ID HPCH_ECOLC Reviewed; 262 AA.
AC B1IS70;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 80.
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=EcolC_3707;
OS Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 /
OS WDCM 00012 / Crooks).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=481805;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Ingram L., Richardson P.;
RT "Complete sequence of Escherichia coli C str. ATCC 8739.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000946; ACA79318.1; -; Genomic_DNA.
DR RefSeq; WP_000431706.1; NZ_MTFT01000024.1.
DR PDB; 4B5S; X-ray; 1.68 A; A/B=1-251.
DR PDB; 4B5T; X-ray; 1.92 A; A/B=1-251.
DR PDB; 4B5U; X-ray; 1.91 A; A/B=1-251.
DR PDB; 4B5V; X-ray; 2.04 A; A/B=1-251.
DR PDB; 4B5W; X-ray; 1.79 A; A/B/C/D/E/F=1-256.
DR PDB; 4B5X; X-ray; 1.80 A; A/B=1-262.
DR PDBsum; 4B5S; -.
DR PDBsum; 4B5T; -.
DR PDBsum; 4B5U; -.
DR PDBsum; 4B5V; -.
DR PDBsum; 4B5W; -.
DR PDBsum; 4B5X; -.
DR AlphaFoldDB; B1IS70; -.
DR SMR; B1IS70; -.
DR GeneID; 75202969; -.
DR KEGG; ecl:EcolC_3707; -.
DR HOGENOM; CLU_059964_1_0_6; -.
DR BRENDA; 4.1.2.52; 2026.
DR UniPathway; UPA00208; UER00422.
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; Phosphoenolpyruvate-binding domains; 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 NCBIfam; TIGR02311; HpaI; 1.
DR PANTHER; PTHR30502; 2-KETO-3-DEOXY-L-RHAMNONATE ALDOLASE; 1.
DR PANTHER; PTHR30502:SF0; PHOSPHOENOLPYRUVATE CARBOXYLASE FAMILY PROTEIN; 1.
DR Pfam; PF03328; HpcH_HpaI; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism; Lyase; Metal-binding.
FT CHAIN 1..262
FT /note="4-hydroxy-2-oxo-heptane-1,7-dioate aldolase"
FT /id="PRO_0000355103"
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"
FT HELIX 4..10
FT /evidence="ECO:0007829|PDB:4B5S"
FT STRAND 15..20
FT /evidence="ECO:0007829|PDB:4B5S"
FT HELIX 25..32
FT /evidence="ECO:0007829|PDB:4B5S"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:4B5S"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:4B5S"
FT HELIX 50..60
FT /evidence="ECO:0007829|PDB:4B5S"
FT STRAND 63..70
FT /evidence="ECO:0007829|PDB:4B5S"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:4B5S"
FT HELIX 76..84
FT /evidence="ECO:0007829|PDB:4B5S"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:4B5S"
FT HELIX 98..107
FT /evidence="ECO:0007829|PDB:4B5S"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:4B5S"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:4B5S"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:4B5S"
FT TURN 127..130
FT /evidence="ECO:0007829|PDB:4B5S"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:4B5S"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:4B5S"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:4B5S"
FT HELIX 151..155
FT /evidence="ECO:0007829|PDB:4B5S"
FT HELIX 157..161
FT /evidence="ECO:0007829|PDB:4B5S"
FT STRAND 166..171
FT /evidence="ECO:0007829|PDB:4B5S"
FT HELIX 173..180
FT /evidence="ECO:0007829|PDB:4B5S"
FT HELIX 189..204
FT /evidence="ECO:0007829|PDB:4B5S"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:4B5S"
FT HELIX 216..224
FT /evidence="ECO:0007829|PDB:4B5S"
FT STRAND 228..234
FT /evidence="ECO:0007829|PDB:4B5S"
FT HELIX 235..249
FT /evidence="ECO:0007829|PDB:4B5S"
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
//
