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Hydroxycinnamoyl-CoA hydratase-lyase (HCHL) (EC 4.1.2.41) (EC 4.2.1.101) (P-hydroxycinnamoyl CoA hydratase/lyase) (Trans-feruloyl-CoA hydratase/vanillin synthase)

 HCHL_PSEFL              Reviewed;         276 AA.
O69762;
05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
28-FEB-2018, entry version 75.
RecName: Full=Hydroxycinnamoyl-CoA hydratase-lyase;
Short=HCHL;
EC=4.1.2.41;
EC=4.2.1.101;
AltName: Full=P-hydroxycinnamoyl CoA hydratase/lyase;
AltName: Full=Trans-feruloyl-CoA hydratase/vanillin synthase;
Pseudomonas fluorescens.
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
Pseudomonadaceae; Pseudomonas.
NCBI_TaxID=294;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-21, FUNCTION,
AND CATALYTIC ACTIVITY.
STRAIN=AN103;
PubMed=9461612; DOI=10.1074/jbc.273.7.4163;
Gasson M.J., Kitamura Y., McLauchlan W.R., Narbad A., Parr A.J.,
Parsons E.L., Payne J., Rhodes M.J., Walton N.J.;
"Metabolism of ferulic acid to vanillin. A bacterial gene of the
enoyl-SCoA hydratase/isomerase superfamily encodes an enzyme for the
hydration and cleavage of a hydroxycinnamic acid SCoA thioester.";
J. Biol. Chem. 273:4163-4170(1998).
[2]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), AND SUBUNIT.
STRAIN=AN103;
PubMed=17139085; DOI=10.1107/S0907444906039199;
Leonard P.M., Brzozowski A.M., Lebedev A., Marshall C.M., Smith D.J.,
Verma C.S., Walton N.J., Grogan G.;
"The 1.8 A resolution structure of hydroxycinnamoyl-coenzyme A
hydratase-lyase (HCHL) from Pseudomonas fluorescens, an enzyme that
catalyses the transformation of feruloyl-coenzyme A to vanillin.";
Acta Crystallogr. D 62:1494-1501(2006).
[3]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH
4-HYDROXY-3-METHOXYBENZALDEHYDE AND ACETYL-COA, BIOPHYSICOCHEMICAL
PROPERTIES, SUBUNIT, AND MUTAGENESIS OF SER-123; GLU-143 AND TYR-239.
STRAIN=AN103;
PubMed=18479250; DOI=10.1042/BJ20080714;
Bennett J.P., Bertin L., Moulton B., Fairlamb I.J., Brzozowski A.M.,
Walton N.J., Grogan G.;
"A ternary complex of hydroxycinnamoyl-CoA hydratase-lyase (HCHL) with
acetyl-CoA and vanillin gives insights into substrate specificity and
mechanism.";
Biochem. J. 414:281-289(2008).
-!- FUNCTION: Catalyzes the hydration of the acyl-CoA thioester of
ferulic acid and the subsequent retro-aldol cleavage of the
hydrated intermediate to yield vanillin (4-hydroxy-3-methoxy-
benzaldehyde). {ECO:0000269|PubMed:9461612}.
-!- CATALYTIC ACTIVITY: 4-hydroxy-3-methoxyphenyl-beta-
hydroxypropanoyl-CoA = feruloyl-CoA + H(2)O.
{ECO:0000269|PubMed:9461612}.
-!- CATALYTIC ACTIVITY: 3-hydroxy-3-(4-hydroxy-3-
methoxyphenyl)propanoyl-CoA = vanillin + acetyl-CoA.
{ECO:0000269|PubMed:9461612}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.0118 mM for ferulic acid {ECO:0000269|PubMed:18479250};
Note=kcat is 3.72 sec(-1) with ferulic acid as substrate.;
-!- SUBUNIT: Homohexamer; dimer of trimers.
{ECO:0000269|PubMed:17139085, ECO:0000269|PubMed:18479250}.
-!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
{ECO:0000305}.
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EMBL; Y13067; CAA73502.1; -; Genomic_DNA.
PDB; 2J5I; X-ray; 1.80 A; A/B/C/D/E/F/G/H/I/J/K/L=1-276.
PDB; 2VSS; X-ray; 2.22 A; A/B/C/D/E/F=1-276.
PDB; 2VSU; X-ray; 1.90 A; A/B/C/D/E/F=1-276.
PDBsum; 2J5I; -.
PDBsum; 2VSS; -.
PDBsum; 2VSU; -.
ProteinModelPortal; O69762; -.
SMR; O69762; -.
eggNOG; ENOG4108D7R; Bacteria.
eggNOG; ENOG410XPS4; LUCA.
BRENDA; 4.2.1.101; 5121.
EvolutionaryTrace; O69762; -.
GO; GO:0050548; F:trans-feruloyl-CoA hydratase activity; IEA:UniProtKB-EC.
GO; GO:0050547; F:vanillin synthase activity; IEA:UniProtKB-EC.
GO; GO:0008152; P:metabolic process; IEA:InterPro.
InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
InterPro; IPR001753; Enoyl-CoA_hydra/iso.
Pfam; PF00378; ECH_1; 1.
SUPFAM; SSF52096; SSF52096; 1.
PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
1: Evidence at protein level;
3D-structure; Direct protein sequencing; Lyase.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:9461612}.
CHAIN 2 276 Hydroxycinnamoyl-CoA hydratase-lyase.
/FTId=PRO_0000418727.
REGION 70 72 Coenzyme A binding.
REGION 142 146 Coenzyme A binding.
BINDING 29 29 Coenzyme A.
BINDING 75 75 Substrate.
BINDING 120 120 Coenzyme A; via carbonyl oxygen.
BINDING 151 151 Substrate; via carbonyl oxygen.
BINDING 239 239 Substrate.
MUTAGEN 123 123 S->A: Reduced kcat compared to wild-type
but not markerdly.
{ECO:0000269|PubMed:18479250}.
MUTAGEN 143 143 E->A: Abolishes catalytic activity.
{ECO:0000269|PubMed:18479250}.
MUTAGEN 239 239 Y->F: Increased KM but retains a
significant amount of catalytic activity
with a kcat 10 times less than that of
the wild-type.
{ECO:0000269|PubMed:18479250}.
CONFLICT 16 16 E -> Q (in Ref. 1; AA sequence).
{ECO:0000305}.
STRAND 9 16 {ECO:0000244|PDB:2J5I}.
STRAND 18 24 {ECO:0000244|PDB:2J5I}.
HELIX 27 29 {ECO:0000244|PDB:2J5I}.
HELIX 35 49 {ECO:0000244|PDB:2J5I}.
STRAND 54 62 {ECO:0000244|PDB:2J5I}.
STRAND 65 67 {ECO:0000244|PDB:2J5I}.
HELIX 72 81 {ECO:0000244|PDB:2J5I}.
HELIX 86 98 {ECO:0000244|PDB:2J5I}.
TURN 99 104 {ECO:0000244|PDB:2J5I}.
STRAND 109 113 {ECO:0000244|PDB:2J5I}.
STRAND 115 118 {ECO:0000244|PDB:2J5I}.
HELIX 119 121 {ECO:0000244|PDB:2J5I}.
HELIX 122 127 {ECO:0000244|PDB:2J5I}.
STRAND 128 134 {ECO:0000244|PDB:2J5I}.
STRAND 138 140 {ECO:0000244|PDB:2J5I}.
HELIX 142 146 {ECO:0000244|PDB:2J5I}.
HELIX 154 161 {ECO:0000244|PDB:2J5I}.
HELIX 164 173 {ECO:0000244|PDB:2J5I}.
STRAND 176 178 {ECO:0000244|PDB:2J5I}.
HELIX 179 184 {ECO:0000244|PDB:2J5I}.
STRAND 187 192 {ECO:0000244|PDB:2J5I}.
HELIX 194 209 {ECO:0000244|PDB:2J5I}.
HELIX 213 226 {ECO:0000244|PDB:2J5I}.
HELIX 231 248 {ECO:0000244|PDB:2J5I}.
SEQUENCE 276 AA; 31008 MW; FDB5AD1539CA7F9A CRC64;
MSTYEGRWKT VKVEIEDGIA FVILNRPEKR NAMSPTLNRE MIDVLETLEQ DPAAGVLVLT
GAGEAWTAGM DLKEYFREVD AGPEILQEKI RREASQWQWK LLRMYAKPTI AMVNGWCFGG
GFSPLVACDL AICADEATFG LSEINWGIPP GNLVSKAMAD TVGHRQSLYY IMTGKTFGGQ
KAAEMGLVNE SVPLAQLREV TIELARNLLE KNPVVLRAAK HGFKRCRELT WEQNEDYLYA
KLDQSRLLDT EGGREQGMKQ FLDDKSIKPG LQAYKR


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