SitesBLAST
Comparing PfGW456L13_1761 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_1761 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)
4nbuB Crystal structure of fabg from bacillus sp (see paper)
46% identity, 100% coverage: 2:232/232 of query aligns to 24:244/244 of 4nbuB
- active site: N111 (= N101), S139 (= S130), Q149 (= Q139), Y152 (= Y142), K156 (= K146)
- binding acetoacetyl-coenzyme a: D93 (= D75), K98 (= K80), S139 (= S130), N146 (= N136), V147 (= V137), Q149 (= Q139), Y152 (= Y142), F184 (= F174), M189 (= M179), K200 (= K190)
- binding 1,4-dihydronicotinamide adenine dinucleotide: D38 (= D16), F39 (≠ L17), V59 (vs. gap), D60 (≠ N42), V61 (= V43), N87 (= N69), A88 (= A70), G89 (= G71), I90 (= I72), T137 (≠ I128), S139 (= S130), Y152 (= Y142), K156 (= K146), P182 (= P172), F184 (= F174), T185 (≠ I175), T187 (= T177), M189 (= M179)
Sites not aligning to the query:
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)
46% identity, 90% coverage: 23:230/232 of query aligns to 45:244/247 of P73574
- P151 (≠ V137) 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 (= K146) mutation to A: Almost no activity on acetoacetyl-CoA.
- F188 (= F174) mutation to Y: 3.3-fold increase in activity on acetoacetyl-CoA.
- N198 (≠ K184) mutation to R: 3.5-fold increase in activity on acetoacetyl-CoA.
Sites not aligning to the query:
- 14 A→G: 4.2-fold increase in activity on acetoacetyl-CoA.
3osuA Crystal structure of the 3-oxoacyl-acyl carrier protein reductase, fabg, from staphylococcus aureus
41% identity, 93% coverage: 18:232/232 of query aligns to 38:246/246 of 3osuA
Sites not aligning to the query:
4nbwA Crystal structure of fabg from plesiocystis pacifica (see paper)
51% identity, 74% coverage: 59:230/232 of query aligns to 75:249/253 of 4nbwA
Sites not aligning to the query:
P73826 Acetoacetyl-CoA reductase; EC 1.1.1.36 from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
40% identity, 95% coverage: 8:228/232 of query aligns to 31:236/240 of P73826
- S134 (= S130) mutation to A: 12% enzymatic activity.
- Y147 (= Y142) mutation to A: No enzymatic activity.
- K151 (= K146) mutation to A: 5% enzymatic activity.
3sj7A Structure of beta-ketoacetyl-coa reductase (fabg) from staphylococcus aureus complex with NADPH (see paper)
41% identity, 93% coverage: 18:232/232 of query aligns to 35:239/239 of 3sj7A
- active site: S138 (= S130), Q148 (= Q139), Y151 (= Y142), K155 (= K146)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: S35 (≠ N18), A58 (≠ C41), N59 (= N42), V60 (= V43), N86 (= N69), A87 (= A70), T109 (≠ V100), S138 (= S130), Y151 (= Y142), K155 (= K146), P181 (= P172), G182 (= G173)
Sites not aligning to the query:
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, 100% coverage: 1:232/232 of query aligns to 24:247/247 of 7tzpG
- binding 1,4-dihydronicotinamide adenine dinucleotide: D39 (= D16), R40 (≠ L17), C63 (= C41), I65 (≠ V43), N91 (= N69), G93 (= G71), I94 (= I72), V114 (= V100), Y155 (= Y142), K159 (= K146), I188 (= I175), T190 (= T177), T193 (= T180)
Sites not aligning to the query:
4jroC Crystal structure of 3-oxoacyl-[acyl-carrier protein]reductase (fabg) from listeria monocytogenes in complex with NADP+
43% identity, 86% coverage: 32:230/232 of query aligns to 53:245/247 of 4jroC
- active site: S142 (= S130), Q152 (= Q139), Y155 (= Y142), K159 (= K146)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: N63 (= N42), V64 (= V43), N90 (= N69), A91 (= A70), I93 (= I72), I113 (≠ V100), S142 (= S130), Y155 (= Y142), K159 (= K146), P185 (= P172), I188 (= I175), T190 (= T177)
Sites not aligning to the query:
4nbtA Crystal structure of fabg from acholeplasma laidlawii (see paper)
44% identity, 83% coverage: 41:232/232 of query aligns to 52:239/239 of 4nbtA
- active site: S132 (= S130), Y145 (= Y142), K149 (= K146)
- binding nicotinamide-adenine-dinucleotide: L52 (≠ C41), N53 (= N42), V54 (= V43), N80 (= N69), A81 (= A70), G82 (= G71), I130 (= I128), S132 (= S130), Y145 (= Y142), K149 (= K146), P177 (= P172), G178 (= G173), I180 (= I175), T182 (= T177)
Sites not aligning to the query:
5vmlA Crystal structure of acetoacetyl-coa reductase from burkholderia pseudomallei 1710b with bound NADP
40% identity, 88% coverage: 30:232/232 of query aligns to 48:244/245 of 5vmlA
- active site: N111 (= N101), S139 (= S130), Y152 (= Y142), K156 (= K146)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G59 (≠ C41), N60 (= N42), V61 (= V43), N87 (= N69), G89 (= G71), I90 (= I72), S139 (= S130), Y152 (= Y142), K156 (= K146), P182 (= P172), G183 (= G173), I185 (= I175)
Sites not aligning to the query:
4dmmB 3-oxoacyl-[acyl-carrier-protein] reductase from synechococcus elongatus pcc 7942 in complex with NADP
44% identity, 82% coverage: 41:230/232 of query aligns to 62:237/240 of 4dmmB
- active site: S142 (= S130), Q152 (= Q139), Y155 (= Y142), K159 (= K146)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: A62 (≠ C41), D63 (≠ N42), V64 (= V43), N90 (= N69), A91 (= A70), L113 (≠ V100), I140 (= I128), S142 (= S130), Y155 (= Y142), K159 (= K146), P185 (= P172), G186 (= G173), I188 (= I175), T190 (= T177), M192 (= M179)
Sites not aligning to the query:
4cqmF Crystal structure of heterotetrameric human ketoacyl reductase complexed with NAD and NADP (see paper)
37% identity, 100% coverage: 1:232/232 of query aligns to 22:239/241 of 4cqmF
- active site: S139 (= S130), Q149 (= Q139), Y152 (= Y142), K156 (= K146)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: A37 (≠ D16), R38 (≠ L17), N39 (= N18), D60 (≠ N42), V61 (= V43), A87 (≠ N69), A88 (= A70), G89 (= G71), V137 (≠ I128), S139 (= S130), Y152 (= Y142), K156 (= K146), V185 (≠ I175), T187 (= T177), M189 (= M179)
Sites not aligning to the query:
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)
37% identity, 100% coverage: 1:232/232 of query aligns to 18:235/237 of Q8N4T8
- R34 (≠ L17) 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 17:18) binding
- D56 (≠ N42) binding
- L70 (≠ V56) to M: in dbSNP:rs2877380
- AAG 83:85 (≠ NAG 69:71) binding
- S135 (= S130) mutation to A: Unable to restore growth of an OAR1-deficient yeast mutant.
- Y148 (= Y142) binding ; mutation to A: Unable to restore growth of an OAR1-deficient yeast mutant.
- K152 (= K146) 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 (= R162) 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 (≠ Y163) 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 175:177) binding
Sites not aligning to the query:
- 9 G→S: Unable to restore growth of an OAR1-deficient yeast mutant.
- 11:14 binding
- 12 R→A: Strongly reduced ability to restore growth of an OAR1-deficient yeast mutant.
4cqlI Crystal structure of heterotetrameric human ketoacyl reductase complexed with NAD (see paper)
38% identity, 97% coverage: 5:230/232 of query aligns to 28:249/251 of 4cqlI
- active site: S146 (= S130), Y159 (= Y142), K163 (= K146)
- binding nicotinamide-adenine-dinucleotide: D39 (= D16), L40 (= L17), A64 (≠ C41), D65 (≠ N42), V66 (= V43), C93 (≠ N69), A94 (= A70), G95 (= G71), I96 (= I72), V116 (= V100), I144 (= I128), S146 (= S130), Y159 (= Y142), K163 (= K146), P189 (= P172), G190 (= G173), I192 (= I175), T194 (= T177), M196 (= M179)
Sites not aligning to the query:
4cqmA Crystal structure of heterotetrameric human ketoacyl reductase complexed with NAD and NADP (see paper)
39% identity, 97% coverage: 5:230/232 of query aligns to 26:246/248 of 4cqmA
- active site: S143 (= S130), Y156 (= Y142), K160 (= K146)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: D37 (= D16), L38 (= L17), A61 (≠ C41), V63 (= V43), C90 (≠ N69), A91 (= A70), G92 (= G71), I93 (= I72), V113 (= V100), I141 (= I128), S143 (= S130), Y156 (= Y142), K160 (= K146), P186 (= P172), G187 (= G173), I189 (= I175), T191 (= T177), P192 (≠ E178), M193 (= M179), T194 (= T180)
Sites not aligning to the query:
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, 98% coverage: 5:232/232 of query aligns to 25:245/248 of Q9KJF1
- D36 (= D16) binding
- D62 (≠ N42) binding
- I63 (≠ V43) binding
- N89 (= N69) binding
- Y153 (= Y142) binding
- K157 (= K146) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 15 binding
7pcsB Structure of the heterotetrameric sdr family member bbscd (see paper)
37% identity, 98% coverage: 5:232/232 of query aligns to 24:244/247 of 7pcsB
Sites not aligning to the query:
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, 93% coverage: 18:232/232 of query aligns to 37:245/246 of P14697
- R40 (≠ K21) binding
- Q47 (≠ A28) 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 41:43) binding
- NAGIT 88:92 (≠ NAGIL 69:73) binding
- D94 (= D75) mutation to A: About 6% of wild-type activity.
- K99 (= K80) mutation to A: Nearly loss of activity.
- Q147 (≠ N136) mutation to A: About 30% of wild-type activity.
- F148 (≠ V137) mutation to A: About 30% of wild-type activity.
- Q150 (= Q139) mutation to A: About 20% of wild-type activity.
- T173 (≠ R162) 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 172:175) binding
- Y185 (≠ F174) mutation to A: Nearly loss of activity.
- R195 (≠ K184) mutation to A: Nearly loss of activity.
Sites not aligning to the query:
3vzsB Crystal structure of phab from ralstonia eutropha in complex with acetoacetyl-coa and NADP (see paper)
38% identity, 93% coverage: 18:232/232 of query aligns to 40:248/249 of 3vzsB
- active site: N115 (= N101), S143 (= S130), Y156 (= Y142), K160 (= K146)
- binding acetoacetyl-coenzyme a: D97 (= D75), Q150 (≠ N136), F151 (≠ V137), Q153 (= Q139), Y156 (= Y142), G187 (= G173), Y188 (≠ F174), R198 (≠ K184)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R43 (≠ K21), G63 (≠ C41), N64 (= N42), V65 (= V43), G93 (= G71), I94 (= I72), T95 (≠ L73), P186 (= P172), I189 (= I175), M193 (= M179), V194 (≠ T180)
Sites not aligning to the query:
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)
37% identity, 86% coverage: 33:232/232 of query aligns to 53:246/247 of 3op4A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: N62 (= N42), V63 (= V43), N89 (= N69), A90 (= A70), I92 (= I72), V139 (≠ I128), S141 (= S130), Y154 (= Y142), K158 (= K146), P184 (= P172), G185 (= G173), I187 (= I175), T189 (= T177), M191 (= M179)
Sites not aligning to the query:
Query Sequence
>PfGW456L13_1761 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_1761
MAEYFAGLGAKLALVDLNQEKLDDAVAACKAQGVEARAYLCNVANEEQVTHMVAQVAEDF
GAIHGLINNAGILRDGLLLKVKDGEMIKMSLAQWQAVIDVNLTGVFLCTREVAAKMVELN
NTGAIINISSISRAGNVGQTNYSAAKAGVAAATVTWAKELARYGIRVAGIAPGFIETEMT
LGMKPEALEKMTAGIPLKRMGKPEEIAHSAAYIFENDYYTGRILEMDGGLRL
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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