HPCH_SALPB
ID HPCH_SALPB Reviewed; 263 AA.
AC A9N6T0;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=SPAB_02446;
OS Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=1016998;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1250 / SPB7;
RG The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Fulton R., Cordes M., 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; CP000886; ABX67827.1; -; Genomic_DNA.
DR RefSeq; WP_000785061.1; NC_010102.1.
DR AlphaFoldDB; A9N6T0; -.
DR SMR; A9N6T0; -.
DR KEGG; spq:SPAB_02446; -.
DR PATRIC; fig|1016998.12.peg.2315; -.
DR HOGENOM; CLU_059964_1_0_6; -.
DR OMA; WNRVDDY; -.
DR BioCyc; SENT1016998:SPAB_RS09930-MON; -.
DR UniPathway; UPA00208; UER00422.
DR Proteomes; UP000008556; 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_0000355109"
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; 27787 MW; 476D25BC13B4B749 CRC64;
MKNAFKDALK AGRPQIGLWL GLANSYSAEL LAGAGFDWLL IDGEHAPNNV QTVLTQLQAI
APYPSQPVVR PSWNDPVQIK QLLDVGAQTL LIPMVQNADE ARNAVAATRY PPAGIRGVGS
ALARASRWNR IPDYLHQAND AMCVLVQIET REAMSNLASI LDVDGIDGVF IGPADLSADM
GFAGNPQHPE VQAAIENAIV QIRAAGKAPG ILMANEALAK RYLELGALFV AVGVDTTLLA
RGAEALAARF GAEKKLSGAS GVY
