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HPCH_KLEP3
ID   HPCH_KLEP3              Reviewed;         263 AA.
AC   B5Y2D2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 65.
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=KPK_4837;
OS   Klebsiella pneumoniae (strain 342).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=507522;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=342;
RX   PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA   Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA   Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA   Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W.,
RA   Methe B.A.;
RT   "Complete genome sequence of the N2-fixing broad host range endophyte
RT   Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL   PLoS Genet. 4:E1000141-E1000141(2008).
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; CP000964; ACI09987.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5Y2D2; -.
DR   SMR; B5Y2D2; -.
DR   EnsemblBacteria; ACI09987; ACI09987; KPK_4837.
DR   KEGG; kpe:KPK_4837; -.
DR   HOGENOM; CLU_059964_1_0_6; -.
DR   OMA; WNRVDDY; -.
DR   OrthoDB; 1797448at2; -.
DR   UniPathway; UPA00208; UER00422.
DR   Proteomes; UP000001734; 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_1000140419"
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;  28058 MW;  C35739546B2BAC35 CRC64;
     MNNAFKDALK AGRPQIGLWL GLCSSYSAEL LAGAGFDWLL IDGEHAPNNV PTVLTQLQAI
     APYPSQPVVR PSWNDPVQIK QLLDVGVQTL LVPMVQNAEE ARLAVRATRY PPAGIRGVGS
     ALARASRWNR VPDYIHQAND AMCVLVQIET REALKNLPQI LDVDGVDGVF IGPADLSADM
     GHGGNPQHPE VQAAIEDAIQ QIRQAGKAPG ILMANEQLAK RYLELGALFV AVGVDTTLLA
     RGAEALAARF GAEKTDLGSS GVY
 
 
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