ID   HOA_ECOLI               Reviewed;         337 AA.
AC   P51020; P77787; Q2MC72;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   27-MAR-2024, entry version 154.
DE   RecName: Full=4-hydroxy-2-oxovalerate aldolase {ECO:0000255|HAMAP-Rule:MF_01656};
DE            Short=HOA {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 {ECO:0000255|HAMAP-Rule:MF_01656};
DE   AltName: Full=4-hydroxy-2-oxopentanoate aldolase {ECO:0000255|HAMAP-Rule:MF_01656};
GN   Name=mhpE {ECO:0000255|HAMAP-Rule:MF_01656};
GN   OrderedLocusNames=b0352, JW0343;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA   Kawamukai M.;
RT   "Complete sequence of the mhp operon.";
RL   Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RA   Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA   Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA   Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT   "Sequence of minutes 4-25 of Escherichia coli.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 95-337.
RC   STRAIN=K12;
RA   Nashimoto H., Saito N.;
RL   Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, AND SUBSTRATE SPECIFICITY.
RX   PubMed=9758851; DOI=10.1128/aem.64.10.4093-4094.1998;
RA   Pollard J.R., Rialland D., Bugg T.D.;
RT   "Substrate selectivity and biochemical properties of 4-hydroxy-2-keto-
RT   pentanoic acid aldolase from Escherichia coli.";
RL   Appl. Environ. Microbiol. 64:4093-4094(1998).
RN   [7]
RP   INTERACTION WITH MHPF.
RX   PubMed=16782065; DOI=10.1016/j.bbrc.2006.06.009;
RA   Lee S.J., Ko J.H., Kang H.Y., Lee Y.;
RT   "Coupled expression of MhpE aldolase and MhpF dehydrogenase in Escherichia
RT   coli.";
RL   Biochem. Biophys. Res. Commun. 346:1009-1015(2006).
CC   -!- FUNCTION: Catalyzes the retro-aldol cleavage of 4-hydroxy-2-
CC       oxopentanoate to pyruvate and acetaldehyde. Is involved in the meta-
CC       cleavage pathway for the degradation of 3-phenylpropanoate.
CC       {ECO:0000269|PubMed:9758851}.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.25-6.75. {ECO:0000269|PubMed:9758851};
CC   -!- PATHWAY: Aromatic compound metabolism; 3-phenylpropanoate degradation.
CC       {ECO:0000255|HAMAP-Rule:MF_01656}.
CC   -!- SUBUNIT: Interacts with MhpF. {ECO:0000255|HAMAP-Rule:MF_01656,
CC       ECO:0000269|PubMed:16782065}.
CC   -!- MISCELLANEOUS: Presumably stereoselective for the 4S-enantiomer of 4-
CC       hydroxy-2-ketovalerate.
CC   -!- SIMILARITY: Belongs to the 4-hydroxy-2-oxovalerate aldolase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01656, ECO:0000305}.
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DR   EMBL; D86239; BAA13057.1; -; Genomic_DNA.
DR   EMBL; U73857; AAB18076.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73455.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76134.1; -; Genomic_DNA.
DR   EMBL; D85613; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; H64762; H64762.
DR   RefSeq; NP_414886.1; NC_000913.3.
DR   RefSeq; WP_001013499.1; NZ_SSZK01000061.1.
DR   AlphaFoldDB; P51020; -.
DR   SMR; P51020; -.
DR   BioGRID; 4261624; 13.
DR   BioGRID; 849406; 1.
DR   DIP; DIP-10209N; -.
DR   IntAct; P51020; 11.
DR   STRING; 511145.b0352; -.
DR   PaxDb; 511145-b0352; -.
DR   EnsemblBacteria; AAC73455; AAC73455; b0352.
DR   GeneID; 75202515; -.
DR   GeneID; 945012; -.
DR   KEGG; ecj:JW0343; -.
DR   KEGG; eco:b0352; -.
DR   PATRIC; fig|1411691.4.peg.1926; -.
DR   EchoBASE; EB3077; -.
DR   eggNOG; COG0119; Bacteria.
DR   HOGENOM; CLU_049173_0_0_6; -.
DR   InParanoid; P51020; -.
DR   OMA; IHAHNNQ; -.
DR   OrthoDB; 9803573at2; -.
DR   PhylomeDB; P51020; -.
DR   BioCyc; EcoCyc:MHPELY-MONOMER; -.
DR   BioCyc; MetaCyc:MHPELY-MONOMER; -.
DR   UniPathway; UPA00714; -.
DR   PRO; PR:P51020; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0003852; F:2-isopropylmalate synthase activity; IBA:GO_Central.
DR   GO; GO:0008701; F:4-hydroxy-2-oxovalerate aldolase activity; IDA:EcoCyc.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019380; P:3-phenylpropionate catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009098; P:leucine biosynthetic process; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; Lyase; Manganese; Metal-binding;
KW   Reference proteome.
FT   CHAIN           1..337
FT                   /note="4-hydroxy-2-oxovalerate aldolase"
FT                   /id="PRO_0000096470"
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   337 AA;  36470 MW;  EDA263721721212F CRC64;
     MNGKKLYISD VTLRDGMHAI RHQYSLENVR QIAKALDDAR VDSIEVAHGD GLQGSSFNYG
     FGAHSDLEWI EAAADVVKHA KIATLLLPGI GTIHDLKNAW QAGARVVRVA THCTEADVSA
     QHIQYARELG MDTVGFLMMS HMTTPENLAK QAKLMEGYGA TCIYVVDSGG AMNMSDIRDR
     FRALKAELKP ETQTGMHAHH NLSLGVANSI AAVEEGCDRI DASLAGMGAG AGNAPLEVFI
     AAADKLGWQH GTDLYALMDA ADDLVRPLQD RPVRVDRETL ALGYAGVYSS FLRHCETAAA
     RYGLSAVDIL VELGKRRMVG GQEDMIVDVA LDLRNNK
//