HOA1_PSEP1
ID HOA1_PSEP1 Reviewed; 352 AA.
AC P51018; A5W4E4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=4-hydroxy-2-oxovalerate aldolase 1 {ECO:0000255|HAMAP-Rule:MF_01656};
DE Short=HOA 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_01656};
DE AltName: Full=4-hydroxy-2-oxopentanoate aldolase 1 {ECO:0000255|HAMAP-Rule:MF_01656};
GN Name=todH; OrderedLocusNames=Pput_2873;
OS Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=351746;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8063106; DOI=10.1016/0378-1119(94)90827-3;
RA Lau P.C., Bergeron H., Labbe D., Wang Y., Brousseau R., Gibson D.T.;
RT "Sequence and expression of the todGIH genes involved in the last three
RT steps of toluene degradation by Pseudomonas putida F1.";
RL Gene 146:7-13(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700007 / DSM 6899 / BCRC 17059 / F1;
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 Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.;
RT "Complete sequence of Pseudomonas putida F1.";
RL Submitted (MAY-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 -!- PATHWAY: Xenobiotic degradation; toluene 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; U09250; AAA61944.1; -; Genomic_DNA.
DR EMBL; CP000712; ABQ79004.1; -; Genomic_DNA.
DR RefSeq; WP_012052593.1; NC_009512.1.
DR AlphaFoldDB; P51018; -.
DR SMR; P51018; -.
DR STRING; 351746.Pput_2873; -.
DR EnsemblBacteria; ABQ79004; ABQ79004; Pput_2873.
DR KEGG; ppf:Pput_2873; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_049173_0_0_6; -.
DR OMA; DLYKMMD; -.
DR OrthoDB; 840579at2; -.
DR BioCyc; MetaCyc:MON-11384; -.
DR UniPathway; UPA00273; -.
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:0042203; P:toluene catabolic process; IEA:UniProtKB-UniPathway.
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 1"
FT /id="PRO_0000072618"
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"
FT CONFLICT 64..65
FT /note="HT -> QS (in Ref. 1; AAA61944)"
FT /evidence="ECO:0000305"
FT CONFLICT 79..80
FT /note="HA -> AS (in Ref. 1; AAA61944)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="R -> G (in Ref. 1; AAA61944)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="S -> T (in Ref. 1; AAA61944)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 352 AA; 38474 MW; 967194FA65C4441A CRC64;
MTQQKLYISD VTLRDGSHAI RHQYTVEQVK QIARALDDAK VDSIEVAHGD GLQGGSFNYG
FGAHTDLEWI EAAASVVKHA KIATLLLPGI GTVHDLKAVY EAGVRVVRVA THCTEADISR
QHIEYARHLG MEAVGFLMMS HMTTPQHLAQ QAKLMESYGA TVCYVVDSGG ALSMNDVRDR
FRAFKDVLKP ETQTGMHAHH NLSLGVANSI VAVENGCDRV DASLAGMGAG AGNAPLEVFI
AAAERMGWNH GTDLYKLMDA ADDLVRPLQD RPVRVDRETL ALGYAGVYSS FLRHSEMAAS
KYGLKTVDIL VELGRRRMVG GQEDMIIDVA LDLLKQQEHE RIRSEPVSSE AN
