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
PubChem 22247451
962
1mkaA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Intermediate-analogue:DAC
1mkaB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Intermediate-analogue:DAC
1mkbA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1mkbB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain 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 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 70;ASP 84
1mkaB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 70;ASP 84
1mkbA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 70;ASP 84
1mkbB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 70;ASP 84

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[6]
Figure 6 p.256-259

References
[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, a 39-kDa protein, derived from H alpha, C alpha, C beta and CO signal assignments and the Chemical Shift Index: comparison with the crystal structure.
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

Created Updated
2004-06-22 2012-06-04