(data stored in ACNUC7421 zone)

SWISSPROT: HOA_SHISS

ID   HOA_SHISS               Reviewed;         337 AA.
AC   Q3Z554;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 82.
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=SSON_0331;
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA   Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA   Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA   Qiang B., Hou Y., Yu J., Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic
RT   agents of bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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:
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   -!- 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; CP000038; AAZ87108.1; -; Genomic_DNA.
DR   SMR; Q3Z554; -.
DR   EnsemblBacteria; AAZ87108; AAZ87108; SSON_0331.
DR   KEGG; ssn:SSON_0331; -.
DR   HOGENOM; HOG000048047; -.
DR   KO; K01666; -.
DR   OMA; FLMMAHS; -.
DR   BioCyc; SSON300269:G1GL2-385-MONOMER; -.
DR   UniPathway; UPA00714; -.
DR   Proteomes; UP000002529; Chromosome.
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: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; Q3Z554.
DR   SWISS-2DPAGE; Q3Z554.
KW   Aromatic hydrocarbons catabolism; Complete proteome; Lyase; Manganese;
KW   Metal-binding.
FT   CHAIN         1    337       4-hydroxy-2-oxovalerate aldolase.
FT                                /FTId=PRO_0000337808.
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;  36502 MW;  A2B4F6A1598DB91A CRC64;
     MNGKKLYISD VTLRDGMHAI RHQYSLENVR QIAKALDDAR VDSIEVAHGD GLQGSSFNYG
     FGAHSDLEWI EAAADVVRHA KIATLLLPGI GTIHDLKNAW QAGARVVRVA THCTEADVSA
     QHIQYARELG MDTVGFLMMS HMTTPENLAK QAKLMEGYGA TCIYVVDSGG AMNMSDIRDR
     FRALKAVLKP ETQTGMHAHH NLSLGVANSI AAVEEGCDRI DASFAGMGAG AGNAPLEVFI
     AAADKLGWQH GTDLYALMDA ADDLVRPLQD RPVRVDRETL ALGYAGVYSS FLRHCETAAA
     RYGLSAVDIL VELGKRRMVG GQEDMIVDVA LDLRNNK
//

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