DB code: S00180
CATH domain | 3.10.129.10 : Thiol Ester Dehydrase; Chain A | Catalytic domain |
---|---|---|
E.C. | 4.2.1.60 | |
CSA | 1mka | |
M-CSA | 1mka | |
MACiE | M0010 |
CATH domain | Related DB codes (homologues) |
---|---|
3.10.129.10 : Thiol Ester Dehydrase; Chain A | S00179 |
Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | RefSeq | Pfam |
---|---|---|---|---|
P0A6Q3 |
3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase
|
EC
4.2.1.59
3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabA Beta-hydroxydecanoyl thioester dehydrase Trans-2-decenoyl-[acyl-carrier-protein] isomerase EC 5.3.3.14 |
NP_415474.1
(Protein)
NC_000913.2 (DNA/RNA sequence) YP_489226.1 (Protein) NC_007779.1 (DNA/RNA sequence) |
PF07977
(FabA)
[Graphical View] |
KEGG enzyme name |
---|
3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase
D-3-hydroxydecanoyl-[acyl-carrier protein] dehydratase 3-hydroxydecanoyl-acyl carrier protein dehydrase 3-hydroxydecanoyl-acyl carrier protein dehydratase beta-hydroxydecanoyl thioester dehydrase beta-hydroxydecanoate dehydrase beta-hydroxydecanoyl thiol ester dehydrase FabA beta-hydroxyacyl-acyl carrier protein dehydratase HDDase beta-hydroxyacyl-ACP dehydrase (3R)-3-hydroxydecanoyl-[acyl-carrier-protein] hydro-lyase |
UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
---|---|---|---|---|---|
P0A6Q3 | FABA_ECOLI | (3R)-3-hydroxydecanoyl-[acyl-carrier-protein] = trans-dec-2-enoyl-[acyl-carrier-protein] + H(2)O. (3R)-3-hydroxydecanoyl-[acyl-carrier-protein] = cis-dec-3-enoyl-[acyl-carrier-protein] + H(2)O. | Homodimer. | Cytoplasm. |
KEGG Pathways | Map code | Pathways | E.C. |
---|---|---|
MAP00061 | Fatty acid biosynthesis |
Compound table | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Substrates | Products | Intermediates | ||||||||||
KEGG-id | C04619 | C05757 | C04180 | C05754 | C05758 | C00001 | ||||||
E.C. | ||||||||||||
Compound | (3R)-3-Hydroxydecanoyl-[acyl-carrier protein] | (R)-3-Hydroxydodecanoyl-[acyl-carrier protein] | 3-Decanoyl-[acyl-carrier protein] | trans-Dec-2-enoyl-[acyl-carrier protein] | trans-Dodec-2-enoyl-[acyl-carrier protein] | H2O | ||||||
Type | carbohydrate,lipid,peptide/protein,phosphate group/phosphate ion,sulfide group | carbohydrate,lipid,peptide/protein,phosphate group/phosphate ion,sulfide group | carbohydrate,lipid,peptide/protein,phosphate group/phosphate ion,sulfide group | carbohydrate,lipid,peptide/protein,phosphate group/phosphate ion,sulfide group | carbohydrate,lipid,peptide/protein,phosphate group/phosphate ion,sulfide group | H2O | ||||||
ChEBI |
15377 15377 |
|||||||||||
PubChem |
22247451 962 22247451 962 |
|||||||||||
1mkaA | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:DAC | ||||||
1mkaB | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:DAC | ||||||
1mkbA | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1mkbB | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
Reference for Active-site residues | ||
---|---|---|
resource | references | E.C. |
Swiss-prot;P0A6Q3 & PDB;1mka |
Active-site residues | ||||||||||
---|---|---|---|---|---|---|---|---|---|---|
PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
1mkaA | HIS 70;ASP 84 | |||||||||
1mkaB | HIS 70;ASP 84 | |||||||||
1mkbA | HIS 70;ASP 84 | |||||||||
1mkbB | HIS 70;ASP 84 |
References for Catalytic Mechanism | ||
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References | Sections | No. of steps in catalysis |
[6]
|
Figure 6 | p.256-259 |
References | |
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[1] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 2832401 |
Journal | J Biol Chem |
Year | 1988 |
Volume | 263 |
Pages | 4641-6 |
Authors | Cronan JE Jr, Li WB, Coleman R, Narasimhan M, de Mendoza D, Schwab JM |
Title | Derived amino acid sequence and identification of active site residues of Escherichia coli beta-hydroxydecanoyl thioester dehydrase. |
Related PDB | |
Related UniProtKB | |
[2] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 2180957 |
Journal | J Biol Chem |
Year | 1990 |
Volume | 265 |
Pages | 5110-2 |
Authors | Sharma A, Henderson BS, Schwab JM, Smith JL |
Title | Crystallization and preliminary X-ray analysis of beta-hydroxydecanoyl thiol ester dehydrase from Escherichia coli. |
Related PDB | |
Related UniProtKB | |
[3] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 8446033 |
Journal | Mol Microbiol |
Year | 1993 |
Volume | 7 |
Pages | 311-22 |
Authors | DiRusso CC, Metzger AK, Heimert TL |
Title | Regulation of transcription of genes required for fatty acid transport and unsaturated fatty acid biosynthesis in Escherichia coli by FadR. |
Related PDB | |
Related UniProtKB | |
[4] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 7836365 |
Journal | J Biol Chem |
Year | 1995 |
Volume | 270 |
Pages | 1092-7 |
Authors | Raman N, DiRusso CC |
Title | Analysis of acyl coenzyme A binding to the transcription factor FadR and identification of amino acid residues in the carboxyl terminus required for ligand binding. |
Related PDB | |
Related UniProtKB | |
[5] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 8765740 |
Journal | J Biomol NMR |
Year | 1996 |
Volume | 7 |
Pages | 335-40 |
Authors | Copie V, Battles JA, Schwab JM, Torchia DA |
Title |
Secondary structure of beta-hydroxydecanoyl thiol ester dehydrase, |
Related PDB | |
Related UniProtKB | |
[6] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). |
Medline ID | 96398612 |
PubMed ID | 8805534 |
Journal | Structure |
Year | 1996 |
Volume | 4 |
Pages | 253-64 |
Authors | Leesong M, Henderson BS, Gillig JR, Schwab JM, Smith JL |
Title | Structure of a dehydratase-isomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: two catalytic activities in one active site. |
Related PDB | 1mka 1mkb |
Related UniProtKB | P0A6Q3 |
[7] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 10871405 |
Journal | Nucleic Acids Res |
Year | 2000 |
Volume | 28 |
Pages | 2551-6 |
Authors | Nakahara T, Zhang QM, Hashiguchi K, Yonei S |
Title | Identification of proteins of Escherichia coli and Saccharomyces cerevisiae that specifically bind to C/C mismatches in DNA. |
Related PDB | |
Related UniProtKB |
Comments |
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Created | Updated |
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2004-06-22 | 2012-06-04 |