DB code: S00328
| RLCP classification | 9.5010.536200.8010 : Hydride transfer | |
|---|---|---|
| CATH domain | 3.40.50.720 : Rossmann fold | Catalytic domain |
| E.C. | 1.1.1.100 | |
| CSA | ||
| M-CSA | ||
| MACiE | ||
| CATH domain | Related DB codes (homologues) |
|---|---|
| 3.40.50.720 : Rossmann fold | S00543 S00551 S00552 S00553 S00602 S00604 S00605 S00608 S00610 S00625 S00319 S00329 S00330 S00331 S00332 D00456 D00457 D00458 S00324 S00320 S00325 S00326 S00327 D00459 S00335 S00336 S00334 T00219 S00339 D00513 D00001 D00002 D00003 D00005 D00007 D00008 D00010 D00012 D00017 D00018 D00023 D00027 D00028 D00031 D00032 D00033 D00034 D00035 D00037 D00048 D00071 D00476 D00481 D00482 D00490 D00492 D00494 D00545 D00601 D00603 D00604 D00605 D00615 D00845 D00857 D00858 M00161 M00171 M00210 T00002 T00010 T00011 T00015 T00227 T00247 T00408 T00414 D00827 D00262 D00274 D00275 M00035 T00109 |
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | RefSeq | Pfam |
|---|---|---|---|---|
| P0AEK2 |
3-oxoacyl-[acyl-carrier-protein] reductase
|
EC
1.1.1.100
3-ketoacyl-acyl carrier protein reductase |
NP_415611.1
(Protein)
NC_000913.2 (DNA/RNA sequence) YP_489361.1 (Protein) NC_007779.1 (DNA/RNA sequence) |
PF00106
(adh_short)
[Graphical View] |
| C3NP04 |
|
None |
YP_002878083.1
(Protein)
NC_012668.1 (DNA/RNA sequence) |
PF00106
(adh_short)
[Graphical View] |
| Q9KQH7 |
3-oxoacyl-[acyl-carrier-protein] reductase
|
EC
1.1.1.100
3-ketoacyl-acyl carrier protein reductase |
NP_231655.1
(Protein)
NC_002505.1 (DNA/RNA sequence) |
PF00106
(adh_short)
[Graphical View] |
| Q9RPT1 |
Rhamnolipids biosynthesis 3-oxoacyl-[acyl-carrier-protein] reductase
|
EC
1.1.1.100
3-ketoacyl-acyl carrier protein reductase |
NP_252077.1
(Protein)
NC_002516.2 (DNA/RNA sequence) |
PF00106
(adh_short)
[Graphical View] |
| Q5NF68 |
|
3-oxoacyl-(Acyl-carrier-protein) reductase
EC 1.1.1.100 |
YP_170324.1
(Protein)
NC_006570.2 (DNA/RNA sequence) |
PF00106
(adh_short)
[Graphical View] |
| Q2YMG6 |
|
Short-chain dehydrogenase/reductase SDR:Glucose/ribitol dehydrogenase
EC 1.1.1.100 |
YP_413943.1
(Protein)
NC_007618.1 (DNA/RNA sequence) |
PF00106
(adh_short)
[Graphical View] |
| P50941 |
3-oxoacyl-[acyl-carrier-protein] reductase
|
EC
1.1.1.100
3-ketoacyl-acyl carrier protein reductase |
NP_221114.1
(Protein)
NC_000963.1 (DNA/RNA sequence) |
PF00106
(adh_short)
[Graphical View] |
| Q3JQ67 |
|
3-oxoacyl-(Acyl-carrier-protein) reductase
EC 1.1.1.100 |
YP_334286.1
(Protein)
NC_007434.1 (DNA/RNA sequence) |
PF00106
(adh_short)
[Graphical View] |
| P0A5Y4 |
3-oxoacyl-[acyl-carrier-protein] reductase
|
EC
1.1.1.100
3-ketoacyl-acyl carrier protein reductase |
NP_215999.1
(Protein)
NC_000962.3 (DNA/RNA sequence) NP_335981.1 (Protein) NC_002755.2 (DNA/RNA sequence) YP_006514867.1 (Protein) NC_018143.1 (DNA/RNA sequence) |
PF00106
(adh_short)
[Graphical View] |
| O67610 |
3-oxoacyl-[acyl-carrier-protein] reductase
|
EC
1.1.1.100
3-ketoacyl-acyl carrier protein reductase |
NP_214176.1
(Protein)
NC_000918.1 (DNA/RNA sequence) |
[Graphical View] |
| Q81JG6 |
|
3-oxoacyl-(Acyl-carrier-protein) reductase
|
NP_846231.1
(Protein)
NC_003997.3 (DNA/RNA sequence) YP_020629.1 (Protein) NC_007530.2 (DNA/RNA sequence) YP_029953.1 (Protein) NC_005945.1 (DNA/RNA sequence) |
PF00106
(adh_short)
[Graphical View] |
| P0A0H9 |
3-oxoacyl-[acyl-carrier-protein] reductase
|
EC
1.1.1.100
3-ketoacyl-acyl carrier protein reductase |
NP_371755.1
(Protein)
NC_002758.2 (DNA/RNA sequence) |
PF00106
(adh_short)
[Graphical View] |
| A3DDY9 |
|
3-oxoacyl-[acyl-carrier-protein] reductase
EC 1.1.1.100 |
YP_001037361.1
(Protein)
NC_009012.1 (DNA/RNA sequence) |
PF00106
(adh_short)
[Graphical View] |
| KEGG enzyme name |
|---|
|
3-oxoacyl-[acyl-carrier-protein] reductase
beta-ketoacyl-[acyl-carrier protein](ACP) reductase beta-ketoacyl acyl carrier protein (ACP) reductase beta-ketoacyl reductase beta-ketoacyl thioester reductase beta-ketoacyl-ACP reductase beta-ketoacyl-acyl carrier protein reductase 3-ketoacyl acyl carrier protein reductase NADPH-specific 3-oxoacyl-[acylcarrier protein]reductase 3-oxoacyl-[ACP]reductase (3R)-3-hydroxyacyl-[acyl-carrier-protein]:NADP+ oxidoreductase |
| UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
|---|---|---|---|---|---|
| P0AEK2 | FABG_ECOLI | (3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP(+) = 3-oxoacyl-[acyl-carrier-protein] + NADPH. | Homotetramer. | ||
| C3NP04 | C3NP04_VIBCJ | ||||
| Q9KQH7 | FABG_VIBCH | (3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP(+) = 3-oxoacyl-[acyl-carrier-protein] + NADPH. | Homotetramer (By similarity). | ||
| Q9RPT1 | RHLG_PSEAE | (3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP(+) = 3-oxoacyl-[acyl-carrier-protein] + NADPH. | |||
| Q5NF68 | Q5NF68_FRATT | ||||
| Q2YMG6 | Q2YMG6_BRUA2 | ||||
| P50941 | FABG_RICPR | (3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP(+) = 3-oxoacyl-[acyl-carrier-protein] + NADPH. | Homotetramer. | ||
| Q3JQ67 | Q3JQ67_BURP1 | ||||
| P0A5Y4 | FABG_MYCTU | (3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP(+) = 3-oxoacyl-[acyl-carrier-protein] + NADPH. | Homotetramer. | ||
| O67610 | FABG_AQUAE | (3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP(+) = 3-oxoacyl-[acyl-carrier-protein] + NADPH. | Homotetramer. | ||
| Q81JG6 | Q81JG6_BACAN | ||||
| P0A0H9 | FABG_STAAM | (3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP(+) = 3-oxoacyl-[acyl-carrier-protein] + NADPH. | Homotetramer. | ||
| A3DDY9 | A3DDY9_CLOTH |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|---|---|
| MAP00061 | Fatty acid biosynthesis | |
| MAP01040 | Biosynthesis of unsaturated fatty acids |
| Compound table | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Substrates | Products | Intermediates | |||||||||
| KEGG-id | C00005 | C00685 | C00080 | C00006 | C01271 | ||||||
| E.C. | |||||||||||
| Compound | NADPH | 3-Oxoacyl-[acyl-carrier protein] | H+ | NADP+ | (3R)-3-Hydroxyacyl-[acyl-carrier protein] | ||||||
| Type | amide group,amine group,nucleotide | carbohydrate,peptide/protein,phosphate group/phosphate ion,sulfide group | others | amide group,amine group,nucleotide | carbohydrate,peptide/protein,phosphate group/phosphate ion,sulfide group | ||||||
| ChEBI |
16474 16474 |
15378 15378 |
18009 18009 |
||||||||
| PubChem |
5884 5884 |
1038 1038 |
5886 5886 |
||||||||
| 1i01A |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1i01B |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1i01C |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1i01D |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1i01E |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1i01F |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1i01G |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1i01H |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1q7bA |
|
|
|
|
|
Unbound | Unbound | Bound:NAP | Unbound | ||
| 1q7bB |
|
|
|
|
|
Unbound | Unbound | Bound:NAP | Unbound | ||
| 1q7bC |
|
|
|
|
|
Unbound | Unbound | Bound:NAP | Unbound | ||
| 1q7bD |
|
|
|
|
|
Unbound | Unbound | Bound:NAP | Unbound | ||
| 1q7cA |
|
|
|
|
|
Unbound | Unbound | Bound:NAP | Unbound | ||
| 1q7cB |
|
|
|
|
|
Unbound | Unbound | Bound:NAP | Unbound | ||
| 3op4A |
|
|
|
|
|
Unbound | Analogue:ACT | Bound:NAP | Unbound | ||
| 3op4B |
|
|
|
|
|
Unbound | Analogue:ACT | Bound:NAP | Unbound | ||
| 3rroA |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 3rroB |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 3rshA |
|
|
|
|
|
Unbound | Unbound | Bound:NAP | Unbound | ||
| 3rshB |
|
|
|
|
|
Unbound | Unbound | Bound:NAP | Unbound | ||
| 2b4qA |
|
|
|
|
|
Unbound | Unbound | Bound:NAP | Unbound | ||
| 2b4qB |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 3lylA |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 3lylB |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 3lylC |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 3lylD |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 3emkA |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 3emkB |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 3emkC |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 3emkD |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 3ennA |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 3ennB |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 3ennC |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 3ennD |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 3f9iA |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 3f9iB |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 3ftpA |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 3ftpB |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 3ftpC |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 3ftpD |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1uzlA |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1uzlB |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1uzmA |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1uzmB |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1uznA |
|
|
|
|
|
Unbound | Unbound | Analogue:NAP | Unbound | ||
| 1uznB |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 2ntnA |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 2ntnB |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 2p68A |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 2p68B |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 2pnfA |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 2pnfB |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 2uvdA |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 2uvdB |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 2uvdC |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 2uvdD |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 2uvdE |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 2uvdF |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 2uvdG |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 2uvdH |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 3osuA |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 3osuB |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 2hq1A |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| Reference for Active-site residues | ||
|---|---|---|
| resource | references | E.C. |
| Swiss-prot;P0AEK2 & literature [14] | ||
| Active-site residues | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 1i01A |
|
|
|
|
|
SER 138;;LYS 155 | invisible Y151 | |||
| 1i01B |
|
|
|
|
|
SER 138;TYR 151;LYS 155 | ||||
| 1i01C |
|
|
|
|
|
SER 138;TYR 151;LYS 155 | ||||
| 1i01D |
|
|
|
|
|
SER 138;TYR 151;LYS 155 | ||||
| 1i01E |
|
|
|
|
|
SER 138;TYR 151;LYS 155 | ||||
| 1i01F |
|
|
|
|
|
SER 138;;LYS 155 | invisible Y151 | |||
| 1i01G |
|
|
|
|
|
;TYR 151;LYS 155 | invisible S138 | |||
| 1i01H |
|
|
|
|
|
;TYR 151;LYS 155 | invisible S138 | |||
| 1q7bA |
|
|
|
|
|
SER 138;TYR 151;LYS 155 | ||||
| 1q7bB |
|
|
|
|
|
SER 138;TYR 151;LYS 155 | ||||
| 1q7bC |
|
|
|
|
|
SER 138;TYR 151;LYS 155 | ||||
| 1q7bD |
|
|
|
|
|
SER 138;TYR 151;LYS 155 | ||||
| 1q7cA |
|
|
|
|
|
SER 138;;LYS 155 | mutant Y151F | |||
| 1q7cB |
|
|
|
|
|
SER 138;;LYS 155 | mutant Y151F | |||
| 3op4A |
|
|
|
|
|
SER 142;TYR 155;LYS 159 | ||||
| 3op4B |
|
|
|
|
|
SER 142;TYR 155;LYS 159 | ||||
| 3rroA |
|
|
|
|
|
SER 142;TYR 155;LYS 159 | ||||
| 3rroB |
|
|
|
|
|
SER 142;TYR 155;LYS 159 | ||||
| 3rshA |
|
|
|
|
|
SER 142;TYR 155;LYS 159 | invisible 195-197 | |||
| 3rshB |
|
|
|
|
|
SER 142;TYR 155;LYS 159 | invisible 195 | |||
| 2b4qA |
|
|
|
|
|
SER 148;TYR 162;LYS 166 | ||||
| 2b4qB |
|
|
|
|
|
SER 148;TYR 162;LYS 166 | ||||
| 3lylA |
|
|
|
|
|
SER 141;TYR 154;LYS 158 | ||||
| 3lylB |
|
|
|
|
|
SER 141;TYR 154;LYS 158 | ||||
| 3lylC |
|
|
|
|
|
SER 141;TYR 154;LYS 158 | ||||
| 3lylD |
|
|
|
|
|
SER 141;TYR 154;LYS 158 | ||||
| 3emkA |
|
|
|
|
|
SER 139;TYR 152;LYS 156 | invisible 190-194 | |||
| 3emkB |
|
|
|
|
|
SER 139;TYR 152;LYS 156 | invisible 186-197 | |||
| 3emkC |
|
|
|
|
|
SER 139;TYR 152;LYS 156 | invisible 185-194 | |||
| 3emkD |
|
|
|
|
|
SER 139;TYR 152;LYS 156 | invisible 187-194 | |||
| 3ennA |
|
|
|
|
|
SER 139;TYR 152;LYS 156 | invisible 188-195 | |||
| 3ennB |
|
|
|
|
|
SER 139;TYR 152;LYS 156 | invisible 188-193 | |||
| 3ennC |
|
|
|
|
|
SER 139;TYR 152;LYS 156 | invisible 187-197 | |||
| 3ennD |
|
|
|
|
|
SER 139;TYR 152;LYS 156 | invisible 187-197 | |||
| 3f9iA |
|
|
|
|
|
SER 135;TYR 148;LYS 152 | invisible 86-98, 139-140, 183-188 | |||
| 3f9iB |
|
|
|
|
|
SER 135;TYR 148;LYS 152 | invisible 88-98, 140 | |||
| 3ftpA |
|
|
|
|
|
SER 143;TYR 156;LYS 160 | ||||
| 3ftpB |
|
|
|
|
|
SER 143;TYR 156;LYS 160 | ||||
| 3ftpC |
|
|
|
|
|
SER 143;TYR 156;LYS 160 | ||||
| 3ftpD |
|
|
|
|
|
SER 143;TYR 156;LYS 160 | ||||
| 1uzlA |
|
|
|
|
|
SER 140;TYR 153;LYS 157 | invisible 95-99, 147-149 | |||
| 1uzlB |
|
|
|
|
|
SER 140;TYR 153;LYS 157 | ||||
| 1uzmA |
|
|
|
|
|
SER 140;TYR 153;LYS 157 | invisible 94-98, 144-148 | |||
| 1uzmB |
|
|
|
|
|
SER 140;TYR 153;LYS 157 | invisible 94-99, 143-149 | |||
| 1uznA |
|
|
|
|
|
SER 140;TYR 153;LYS 157 | ||||
| 1uznB |
|
|
|
|
|
SER 140;TYR 153;LYS 157 | invisible 189-201 | |||
| 2ntnA |
|
|
|
|
|
SER 140;TYR 153;LYS 157 | invisible 92-99, 142-149, 196-198 | |||
| 2ntnB |
|
|
|
|
|
SER 140;TYR 153;LYS 157 | invisible 92-99, 142-149, 189-202 | |||
| 2p68A |
|
|
|
|
|
SER 144;TYR 157;LYS 161 | ||||
| 2p68B |
|
|
|
|
|
SER 144;TYR 157;LYS 161 | invisible 199-203 | |||
| 2pnfA |
|
|
|
|
|
SER 144;TYR 157;LYS 161 | ||||
| 2pnfB |
|
|
|
|
|
SER 144;TYR 157;LYS 161 | ||||
| 2uvdA |
|
|
|
|
|
SER 141;TYR 154;LYS 158 | ||||
| 2uvdB |
|
|
|
|
|
SER 141;TYR 154;LYS 158 | ||||
| 2uvdC |
|
|
|
|
|
SER 141;TYR 154;LYS 158 | ||||
| 2uvdD |
|
|
|
|
|
SER 141;TYR 154;LYS 158 | ||||
| 2uvdE |
|
|
|
|
|
SER 141;TYR 154;LYS 158 | ||||
| 2uvdF |
|
|
|
|
|
SER 141;TYR 154;LYS 158 | ||||
| 2uvdG |
|
|
|
|
|
SER 141;TYR 154;LYS 158 | ||||
| 2uvdH |
|
|
|
|
|
SER 141;TYR 154;LYS 158 | ||||
| 3osuA |
|
|
|
|
|
SER 141;TYR 154;LYS 158 | ||||
| 3osuB |
|
|
|
|
|
SER 141;TYR 154;LYS 158 | ||||
| 2hq1A |
|
|
|
|
|
SER 142;TYR 155;LYS 159 | ||||
| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
|
[8]
|
Fig.3, p.342 | |
|
[13]
|
p.458-459 | |
|
[14]
|
Fig.7, p.424-425 | |
|
[17]
|
Fig.2, p.566 | |
| References | |
|---|---|
| [1] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 6756317 |
| Journal | Arch Biochem Biophys |
| Year | 1982 |
| Volume | 218 |
| Pages | 77-91 |
| Authors | Shimakata T, Stumpf PK |
| Title |
Purification and characterizations of beta-Ketoacyl-[acyl-carrier-protein] reductase, |
| Related PDB | |
| Related UniProtKB | |
| [2] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 1562581 |
| Journal | Biochim Biophys Acta |
| Year | 1992 |
| Volume | 1120 |
| Pages | 151-9 |
| Authors | Sheldon PS, Kekwick RG, Smith CG, Sidebottom C, Slabas AR |
| Title | 3-Oxoacyl-[ACP] reductase from oilseed rape (Brassica napus). |
| Related PDB | |
| Related UniProtKB | |
| [3] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8550484 |
| Journal | J Bacteriol |
| Year | 1996 |
| Volume | 178 |
| Pages | 571-3 |
| Authors | Shen Z, Byers DM |
| Title |
Isolation of Vibrio harveyi acyl carrier protein and the fabG, |
| Related PDB | |
| Related UniProtKB | |
| [4] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9342868 |
| Journal | Plant Physiol |
| Year | 1997 |
| Volume | 115 |
| Pages | 501-10 |
| Authors | Xu X, Dietrich CR, Delledonne M, Xia Y, Wen TJ, Robertson DS, Nikolau BJ, Schnable PS |
| Title | Sequence analysis of the cloned glossy8 gene of maize suggests that it may code for a beta-ketoacyl reductase required for the biosynthesis of cuticular waxes. |
| Related PDB | |
| Related UniProtKB | |
| [5] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9761917 |
| Journal | Acta Crystallogr D Biol Crystallogr |
| Year | 1998 |
| Volume | 54 |
| Pages | 427-9 |
| Authors | Rafferty JB, Fisher M, Langridge SJ, Martindale W, Thomas NC, Simon JW, Bithell S, Slabas AR, Rice DW |
| Title | Crystallization of the NADP-dependent beta-keto acyl carrier protein reductase from Escherichia coli. |
| Related PDB | |
| Related UniProtKB | |
| [6] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10666637 |
| Journal | Acta Crystallogr D Biol Crystallogr |
| Year | 2000 |
| Volume | 56 |
| Pages | 86-8 |
| Authors | Fisher M, Sedelnikova SE, Martindale W, Thomas NC, Simon JW, Slabas AR, Rafferty JB |
| Title | Crystallization of the NADP-dependent beta-keto acyl-carrier protein reductase from Brassica napus. |
| Related PDB | |
| Related UniProtKB | |
| [7] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10747933 |
| Journal | J Biol Chem |
| Year | 2000 |
| Volume | 275 |
| Pages | 16857-64 |
| Authors | Kremer L, Douglas JD, Baulard AR, Morehouse C, Guy MR, Alland D, Dover LG, Lakey JH, Jacobs WR Jr, Brennan PJ, Minnikin DE, Besra GS |
| Title | Thiolactomycin and related analogues as novel anti-mycobacterial agents targeting KasA and KasB condensing enzymes in Mycobacterium tuberculosis. |
| Related PDB | |
| Related UniProtKB | |
| [8] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10801480 |
| Journal | Structure Fold Des |
| Year | 2000 |
| Volume | 8 |
| Pages | 339-47 |
| Authors | Fisher M, Kroon JT, Martindale W, Stuitje AR, Slabas AR, Rafferty JB |
| Title | The X-ray structure of Brassica napus beta-keto acyl carrier protein reductase and its implications for substrate binding and catalysis. |
| Related PDB | |
| Related UniProtKB | |
| [9] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). |
| Medline ID | |
| PubMed ID | 11669613 |
| Journal | Biochemistry |
| Year | 2001 |
| Volume | 40 |
| Pages | 12772-81 |
| Authors | Price AC, Zhang YM, Rock CO, White SW |
| Title | Structure of beta-ketoacyl-[acyl carrier protein] reductase from Escherichia coli: negative cooperativity and its structural basis. |
| Related PDB | 1i01 |
| Related UniProtKB | P0AEK2 |
| [10] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 12079383 |
| Journal | J Mol Biol |
| Year | 2002 |
| Volume | 320 |
| Pages | 249-61 |
| Authors | Cohen-Gonsaud M, Ducasse S, Hoh F, Zerbib D, Labesse G, Quemard A |
| Title |
Crystal structure of MabA from Mycobacterium tuberculosis, |
| Related PDB | 1uzl 1uzm 1unz |
| Related UniProtKB | |
| [11] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11932442 |
| Journal | Microbiology |
| Year | 2002 |
| Volume | 148 |
| Pages | 951-60 |
| Authors | Marrakchi H, Ducasse S, Labesse G, Montrozier H, Margeat E, Emorine L, Charpentier X, Daffe M, Quemard A |
| Title |
MabA (FabG1), |
| Related PDB | |
| Related UniProtKB | |
| [12] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 14527946 |
| Journal | J Biol Chem |
| Year | 2003 |
| Volume | 278 |
| Pages | 52935-43 |
| Authors | Zhang YM, Wu B, Zheng J, Rock CO |
| Title | Key residues responsible for acyl carrier protein and beta-ketoacyl-acyl carrier protein reductase (FabG) interaction. |
| Related PDB | |
| Related UniProtKB | |
| [13] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 12524453 |
| Journal | Proc Natl Acad Sci U S A |
| Year | 2003 |
| Volume | 100 |
| Pages | 455-60 |
| Authors | Yang JK, Park MS, Waldo GS, Suh SW |
| Title | Directed evolution approach to a structural genomics project: Rv2002 from Mycobacterium tuberculosis. |
| Related PDB | |
| Related UniProtKB | |
| [14] | |
| Resource | |
| Comments | X-ray crystallography |
| Medline ID | |
| PubMed ID | 15016358 |
| Journal | Structure (Camb) |
| Year | 2004 |
| Volume | 12 |
| Pages | 417-28 |
| Authors | Price AC, Zhang YM, Rock CO, White SW |
| Title | Cofactor-induced conformational rearrangements establish a catalytically competent active site and a proton relay conduit in FabG. |
| Related PDB | 1q7b 1q7c |
| Related UniProtKB | |
| [15] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 16624803 |
| Journal | J Biol Chem |
| Year | 2006 |
| Volume | 281 |
| Pages | 18025-32 |
| Authors | Miller DJ, Zhang YM, Rock CO, White SW |
| Title |
Structure of RhlG, |
| Related PDB | 2b4q |
| Related UniProtKB | |
| [16] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 17642518 |
| Journal | Acta Crystallogr D Biol Crystallogr |
| Year | 2007 |
| Volume | 63 |
| Pages | 923-5 |
| Authors | Poncet-Montange G, Ducasse-Cabanot S, Quemard A, Labesse G, Cohen-Gonsaud M |
| Title | Lack of dynamics in the MabA active site kills the enzyme activity: practical consequences for drug-design studies. |
| Related PDB | 2ntn |
| Related UniProtKB | |
| [17] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 17894349 |
| Journal | Proteins |
| Year | 2008 |
| Volume | 70 |
| Pages | 562-7 |
| Authors | Zaccai NR, Carter LG, Berrow NS, Sainsbury S, Nettleship JE, Walter TS, Harlos K, Owens RJ, Wilson KS, Stuart DI, Esnouf RM |
| Title | Crystal structure of a 3-oxoacyl-(acylcarrier protein) reductase (BA3989) from Bacillus anthracis at 2.4-A resolution. |
| Related PDB | 2uvd |
| Related UniProtKB | |
| Comments |
|---|
|
Although this enzyme binds calcium ions, This enzyme belongs to the short-chain dehydrogenase/reductase (SDR) superfamily, (A) Hydride transfer from NADPH to keto-substrate (Reduction): |
| Created | Updated |
|---|---|
| 2004-05-12 | 2012-06-01 |