVHDLREAY AAGARVVRVA THCTEADTAR
QHIETARSMG MNVAGFLMMS HMIPPDRLAG QAKLMESYGA HCVYVVDSGG ALTMDGVRAR
FRAFKDVLDP KTETGMHAHH NLSLGVANSI VAVEEGCDRI DASLAGMGAG AGNAPLEVFI
AAAERMGWHH GCDLYQLMDA ADDIVRPLQD RPVRVDRETL ALGYAGVYSS FLRHAESAAG
KYGLKTVDIL VELGRRRMVG GQEDMIVDVA LDLQRSGGAK SREAA