SitesBLAST
Comparing PP_2783 FitnessBrowser__Putida:PP_2783 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)
3osuA Crystal structure of the 3-oxoacyl-acyl carrier protein reductase, fabg, from staphylococcus aureus
45% identity, 98% coverage: 4:244/245 of query aligns to 5:246/246 of 3osuA
3sj7A Structure of beta-ketoacetyl-coa reductase (fabg) from staphylococcus aureus complex with NADPH (see paper)
44% identity, 98% coverage: 4:244/245 of query aligns to 2:239/239 of 3sj7A
- active site: G12 (= G14), S138 (= S140), Q148 (= Q150), Y151 (= Y153), K155 (= K157)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G10), S10 (= S12), R11 (= R13), I13 (= I15), N31 (≠ S33), Y32 (= Y34), A33 (≠ V35), G34 (≠ R36), S35 (≠ D37), A58 (≠ C60), N59 (≠ D61), V60 (= V62), N86 (= N88), A87 (= A89), T109 (= T111), S138 (= S140), Y151 (= Y153), K155 (= K157), P181 (= P183), G182 (= G184)
4jroC Crystal structure of 3-oxoacyl-[acyl-carrier protein]reductase (fabg) from listeria monocytogenes in complex with NADP+
44% identity, 98% coverage: 4:244/245 of query aligns to 6:247/247 of 4jroC
- active site: G16 (= G14), S142 (= S140), Q152 (= Q150), Y155 (= Y153), K159 (= K157)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G10), S14 (= S12), R15 (= R13), G16 (= G14), I17 (= I15), N35 (≠ S33), Y36 (= Y34), N37 (≠ V35), G38 (≠ R36), S39 (≠ D37), N63 (≠ D61), V64 (= V62), N90 (= N88), A91 (= A89), I93 (= I91), I113 (≠ T111), S142 (= S140), Y155 (= Y153), K159 (= K157), P185 (= P183), I188 (≠ V186), T190 (= T188)
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)
42% identity, 100% coverage: 1:244/245 of query aligns to 4:246/247 of P73574
- A14 (≠ G11) mutation to G: 4.2-fold increase in activity on acetoacetyl-CoA.
- P151 (≠ K148) 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 (= K157) mutation to A: Almost no activity on acetoacetyl-CoA.
- F188 (≠ I185) mutation to Y: 3.3-fold increase in activity on acetoacetyl-CoA.
- N198 (≠ H198) mutation to R: 3.5-fold increase in activity on acetoacetyl-CoA.
4cqmF Crystal structure of heterotetrameric human ketoacyl reductase complexed with NAD and NADP (see paper)
42% identity, 99% coverage: 3:244/245 of query aligns to 6:239/241 of 4cqmF
- active site: G17 (= G14), S139 (= S140), Q149 (= Q150), Y152 (= Y153), K156 (= K157)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G10), R16 (= R13), G17 (= G14), I18 (= I15), A37 (≠ Y34), R38 (≠ V35), N39 (≠ R36), D60 (= D61), V61 (= V62), A87 (≠ N88), A88 (= A89), G89 (= G90), V137 (≠ L138), S139 (= S140), Y152 (= Y153), K156 (= K157), V185 (= V186), T187 (= T188), M189 (= M190)
Q8N4T8 3-oxoacyl-[acyl-carrier-protein] reductase; 3-ketoacyl-[acyl-carrier-protein] reductase beta subunit; KAR beta subunit; Carbonyl reductase family member 4; CBR4; Quinone reductase CBR4; Short chain dehydrogenase/reductase family 45C member 1; EC 1.1.1.100; EC 1.6.5.10 from Homo sapiens (Human) (see 4 papers)
42% identity, 99% coverage: 3:244/245 of query aligns to 2:235/237 of Q8N4T8
- G9 (= G10) mutation to S: Unable to restore growth of an OAR1-deficient yeast mutant.
- SRGI 11:14 (= SRGI 12:15) binding
- R12 (= R13) mutation to A: Strongly reduced ability to restore growth of an OAR1-deficient yeast mutant.
- R34 (≠ V35) mutation to A: Strongly reduced ability to restore growth of an OAR1-deficient yeast mutant. Strongly reduces NADPH-dependent reductase activity with acetoacetyl-CoA and 9,10-phenanthrene quinone. No effect on NADH-dependent reductase activities.
- RN 34:35 (≠ VR 35:36) binding
- D56 (= D61) binding
- L70 (≠ V75) to M: in dbSNP:rs2877380
- AAG 83:85 (≠ NAG 88:90) binding
- S135 (= S140) mutation to A: Unable to restore growth of an OAR1-deficient yeast mutant.
- Y148 (= Y153) binding ; mutation to A: Unable to restore growth of an OAR1-deficient yeast mutant.
- K152 (= K157) binding ; mutation to A: Unable to restore growth of an OAR1-deficient yeast mutant. Abolishes NADPH-dependent reductase activity with acetoacetyl-CoA. Strongly reduces NADPH-dependent reductase activity with 9,10-phenanthrene quinone. No effect on NADH-dependent reductase activities.
- R168 (≠ P173) mutation to E: Strongly reduced ability to restore growth of an OAR1-deficient yeast mutant. Increases NADPH-dependent reductase activity with acetoacetyl-CoA. Reduces NADPH-dependent reductase activity with 9,10-phenanthrene quinone. No effect on NADH-dependent reductase activities.
- K169 (≠ R174) mutation to E: Unable to restore growth of an OAR1-deficient yeast mutant. Increases NADPH-dependent reductase activity with acetoacetyl-CoA. Reduces NADPH-dependent reductase activity with 9,10-phenanthrene quinone. No effect on NADH-dependent reductase activities.
- VHT 181:183 (≠ VST 186:188) binding
4dmmB 3-oxoacyl-[acyl-carrier-protein] reductase from synechococcus elongatus pcc 7942 in complex with NADP
43% identity, 100% coverage: 1:244/245 of query aligns to 3:239/240 of 4dmmB
- active site: G16 (= G14), S142 (= S140), Q152 (= Q150), Y155 (= Y153), K159 (= K157)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G10), S14 (= S12), R15 (= R13), G16 (= G14), I17 (= I15), A37 (≠ V35), S38 (≠ R36), S39 (≠ D37), A62 (≠ C60), D63 (= D61), V64 (= V62), N90 (= N88), A91 (= A89), L113 (≠ T111), I140 (≠ L138), S142 (= S140), Y155 (= Y153), K159 (= K157), P185 (= P183), G186 (= G184), I188 (≠ V186), T190 (= T188), M192 (= M190)
6wprA Crystal structure of a putative 3-oxoacyl-acp reductase (fabg) with NADP(h) from acinetobacter baumannii (see paper)
40% identity, 100% coverage: 1:244/245 of query aligns to 1:243/244 of 6wprA
- active site: G16 (= G14), S138 (= S140), Y151 (= Y153)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G12 (= G10), S14 (= S12), R15 (= R13), T37 (≠ A39), L58 (≠ C60), D59 (= D61), V60 (= V62), N86 (= N88), A87 (= A89), G88 (= G90), I89 (= I91), I136 (≠ L138), Y151 (= Y153), K155 (= K157), P181 (= P183)
6t62A Crystal structure of acinetobacter baumannii fabg in complex with NADPH at 1.8 a resolution (see paper)
40% identity, 99% coverage: 3:244/245 of query aligns to 5:243/244 of 6t62A
- active site: G16 (= G14), S138 (= S140), Y151 (= Y153)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G10), S14 (= S12), R15 (= R13), A36 (≠ E38), T37 (≠ A39), L58 (≠ C60), D59 (= D61), V60 (= V62), N86 (= N88), A87 (= A89), G88 (= G90), I89 (= I91), I136 (≠ L138), S137 (= S139), S138 (= S140), Y151 (= Y153), K155 (= K157), P181 (= P183), G182 (= G184), I184 (≠ V186), M188 (= M190)
6t77A Crystal structure of klebsiella pneumoniae fabg(NADPH-dependent) NADP- complex at 1.75 a resolution (see paper)
40% identity, 98% coverage: 4:244/245 of query aligns to 6:243/244 of 6t77A
- active site: G16 (= G14), S138 (= S140), Y151 (= Y153)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G10), S14 (= S12), R15 (= R13), T37 (≠ A39), L58 (≠ C60), N59 (≠ D61), V60 (= V62), A87 (= A89), G88 (= G90), I89 (= I91)
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)
40% identity, 98% coverage: 4:244/245 of query aligns to 9:246/247 of 3op4A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G10), S17 (= S12), R18 (= R13), I20 (= I15), T40 (≠ A39), N62 (≠ D61), V63 (= V62), N89 (= N88), A90 (= A89), I92 (= I91), V139 (≠ L138), S141 (= S140), Y154 (= Y153), K158 (= K157), P184 (= P183), G185 (= G184), I187 (≠ V186), T189 (= T188), M191 (= M190)
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)
40% identity, 98% coverage: 4:244/245 of query aligns to 6:243/244 of P0AEK2
- GASR 12:15 (≠ GGSR 10:13) binding
- T37 (≠ A39) binding
- NV 59:60 (≠ DV 61:62) binding
- N86 (= N88) binding
- Y151 (= Y153) mutation to F: Defect in the affinity for NADPH.
- YAAAK 151:155 (= YAAAK 153:157) binding
- A154 (= A156) mutation to T: Decreases in the thermolability of the reductase; when associated with K-233.
- K155 (= K157) mutation to A: Defect in the affinity for NADPH.
- I184 (≠ V186) 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)
40% identity, 98% coverage: 4:244/245 of query aligns to 5:242/243 of 1q7bA
- active site: G15 (= G14), E101 (≠ D104), S137 (= S140), Q147 (= Q150), Y150 (= Y153), K154 (= K157)
- binding calcium ion: E232 (= E234), T233 (≠ V235)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G11 (= G10), S13 (= S12), R14 (= R13), T36 (≠ A39), N58 (≠ D61), V59 (= V62), N85 (= N88), A86 (= A89), G87 (= G90), I88 (= I91), S137 (= S140), Y150 (= Y153), K154 (= K157), P180 (= P183), G181 (= G184), I183 (≠ V186)
1edoA The x-ray structure of beta-keto acyl carrier protein reductase from brassica napus complexed with NADP+ (see paper)
39% identity, 97% coverage: 5:242/245 of query aligns to 3:242/244 of 1edoA
- active site: G12 (= G14), S138 (= S140), Y151 (= Y153), K155 (= K157)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G10), S10 (= S12), R11 (= R13), I13 (= I15), N31 (≠ S33), Y32 (= Y34), A33 (≠ V35), R34 (= R36), S35 (≠ D37), D59 (= D61), V60 (= V62), N86 (= N88), A87 (= A89), S138 (= S140), Y151 (= Y153), K155 (= K157), P181 (= P183), G182 (= G184), I184 (≠ V186), S186 (≠ T188), M188 (= M190)
1q7cA The structure of betaketoacyl-[acp] reductase y151f mutant in complex with NADPH fragment (see paper)
40% identity, 98% coverage: 4:244/245 of query aligns to 5:242/243 of 1q7cA
- active site: G15 (= G14), S137 (= S140), Q147 (= Q150), F150 (≠ Y153), K154 (= K157)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G11 (= G10), S13 (= S12), R14 (= R13), A35 (≠ E38), T36 (≠ A39), L57 (≠ C60), N58 (≠ D61), V59 (= V62), G87 (= G90), I88 (= I91)
4nbuB Crystal structure of fabg from bacillus sp (see paper)
37% identity, 100% coverage: 1:244/245 of query aligns to 5:244/244 of 4nbuB
- active site: G18 (= G14), N111 (= N112), S139 (= S140), Q149 (= Q150), Y152 (= Y153), K156 (= K157)
- binding acetoacetyl-coenzyme a: D93 (= D94), K98 (≠ T99), S139 (= S140), N146 (≠ G147), V147 (≠ K148), Q149 (= Q150), Y152 (= Y153), F184 (≠ I185), M189 (= M190), K200 (≠ E201)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G10), N17 (≠ R13), G18 (= G14), I19 (= I15), D38 (≠ Y34), F39 (≠ V35), V59 (≠ C60), D60 (= D61), V61 (= V62), N87 (= N88), A88 (= A89), G89 (= G90), I90 (= I91), T137 (≠ L138), S139 (= S140), Y152 (= Y153), K156 (= K157), P182 (= P183), F184 (≠ I185), T185 (≠ V186), T187 (= T188), M189 (= M190)
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)
39% identity, 98% coverage: 4:244/245 of query aligns to 6:243/244 of P0A2C9
- M125 (= M127) mutation to I: Loss of the temperature-sensitive phenotype; when associated with T-223.
- A223 (= A225) mutation to T: Loss of the temperature-sensitive phenotype; when associated with I-125.
- S224 (vs. gap) 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.
4i08A Crystal structure of beta-ketoacyl-acyl carrier protein reductase (fabg) from vibrio cholerae in complex with NADPH (see paper)
40% identity, 98% coverage: 4:244/245 of query aligns to 9:242/243 of 4i08A
- active site: G19 (= G14), N113 (= N112), S141 (= S140), Q151 (= Q150), Y154 (= Y153), K158 (= K157)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G15 (= G10), S17 (= S12), R18 (= R13), I20 (= I15), T40 (≠ A39), N62 (≠ D61), V63 (= V62), N89 (= N88), A90 (= A89), G140 (≠ S139), S141 (= S140), Y154 (= Y153), K158 (= K157), P184 (= P183), G185 (= G184), T189 (= T188)
7emgB Carbonyl reductase variant 4 (r123c/l209p/f183y/v61k) from serratia marcescens complexed with NADP+ (see paper)
40% identity, 98% coverage: 4:244/245 of query aligns to 5:242/243 of 7emgB
P14697 Acetoacetyl-CoA reductase; EC 1.1.1.36 from Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337) (Ralstonia eutropha) (see 2 papers)
38% identity, 100% coverage: 1:244/245 of query aligns to 1:245/246 of P14697
- GGI 13:15 (≠ RGI 13:15) binding
- G35 (≠ V35) binding
- R40 (≠ S40) binding
- Q47 (= Q47) mutation to L: 2.4-fold increase in activity. 2-fold decrease in affinity for NADPH and 2.8-fold decrease in affinity for acetoacetyl-CoA.
- GNV 60:62 (≠ CDV 60:62) binding
- NAGIT 88:92 (= NAGIT 88:92) binding
- D94 (= D94) mutation to A: About 6% of wild-type activity.
- K99 (≠ T99) mutation to A: Nearly loss of activity.
- Q147 (≠ G147) mutation to A: About 30% of wild-type activity.
- F148 (≠ K148) mutation to A: About 30% of wild-type activity.
- Q150 (= Q150) mutation to A: About 20% of wild-type activity.
- T173 (≠ P173) mutation to S: 3.5-fold increase in activity. 4-fold decrease in affinity for NADPH and 2.4-fold decrease in affinity for acetoacetyl-CoA.
- PGYI 183:186 (≠ PGIV 183:186) binding
- Y185 (≠ I185) mutation to A: Nearly loss of activity.
- R195 (≠ V195) mutation to A: Nearly loss of activity.
Query Sequence
>PP_2783 FitnessBrowser__Putida:PP_2783
MTQKIAVVTGGSRGIGKSIVLALAGAGYQVAFSYVRDEASAAALQAQVEGLGRDCLAVQC
DVKEAPSIQAFFERVEQRFERIDLLVNNAGITRDGLLATQSLNDITEVIQTNLVGTLLCC
QQVLPCMMRQRSGCIVNLSSVAAQKPGKGQSNYAAAKGGVEALTRALAVELAPRNIRVNA
VAPGIVSTDMSQALVGAHEQEIQSRLLIKRFARPEEIADAVLYLAERGLYITGEVLSVNG
GLKMP
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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