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HPCH_ECOLC
ID   HPCH_ECOLC              Reviewed;         262 AA.
AC   B1IS70;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=EcolC_3707;
OS   Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 /
OS   WDCM 00012 / Crooks).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=481805;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Ingram L., Richardson P.;
RT   "Complete sequence of Escherichia coli C str. ATCC 8739.";
RL   Submitted (FEB-2008) 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; CP000946; ACA79318.1; -; Genomic_DNA.
DR   RefSeq; WP_000431706.1; NZ_CP022959.1.
DR   PDB; 4B5S; X-ray; 1.68 A; A/B=1-251.
DR   PDB; 4B5T; X-ray; 1.92 A; A/B=1-251.
DR   PDB; 4B5U; X-ray; 1.91 A; A/B=1-251.
DR   PDB; 4B5V; X-ray; 2.04 A; A/B=1-251.
DR   PDB; 4B5W; X-ray; 1.79 A; A/B/C/D/E/F=1-256.
DR   PDB; 4B5X; X-ray; 1.80 A; A/B=1-262.
DR   PDBsum; 4B5S; -.
DR   PDBsum; 4B5T; -.
DR   PDBsum; 4B5U; -.
DR   PDBsum; 4B5V; -.
DR   PDBsum; 4B5W; -.
DR   PDBsum; 4B5X; -.
DR   AlphaFoldDB; B1IS70; -.
DR   SMR; B1IS70; -.
DR   KEGG; ecl:EcolC_3707; -.
DR   HOGENOM; CLU_059964_1_0_6; -.
DR   OMA; WNRVDDY; -.
DR   BRENDA; 4.1.2.52; 2026.
DR   UniPathway; UPA00208; UER00422.
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   1: Evidence at protein level;
KW   3D-structure; Aromatic hydrocarbons catabolism; Lyase; Metal-binding.
FT   CHAIN           1..262
FT                   /note="4-hydroxy-2-oxo-heptane-1,7-dioate aldolase"
FT                   /id="PRO_0000355103"
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"
FT   HELIX           4..10
FT                   /evidence="ECO:0007829|PDB:4B5S"
FT   STRAND          15..20
FT                   /evidence="ECO:0007829|PDB:4B5S"
FT   HELIX           25..32
FT                   /evidence="ECO:0007829|PDB:4B5S"
FT   STRAND          37..42
FT                   /evidence="ECO:0007829|PDB:4B5S"
FT   TURN            43..45
FT                   /evidence="ECO:0007829|PDB:4B5S"
FT   HELIX           50..60
FT                   /evidence="ECO:0007829|PDB:4B5S"
FT   STRAND          63..70
FT                   /evidence="ECO:0007829|PDB:4B5S"
FT   STRAND          72..74
FT                   /evidence="ECO:0007829|PDB:4B5S"
FT   HELIX           76..84
FT                   /evidence="ECO:0007829|PDB:4B5S"
FT   STRAND          89..93
FT                   /evidence="ECO:0007829|PDB:4B5S"
FT   HELIX           98..107
FT                   /evidence="ECO:0007829|PDB:4B5S"
FT   TURN            111..113
FT                   /evidence="ECO:0007829|PDB:4B5S"
FT   HELIX           120..122
FT                   /evidence="ECO:0007829|PDB:4B5S"
FT   HELIX           124..126
FT                   /evidence="ECO:0007829|PDB:4B5S"
FT   TURN            127..130
FT                   /evidence="ECO:0007829|PDB:4B5S"
FT   HELIX           134..137
FT                   /evidence="ECO:0007829|PDB:4B5S"
FT   HELIX           139..141
FT                   /evidence="ECO:0007829|PDB:4B5S"
FT   STRAND          143..148
FT                   /evidence="ECO:0007829|PDB:4B5S"
FT   HELIX           151..155
FT                   /evidence="ECO:0007829|PDB:4B5S"
FT   HELIX           157..161
FT                   /evidence="ECO:0007829|PDB:4B5S"
FT   STRAND          166..171
FT                   /evidence="ECO:0007829|PDB:4B5S"
FT   HELIX           173..180
FT                   /evidence="ECO:0007829|PDB:4B5S"
FT   HELIX           189..204
FT                   /evidence="ECO:0007829|PDB:4B5S"
FT   STRAND          207..212
FT                   /evidence="ECO:0007829|PDB:4B5S"
FT   HELIX           216..224
FT                   /evidence="ECO:0007829|PDB:4B5S"
FT   STRAND          228..234
FT                   /evidence="ECO:0007829|PDB:4B5S"
FT   HELIX           235..249
FT                   /evidence="ECO:0007829|PDB:4B5S"
SQ   SEQUENCE   262 AA;  28073 MW;  374F576B6C53587F CRC64;
     MENSFKAALK AGRPQIGLWL GLSSSYSAEL LAGAGFDWLL IDGEHAPNNV QTVLTQLQAI
     APYPSQPVVR PSWNDPVQIK QLLDVGTQTL LVPMVQNADE AREAVRATRY PPAGIRGVGS
     ALARASRWNR IPDYLQKAND QMCVLVQIET REAMKNLPQI LDVEGVDGVF IGPADLSADM
     GYAGNPQHPE VQAAIEQAIV QIRESGKAPG ILIANEQLAK RYLELGALFV AVGVDTTLLA
     RAAEALAARF GAQATAVKPG VY
 
 
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