HOA2_NOVAD
ID HOA2_NOVAD Reviewed; 343 AA.
AC A4XDT6;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=Saro_3852;
OS Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CCUG
OS 56034 / CIP 105152 / NBRC 16084 / F199).
OG Plasmid pNL1.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=279238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700278 / DSM 12444 / CCUG 56034 / CIP 105152 / NBRC 16084 /
RC F199;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Han C., Thomson S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Ivanova N., Fredrickson J., Romine M.F., Richardson P.;
RT "Complete sequence of plasmid pNL1 of Novosphingobium aromaticivorans DSM
RT 12444.";
RL Submitted (APR-2007) 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: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; CP000676; ABP64097.1; -; Genomic_DNA.
DR RefSeq; WP_010891015.1; NC_009426.1.
DR AlphaFoldDB; A4XDT6; -.
DR SMR; A4XDT6; -.
DR EnsemblBacteria; ABP64097; ABP64097; Saro_3852.
DR KEGG; nar:Saro_3852; -.
DR HOGENOM; CLU_049173_0_0_5; -.
DR OMA; YVGGQED; -.
DR OrthoDB; 840579at2; -.
DR Proteomes; UP000009134; Plasmid pNL1.
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..343
FT /note="4-hydroxy-2-oxovalerate aldolase 2"
FT /id="PRO_0000387874"
FT DOMAIN 10..262
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT ACT_SITE 22
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 18..19
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 19
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 172
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 201
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 203
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 292
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT SITE 18
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
SQ SEQUENCE 343 AA; 36859 MW; 465022794BBCDCF9 CRC64;
MTFDPTSDRL YIQDVTLRDG MHAILHMYGT DSVRTIAKAL DEAGVDAIEV SHGDGLNGST
FNYGFGAHTD WDWIEAAADV IKNAVLTTLL VPGIGTAEEL KRAYSMGVRS VRVATHCTEA
DVGKQHIGIA RDLGMDVSGF LMMSHMIEPE ALAQQALLME SYGAHCVYVT DSGGALDMDG
VIARLQAYDR VLKPETQRGI HAHHNLSLGV ANSIVAAQAG AVRIDASLAG MGAGAGNAPL
EVFIAAANRK GWKHGCDVMA LMDAADDIIR PLQDRPVRVD RETLSLGYAG VYSSFLRHAE
KAAEQYGIDT REILVELGNR RMVGGQEDMI IDVALDLIKA KAN
