ID MHPE_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 16-JUN-2009, entry version 63. DE RecName: Full=4-hydroxy-2-oxovalerate aldolase; DE Short=HOA; DE EC=4.1.3.39; DE AltName: Full=4-hydroxy-2-keto-pentanoic acid aldolase; GN Name=mhpE; Synonyms=mhpF; OrderedLocusNames=b0352, JW0343; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; 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.; 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 MEDLINE=97426617; 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., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(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 RT MG1655 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; 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 RT Escherichia coli."; RL Biochem. Biophys. Res. Commun. 346:1009-1015(2006). CC -!- FUNCTION: Catalyzes the fission of 4-hydroxy-2-ketovalerate to CC yield pyruvate and acetaldehyde. CC -!- CATALYTIC ACTIVITY: 4-hydroxy-2-oxopentanoate = acetaldehyde + CC pyruvate. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 6.25-6.75; CC -!- PATHWAY: Aromatic compound metabolism; 3-phenylpropionic acid CC degradation. CC -!- SUBUNIT: Interacts with mhpF. CC -!- INTERACTION: CC P77580:mhpF; NbExp=1; IntAct=EBI-1116093, EBI-1116083; CC -!- MISCELLANEOUS: Presumably stereoselective for the 4S-enantiomer of CC 4-hydroxy-2-ketovalerate. CC -!- SIMILARITY: Belongs to the mhpE aldolase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- 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; AP_001004.1; -. DR RefSeq; NP_414886.1; -. DR HSSP; P51016; 1NVM. DR SMR; P51020; 4-333. DR IntAct; P51020; 10. DR GeneID; 945012; -. DR GenomeReviews; AP009048_GR; JW0343. DR GenomeReviews; U00096_GR; b0352. DR KEGG; ecj:JW0343; -. DR KEGG; eco:b0352; -. DR EchoBASE; EB3077; -. DR EcoGene; EG13292; mhpE. DR HOGENOM; P51020; -. DR OMA; P51020; ATCVYVV. DR BioCyc; EcoCyc:MHPELY-MON; -. DR BioCyc; MetaCyc:MHPELY-MON; -. DR GO; GO:0008701; F:4-hydroxy-2-oxovalerate aldolase activity; IEA:HAMAP. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:HAMAP. DR HAMAP; MF_01656; -; 1. DR InterPro; IPR017629; 4OH_2_O-val_aldolase. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR012425; DmpG_comm. DR InterPro; IPR000891; PYR_CT. DR Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1. 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; Complete proteome; Lyase. FT CHAIN 1 337 4-hydroxy-2-oxovalerate aldolase. FT /FTId=PRO_0000096470. 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 //