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HPCH_ECOSE
ID   HPCH_ECOSE              Reviewed;         262 AA.
AC   B6I2N1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=4-hydroxy-2-oxo-heptane-1,7-dioate aldolase {ECO:0000255|HAMAP-Rule:MF_01292};
DE            EC=4.1.2.52 {ECO:0000255|HAMAP-Rule:MF_01292};
DE   AltName: Full=2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase {ECO:0000255|HAMAP-Rule:MF_01292};
DE            Short=HHED aldolase {ECO:0000255|HAMAP-Rule:MF_01292};
DE   AltName: Full=4-hydroxy-2-ketoheptane-1,7-dioate aldolase {ECO:0000255|HAMAP-Rule:MF_01292};
DE            Short=HKHD aldolase {ECO:0000255|HAMAP-Rule:MF_01292};
GN   Name=hpcH {ECO:0000255|HAMAP-Rule:MF_01292};
GN   Synonyms=hpaI {ECO:0000255|HAMAP-Rule:MF_01292};
GN   OrderedLocusNames=ECSE_4624;
OS   Escherichia coli (strain SE11).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=409438;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SE11;
RX   PubMed=18931093; DOI=10.1093/dnares/dsn026;
RA   Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H., Ooka T.,
RA   Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.;
RT   "Complete genome sequence and comparative analysis of the wild-type
RT   commensal Escherichia coli strain SE11 isolated from a healthy adult.";
RL   DNA Res. 15:375-386(2008).
CC   -!- FUNCTION: Catalyzes the reversible retro-aldol cleavage of 4-hydroxy-2-
CC       ketoheptane-1,7-dioate (HKHD) to pyruvate and succinic semialdehyde.
CC       {ECO:0000255|HAMAP-Rule:MF_01292}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-hydroxy-2-oxoheptanedioate = pyruvate + succinate
CC         semialdehyde; Xref=Rhea:RHEA:25788, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:57706, ChEBI:CHEBI:73036; EC=4.1.2.52;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01292};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01292};
CC       Note=Binds 1 divalent metal cation per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01292};
CC   -!- PATHWAY: Aromatic compound metabolism; 4-hydroxyphenylacetate
CC       degradation; pyruvate and succinate semialdehyde from 4-
CC       hydroxyphenylacetate: step 7/7. {ECO:0000255|HAMAP-Rule:MF_01292}.
CC   -!- SUBUNIT: Homohexamer; trimer of dimers. {ECO:0000255|HAMAP-
CC       Rule:MF_01292}.
CC   -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01292}.
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DR   EMBL; AP009240; BAG80148.1; -; Genomic_DNA.
DR   RefSeq; WP_000431706.1; NC_011415.1.
DR   AlphaFoldDB; B6I2N1; -.
DR   SMR; B6I2N1; -.
DR   EnsemblBacteria; BAG80148; BAG80148; ECSE_4624.
DR   KEGG; ecy:ECSE_4624; -.
DR   HOGENOM; CLU_059964_1_0_6; -.
DR   OMA; WNRVDDY; -.
DR   UniPathway; UPA00208; UER00422.
DR   Proteomes; UP000008199; Chromosome.
DR   GO; GO:0018802; F:2,4-dihydroxyhept-2-ene-1,7-dioate aldolase activity; IEA:InterPro.
DR   GO; GO:0043863; F:4-hydroxy-2-ketopimelate aldolase activity; IEA:RHEA.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0010124; P:phenylacetate catabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.60; -; 1.
DR   HAMAP; MF_01292; HKHD_aldolase; 1.
DR   InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR   InterPro; IPR023701; HKHD_aldolase_ent.
DR   InterPro; IPR012689; HpaI.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   Pfam; PF03328; HpcH_HpaI; 1.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   TIGRFAMs; TIGR02311; HpaI; 1.
PE   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism; Lyase; Metal-binding.
FT   CHAIN           1..262
FT                   /note="4-hydroxy-2-oxo-heptane-1,7-dioate aldolase"
FT                   /id="PRO_1000140418"
FT   ACT_SITE        45
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01292"
FT   BINDING         147
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01292"
FT   BINDING         149
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01292"
FT   BINDING         174
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01292"
FT   BINDING         175
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01292"
FT   BINDING         175
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01292"
FT   SITE            70
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01292"
FT   SITE            84
FT                   /note="Increases basicity of active site His"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01292"
SQ   SEQUENCE   262 AA;  28073 MW;  374F576B6C53587F CRC64;
     MENSFKAALK AGRPQIGLWL GLSSSYSAEL LAGAGFDWLL IDGEHAPNNV QTVLTQLQAI
     APYPSQPVVR PSWNDPVQIK QLLDVGTQTL LVPMVQNADE AREAVRATRY PPAGIRGVGS
     ALARASRWNR IPDYLQKAND QMCVLVQIET REAMKNLPQI LDVEGVDGVF IGPADLSADM
     GYAGNPQHPE VQAAIEQAIV QIRESGKAPG ILIANEQLAK RYLELGALFV AVGVDTTLLA
     RAAEALAARF GAQATAVKPG VY
 
 
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