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HPCH_SALPK
ID   HPCH_SALPK              Reviewed;         263 AA.
AC   B5BBH8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 66.
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=SSPA1621;
OS   Salmonella paratyphi A (strain AKU_12601).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=554290;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AKU_12601;
RX   PubMed=19159446; DOI=10.1186/1471-2164-10-36;
RA   Holt K.E., Thomson N.R., Wain J., Langridge G.C., Hasan R., Bhutta Z.A.,
RA   Quail M.A., Norbertczak H., Walker D., Simmonds M., White B., Bason N.,
RA   Mungall K., Dougan G., Parkhill J.;
RT   "Pseudogene accumulation in the evolutionary histories of Salmonella
RT   enterica serovars Paratyphi A and Typhi.";
RL   BMC Genomics 10:36-36(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}.
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DR   EMBL; FM200053; CAR59810.1; -; Genomic_DNA.
DR   RefSeq; WP_000785059.1; NC_011147.1.
DR   AlphaFoldDB; B5BBH8; -.
DR   SMR; B5BBH8; -.
DR   KEGG; sek:SSPA1621; -.
DR   HOGENOM; CLU_059964_1_0_6; -.
DR   OMA; WNRVDDY; -.
DR   UniPathway; UPA00208; UER00422.
DR   Proteomes; UP000001869; 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_1000140426"
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;  27758 MW;  52CC25BC0244BBB9 CRC64;
     MKNAFKDALK AGRPQIGLWL GLANSYSAEL LAGAGFDWLL IDGEHAPNNV QTVLTQLQAI
     APYPSQPVVR PSWNDPVQIK QLLDVGAQTL LIPMVQNADE ARNAVAATRY PPAGIRGVGS
     ALARASRWNR IPDYLHLAND AMCVLVQIET REAMSNLASI LDVDGIDGVF IGPADLSADM
     GFAGNPQHPE VQAAIENAIV QIRAAGKAPG ILMANEALAK RYLELGALFV AVGVDTTLLA
     RGAEALAARF GAEKNLSGAS GVY
 
 
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