SitesBLAST
Comparing AO356_18385 FitnessBrowser__pseudo5_N2C3_1:AO356_18385 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)
4nbuB Crystal structure of fabg from bacillus sp (see paper)
46% identity, 99% coverage: 2:250/252 of query aligns to 4:242/244 of 4nbuB
- active site: G18 (= G16), N111 (= N121), S139 (= S150), Q149 (= Q159), Y152 (= Y162), K156 (= K166)
- binding acetoacetyl-coenzyme a: D93 (= D95), K98 (= K108), S139 (= S150), N146 (= N156), V147 (= V157), Q149 (= Q159), Y152 (= Y162), F184 (= F194), M189 (= M199), K200 (= K210)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G12), N17 (≠ Q15), G18 (= G16), I19 (≠ L17), D38 (= D36), F39 (≠ L37), V59 (vs. gap), D60 (≠ N62), V61 (= V63), N87 (= N89), A88 (= A90), G89 (= G91), I90 (= I92), T137 (≠ I148), S139 (= S150), Y152 (= Y162), K156 (= K166), P182 (= P192), F184 (= F194), T185 (≠ I195), T187 (= T197), M189 (= M199)
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)
44% identity, 98% coverage: 3:250/252 of query aligns to 4:244/247 of P73574
- A14 (≠ G13) mutation to G: 4.2-fold increase in activity on acetoacetyl-CoA.
- P151 (≠ V157) 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 (= K166) mutation to A: Almost no activity on acetoacetyl-CoA.
- F188 (= F194) mutation to Y: 3.3-fold increase in activity on acetoacetyl-CoA.
- N198 (≠ K204) mutation to R: 3.5-fold increase in activity on acetoacetyl-CoA.
3osuA Crystal structure of the 3-oxoacyl-acyl carrier protein reductase, fabg, from staphylococcus aureus
41% identity, 99% coverage: 1:250/252 of query aligns to 1:244/246 of 3osuA
4nbwA Crystal structure of fabg from plesiocystis pacifica (see paper)
45% identity, 98% coverage: 6:252/252 of query aligns to 2:251/253 of 4nbwA
- active site: G12 (= G16), S146 (= S150), Y159 (= Y162), K163 (= K166)
- binding nicotinamide-adenine-dinucleotide: G8 (= G12), N11 (≠ Q15), G12 (= G16), I13 (≠ L17), D32 (= D36), L33 (= L37), V57 (≠ C61), D58 (≠ N62), V59 (= V63), N85 (= N89), A86 (= A90), G87 (= G91), S146 (= S150), Y159 (= Y162), K163 (= K166), I192 (= I195), T194 (= T197)
P73826 Acetoacetyl-CoA reductase; EC 1.1.1.36 from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
39% identity, 98% coverage: 1:248/252 of query aligns to 4:236/240 of P73826
- S134 (= S150) mutation to A: 12% enzymatic activity.
- Y147 (= Y162) mutation to A: No enzymatic activity.
- K151 (= K166) mutation to A: 5% enzymatic activity.
3sj7A Structure of beta-ketoacetyl-coa reductase (fabg) from staphylococcus aureus complex with NADPH (see paper)
41% identity, 97% coverage: 6:250/252 of query aligns to 2:237/239 of 3sj7A
- active site: G12 (= G16), S138 (= S150), Q148 (= Q159), Y151 (= Y162), K155 (= K166)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G12), S10 (≠ C14), R11 (≠ Q15), I13 (≠ L17), N31 (vs. gap), Y32 (≠ V35), A33 (≠ D36), G34 (≠ L37), S35 (≠ N38), A58 (≠ C61), N59 (= N62), V60 (= V63), N86 (= N89), A87 (= A90), T109 (≠ V120), S138 (= S150), Y151 (= Y162), K155 (= K166), P181 (= P192), G182 (= G193)
7tzpG Crystal structure of putataive short-chain dehydrogenase/reductase (fabg) from klebsiella pneumoniae subsp. Pneumoniae ntuh-k2044 in complex with nadh (see paper)
38% identity, 99% coverage: 1:250/252 of query aligns to 4:245/247 of 7tzpG
- binding 1,4-dihydronicotinamide adenine dinucleotide: G15 (= G12), R18 (≠ Q15), G19 (= G16), I20 (≠ L17), D39 (= D36), R40 (≠ L37), C63 (= C61), I65 (≠ V63), N91 (= N89), G93 (= G91), I94 (= I92), V114 (= V120), Y155 (= Y162), K159 (= K166), I188 (= I195), T190 (= T197), T193 (= T200)
4jroC Crystal structure of 3-oxoacyl-[acyl-carrier protein]reductase (fabg) from listeria monocytogenes in complex with NADP+
39% identity, 99% coverage: 1:250/252 of query aligns to 1:245/247 of 4jroC
- active site: G16 (= G16), S142 (= S150), Q152 (= Q159), Y155 (= Y162), K159 (= K166)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G12), S14 (≠ C14), R15 (≠ Q15), G16 (= G16), I17 (≠ L17), N35 (vs. gap), Y36 (≠ V35), N37 (≠ D36), G38 (≠ L37), S39 (≠ N38), N63 (= N62), V64 (= V63), N90 (= N89), A91 (= A90), I93 (= I92), I113 (≠ V120), S142 (= S150), Y155 (= Y162), K159 (= K166), P185 (= P192), I188 (= I195), T190 (= T197)
4nbtA Crystal structure of fabg from acholeplasma laidlawii (see paper)
41% identity, 100% coverage: 2:252/252 of query aligns to 2:239/239 of 4nbtA
- active site: G16 (= G16), S132 (= S150), Y145 (= Y162), K149 (= K166)
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), K15 (≠ Q15), G16 (= G16), L17 (= L17), D36 (= D36), L37 (= L37), L52 (= L60), N53 (= N62), V54 (= V63), N80 (= N89), A81 (= A90), G82 (= G91), I130 (= I148), S132 (= S150), Y145 (= Y162), K149 (= K166), P177 (= P192), G178 (= G193), I180 (= I195), T182 (= T197)
4cqmF Crystal structure of heterotetrameric human ketoacyl reductase complexed with NAD and NADP (see paper)
38% identity, 98% coverage: 5:252/252 of query aligns to 6:239/241 of 4cqmF
- active site: G17 (= G16), S139 (= S150), Q149 (= Q159), Y152 (= Y162), K156 (= K166)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G12), R16 (≠ Q15), G17 (= G16), I18 (≠ L17), A37 (≠ D36), R38 (≠ L37), N39 (= N38), D60 (≠ N62), V61 (= V63), A87 (≠ N89), A88 (= A90), G89 (= G91), V137 (≠ I148), S139 (= S150), Y152 (= Y162), K156 (= K166), V185 (≠ I195), T187 (= T197), M189 (= M199)
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)
38% identity, 98% coverage: 5:252/252 of query aligns to 2:235/237 of Q8N4T8
- G9 (= G12) mutation to S: Unable to restore growth of an OAR1-deficient yeast mutant.
- SRGI 11:14 (≠ CQGL 14:17) binding
- R12 (≠ Q15) mutation to A: Strongly reduced ability to restore growth of an OAR1-deficient yeast mutant.
- R34 (≠ L37) 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 (≠ LN 37:38) binding
- D56 (≠ N62) binding
- L70 (≠ V76) to M: in dbSNP:rs2877380
- AAG 83:85 (≠ NAG 89:91) binding
- S135 (= S150) mutation to A: Unable to restore growth of an OAR1-deficient yeast mutant.
- Y148 (= Y162) binding ; mutation to A: Unable to restore growth of an OAR1-deficient yeast mutant.
- K152 (= K166) 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 (= R182) 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 (≠ Y183) 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 (≠ IET 195:197) binding
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)
36% identity, 99% coverage: 1:250/252 of query aligns to 4:244/247 of 3op4A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G12), S17 (≠ C14), R18 (≠ Q15), I20 (≠ L17), T40 (≠ N38), N62 (= N62), V63 (= V63), N89 (= N89), A90 (= A90), I92 (= I92), V139 (≠ I148), S141 (= S150), Y154 (= Y162), K158 (= K166), P184 (= P192), G185 (= G193), I187 (= I195), T189 (= T197), M191 (= M199)
Q9KJF1 (2S)-[(R)-hydroxy(phenyl)methyl]succinyl-CoA dehydrogenase subunit BbsD; (S,R)-2-(alpha-hydroxybenzyl)succinyl-CoA dehydrogenase subunit BbsD; EC 1.1.1.429 from Thauera aromatica (see 2 papers)
37% identity, 99% coverage: 1:249/252 of query aligns to 1:242/248 of Q9KJF1
- M1 (= M1) modified: Initiator methionine, Removed
- S15 (≠ Q15) binding
- D36 (= D36) binding
- D62 (≠ N62) binding
- I63 (≠ V63) binding
- N89 (= N89) binding
- Y153 (= Y162) binding
- K157 (= K166) binding
4dmmB 3-oxoacyl-[acyl-carrier-protein] reductase from synechococcus elongatus pcc 7942 in complex with NADP
40% identity, 99% coverage: 1:250/252 of query aligns to 1:237/240 of 4dmmB
- active site: G16 (= G16), S142 (= S150), Q152 (= Q159), Y155 (= Y162), K159 (= K166)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G12), S14 (≠ C14), R15 (≠ Q15), G16 (= G16), I17 (≠ L17), A37 (≠ L37), S38 (≠ N38), S39 (≠ Q39), A62 (≠ C61), D63 (≠ N62), V64 (= V63), N90 (= N89), A91 (= A90), L113 (≠ V120), I140 (= I148), S142 (= S150), Y155 (= Y162), K159 (= K166), P185 (= P192), G186 (= G193), I188 (= I195), T190 (= T197), M192 (= M199)
7pcsB Structure of the heterotetrameric sdr family member bbscd (see paper)
37% identity, 98% coverage: 3:249/252 of query aligns to 2:241/247 of 7pcsB
- binding nicotinamide-adenine-dinucleotide: G11 (= G12), M16 (≠ L17), D35 (= D36), I36 (≠ L37), I62 (≠ V63), N88 (= N89), G90 (= G91), I138 (= I148), S140 (= S150), Y152 (= Y162), K156 (= K166), I185 (= I195)
7emgB Carbonyl reductase variant 4 (r123c/l209p/f183y/v61k) from serratia marcescens complexed with NADP+ (see paper)
35% identity, 97% coverage: 6:250/252 of query aligns to 5:240/243 of 7emgB
6t77A Crystal structure of klebsiella pneumoniae fabg(NADPH-dependent) NADP- complex at 1.75 a resolution (see paper)
36% identity, 99% coverage: 1:250/252 of query aligns to 1:241/244 of 6t77A
- active site: G16 (= G16), S138 (= S150), Y151 (= Y162)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G12), S14 (≠ C14), R15 (≠ Q15), T37 (≠ N38), L58 (≠ C61), N59 (= N62), V60 (= V63), A87 (= A90), G88 (= G91), I89 (= I92)
5vmlA Crystal structure of acetoacetyl-coa reductase from burkholderia pseudomallei 1710b with bound NADP
36% identity, 99% coverage: 4:252/252 of query aligns to 1:244/245 of 5vmlA
- active site: G13 (= G16), N111 (= N121), S139 (= S150), Y152 (= Y162), K156 (= K166)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G9 (= G12), G12 (≠ Q15), G13 (= G16), I14 (≠ L17), C33 (≠ V35), G34 (≠ D36), R39 (≠ K41), G59 (≠ C61), N60 (= N62), V61 (= V63), N87 (= N89), G89 (= G91), I90 (= I92), S139 (= S150), Y152 (= Y162), K156 (= K166), P182 (= P192), G183 (= G193), I185 (= I195)
4i08A Crystal structure of beta-ketoacyl-acyl carrier protein reductase (fabg) from vibrio cholerae in complex with NADPH (see paper)
36% identity, 99% coverage: 1:250/252 of query aligns to 4:240/243 of 4i08A
- active site: G19 (= G16), N113 (= N121), S141 (= S150), Q151 (= Q159), Y154 (= Y162), K158 (= K166)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G15 (= G12), S17 (≠ C14), R18 (≠ Q15), I20 (≠ L17), T40 (≠ N38), N62 (= N62), V63 (= V63), N89 (= N89), A90 (= A90), G140 (≠ S149), S141 (= S150), Y154 (= Y162), K158 (= K166), P184 (= P192), G185 (= G193), T189 (= T197)
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)
35% identity, 99% coverage: 3:252/252 of query aligns to 1:245/246 of P14697
- GGI 13:15 (≠ QGL 15:17) binding
- G35 (≠ D36) binding
- R40 (≠ K41) binding
- Q47 (≠ A48) 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 (≠ CNV 61:63) binding
- NAGIT 88:92 (≠ NAGIL 89:93) binding
- D94 (= D95) mutation to A: About 6% of wild-type activity.
- K99 (= K108) mutation to A: Nearly loss of activity.
- Q147 (≠ N156) mutation to A: About 30% of wild-type activity.
- F148 (≠ V157) mutation to A: About 30% of wild-type activity.
- Q150 (= Q159) mutation to A: About 20% of wild-type activity.
- T173 (≠ R182) 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 (≠ PGFI 192:195) binding
- Y185 (≠ F194) mutation to A: Nearly loss of activity.
- R195 (≠ K204) mutation to A: Nearly loss of activity.
Query Sequence
>AO356_18385 FitnessBrowser__pseudo5_N2C3_1:AO356_18385
MQLTDKVIIITGGCQGLGRSMAEYFADKGAKLALVDLNQEKLDQAVAACAAKGVEARAYL
CNVANEDQVIDMVARVAEDFGAIHGLINNAGILRDGLLLKVKDGEMTKMSLAQWQAVIDV
NLTGVFLCTREVAAKMVELKNSGAIINISSISRAGNVGQTNYSAAKAGVAAATVTWAKEL
ARYGIRVAGIAPGFIETEMTLGMKPEALEKMTSGIPLKRMGKPEEIAHSAAYIFENDYYT
GRILEMDGGLRI
Or try a new SitesBLAST search
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