HPCH_SALPC
ID HPCH_SALPC Reviewed; 263 AA.
AC C0Q8A0;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 61.
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=SPC_2644;
OS Salmonella paratyphi C (strain RKS4594).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=476213;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RKS4594;
RX PubMed=19229335; DOI=10.1371/journal.pone.0004510;
RA Liu W.-Q., Feng Y., Wang Y., Zou Q.-H., Chen F., Guo J.-T., Peng Y.-H.,
RA Jin Y., Li Y.-G., Hu S.-N., Johnston R.N., Liu G.-R., Liu S.-L.;
RT "Salmonella paratyphi C: genetic divergence from Salmonella choleraesuis
RT and pathogenic convergence with Salmonella typhi.";
RL PLoS ONE 4:E4510-E4510(2009).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000857; ACN46745.1; -; Genomic_DNA.
DR RefSeq; WP_000785083.1; NC_012125.1.
DR AlphaFoldDB; C0Q8A0; -.
DR SMR; C0Q8A0; -.
DR EnsemblBacteria; ACN46745; ACN46745; SPC_2644.
DR KEGG; sei:SPC_2644; -.
DR HOGENOM; CLU_059964_1_0_6; -.
DR OMA; WNRVDDY; -.
DR UniPathway; UPA00208; UER00422.
DR Proteomes; UP000001599; 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..263
FT /note="4-hydroxy-2-oxo-heptane-1,7-dioate aldolase"
FT /id="PRO_1000165274"
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; 27857 MW; 5F2755A2E9B4A309 CRC64;
MKNAFKDTLK AGRPQIGLWL GLANSYSAEL LAGAGFDWLL IDGEHAPNNV QTVLTQLQAI
APYPSQPVVR PSWNDPVQIK QLLDVGAQTL LIPMVQNADE ARNAVAATRY PPAGIRGVGS
ALARASRWNR IPDYLHQAND AMCVLVQIET REAMSNLASI LDVDGIDGVF IGPADLSADM
GFAGNPQHPE VQAAIENAIV QIRAAGKAPG ILMANEPLAK RYLELGALFV AVGVDTTLLA
RGAEALAARF GVEKNLSGAS GVY
