HOA_ECOLI
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 03-AUG-2022, entry version 146.
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; Proteobacteria; 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; P51020; -.
DR PRIDE; P51020; -.
DR EnsemblBacteria; AAC73455; AAC73455; b0352.
DR EnsemblBacteria; BAE76134; BAE76134; BAE76134.
DR GeneID; 66671344; -.
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; DLYKMMD; -.
DR PhylomeDB; P51020; -.
DR BioCyc; EcoCyc:MHPELY-MON; -.
DR BioCyc; MetaCyc:MHPELY-MON; -.
DR UniPathway; UPA00714; -.
DR PRO; PR:P51020; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; 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 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
