DB code: D00871
RLCP classification | 3.1177.220085.58 : Transfer | |
---|---|---|
1.51.790.101 : Hydrolysis | ||
3.1197.15025.150 : Transfer | ||
CATH domain | 3.40.47.10 : Peroxisomal Thiolase; Chain A, domain 1 | Catalytic domain |
3.40.47.10 : Peroxisomal Thiolase; Chain A, domain 1 | Catalytic domain | |
E.C. | 2.3.1.179 | |
CSA | 1kas | |
M-CSA | 1kas | |
MACiE |
CATH domain | Related DB codes (homologues) |
---|---|
3.40.47.10 : Peroxisomal Thiolase; Chain A, domain 1 | D00090 D00411 D00509 D00825 D00826 D00867 |
Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | RefSeq | Pfam |
---|---|---|---|---|
P0AAI5 |
3-oxoacyl-[acyl-carrier-protein] synthase 2
|
EC
2.3.1.179
3-oxoacyl-[acyl-carrier-protein] synthase II Beta-ketoacyl-ACP synthase II KAS II |
NP_415613.1
(Protein)
NC_000913.2 (DNA/RNA sequence) YP_489363.1 (Protein) NC_007779.1 (DNA/RNA sequence) |
PF00109
(ketoacyl-synt)
PF02801 (Ketoacyl-synt_C) [Graphical View] |
Q6G441 |
3-oxoacyl-[acyl-carrier-protein] synthase 2
|
EC
2.3.1.179
|
YP_033372.1
(Protein)
NC_005956.1 (DNA/RNA sequence) |
PF00109
(ketoacyl-synt)
PF02801 (Ketoacyl-synt_C) [Graphical View] |
Q8YFP7 |
3-oxoacyl-[acyl-carrier-protein] synthase 2
|
EC
2.3.1.179
|
NP_540390.1
(Protein)
NC_003317.1 (DNA/RNA sequence) |
PF00109
(ketoacyl-synt)
PF02801 (Ketoacyl-synt_C) [Graphical View] |
A4JL30 |
3-oxoacyl-[acyl-carrier-protein] synthase 2
|
EC
2.3.1.179
|
YP_001116448.1
(Protein)
NC_009255.1 (DNA/RNA sequence) |
PF00109
(ketoacyl-synt)
PF02801 (Ketoacyl-synt_C) [Graphical View] |
P73283 |
3-oxoacyl-[acyl-carrier-protein] synthase 2
|
EC
2.3.1.179
3-oxoacyl-[acyl-carrier-protein] synthase II Beta-ketoacyl-ACP synthase II KAS II |
NP_440631.1
(Protein)
NC_000911.1 (DNA/RNA sequence) YP_005650690.1 (Protein) NC_017277.1 (DNA/RNA sequence) YP_007450514.1 (Protein) NC_020286.1 (DNA/RNA sequence) |
PF00109
(ketoacyl-synt)
PF02801 (Ketoacyl-synt_C) [Graphical View] |
Q5SL80 |
3-oxoacyl-[acyl-carrier-protein] synthase 2
|
EC
2.3.1.179
|
YP_143679.1
(Protein)
NC_006461.1 (DNA/RNA sequence) |
PF00109
(ketoacyl-synt)
PF02801 (Ketoacyl-synt_C) [Graphical View] |
Q8NXE1 |
3-oxoacyl-[acyl-carrier-protein] synthase 2
|
EC
2.3.1.179
3-oxoacyl-[acyl-carrier-protein] synthase II Beta-ketoacyl-ACP synthase II KAS II |
NP_645683.1
(Protein)
NC_003923.1 (DNA/RNA sequence) |
PF00109
(ketoacyl-synt)
PF02801 (Ketoacyl-synt_C) [Graphical View] |
Q8Y574 |
3-oxoacyl-[acyl-carrier-protein] synthase 2
|
EC
2.3.1.179
|
NP_465725.1
(Protein)
NC_003210.1 (DNA/RNA sequence) |
PF00109
(ketoacyl-synt)
PF02801 (Ketoacyl-synt_C) [Graphical View] |
Q9FBC2 |
3-oxoacyl-[acyl-carrier-protein] synthase 2
|
EC
2.3.1.179
|
PF00109
(ketoacyl-synt)
PF02801 (Ketoacyl-synt_C) [Graphical View] |
KEGG enzyme name |
---|
beta-ketoacyl-acyl-carrier-protein synthase II
KASII KAS II FabF 3-oxoacyl-acyl carrier protein synthase I beta-ketoacyl-ACP synthase II (Z)-hexadec-11-enoyl-[acyl-carrier-protein]:malonyl-[acyl-carrier-protein] C-acyltransferase (decarboxylating) |
UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
---|---|---|---|---|---|
P0AAI5 | FABF_ECOLI | (Z)-hexadec-11-enoyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = (Z)-3-oxooctadec-13-enoyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein]. | Homodimer. | ||
Q6G441 | Q6G441_BARHE | ||||
Q8YFP7 | Q8YFP7_BRUME | (Z)-hexadec-11-enoyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = (Z)-3-oxooctadec-13-enoyl-[acyl-carrier-protein] + CO(2) + [acyl-carrier-protein]. | |||
A4JL30 | A4JL30_BURVG | (Z)-hexadec-11-enoyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = (Z)-3-oxooctadec-13-enoyl-[acyl-carrier-protein] + CO(2) + [acyl-carrier-protein]. | |||
P73283 | FABF_SYNY3 | (Z)-hexadec-11-enoyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = (Z)-3-oxooctadec-13-enoyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein]. | Homodimer. | ||
Q5SL80 | Q5SL80_THET8 | ||||
Q8NXE1 | FABF_STAAW | (Z)-hexadec-11-enoyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = (Z)-3-oxooctadec-13-enoyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein]. | |||
Q8Y574 | Q8Y574_LISMO | (Z)-hexadec-11-enoyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = (Z)-3-oxooctadec-13-enoyl-[acyl-carrier-protein] + CO(2) + [acyl-carrier-protein]. | |||
Q9FBC2 | Q9FBC2_STRPN |
KEGG Pathways | Map code | Pathways | E.C. |
---|---|---|
MAP00061 | Fatty acid biosynthesis |
Compound table | ||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Substrates | Products | Intermediates | ||||||||||||||
KEGG-id | C01209 | L00039 | C00001 | C00288 | C00229 | L00040 | I00138 | I00139 | I00140 | I00134 | I00141 | |||||
E.C. | ||||||||||||||||
Compound | malonyl-[acyl-carrier-protein] | (Z)-hexadec-11-enoyl-[acyl-carrier protein] | H2O | Bicabonate(HCO3-) | [acyl-carrier-protein] | (Z)-3-oxooctadec-13-enoyl-[acyl-carrier protein] | Peptidyl-Cys-tetrahedral-(Z)-hexadec-11-enoyl-[acyl-carrier protein] | Peptidyl-Cys-S-(Z)-hexadec-11-enoyl | [Acyl-carrier protein]-tetrahedral-malonyl group | [Acyl-carrier protein]-decarboxylated malonyl group (Peptidyl-Ser-phosphopantetheine-S-enolate) | Peptidyl-Cys-tetrahedral-(Z)-hexadec-11-enoyl-keto-[acyl-carrier protein] | |||||
Type | carbohydrate,carboxyl group,peptide/protein,phosphate group/phosphate ion,sulfide group | carbohydrate,lipid,peptide/protein,phosphate group/phosphate ion,sulfide group | H2O | carboxyl group | carbohydrate,peptide/protein,phosphate group/phosphate ion,sulfhydryl group | carbohydrate,lipid,peptide/protein,phosphate group/phosphate ion,sulfide group | ||||||||||
ChEBI |
15377 15377 |
17544 17544 |
||||||||||||||
PubChem |
22247451 962 22247451 962 |
22647601 769 22647601 769 |
||||||||||||||
1b3nA01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Transition-state-analogue:CER | ||||||
1kas001 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2gfvA01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2gfwA01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2gfxA01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2gfyA01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:DAO | Unbound | Unbound | Unbound | ||||||
3g0yA01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
3g11A01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
3hnzA01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
3ho2A01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
3ho9A01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
3i8pA01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
3e60A01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
3e60B01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
3kzuA01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
3kzuB01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
3kzuC01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
4ddoA01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
4f32A01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
4f32B01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1e5mA01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1j3nA01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1j3nB01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2gqdA01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2gqdB01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
3o04A01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1ox0A01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1oxhA01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1oxhB01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1oxhC01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1oxhD01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2almA01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2rjtA01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2rjtB01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2rjtC01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2rjtD01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1b3nA02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1kas002 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2gfvA02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2gfwA02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2gfxA02 | Analogue:PMN | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2gfyA02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
3g0yA02 | Analogue:P9A | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
3g11A02 | Analogue:P9C | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
3hnzA02 | Analogue:PMN | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
3ho2A02 | Analogue:N32 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
3ho9A02 | Analogue:N3A | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
3i8pA02 | Analogue:840 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
3e60A02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
3e60B02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
3kzuA02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
3kzuB02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
3kzuC02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
4ddoA02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
4f32A02 | Analogue:N32 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
4f32B02 | Analogue:N32 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1e5mA02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1j3nA02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1j3nB02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2gqdA02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2gqdB02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
3o04A02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1ox0A02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1oxhA02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1oxhB02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1oxhC02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1oxhD02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2almA02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2rjtA02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2rjtB02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2rjtC02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2rjtD02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
Reference for Active-site residues | ||
---|---|---|
resource | references | E.C. |
literature [1], [8], [10], [13], [14], [15], [16], [17], [20], [24], [30] [31] & CSA;1dd8 |
Active-site residues | ||||||||||
---|---|---|---|---|---|---|---|---|---|---|
PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
1b3nA01 | CYS 163 | CYS 163 | ||||||||
1kas001 | CYS 163 | CYS 163 | ||||||||
2gfvA01 | mutant C163Q | |||||||||
2gfwA01 | CYS 163 | CYS 163 | ||||||||
2gfxA01 | mutant C163Q | |||||||||
2gfyA01 | CYS 163 | CYS 163 | ||||||||
3g0yA01 | mutant C163Q | |||||||||
3g11A01 | mutant C163Q | |||||||||
3hnzA01 | mutant C163A | |||||||||
3ho2A01 | mutant C163A | |||||||||
3ho9A01 | mutant C163A | |||||||||
3i8pA01 | mutant C163A | |||||||||
3e60A01 | CYS 170 | CYS 170 | ||||||||
3e60B01 | CYS 170 | CYS 170 | ||||||||
3kzuA01 | CYS 170 | CYS 170 | ||||||||
3kzuB01 | CYS 170 | CYS 170 | ||||||||
3kzuC01 | CYS 170 | CYS 170 | ||||||||
4ddoA01 | CYS 172 | CYS 172 | ||||||||
4f32A01 | CSU 172(Cysteine-S-Sulfonic acid) | CSU 172 | ||||||||
4f32B01 | CSU 172(Cysteine-S-Sulfonic acid) | CSU 172 | ||||||||
1e5mA01 | CYS 167 | CYS 167 | ||||||||
1j3nA01 | CYS 161 | CYS 161 | ||||||||
1j3nB01 | CYS 161 | CYS 161 | ||||||||
2gqdA01 | CYS 165 | CYS 165 | ||||||||
2gqdB01 | CYS 165 | CYS 165 | ||||||||
3o04A01 | CYS 164 | CYS 164 | ||||||||
1ox0A01 | CYS 164 | CYS 164 | ||||||||
1oxhA01 | CYS 164 | CYS 164 | ||||||||
1oxhB01 | CYS 164 | CYS 164 | ||||||||
1oxhC01 | CYS 164 | CYS 164 | ||||||||
1oxhD01 | CYS 164 | CYS 164 | ||||||||
2almA01 | CYS 164 | CYS 164 | ||||||||
2rjtA01 | CYS 164 | CYS 164 | ||||||||
2rjtB01 | CYS 164 | CYS 164 | ||||||||
2rjtC01 | CYS 164 | CYS 164 | ||||||||
2rjtD01 | CYS 164 | CYS 164 | ||||||||
1b3nA02 | HIS 303;LYS 335;HIS 340 | PHE 400 | ||||||||
1kas002 | HIS 303;LYS 335;HIS 340 | PHE 400 | ||||||||
2gfvA02 | HIS 303;LYS 335;HIS 340 | PHE 400 | ||||||||
2gfwA02 | HIS 303;LYS 335;HIS 340 | PHE 400 | ||||||||
2gfxA02 | HIS 303;LYS 335;HIS 340 | PHE 400 | ||||||||
2gfyA02 | HIS 303;;HIS 340 | PHE 400 | mutant K335A | |||||||
3g0yA02 | HIS 303;LYS 335;HIS 340 | PHE 400 | ||||||||
3g11A02 | HIS 303;LYS 335;HIS 340 | PHE 400 | ||||||||
3hnzA02 | HIS 303;LYS 335;HIS 340 | PHE 400 | ||||||||
3ho2A02 | HIS 303;LYS 335;HIS 340 | PHE 400 | ||||||||
3ho9A02 | HIS 303;LYS 335;HIS 340 | PHE 400 | ||||||||
3i8pA02 | HIS 303;LYS 335;HIS 340 | PHE 400 | ||||||||
3e60A02 | HIS 311;LYS 342;HIS 347 | PHE 406 | ||||||||
3e60B02 | HIS 311;LYS 342;HIS 347 | PHE 406 | ||||||||
3kzuA02 | HIS 311;LYS 342;HIS 347 | PHE 406 | ||||||||
3kzuB02 | HIS 311;LYS 342;HIS 347 | PHE 406 | ||||||||
3kzuC02 | HIS 311;LYS 342;HIS 347 | PHE 406 | ||||||||
4ddoA02 | HIS 313;LYS 344;HIS 349 | PHE 409 | ||||||||
4f32A02 | HIS 313;LYS 344;HIS 349 | PHE 409 | ||||||||
4f32B02 | HIS 313;LYS 344;HIS 349 | PHE 409 | ||||||||
1e5mA02 | HIS 307;LYS 339;HIS 344 | PHE 403 | ||||||||
1j3nA02 | HIS 301;LYS 333;HIS 338 | PHE 396 | ||||||||
1j3nB02 | HIS 301;LYS 333;HIS 338 | PHE 396 | ||||||||
2gqdA02 | HIS 304;LYS 336;HIS 341 | PHE 400 | ||||||||
2gqdB02 | HIS 304;LYS 336;HIS 341 | PHE 400 | ||||||||
3o04A02 | HIS 303;LYS 335;HIS 340 | PHE 399 | ||||||||
1ox0A02 | HIS 303;LYS 332;HIS 337 | PHE 396 | ||||||||
1oxhA02 | HIS 303;LYS 332;HIS 337 | PHE 396 | ||||||||
1oxhB02 | HIS 303;LYS 332;HIS 337 | PHE 396 | ||||||||
1oxhC02 | HIS 303;LYS 332;HIS 337 | PHE 396 | ||||||||
1oxhD02 | HIS 303;LYS 332;HIS 337 | PHE 396 | ||||||||
2almA02 | ;LYS 332;HIS 337 | PHE 396 | mutant H303A, G379A | |||||||
2rjtA02 | HIS 303;LYS 332;HIS 337 | PHE 396 | mutant E22A, E94A, E325A, E383A, E409A | |||||||
2rjtB02 | HIS 303;LYS 332;HIS 337 | PHE 396 | mutant E22A, E94A, E325A, E383A, E409A | |||||||
2rjtC02 | HIS 303;LYS 332;HIS 337 | PHE 396 | mutant E22A, E94A, E325A, E383A, E409A | |||||||
2rjtD02 | HIS 303;LYS 332;HIS 337 | PHE 396 | mutant E22A, E94A, E325A, E383A, E409A |
References for Catalytic Mechanism | ||
---|---|---|
References | Sections | No. of steps in catalysis |
[1]
|
p.1186-1189 | |
[3]
|
Fig.1B, p.603-604 | |
[5]
|
p.9842-9844 | |
[6]
|
Table 4, p.496-498 | |
[7]
|
Fig.6, p.10883-10887 | |
[8]
|
p.4139-4141 | |
[9]
|
Fig.8, p.431-433 | |
[11]
|
Fig.7c, p.810-814 | |
[13]
|
Fig.6, p.17396-17398 | |
[15]
|
p.361-363 | |
[16]
|
Fig.5, p.696-697 |
References | |
---|---|
[1] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). |
Medline ID | |
PubMed ID | 9482715 |
Journal | EMBO J |
Year | 1998 |
Volume | 17 |
Pages | 1183-91 |
Authors | Huang W, Jia J, Edwards P, Dehesh K, Schneider G, Lindqvist Y |
Title | Crystal structure of beta-ketoacyl-acyl carrier protein synthase II from E.coli reveals the molecular architecture of condensing enzymes. |
Related PDB | 1kas |
Related UniProtKB | P0AAI5 |
[2] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS). |
Medline ID | |
PubMed ID | 10037680 |
Journal | J Biol Chem |
Year | 1999 |
Volume | 274 |
Pages | 6031-4 |
Authors | Moche M, Schneider G, Edwards P, Dehesh K, Lindqvist Y |
Title |
Structure of the complex between the antibiotic cerulenin and its target, |
Related PDB | 1b3n |
Related UniProtKB | P0AAI5 |
[3] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 11171140 |
Journal | Biochem Soc Trans |
Year | 2000 |
Volume | 28 |
Pages | 601-7 |
Authors | von Wettstein-Knowles P, Olsen J, Arnvig Mcguire K, Larsen S |
Title | Molecular aspects of beta-ketoacyl synthase (KAS) catalysis. |
Related PDB | |
Related UniProtKB | |
[4] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). |
Medline ID | |
PubMed ID | 10673437 |
Journal | Structure |
Year | 2000 |
Volume | 8 |
Pages | 185-95 |
Authors | Davies C, Heath RJ, White SW, Rock CO |
Title | The 1.8 A crystal structure and active-site architecture of beta-ketoacyl-acyl carrier protein synthase III (FabH) from escherichia coli. |
Related PDB | 1ebl |
Related UniProtKB | P0A6R0 |
[5] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 11502177 |
Journal | Biochemistry |
Year | 2001 |
Volume | 40 |
Pages | 9836-45 |
Authors | McGuire KA, Siggaard-Andersen M, Bangera MG, Olsen JG, von Wettstein-Knowles P |
Title | beta-Ketoacyl-[acyl carrier protein] synthase I of Escherichia coli: aspects of the condensation mechanism revealed by analyses of mutations in the active site pocket. |
Related PDB | |
Related UniProtKB | |
[6] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS). |
Medline ID | |
PubMed ID | 11152607 |
Journal | J Mol Biol |
Year | 2001 |
Volume | 305 |
Pages | 491-503 |
Authors | Moche M, Dehesh K, Edwards P, Lindqvist Y |
Title |
The crystal structure of beta-ketoacyl-acyl carrier protein synthase II from Synechocystis sp. |
Related PDB | 1e5m |
Related UniProtKB | P73283 |
[7] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 12196027 |
Journal | Biochemistry |
Year | 2002 |
Volume | 41 |
Pages | 10877-87 |
Authors | Witkowski A, Joshi AK, Smith S |
Title | Mechanism of the beta-ketoacyl synthase reaction catalyzed by the animal fatty acid synthase. |
Related PDB | |
Related UniProtKB | |
[8] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 12837788 |
Journal | J Bacteriol |
Year | 2003 |
Volume | 185 |
Pages | 4136-43 |
Authors | Price AC, Rock CO, White SW |
Title | The 1.3-Angstrom-resolution crystal structure of beta-ketoacyl-acyl carrier protein synthase II from Streptococcus pneumoniae. |
Related PDB | 1ox0 1oxh |
Related UniProtKB | |
[9] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 12866053 |
Journal | Proteins |
Year | 2003 |
Volume | 52 |
Pages | 427-35 |
Authors | Dawe JH, Porter CT, Thornton JM, Tabor AB |
Title | A template search reveals mechanistic similarities and differences in beta-ketoacyl synthases (KAS) and related enzymes. |
Related PDB | |
Related UniProtKB | |
[10] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 15286722 |
Journal | Nat Struct Mol Biol |
Year | 2004 |
Volume | 11 |
Pages | 888-93 |
Authors | Keatinge-Clay AT, Maltby DA, Medzihradszky KF, Khosla C, Stroud RM |
Title | An antibiotic factory caught in action. |
Related PDB | 1tqy |
Related UniProtKB | |
[11] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 15952903 |
Journal | Annu Rev Biochem |
Year | 2005 |
Volume | 74 |
Pages | 791-831 |
Authors | White SW, Zheng J, Zhang YM, Rock |
Title | The structural biology of type II fatty acid biosynthesis. |
Related PDB | |
Related UniProtKB | |
[12] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 16356722 |
Journal | Trends Biochem Sci |
Year | 2005 |
Volume | 31 |
Pages | 64-71 |
Authors | Haapalainen AM, Merilainen G, Wierenga RK |
Title | The thiolase superfamily: condensing enzymes with diverse reaction specificities. |
Related PDB | |
Related UniProtKB | |
[13] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 16618705 |
Journal | J Biol Chem |
Year | 2006 |
Volume | 281 |
Pages | 17390-9 |
Authors | Zhang YM, Hurlbert J, White SW, Rock CO |
Title |
Roles of the active site water, |
Related PDB | 2alm |
Related UniProtKB | |
[14] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 16710421 |
Journal | Nature |
Year | 2006 |
Volume | 441 |
Pages | 358-61 |
Authors | Wang J, Soisson SM, Young K, Shoop W, Kodali S, Galgoci A, Painter R, Parthasarathy G, Tang YS, Cummings R, Ha S, Dorso K, Motyl M, Jayasuriya H, Ondeyka J, Herath K, Zhang C, Hernandez L, Allocco J, Basilio A, Tormo JR, Genilloud O, Vicente F, Pelaez F, Colwell L, Lee SH, Michael B, Felcetto T, Gill C, Silver LL, Hermes JD, Bartizal K, Barrett J, Schmatz D, Becker JW, Cully D, Singh SB |
Title | Platensimycin is a selective FabF inhibitor with potent antibiotic properties. |
Related PDB | 2gfv 2gfw 2gfx 2gfy |
Related UniProtKB | |
[15] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 18453702 |
Journal | Acta Crystallogr Sect F Struct Biol Cryst Commun |
Year | 2008 |
Volume | 64 |
Pages | 358-66 |
Authors | Bagautdinov B, Ukita Y, Miyano M, Kunishima N |
Title | Structure of 3-oxoacyl-(acyl-carrier protein) synthase II from Thermus thermophilus HB8. |
Related PDB | 1j3n |
Related UniProtKB | |
[16] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 18824113 |
Journal | Mol Phylogenet Evol |
Year | 2008 |
Volume | 49 |
Pages | 691-701 |
Authors | Jiang C, Kim SY, Suh DY |
Title | Divergent evolution of the thiolase superfamily and chalcone synthase family. |
Related PDB | |
Related UniProtKB | |
[17] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 19233644 |
Journal | Bioorg Med Chem Lett |
Year | 2009 |
Volume | 19 |
Pages | 1623-7 |
Authors | Shen HC, Ding FX, Singh SB, Parthasarathy G, Soisson SM, Ha SN, Chen X, Kodali S, Wang J, Dorso K, Tata JR, Hammond ML, Maccoss M, Colletti SL |
Title | Synthesis and biological evaluation of platensimycin analogs. |
Related PDB | 3g0y 3g11 |
Related UniProtKB | |
[18] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 19581087 |
Journal | Bioorg Med Chem Lett |
Year | 2009 |
Volume | 19 |
Pages | 4756-9 |
Authors | Singh SB, Ondeyka JG, Herath KB, Zhang C, Jayasuriya H, Zink DL, Parthasarathy G, Becker JW, Wang J, Soisson SM |
Title |
Isolation, |
Related PDB | 3hnz 3ho2 3ho9 3i8p |
Related UniProtKB |
Comments |
---|
This enzyme belongs to thiolase superfamily (see [11] and [12]). Moreover, According to the literatre, (A) Transfer of acyl group from sulfur atom of acyl-ACP to catalytic cysteine (see [15]): (A0) Lys335 modulates the activity of His303 and His340. (A1) His340 (of 1b3n) may act as a general base to deprotonate the nucleophile, (A2) The activated thiol group of Cys163 makes a nucleophilic attack on the acyl group of acyl-ACP, (A3) His303 may act as a general acid to protonate the leaving sulfur atom of ACP, (B) Hydrolysis of carbon-carbon bond one of which is carboxyl carbon of malonyl-ACP,forming carbanion/enolate transition-state (I00134) (see [7] and [13]): (B0) Lys335 modulates the activity of His303 and His340. (B1) His303 acts as a general base to deprotonate a nearby water molecule to activate it. (B2) The activated water makes a nucleophilic attack on the carboxyl carbon (C3), (B3) The tetrahedral transition-state collapses, (C) Transfer of acyl group from catalytic cysteine to carbanion on the transition-state (I00134): (C0) Protonated His340 stabilizes the enol group of the transition-state (I00134). (C1) The carbanion makes a nucleophilic attack on the acyl group of the intermediate (I00139), (C2) His340 may act as a general acid to protonate the leaving catalytic residue, |
Created | Updated |
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2009-11-17 | 2012-07-24 |