SitesBLAST
Comparing PfGW456L13_3426 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_3426 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)
7x5jC Acp-dependent oxoacyl reductase
39% identity, 92% coverage: 6:255/273 of query aligns to 2:255/256 of 7x5jC
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G11 (= G15), S13 (≠ G17), G15 (= G19), L16 (= L20), N36 (≠ D39), R37 (≠ I40), N38 (= N41), D62 (= D65), V63 (= V66), N89 (= N92), A90 (= A93), A91 (= A94), V114 (= V121), I141 (≠ A148), Y156 (= Y163), K160 (= K167), L186 (≠ I193), G187 (= G194), V188 (≠ L195), R194 (vs. gap), S197 (≠ P197), S198 (= S198)
4nbuB Crystal structure of fabg from bacillus sp (see paper)
37% identity, 90% coverage: 5:251/273 of query aligns to 4:242/244 of 4nbuB
- active site: G18 (= G19), N111 (= N122), S139 (= S150), Q149 (≠ L160), Y152 (= Y163), K156 (= K167)
- binding acetoacetyl-coenzyme a: D93 (= D104), K98 (≠ N109), S139 (= S150), N146 (≠ D157), V147 (≠ M158), Q149 (≠ L160), Y152 (= Y163), F184 (≠ L195), M189 (= M202), K200 (≠ I209)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G15), N17 (≠ G18), G18 (= G19), I19 (≠ L20), D38 (= D39), F39 (≠ I40), V59 (≠ T64), D60 (= D65), V61 (= V66), N87 (= N92), A88 (= A93), G89 (≠ A94), I90 (= I95), T137 (≠ A148), S139 (= S150), Y152 (= Y163), K156 (= K167), P182 (≠ I193), F184 (≠ L195), T185 (≠ S198), T187 (≠ H200), M189 (= M202)
4fn4A Short-chain NAD(h)-dependent dehydrogenase/reductase from sulfolobus acidocaldarius (see paper)
35% identity, 92% coverage: 2:252/273 of query aligns to 1:252/254 of 4fn4A
- active site: G18 (= G19), S144 (= S150), Y157 (= Y163), K161 (= K167), S202 (= S198)
- binding nicotinamide-adenine-dinucleotide: G14 (= G15), S17 (≠ G18), G18 (= G19), I19 (≠ L20), E38 (≠ D39), L39 (≠ I40), R43 (≠ G44), A63 (≠ T64), D64 (= D65), V65 (= V66), N91 (= N92), G93 (≠ A94), I94 (= I95), T142 (≠ A148), S144 (= S150), Y157 (= Y163), K161 (= K167), P187 (vs. gap), V190 (vs. gap), T192 (vs. gap), N193 (≠ Q192), I194 (= I193)
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)
38% identity, 89% coverage: 9:252/273 of query aligns to 6:244/248 of Q9KJF1
- S15 (≠ G18) binding
- D36 (= D39) binding
- D62 (= D65) binding
- I63 (≠ V66) binding
- N89 (= N92) binding
- Y153 (= Y163) binding
- K157 (= K167) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
7pcsB Structure of the heterotetrameric sdr family member bbscd (see paper)
38% identity, 89% coverage: 9:252/273 of query aligns to 5:243/247 of 7pcsB
- binding nicotinamide-adenine-dinucleotide: G11 (= G15), M16 (≠ L20), D35 (= D39), I36 (= I40), I62 (≠ V66), N88 (= N92), G90 (≠ A94), I138 (≠ A148), S140 (= S150), Y152 (= Y163), K156 (= K167), I185 (vs. gap)
A0A3Q8GL18 (+)-cis,trans-nepetalactol synthase NEPS1; Nepetalactol-related short-chain dehydrogenase; Nepetalactol dehydrogenase; Nepetalactol-related short-chain reductase 1; Nepetalactol-related SDR1; NmNEPS1; EC 5.5.1.34; EC 1.1.1.419 from Nepeta racemosa (Catmint) (Raceme catnip) (see paper)
36% identity, 90% coverage: 5:251/273 of query aligns to 14:262/271 of A0A3Q8GL18
- N125 (= N122) mutation to A: Strongly reduced cis-trans-nepetalactone levels.
- T152 (≠ A148) mutation to N: Absence of cis-trans-nepetalactone.
- T153 (= T149) mutation to A: Almost normal cis-trans-nepetalactone levels.
- T154 (≠ S150) mutation to G: Loss of dehydrogenase activity and strongly enhanced cis-trans-nepetalactol levels associated with a huge increase in Km for cis-trans-nepetalactol.
- P155 (≠ G151) mutation to S: Strongly reduced cis-trans-nepetalactone levels.
- L156 (= L152) mutation to S: Reduced dehydrogenase activity and absence of cis-trans-nepetalactone.
- Y167 (= Y163) mutation to F: Absence of cis-trans-nepetalactone.
- K171 (= K167) mutation to M: Absence of cis-trans-nepetalactone.
- S198 (≠ Q192) mutation to M: Absence of cis-trans-nepetalactone.
- V199 (≠ I193) mutation to A: Almost normal cis-trans-nepetalactone levels.
- T202 (≠ A196) mutation to A: Absence of cis-trans-nepetalactone.
8cxaA Crystal structure of 3-oxoacyl-[acyl-carrier-protein] reductase from mycobacterium smegmatis with bound NAD
37% identity, 90% coverage: 5:251/273 of query aligns to 2:248/251 of 8cxaA
- binding nicotinamide-adenine-dinucleotide: G12 (= G15), Q15 (≠ G18), G16 (= G19), I17 (≠ L20), D36 (= D39), V63 (= V66), N89 (= N92), A91 (= A94), S94 (≠ N97), I142 (≠ A148), S143 (≠ T149), S144 (= S150), Y157 (= Y163), K161 (= K167), P187 (vs. gap), H188 (vs. gap), I190 (vs. gap), I194 (≠ A196)
4wecA Crystal structure of a short chain dehydrogenase from mycobacterium smegmatis
35% identity, 92% coverage: 3:253/273 of query aligns to 5:252/258 of 4wecA
- active site: G21 (= G19), S143 (= S150), Q154 (≠ L160), Y157 (= Y163), K161 (= K167)
- binding nicotinamide-adenine-dinucleotide: G17 (= G15), A19 (≠ G17), S20 (≠ G18), G21 (= G19), I22 (≠ L20), D41 (= D39), I42 (= I40), V61 (≠ T64), D62 (= D65), V63 (= V66), N89 (= N92), T141 (≠ A148), Y157 (= Y163), K161 (= K167), P187 (≠ I193), P189 (≠ A201), V190 (≠ M202)
4jroC Crystal structure of 3-oxoacyl-[acyl-carrier protein]reductase (fabg) from listeria monocytogenes in complex with NADP+
36% identity, 90% coverage: 6:250/273 of query aligns to 3:244/247 of 4jroC
- active site: G16 (= G19), S142 (= S150), Q152 (≠ L160), Y155 (= Y163), K159 (= K167)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G15), S14 (≠ G17), R15 (≠ G18), G16 (= G19), I17 (≠ L20), N35 (= N41), Y36 (≠ F42), N37 (≠ E43), G38 (= G44), S39 (≠ A45), N63 (≠ D65), V64 (= V66), N90 (= N92), A91 (= A93), I93 (= I95), I113 (≠ V121), S142 (= S150), Y155 (= Y163), K159 (= K167), P185 (≠ I193), I188 (≠ A196), T190 (≠ S198)
6ixmC Crystal structure of the ketone reductase chkred20 from the genome of chryseobacterium sp. Ca49 complexed with NAD (see paper)
31% identity, 92% coverage: 4:253/273 of query aligns to 1:247/248 of 6ixmC
- active site: G16 (= G19), S142 (= S150), Y155 (= Y163), K159 (= K167)
- binding nicotinamide-adenine-dinucleotide: G12 (= G15), S15 (≠ G18), G16 (= G19), I17 (≠ L20), D36 (= D39), I37 (= I40), A61 (≠ T64), D62 (= D65), T63 (≠ V66), N89 (= N92), A90 (= A93), M140 (≠ A148), S142 (= S150), Y155 (= Y163), K159 (= K167), P185 (≠ L195), A186 (= A196), Y187 (≠ P197), I188 (≠ S198), L192 (≠ M202)
Q9LBG2 Levodione reductase; (6R)-2,2,6-trimethyl-1,4-cyclohexanedione reductase; EC 1.1.1.- from Leifsonia aquatica (Corynebacterium aquaticum) (see paper)
35% identity, 92% coverage: 3:253/273 of query aligns to 8:265/267 of Q9LBG2
- 17:42 (vs. 12:37, 46% identical) binding
- E103 (= E99) mutation E->A,D,N,Q: 26-fold increase in Km and a much lower enantiomeric excess of the reaction products.
3osuA Crystal structure of the 3-oxoacyl-acyl carrier protein reductase, fabg, from staphylococcus aureus
34% identity, 89% coverage: 9:251/273 of query aligns to 5:244/246 of 3osuA
F1SWA0 Zerumbone synthase; EC 1.1.1.326 from Zingiber zerumbet (Shampoo ginger) (Amomum zerumbet) (see paper)
33% identity, 92% coverage: 5:255/273 of query aligns to 2:262/267 of F1SWA0
- S142 (= S150) mutation to A: Strong reduction in oxidoreductase activity toward 8-hydroxy-alpha-humulene and borneol.
- S144 (≠ L152) mutation to A: Increased oxidoreductase activity toward 8-hydroxy-alpha-humulene and borneol.
- Y155 (= Y163) mutation to A: Strong reduction in oxidoreductase activity toward 8-hydroxy-alpha-humulene and borneol.
- K159 (= K167) mutation to A: Abolishes all oxidoreductase activity.
4cqlI Crystal structure of heterotetrameric human ketoacyl reductase complexed with NAD (see paper)
33% identity, 90% coverage: 5:251/273 of query aligns to 5:249/251 of 4cqlI
- active site: G19 (= G19), S146 (= S150), Y159 (= Y163), K163 (= K167)
- binding nicotinamide-adenine-dinucleotide: S18 (≠ G18), G19 (= G19), I20 (≠ L20), D39 (= D39), L40 (≠ I40), A64 (≠ T64), D65 (= D65), V66 (= V66), C93 (≠ A98), A94 (≠ E99), G95 (≠ Q100), I96 (≠ R101), V116 (= V121), I144 (≠ A148), S146 (= S150), Y159 (= Y163), K163 (= K167), P189 (≠ I193), G190 (= G194), I192 (vs. gap), T194 (≠ A196), M196 (≠ S198)
4cqmA Crystal structure of heterotetrameric human ketoacyl reductase complexed with NAD and NADP (see paper)
33% identity, 90% coverage: 5:251/273 of query aligns to 3:246/248 of 4cqmA
- active site: G17 (= G19), S143 (= S150), Y156 (= Y163), K160 (= K167)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G15), S16 (≠ G18), G17 (= G19), I18 (≠ L20), D37 (= D39), L38 (≠ I40), A61 (≠ T64), V63 (= V66), C90 (≠ A98), A91 (≠ E99), G92 (≠ Q100), I93 (≠ R101), V113 (= V121), I141 (≠ A148), S143 (= S150), Y156 (= Y163), K160 (= K167), P186 (≠ I193), G187 (= G194), I189 (vs. gap), T191 (≠ A196), P192 (= P197), M193 (≠ S198), T194 (≠ E199)
1iy8A Crystal structure of levodione reductase (see paper)
35% identity, 91% coverage: 5:253/273 of query aligns to 1:256/258 of 1iy8A
- active site: G15 (= G19), S143 (= S150), Q153 (≠ L160), Y156 (= Y163), K160 (= K167)
- binding nicotinamide-adenine-dinucleotide: G11 (= G15), S14 (≠ G18), G15 (= G19), L16 (= L20), D35 (= D39), V36 (≠ I40), A62 (≠ T64), D63 (= D65), V64 (= V66), N90 (= N92), G92 (≠ A94), I93 (= I95), T141 (≠ A148), S143 (= S150), Y156 (= Y163), K160 (= K167), P186 (≠ I193), G187 (= G194), T191 (≠ A196), P192 (= P197), M193 (vs. gap)
3sj7A Structure of beta-ketoacetyl-coa reductase (fabg) from staphylococcus aureus complex with NADPH (see paper)
34% identity, 89% coverage: 9:251/273 of query aligns to 2:237/239 of 3sj7A
- active site: G12 (= G19), S138 (= S150), Q148 (≠ L160), Y151 (= Y163), K155 (= K167)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G15), S10 (≠ G17), R11 (≠ G18), I13 (≠ L20), N31 (= N41), Y32 (≠ F42), A33 (vs. gap), G34 (vs. gap), S35 (vs. gap), A58 (≠ T64), N59 (≠ D65), V60 (= V66), N86 (= N92), A87 (= A93), T109 (≠ V121), S138 (= S150), Y151 (= Y163), K155 (= K167), P181 (≠ I193), G182 (= G194)
6vspA Structure of serratia marcescens 2,3-butanediol dehydrogenase mutant q247a (see paper)
32% identity, 94% coverage: 4:259/273 of query aligns to 1:251/251 of 6vspA
- active site: G16 (= G19), S138 (= S150), Y151 (= Y163)
- binding nicotinamide-adenine-dinucleotide: G12 (= G15), N15 (≠ G18), G16 (= G19), M17 (≠ L20), D36 (= D39), W37 (≠ I40), W37 (≠ I40), A38 (≠ N41), I59 (≠ T64), D60 (= D65), V61 (= V66), N87 (= N92), A88 (= A93), G89 (≠ A94), V90 (≠ I95), V110 (= V121), T136 (≠ A148), S138 (= S150), Y151 (= Y163), K155 (= K167), P181 (≠ I193), S182 (≠ G194), L183 (= L195), V184 (≠ A196), T186 (≠ S198), N187 (≠ E199), M188 (vs. gap), T189 (vs. gap)
6vspB Structure of serratia marcescens 2,3-butanediol dehydrogenase mutant q247a (see paper)
32% identity, 90% coverage: 4:250/273 of query aligns to 3:242/252 of 6vspB
6xewA Structure of serratia marcescens 2,3-butanediol dehydrogenase (see paper)
32% identity, 94% coverage: 4:259/273 of query aligns to 1:251/251 of 6xewA
- active site: G16 (= G19), S138 (= S150), Y151 (= Y163)
- binding r,3-hydroxybutan-2-one: S138 (= S150), S140 (≠ L152), Y151 (= Y163)
- binding s,3-hydroxybutan-2-one: S138 (= S150), Y151 (= Y163), S182 (≠ G194)
- binding nicotinamide-adenine-dinucleotide: G12 (= G15), N15 (≠ G18), G16 (= G19), M17 (≠ L20), D36 (= D39), W37 (≠ I40), W37 (≠ I40), A38 (≠ N41), I59 (≠ T64), D60 (= D65), V61 (= V66), N87 (= N92), A88 (= A93), G89 (≠ A94), V110 (= V121), T136 (≠ A148), S138 (= S150), Y151 (= Y163), K155 (= K167), S182 (≠ G194), L183 (= L195), V184 (≠ A196), T186 (≠ S198), N187 (≠ E199), M188 (vs. gap), T189 (vs. gap)
Query Sequence
>PfGW456L13_3426 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_3426
MSTGKLAGRVAIITGSGGGLGAECARVLASHGASIAVVDINFEGATAVAQSLVAEGHQAL
AIATDVSSEDDVRAMVAQVKERFGRIDILHNNAAILNAEQRQLDRDFVNLDMQAWDRAIA
VNLRGAVLCTKHVIPVMLENGKGSIIFATSGLGMQGDMSLTGYATSKAGLMMLPRMVASQ
YGKQGIRGNAVQIGLAPSEHAMPEPLLDILRDNHCTAELGTPRQIADVVAFLASDESSFV
TGTTLVADGGFSSHTPSLVAMRALFAQMGRTGM
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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