(data stored in ACNUC7421 zone)

SWISSPROT: HOA_ECO57

ID   HOA_ECO57               Reviewed;         337 AA.
AC   Q8X5J8; Q7AH49;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   30-AUG-2017, entry version 97.
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=Z0452, ECs0407;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Catalyzes the retro-aldol cleavage of 4-hydroxy-2-
CC       oxopentanoate to pyruvate and acetaldehyde. Is involved in the
CC       meta-cleavage pathway for the degradation of aromatic compounds.
CC       {ECO:0000255|HAMAP-Rule:MF_01656}.
CC   -!- CATALYTIC ACTIVITY: (S)-4-hydroxy-2-oxopentanoate = acetaldehyde +
CC       pyruvate. {ECO:0000255|HAMAP-Rule:MF_01656}.
CC   -!- PATHWAY: Aromatic compound metabolism; 3-phenylpropanoate
CC       degradation. {ECO:0000255|HAMAP-Rule:MF_01656}.
CC   -!- SUBUNIT: Interacts with MhpF. {ECO:0000255|HAMAP-Rule:MF_01656}.
CC   -!- SIMILARITY: Belongs to the 4-hydroxy-2-oxovalerate aldolase
CC       family. {ECO:0000255|HAMAP-Rule:MF_01656}.
DR   EMBL; AE005174; AAG54703.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33830.1; -; Genomic_DNA.
DR   PIR; C85530; C85530.
DR   PIR; G90679; G90679.
DR   RefSeq; NP_308434.1; NC_002695.1.
DR   RefSeq; WP_001013510.1; NZ_MWVM01000022.1.
DR   ProteinModelPortal; Q8X5J8; -.
DR   SMR; Q8X5J8; -.
DR   STRING; 155864.Z0452; -.
DR   EnsemblBacteria; AAG54703; AAG54703; Z0452.
DR   EnsemblBacteria; BAB33830; BAB33830; BAB33830.
DR   GeneID; 914509; -.
DR   KEGG; ece:Z0452; -.
DR   KEGG; ecs:ECs0407; -.
DR   PATRIC; fig|386585.9.peg.502; -.
DR   eggNOG; ENOG4105DF3; Bacteria.
DR   eggNOG; COG0119; LUCA.
DR   HOGENOM; HOG000048047; -.
DR   KO; K01666; -.
DR   UniPathway; UPA00714; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0008701; F:4-hydroxy-2-oxovalerate aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019380; P:3-phenylpropionate 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   ProDom; PD005364; DmpG_comm; 1.
DR   TIGRFAMs; TIGR03217; 4OH_2_O_val_ald; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q8X5J8.
DR   SWISS-2DPAGE; Q8X5J8.
KW   Aromatic hydrocarbons catabolism; Complete proteome; Lyase; Manganese;
KW   Metal-binding.
FT   CHAIN         1    337       4-hydroxy-2-oxovalerate aldolase.
FT                                /FTId=PRO_0000337805.
FT   DOMAIN        6    258       Pyruvate carboxyltransferase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01151}.
FT   REGION       14     15       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01656}.
FT   ACT_SITE     18     18       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01656}.
FT   METAL        15     15       Manganese. {ECO:0000255|HAMAP-
FT                                Rule:MF_01656}.
FT   METAL       197    197       Manganese; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01656}.
FT   METAL       199    199       Manganese; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01656}.
FT   BINDING     168    168       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01656}.
FT   BINDING     197    197       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01656}.
FT   BINDING     288    288       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01656}.
FT   SITE         14     14       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_01656}.
SQ   SEQUENCE   337 AA;  36438 MW;  F7E6BA39FB1B0312 CRC64;
     MNGKKLYISD VTLRDGMHAI RHQYSLENVR QIAKALDDAR VDSIEVAHGD GLQGSSFNYG
     FGAHSDLEWI EAAADVVKHA KIATLLLPGI GTIHDLKNAW QAGARVVRVA THCTEADVSA
     QHIQYARELG MDTVGFLMMS HMTTPENLAK QAKLMEGYGA TCIYVVDSGG AMNMSDIRDR
     FRALKAVLKP ETQTGMHAHH NLSLGVANSI AAVEEGCDRI DASLAGMGAG AGNAPLEVFI
     AAVDKLGWQH GADLYALMDA ADDLVRPLQD RPVRVDRETL ALGYAGVYSS FLRHCETAAA
     RYGLSAVDIL VELGKRRMVG GQEDMIVDVA LDLRNNK
//

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