SitesBLAST
Comparing Pf6N2E2_1839 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_1839 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
6t77A Crystal structure of klebsiella pneumoniae fabg(NADPH-dependent) NADP- complex at 1.75 a resolution (see paper)
46% identity, 98% coverage: 5:242/244 of query aligns to 2:241/244 of 6t77A
- active site: G16 (= G19), S138 (= S135), Y151 (= Y148)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G15), S14 (= S17), R15 (≠ K18), T37 (≠ Q40), L58 (= L59), N59 (≠ D60), V60 (= V61), A87 (= A84), G88 (= G85), I89 (≠ Y86)
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)
46% identity, 96% coverage: 8:242/244 of query aligns to 5:241/244 of P0AEK2
- GASR 12:15 (≠ GGSK 15:18) binding
- T37 (≠ Q40) binding
- NV 59:60 (≠ DV 60:61) binding
- N86 (= N83) binding
- Y151 (= Y148) mutation to F: Defect in the affinity for NADPH.
- YAAAK 151:155 (= YAAAK 148:152) binding
- A154 (= A151) mutation to T: Decreases in the thermolability of the reductase; when associated with K-233.
- K155 (= K152) mutation to A: Defect in the affinity for NADPH.
- I184 (≠ V181) binding
- E233 (= E234) 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)
46% identity, 96% coverage: 8:242/244 of query aligns to 4:240/243 of 1q7bA
- active site: G15 (= G19), E101 (≠ Q99), S137 (= S135), Q147 (≠ G145), Y150 (= Y148), K154 (= K152)
- binding calcium ion: E232 (= E234), T233 (= T235)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G11 (= G15), S13 (= S17), R14 (≠ K18), T36 (≠ Q40), N58 (≠ D60), V59 (= V61), N85 (= N83), A86 (= A84), G87 (= G85), I88 (≠ Y86), S137 (= S135), Y150 (= Y148), K154 (= K152), P180 (= P178), G181 (= G179), I183 (≠ V181)
P0A2C9 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 Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
45% identity, 98% coverage: 5:242/244 of query aligns to 2:241/244 of P0A2C9
- M125 (= M122) mutation to I: Loss of the temperature-sensitive phenotype; when associated with T-223.
- A223 (= A224) mutation to T: Loss of the temperature-sensitive phenotype; when associated with I-125.
- S224 (= S225) mutation to F: Distorts the local conformation and prevent stacking around Phe-221. The S224F mutation would additionally disrupt the hydrogen bond formed between Ser-224 and Glu-226.
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)
44% identity, 97% coverage: 6:242/244 of query aligns to 6:244/247 of 3op4A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G15), S17 (= S17), R18 (≠ K18), I20 (= I20), T40 (≠ Q40), N62 (≠ D60), V63 (= V61), N89 (= N83), A90 (= A84), I92 (≠ Y86), V139 (= V133), S141 (= S135), Y154 (= Y148), K158 (= K152), P184 (= P178), G185 (= G179), I187 (≠ V181), T189 (= T183), M191 (≠ L185)
1q7cA The structure of betaketoacyl-[acp] reductase y151f mutant in complex with NADPH fragment (see paper)
45% identity, 96% coverage: 8:242/244 of query aligns to 4:240/243 of 1q7cA
- active site: G15 (= G19), S137 (= S135), Q147 (≠ G145), F150 (≠ Y148), K154 (= K152)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G11 (= G15), S13 (= S17), R14 (≠ K18), A35 (= A39), T36 (≠ Q40), L57 (= L59), N58 (≠ D60), V59 (= V61), G87 (= G85), I88 (≠ Y86)
4i08A Crystal structure of beta-ketoacyl-acyl carrier protein reductase (fabg) from vibrio cholerae in complex with NADPH (see paper)
44% identity, 97% coverage: 6:242/244 of query aligns to 6:240/243 of 4i08A
- active site: G19 (= G19), N113 (= N107), S141 (= S135), Q151 (≠ G145), Y154 (= Y148), K158 (= K152)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G15 (= G15), S17 (= S17), R18 (≠ K18), I20 (= I20), T40 (≠ Q40), N62 (≠ D60), V63 (= V61), N89 (= N83), A90 (= A84), G140 (= G134), S141 (= S135), Y154 (= Y148), K158 (= K152), P184 (= P178), G185 (= G179), T189 (= T183)
4nbuB Crystal structure of fabg from bacillus sp (see paper)
40% identity, 98% coverage: 3:242/244 of query aligns to 2:242/244 of 4nbuB
- active site: G18 (= G19), N111 (= N107), S139 (= S135), Q149 (≠ G145), Y152 (= Y148), K156 (= K152)
- binding acetoacetyl-coenzyme a: D93 (≠ H89), K98 (= K94), S139 (= S135), N146 (≠ S142), V147 (≠ K143), Q149 (≠ G145), Y152 (= Y148), F184 (≠ P180), M189 (≠ L185), K200 (≠ A200)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G15), N17 (≠ K18), G18 (= G19), I19 (= I20), D38 (≠ A39), F39 (vs. gap), V59 (≠ L59), D60 (= D60), V61 (= V61), N87 (= N83), A88 (= A84), G89 (= G85), I90 (≠ Y86), T137 (≠ V133), S139 (= S135), Y152 (= Y148), K156 (= K152), P182 (= P178), F184 (≠ P180), T185 (≠ V181), T187 (= T183), M189 (≠ L185)
7emgB Carbonyl reductase variant 4 (r123c/l209p/f183y/v61k) from serratia marcescens complexed with NADP+ (see paper)
42% identity, 98% coverage: 5:242/244 of query aligns to 1:240/243 of 7emgB
4wecA Crystal structure of a short chain dehydrogenase from mycobacterium smegmatis
42% identity, 99% coverage: 1:242/244 of query aligns to 4:250/258 of 4wecA
- active site: G21 (= G19), S143 (= S135), Q154 (≠ A146), Y157 (= Y148), K161 (= K152)
- binding nicotinamide-adenine-dinucleotide: G17 (= G15), A19 (≠ S17), S20 (≠ K18), G21 (= G19), I22 (= I20), D41 (≠ A39), I42 (≠ Q40), V61 (≠ L59), D62 (= D60), V63 (= V61), N89 (= N83), T141 (≠ V133), Y157 (= Y148), K161 (= K152), P187 (= P178), P189 (= P180), V190 (= V181)
4nbtA Crystal structure of fabg from acholeplasma laidlawii (see paper)
42% identity, 98% coverage: 4:242/244 of query aligns to 1:237/239 of 4nbtA
- active site: G16 (= G19), S132 (= S135), Y145 (= Y148), K149 (= K152)
- binding nicotinamide-adenine-dinucleotide: G12 (= G15), K15 (= K18), G16 (= G19), L17 (≠ I20), D36 (= D41), L37 (≠ M42), L52 (= L59), N53 (≠ D60), V54 (= V61), N80 (= N83), A81 (= A84), G82 (= G85), I130 (≠ V133), S132 (= S135), Y145 (= Y148), K149 (= K152), P177 (= P178), G178 (= G179), I180 (≠ V181), T182 (= T183)
5ovlA Crystal structure of maba bound to NADP+ from m. Smegmatis (see paper)
42% identity, 98% coverage: 5:243/244 of query aligns to 6:238/241 of 5ovlA
- active site: G20 (= G19), S134 (= S135), Y147 (= Y148), L154 (≠ V155)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G16 (= G15), N18 (≠ S17), R19 (≠ K18), G20 (= G19), I21 (= I20), R41 (≠ Q40), D55 (= D60), V56 (= V61), N82 (= N83), A83 (= A84), I85 (≠ Y86), T105 (≠ V106), I132 (≠ V133), S134 (= S135), Y147 (= Y148), K151 (= K152), P177 (= P178), G178 (= G179), I180 (≠ V181)
P71534 3-oxoacyl-[acyl-carrier-protein] reductase MabA; 3-ketoacyl-acyl carrier protein reductase; Acetoacetyl-CoA reductase; Beta-ketoacyl-ACP reductase; Beta-ketoacyl-acyl carrier protein reductase; EC 1.1.1.100; EC 1.1.1.36 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
42% identity, 98% coverage: 5:243/244 of query aligns to 20:252/255 of P71534
5ovkA Crystal structure maba bound to NADPH from m. Smegmatis (see paper)
42% identity, 98% coverage: 5:243/244 of query aligns to 7:239/242 of 5ovkA
6wprA Crystal structure of a putative 3-oxoacyl-acp reductase (fabg) with NADP(h) from acinetobacter baumannii (see paper)
39% identity, 97% coverage: 6:242/244 of query aligns to 1:241/244 of 6wprA
- active site: G16 (= G19), S138 (= S135), Y151 (= Y148)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G12 (= G15), S14 (= S17), R15 (≠ K18), T37 (≠ Q40), L58 (= L59), D59 (= D60), V60 (= V61), N86 (= N83), A87 (= A84), G88 (= G85), I89 (≠ Y86), I136 (≠ V133), Y151 (= Y148), K155 (= K152), P181 (= P178)
6t62A Crystal structure of acinetobacter baumannii fabg in complex with NADPH at 1.8 a resolution (see paper)
39% identity, 95% coverage: 11:242/244 of query aligns to 8:241/244 of 6t62A
- active site: G16 (= G19), S138 (= S135), Y151 (= Y148)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G15), S14 (= S17), R15 (≠ K18), A36 (= A39), T37 (≠ Q40), L58 (= L59), D59 (= D60), V60 (= V61), N86 (= N83), A87 (= A84), G88 (= G85), I89 (≠ Y86), I136 (≠ V133), S137 (≠ G134), S138 (= S135), Y151 (= Y148), K155 (= K152), P181 (= P178), G182 (= G179), I184 (≠ V181), M188 (≠ L185)
P9WGT3 3-oxoacyl-[acyl-carrier-protein] reductase MabA; 3-ketoacyl reductase; 3-ketoacyl-acyl carrier protein reductase; Acetoacetyl-CoA reductase; Beta-ketoacyl-acyl carrier protein reductase; Beta-ketoacyl-ACP reductase; Mycolic acid biosynthesis A; EC 1.1.1.100; EC 1.1.1.36 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 7 papers)
41% identity, 95% coverage: 12:243/244 of query aligns to 19:244/247 of P9WGT3
- T21 (= T14) modified: Phosphothreonine; mutation to A: Slight decrease in phosphorylation by PknB. Lack of phosphorylation by PknB; when associated with A-114 and A-191.
- RGI 25:27 (≠ KGI 18:20) binding
- R47 (≠ Q40) binding
- C60 (≠ L59) mutation to V: Displays a lower activity than the wild-type and a slightly decreased affinity for the cofactor. Retains 84% of activity; when associated with L-144. Totally inactive; when associated with A-139 and L-144.
- DV 61:62 (= DV 60:61) binding
- G90 (= G85) binding
- T114 (≠ E109) modified: Phosphothreonine; mutation to A: Slight decrease in phosphorylation by PknB. Lack of phosphorylation by PknB; when associated with A-21 and A-191.
- G139 (= G134) mutation to A: Complete protein inactivation and freezes the catalytic site into its closed form. Totally inactive; when associated with V-60 and L-144.
- S140 (= S135) mutation to A: Loss of activity. Can still bind NADPH.; mutation to T: Loss of activity. Impaired NADPH binding.
- S144 (≠ R139) mutation to L: Stabilizes the catalytic loop in its open active form. Retains 84% of activity; when associated with V-60. Totally inactive; when associated with V-60 and A-139.
- Y185 (≠ P180) mutation to L: 70% decrease in activity with acetoacetyl-CoA as substrate. Does not affect NADP binding.
- T191 (≠ L186) modified: Phosphothreonine; mutation to A: Retains 22% of wild-type reductase activity. Strong decrease in phosphorylation by PknB. Lack of phosphorylation by PknB; when associated with A-21 and A-114.; mutation to D: Phosphomimetic mutant that retains less than 10% of wild-type reductase activity. Impaired NADPH binding. Overproduction of the mutant leads to a significant inhibition of de novo biosynthesis of mycolic acids.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1uznA Maba from mycobacterium tuberculosis (see paper)
41% identity, 95% coverage: 12:243/244 of query aligns to 11:236/239 of 1uznA
- active site: G18 (= G19), S132 (= S135), Y145 (= Y148), K149 (= K152)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G14 (= G15), N16 (≠ S17), R17 (≠ K18), I19 (= I20), R39 (≠ Q40), D53 (= D60), V54 (= V61), A81 (= A84), G82 (= G85)
P73574 3-oxoacyl-[acyl-carrier-protein] reductase; 3-ketoacyl-acyl carrier protein reductase; EC 1.1.1.100 from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
41% identity, 98% coverage: 3:242/244 of query aligns to 1:244/247 of P73574
- A14 (≠ G16) mutation to G: 4.2-fold increase in activity on acetoacetyl-CoA.
- P151 (≠ K143) mutation to F: 2.7-fold increase in activity on acetoacetyl-CoA.; mutation to V: 5.7-fold increase in activity on acetoacetyl-CoA.
- K160 (= K152) mutation to A: Almost no activity on acetoacetyl-CoA.
- F188 (≠ P180) mutation to Y: 3.3-fold increase in activity on acetoacetyl-CoA.
- N198 (≠ G193) mutation to R: 3.5-fold increase in activity on acetoacetyl-CoA.
3tzcA Crystal structure of 3-ketoacyl-(acyl-carrier-protein) reductase (fabg)(y155f) from vibrio cholerae (see paper)
41% identity, 97% coverage: 6:242/244 of query aligns to 6:223/224 of 3tzcA
Query Sequence
>Pf6N2E2_1839 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_1839
MTMRALTGQRAFVTGGSKGIGEAIVRRLAAEGAKVVIAAQDMISAERLADEVGGLAVRLD
VTDLLEVERVVTMLGPFEILVNNAGYDQHDFFTKTTVEQWRYLLAVNLEGVFASTHAALP
AMQAAGYGRIINVGSEAGRQGSKGGAVYAAAKGGVIAFSKSIARENARYGITVNVVAPGP
VDTPLLRKALDRGGEKLLAAMEASTLVGRLGEPNEVAAAVVFLASRDASFITGETLGVSG
GMGC
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory