HPCH_SALAR
ID HPCH_SALAR Reviewed; 263 AA.
AC A9MH59;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=SARI_01895;
OS Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=41514;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980;
RG The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (NOV-2007) 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; CP000880; ABX21778.1; -; Genomic_DNA.
DR RefSeq; WP_000785079.1; NC_010067.1.
DR AlphaFoldDB; A9MH59; -.
DR SMR; A9MH59; -.
DR STRING; 41514.SARI_01895; -.
DR EnsemblBacteria; ABX21778; ABX21778; SARI_01895.
DR KEGG; ses:SARI_01895; -.
DR HOGENOM; CLU_059964_1_0_6; -.
DR OMA; WNRVDDY; -.
DR OrthoDB; 1797448at2; -.
DR UniPathway; UPA00208; UER00422.
DR Proteomes; UP000002084; 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; Reference proteome.
FT CHAIN 1..263
FT /note="4-hydroxy-2-oxo-heptane-1,7-dioate aldolase"
FT /id="PRO_0000355106"
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 263 AA; 27703 MW; C38717612901B6D5 CRC64;
MKNAFKDALK AGRPQIGLWL GLANSYSAEL VAGAGFDWLL IDGEHAPNNV QTVLTQLQAI
APYPSQPVVR PSWNDPVQIK QLLDVGAQTL LVPMVQNADE ARDAVAATRY PPAGIRGVGS
ALARASRWNR IPDYLHEAND AMCVLVQIET REAMSNLASI LDVDGIDGVF IGPADLSADM
GFAGNPQHPA VQAAIENAIV QIRAAGKAPG ILMANEALAK RYLELGALFV AVGVDTTLLA
RGAEALAARF GAEKKLSGAS GVY
