HPCH_SHIFL
ID HPCH_SHIFL Reviewed; 267 AA.
AC Q83P19; Q7BYH4;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=SF4379, S4649;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN45795.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP19573.1; -; Genomic_DNA.
DR RefSeq; NP_710088.1; NC_004337.2.
DR RefSeq; WP_000431715.1; NZ_WPGW01000045.1.
DR AlphaFoldDB; Q83P19; -.
DR SMR; Q83P19; -.
DR STRING; 198214.SF4379; -.
DR EnsemblBacteria; AAN45795; AAN45795; SF4379.
DR EnsemblBacteria; AAP19573; AAP19573; S4649.
DR GeneID; 1023444; -.
DR KEGG; sfl:SF4379; -.
DR KEGG; sfx:S4649; -.
DR PATRIC; fig|198214.7.peg.5162; -.
DR HOGENOM; CLU_059964_1_0_6; -.
DR OMA; WNRVDDY; -.
DR OrthoDB; 1797448at2; -.
DR UniPathway; UPA00208; UER00422.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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..267
FT /note="4-hydroxy-2-oxo-heptane-1,7-dioate aldolase"
FT /id="PRO_0000355114"
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 267 AA; 28722 MW; D127E8D668A2DC6B CRC64;
MENSFKAALK AGRPQIGLWL GLSSSYSAEL LAGPGFDWLL IDGEHAPNNV QTVLTQLQAI
APYPSQPVVR PSWNDPVQIK QLLDVGTQTL LVPMVQNADE ARKAVRATRY PPAGIRGVGS
ALARASRWNR IPDYLQKAND QMCVLVQIET REAMKNLPQI LDVEGVDGVF IGPADLSADM
GYAGNPQHPE VQAAIEQAIV QIREAGKAPG ILIANEQLAK RYLELGALFV AVGVDTTLLA
RAAEALAARF GNSSSISMAK QNNNSVY
