EzCatDB: S00180

DB codeS00180
CATH domainDomain 13.10.129.10Catalytic domain
E.C.4.2.1.60
CSA1mka
MACiEM0010

CATH domainRelated DB codes (homologues)
3.10.129.10S00179

Enzyme Name
Swiss-protKEGG

P0A6Q3
Protein name3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase3-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
SynonymsEC 4.2.1.60
Beta-hydroxydecanoyl thioester dehydrase

KEGG pathways
MAP codePathways
MAP00061Fatty acid biosynthesis

Swiss-prot:Accession NumberP0A6Q3
Entry nameFABA_ECOLI
Activity(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.
SubunitHomodimer.
Subcellular locationCytoplasm.
Cofactor


SubstratesProductsintermediates
KEGG-idC04619C05757C04180C05754C05758C00001
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
Typecarbohydrate,lipid,peptide/protein,phosphate group/phosphate ion,sulfide groupcarbohydrate,lipid,peptide/protein,phosphate group/phosphate ion,sulfide groupcarbohydrate,lipid,peptide/protein,phosphate group/phosphate ion,sulfide groupcarbohydrate,lipid,peptide/protein,phosphate group/phosphate ion,sulfide groupcarbohydrate,lipid,peptide/protein,phosphate group/phosphate ion,sulfide groupH2O
1mkaAUnboundUnboundUnboundUnboundUnbound
Intermediate-analogue:DAC
1mkaBUnboundUnboundUnboundUnboundUnbound
Intermediate-analogue:DAC
1mkbAUnboundUnboundUnboundUnboundUnbound
Unbound
1mkbBUnboundUnboundUnboundUnboundUnbound
Unbound

Active-site residues
resource
Swiss-prot;P0A6Q3 & PDB;1mka
pdbCatalytic residues
1mkaAHIS 70;ASP 84
1mkaBHIS 70;ASP 84
1mkbAHIS 70;ASP 84
1mkbBHIS 70;ASP 84

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[6]Figure 6p.256-259

references
[1]
PubMed ID2832401
JournalJ Biol Chem
Year1988
Volume263
Pages4641-6
AuthorsCronan JE Jr, Li WB, Coleman R, Narasimhan M, de Mendoza D, Schwab JM
TitleDerived amino acid sequence and identification of active site residues of Escherichia coli beta-hydroxydecanoyl thioester dehydrase.
[2]
PubMed ID2180957
JournalJ Biol Chem
Year1990
Volume265
Pages5110-2
AuthorsSharma A, Henderson BS, Schwab JM, Smith JL
TitleCrystallization and preliminary X-ray analysis of beta-hydroxydecanoyl thiol ester dehydrase from Escherichia coli.
[3]
PubMed ID8446033
JournalMol Microbiol
Year1993
Volume7
Pages311-22
AuthorsDiRusso CC, Metzger AK, Heimert TL
TitleRegulation of transcription of genes required for fatty acid transport and unsaturated fatty acid biosynthesis in Escherichia coli by FadR.
[4]
PubMed ID7836365
JournalJ Biol Chem
Year1995
Volume270
Pages1092-7
AuthorsRaman N, DiRusso CC
TitleAnalysis of acyl coenzyme A binding to the transcription factor FadR and identification of amino acid residues in the carboxyl terminus required for ligand binding.
[5]
PubMed ID8765740
JournalJ Biomol NMR
Year1996
Volume7
Pages335-40
AuthorsCopie V, Battles JA, Schwab JM, Torchia DA
TitleSecondary 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.
[6]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
Medline ID96398612
PubMed ID8805534
JournalStructure
Year1996
Volume4
Pages253-64
AuthorsLeesong M, Henderson BS, Gillig JR, Schwab JM, Smith JL
TitleStructure of a dehydratase-isomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: two catalytic activities in one active site.
Related PDB1mka,1mkb
Related Swiss-protP0A6Q3
[7]
PubMed ID10871405
JournalNucleic Acids Res
Year2000
Volume28
Pages2551-6
AuthorsNakahara T, Zhang QM, Hashiguchi K, Yonei S
TitleIdentification of proteins of Escherichia coli and Saccharomyces cerevisiae that specifically bind to C/C mismatches in DNA.


createdupdated
2004-06-222012-06-04
Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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