SitesBLAST
Comparing AZOBR_RS29790 AZOBR_RS29790 3-ketoacyl-ACP reductase to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
6b9uA Crystal structure of 3-ketoacyl-(acyl-carrier-protein) reductase from brucella melitensis complexed with nadh
47% identity, 98% coverage: 5:250/250 of query aligns to 2:244/244 of 6b9uA
- active site: G15 (= G18), S142 (= S141), L152 (= L151), Y155 (= Y154), K159 (= K158)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G11 (= G14), S14 (≠ Q17), G15 (= G18), F16 (≠ L19), D35 (= D38), R36 (≠ I39), D37 (≠ N40), A57 (= A60), D58 (≠ N61), I59 (≠ V62), N85 (= N88), A86 (= A89), G87 (= G90), I88 (≠ S91), V109 (≠ L112), V140 (≠ L139), A141 (≠ G140), S142 (= S141), Y155 (= Y154), K159 (= K158), P185 (= P184), V186 (= V185), A187 (= A186), G188 (≠ T187), T190 (= T189), P191 (= P190), L192 (= L191), F196 (= F195)
7krmC Putative fabg bound to nadh from acinetobacter baumannii
37% identity, 98% coverage: 5:250/250 of query aligns to 3:243/244 of 7krmC
- active site: G18 (= G18), S140 (= S141), Y155 (= Y154)
- binding nicotinamide-adenine-dinucleotide: G12 (= G14), A14 (= A16), S15 (vs. gap), G18 (= G18), I19 (≠ L19), D38 (= D38), L39 (≠ I39), A60 (= A60), N61 (= N61), V62 (= V62), N88 (= N88), A89 (= A89), G90 (= G90), I91 (≠ S91), V111 (≠ L112), L138 (= L139), S139 (≠ G140), S140 (= S141), Y155 (= Y154), K159 (= K158), P185 (= P184), G186 (≠ V185), I188 (≠ T187), T190 (= T189)
4nbuB Crystal structure of fabg from bacillus sp (see paper)
39% identity, 98% coverage: 4:247/250 of query aligns to 4:241/244 of 4nbuB
- active site: G18 (= G18), N111 (= N113), S139 (= S141), Q149 (≠ L151), Y152 (= Y154), K156 (= K158)
- binding acetoacetyl-coenzyme a: T91 (= T92), D93 (≠ N95), K98 (≠ N100), S139 (= S141), T141 (≠ A143), N146 (≠ R148), V147 (≠ P149), G148 (= G150), Q149 (≠ L151), Y152 (= Y154), F184 (≠ A186), M189 (≠ L191), K200 (≠ R206)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G14), A16 (= A16), N17 (≠ Q17), G18 (= G18), I19 (≠ L19), D38 (= D38), F39 (≠ I39), N40 (= N40), V59 (≠ A60), D60 (≠ N61), V61 (= V62), N87 (= N88), A88 (= A89), G89 (= G90), I90 (≠ S91), V110 (≠ L112), T137 (≠ L139), S138 (≠ G140), S139 (= S141), Y152 (= Y154), K156 (= K158), P182 (= P184), G183 (≠ V185), F184 (≠ A186), T185 (= T187), T187 (= T189), A188 (≠ P190), M189 (≠ L191), V190 (≠ L192)
3op4A Crystal structure of putative 3-ketoacyl-(acyl-carrier-protein) reductase from vibrio cholerae o1 biovar eltor str. N16961 in complex with NADP+ (see paper)
39% identity, 97% coverage: 5:247/250 of query aligns to 6:243/247 of 3op4A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G14), S17 (≠ A16), R18 (≠ Q17), G19 (= G18), I20 (≠ L19), A39 (≠ D38), T40 (≠ I39), L61 (≠ A60), N62 (= N61), V63 (= V62), N89 (= N88), A90 (= A89), G91 (= G90), I92 (≠ S91), T112 (≠ L112), V139 (≠ L139), G140 (= G140), S141 (= S141), Y154 (= Y154), K158 (= K158), P184 (= P184), G185 (≠ V185), F186 (≠ A186), I187 (≠ T187), T189 (= T189), D190 (≠ P190), M191 (≠ L191)
4i08A Crystal structure of beta-ketoacyl-acyl carrier protein reductase (fabg) from vibrio cholerae in complex with NADPH (see paper)
39% identity, 97% coverage: 5:247/250 of query aligns to 6:239/243 of 4i08A
- active site: G19 (= G18), N113 (= N113), S141 (= S141), Q151 (≠ L151), Y154 (= Y154), K158 (= K158)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G15 (= G14), S17 (≠ A16), R18 (≠ Q17), G19 (= G18), I20 (≠ L19), A39 (≠ D38), T40 (≠ I39), L61 (≠ A60), N62 (= N61), V63 (= V62), N89 (= N88), A90 (= A89), G91 (= G90), I92 (≠ S91), T112 (≠ L112), V139 (≠ L139), G140 (= G140), S141 (= S141), Y154 (= Y154), K158 (= K158), P184 (= P184), G185 (≠ V185), F186 (≠ A186), I187 (≠ T187), T189 (= T189)
8cxaA Crystal structure of 3-oxoacyl-[acyl-carrier-protein] reductase from mycobacterium smegmatis with bound NAD
40% identity, 98% coverage: 4:247/250 of query aligns to 2:247/251 of 8cxaA
- binding nicotinamide-adenine-dinucleotide: G12 (= G14), A14 (= A16), Q15 (= Q17), G16 (= G18), I17 (≠ L19), D36 (= D38), I37 (= I39), V61 (≠ A60), D62 (≠ N61), V63 (= V62), N89 (= N88), A90 (= A89), A91 (≠ G90), I92 (vs. gap), F93 (vs. gap), S94 (= S91), V115 (≠ L112), I142 (≠ L139), S143 (≠ G140), S144 (= S141), Y157 (= Y154), K161 (= K158), P187 (= P184), H188 (vs. gap), G189 (vs. gap), I190 (≠ V185), I194 (≠ T189)
2cfcA Structural basis for stereo selectivity in the (r)- and (s)-hydroxypropylethane thiosulfonate dehydrogenases (see paper)
38% identity, 96% coverage: 8:246/250 of query aligns to 3:245/250 of 2cfcA
- active site: G13 (= G18), S142 (= S141), Y155 (= Y154), K159 (= K158)
- binding (2-[2-ketopropylthio]ethanesulfonate: T91 (= T92), S142 (= S141), V143 (≠ T142), A144 (= A143), F149 (≠ R148), R152 (≠ L151), Y155 (= Y154), G186 (≠ V185), T193 (≠ L192), W195 (≠ T194), R196 (≠ F195)
- binding nicotinamide-adenine-dinucleotide: G9 (= G14), S11 (≠ A16), S12 (≠ Q17), G13 (= G18), N14 (≠ L19), D33 (= D38), L34 (≠ I39), A59 (= A60), D60 (≠ N61), V61 (= V62), N87 (= N88), A88 (= A89), G89 (= G90), I90 (≠ S91), V113 (≠ L112), I140 (≠ L139), A141 (≠ G140), Y155 (= Y154), K159 (= K158), P185 (= P184), G186 (≠ V185), M187 (≠ A186), I188 (≠ T187), T190 (= T189), P191 (= P190), M192 (≠ L191), T193 (≠ L192)
Q56840 2-(R)-hydroxypropyl-CoM dehydrogenase; R-HPCDH; 2-[(R)-2-hydroxypropylthio]ethanesulfonate dehydrogenase; Aliphatic epoxide carboxylation component III; Epoxide carboxylase component III; RHPCDH1; EC 1.1.1.268 from Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2) (see 4 papers)
38% identity, 96% coverage: 8:246/250 of query aligns to 3:245/250 of Q56840
- SGN 12:14 (≠ QGL 17:19) binding
- D33 (= D38) binding
- DV 60:61 (≠ NV 61:62) binding
- N87 (= N88) binding
- S142 (= S141) mutation to A: Retains weak activity. 120-fold decrease in kcat.; mutation to C: Loss of activity.
- R152 (≠ L151) binding ; mutation to A: Almost loss of activity with the natural substrate 2-KPC, but does not affect activity with 2-butanone as substrate.
- Y155 (= Y154) mutation Y->E,F: Loss of activity.
- K159 (= K158) mutation to A: Loss of activity.
- R179 (= R178) mutation to A: Loss of activity.
- IETPM 188:192 (≠ TETPL 187:191) binding
- WR 195:196 (≠ TF 194:195) binding
- R196 (≠ F195) mutation to A: Almost loss of activity with the natural substrate 2-KPC, but does not affect activity with 2-butanone as substrate.
- R203 (= R204) mutation to A: Slight decrease in catalytic efficiency.
- R209 (≠ I210) mutation to A: Does not affect catalytic efficiency.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
6t77A Crystal structure of klebsiella pneumoniae fabg(NADPH-dependent) NADP- complex at 1.75 a resolution (see paper)
37% identity, 97% coverage: 5:247/250 of query aligns to 3:240/244 of 6t77A
- active site: G16 (= G18), S138 (= S141), Y151 (= Y154)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G14), S14 (≠ A16), R15 (≠ Q17), A36 (≠ D38), T37 (≠ I39), L58 (≠ A60), N59 (= N61), V60 (= V62), A87 (= A89), G88 (= G90), I89 (≠ S91), T109 (≠ L112)
6pejA Structure of sorbitol dehydrogenase from sinorhizobium meliloti 1021 bound to sorbitol
39% identity, 98% coverage: 3:247/250 of query aligns to 2:253/257 of 6pejA
- active site: G17 (= G18), S140 (= S141), Y153 (= Y154)
- binding sorbitol: F91 (≠ H93), S140 (= S141), Q141 (≠ T142), A142 (= A143), R145 (= R146), E147 (≠ R148), Y153 (= Y154), G184 (≠ V185), V185 (≠ A186), H190 (vs. gap), W191 (vs. gap), F198 (≠ L192), V213 (≠ M208)
7v0hG Crystal structure of putative glucose 1-dehydrogenase from burkholderia cenocepacia in complex with NADP and a potential reaction product
39% identity, 98% coverage: 3:247/250 of query aligns to 7:251/253 of 7v0hG
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G18 (= G14), S20 (≠ A16), K21 (≠ Q17), G22 (= G18), I23 (≠ L19), N41 (= N40), Y42 (≠ G41), A43 (≠ D42), S44 (≠ A43), S45 (≠ A44), G68 (≠ A60), D69 (≠ N61), V70 (= V62), N96 (= N88), S97 (≠ A89), G98 (= G90), V99 (≠ T92), Y100 (≠ H93), T119 (≠ L112), I144 (≠ L139), S145 (≠ G140), S146 (= S141), Y159 (= Y154), K163 (= K158), P189 (= P184), G190 (vs. gap), M191 (vs. gap), I192 (≠ V185), T194 (= T187), E195 (= E188), G196 (≠ T189), T197 (≠ P190)
- binding (2R)-2-(hydroxymethyl)pentanedioic acid: Y100 (≠ H93), F102 (≠ N95), S146 (= S141), V147 (≠ T142), V148 (≠ A143), Y159 (= Y154), G190 (vs. gap), M191 (vs. gap), I202 (≠ F195), V211 (≠ M207)
P0AEK2 3-oxoacyl-[acyl-carrier-protein] reductase FabG; 3-ketoacyl-acyl carrier protein reductase; Beta-Ketoacyl-acyl carrier protein reductase; Beta-ketoacyl-ACP reductase; EC 1.1.1.100 from Escherichia coli (strain K12) (see 2 papers)
37% identity, 97% coverage: 5:247/250 of query aligns to 3:240/244 of P0AEK2
- GASR 12:15 (≠ GAAQ 14:17) binding
- T37 (≠ I39) binding
- NV 59:60 (= NV 61:62) binding
- N86 (= N88) binding
- Y151 (= Y154) mutation to F: Defect in the affinity for NADPH.
- YAAAK 151:155 (≠ YNATK 154:158) binding
- A154 (≠ T157) mutation to T: Decreases in the thermolability of the reductase; when associated with K-233.
- K155 (= K158) mutation to A: Defect in the affinity for NADPH.
- I184 (≠ T187) binding
- E233 (≠ V240) mutation to K: Decreases in the thermolability of the reductase; when associated with T-154.
1q7bA The structure of betaketoacyl-[acp] reductase from e. Coli in complex with NADP+ (see paper)
37% identity, 97% coverage: 5:247/250 of query aligns to 2:239/243 of 1q7bA
- active site: G15 (= G18), E101 (= E105), S137 (= S141), Q147 (≠ L151), Y150 (= Y154), K154 (= K158)
- binding calcium ion: E232 (≠ V240), T233 (≠ V241)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G11 (= G14), S13 (≠ A16), R14 (≠ Q17), I16 (≠ L19), A35 (≠ D38), T36 (≠ I39), L57 (≠ A60), N58 (= N61), V59 (= V62), N85 (= N88), A86 (= A89), G87 (= G90), I88 (≠ S91), T108 (≠ L112), I135 (≠ L139), G136 (= G140), S137 (= S141), Y150 (= Y154), K154 (= K158), P180 (= P184), G181 (≠ V185), F182 (≠ A186), I183 (≠ T187)
4jroC Crystal structure of 3-oxoacyl-[acyl-carrier protein]reductase (fabg) from listeria monocytogenes in complex with NADP+
39% identity, 97% coverage: 5:247/250 of query aligns to 3:244/247 of 4jroC
- active site: G16 (= G18), S142 (= S141), Q152 (≠ L151), Y155 (= Y154), K159 (= K158)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G14), S14 (≠ A16), R15 (≠ Q17), G16 (= G18), I17 (≠ L19), N35 (≠ D38), Y36 (≠ I39), N37 (= N40), G38 (= G41), S39 (vs. gap), A62 (= A60), N63 (= N61), V64 (= V62), N90 (= N88), A91 (= A89), G92 (= G90), I93 (≠ S91), I113 (≠ L112), A141 (≠ G140), S142 (= S141), Y155 (= Y154), K159 (= K158), P185 (= P184), G186 (≠ P190), I188 (≠ L192), T190 (= T194)
1q7cA The structure of betaketoacyl-[acp] reductase y151f mutant in complex with NADPH fragment (see paper)
37% identity, 97% coverage: 5:247/250 of query aligns to 2:239/243 of 1q7cA
- active site: G15 (= G18), S137 (= S141), Q147 (≠ L151), F150 (≠ Y154), K154 (= K158)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G11 (= G14), S13 (≠ A16), R14 (≠ Q17), A35 (≠ D38), T36 (≠ I39), L57 (≠ A60), N58 (= N61), V59 (= V62), A86 (= A89), G87 (= G90), I88 (≠ S91), T108 (≠ L112)
6ixmC Crystal structure of the ketone reductase chkred20 from the genome of chryseobacterium sp. Ca49 complexed with NAD (see paper)
35% identity, 97% coverage: 5:247/250 of query aligns to 3:244/248 of 6ixmC