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Database: UniProt
Entry: F8T7H8_9PSED
LinkDB: F8T7H8_9PSED
Original site: F8T7H8_9PSED 
ID   F8T7H8_9PSED            Unreviewed;       346 AA.
AC   F8T7H8;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 43.
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   Name=xyl-likeK {ECO:0000313|EMBL:AEI87378.1};
OS   Pseudomonas sp. OX1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=320855 {ECO:0000313|EMBL:AEI87378.1};
RN   [1] {ECO:0000313|EMBL:AEI87378.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=OX1 {ECO:0000313|EMBL:AEI87378.1};
RX   PubMed=23009925; DOI=10.1016/j.biochi.2012.09.018;
RA   Bertini L., Cafaro V., Proietti S., Caporale C., Capasso P., Caruso C.,
RA   Di Donato A.;
RT   "Deepening TOL and TOU catabolic pathways of Pseudomonas sp. OX1: cloning,
RT   sequencing and characterization of the lower pathways.";
RL   Biochimie 95:241-250(2013).
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}.
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DR   EMBL; HQ713510; AEI87378.1; -; Genomic_DNA.
DR   AlphaFoldDB; F8T7H8; -.
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          8..260
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   ACT_SITE        20
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT   BINDING         16..17
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT   BINDING         17
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT   BINDING         170
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT   BINDING         199
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT   BINDING         199
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         290
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT   SITE            16
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
SQ   SEQUENCE   346 AA;  37119 MW;  7F95766B91E7DA37 CRC64;
     MNLQGKNVTL HDMSLRDGMH AKRHQISLEQ MIAVATGLDA AGMPLIEITH GDGLGGRSIN
     YGFPAHSDEE YLRAVIPRLK QAKVSALLLP GIGTVDHLKV ALDCGVSTIR VATHCTEADV
     SEQHIGMSRK LGADTVGFLM MAHMISAEKV LEQARLMESY GANCIYCTDS AGYMLPDEVS
     EKIGLLRAEL NPATEIGFHG HHNMGMAIAN SLAAIEAGAS RIDGSVAGLG AGAGNTPLEV
     FVAVCKRMGV ETGIDLYKIM DVAEDIVVPM MDQPIRVDRD ALTLGYAGVY SSFLLFAQRA
     EKKYGVPARD ILVELGRRGT VGGQEDMIED LALDMSRARQ NQKVSA
//
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