SitesBLAST
Comparing PfGW456L13_4129 Oxidoreductase, short chain dehydrogenase/reductase family 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)
5wuwA Serratia marcescens short-chain dehydrogenase/reductase f98l/f202l mutant (see paper)
69% identity, 98% coverage: 6:248/248 of query aligns to 3:245/245 of 5wuwA
- active site: G16 (= G19), S140 (= S143), Y154 (= Y157), L161 (= L164)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G15), R15 (= R18), I17 (= I20), Y36 (= Y39), A37 (≠ V40), A38 (≠ S41), D63 (= D66), S64 (= S67), N90 (= N93), A91 (= A94), G92 (= G95), Y154 (= Y157), K158 (= K161), G185 (= G188), P186 (= P189), V187 (= V190)
6j7uA Crystal structure of blue fluorescent protein from metagenomic library in complex with NADPH (see paper)
55% identity, 99% coverage: 4:248/248 of query aligns to 1:247/247 of 6j7uA
- active site: G16 (= G19), S142 (= S143), Y156 (= Y157)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G12 (= G15), S14 (= S17), R15 (= R18), I17 (= I20), Y36 (= Y39), V37 (= V40), S38 (= S41), S41 (≠ A44), D65 (= D66), S66 (= S67), N92 (= N93), A93 (= A94), G94 (= G95), I115 (= I116), G141 (= G142), S142 (= S143), Y156 (= Y157), K160 (= K161), P186 (= P187), T191 (= T192), M193 (= M194), N194 (= N195)
5u2wA Crystal structure of a short chain dehydrogenase from burkholderia cenocepacia j2315 in complex with NADP
56% identity, 99% coverage: 4:248/248 of query aligns to 2:246/246 of 5u2wA
- active site: G17 (= G19), S141 (= S143), M152 (≠ G154), Y155 (= Y157), K159 (= K161)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G15), S15 (= S17), R16 (= R18), G17 (= G19), I18 (= I20), Y37 (= Y39), E38 (≠ V40), K39 (≠ S41), S40 (= S42), A63 (= A65), D64 (= D66), S65 (= S67), N91 (= N93), A92 (= A94), G93 (= G95), T139 (≠ I141), Y155 (= Y157), K159 (= K161), P185 (= P187), G186 (= G188), T188 (≠ V190), T190 (= T192), M192 (= M194), N193 (= N195)
P39333 Cyclic-di-GMP-binding biofilm dispersal mediator protein from Escherichia coli (strain K12) (see paper)
52% identity, 98% coverage: 6:248/248 of query aligns to 4:237/237 of P39333
- E50 (≠ G57) mutation E->Q,V: Shows higher affinity for cyclic-di-GMP, increases swimming motility and biofilm dispersal. Biofilm formation is almost completely removed.
5z2lK Crystal structure of bdca in complex with NADPH (see paper)
52% identity, 98% coverage: 6:248/248 of query aligns to 3:236/244 of 5z2lK
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: S14 (= S17), R15 (= R18), I17 (= I20), Y36 (= Y39), A37 (≠ V40), G38 (≠ S41), S39 (= S42), T57 (≠ A65), D58 (= D66), S59 (= S67), N81 (= N93), A82 (= A94), G83 (= G95), I129 (= I141), S131 (= S143), Y145 (= Y157), K149 (= K161), P175 (= P187), I178 (≠ V190), T180 (= T192), A182 (≠ M194), N183 (= N195)
4jroC Crystal structure of 3-oxoacyl-[acyl-carrier protein]reductase (fabg) from listeria monocytogenes in complex with NADP+
40% identity, 97% coverage: 6:246/248 of query aligns to 3:245/247 of 4jroC
- active site: G16 (= G19), S142 (= S143), Q152 (≠ G154), Y155 (= Y157), K159 (= K161)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G15), S14 (= S17), R15 (= R18), G16 (= G19), I17 (= I20), N35 (≠ T38), Y36 (= Y39), N37 (≠ V40), G38 (≠ S41), S39 (= S42), N63 (≠ D66), V64 (≠ S67), N90 (= N93), A91 (= A94), I93 (≠ V96), I113 (= I116), S142 (= S143), Y155 (= Y157), K159 (= K161), P185 (= P187), I188 (≠ V190), T190 (= T192)
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)
39% identity, 97% coverage: 6:246/248 of query aligns to 4:244/247 of P73574
- A14 (≠ G16) mutation to G: 4.2-fold increase in activity on acetoacetyl-CoA.
- P151 (≠ A152) 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 (= K161) mutation to A: Almost no activity on acetoacetyl-CoA.
- F188 (≠ P189) mutation to Y: 3.3-fold increase in activity on acetoacetyl-CoA.
- N198 (≠ F201) 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
39% identity, 96% coverage: 9:246/248 of query aligns to 5:244/246 of 3osuA
7v0hG Crystal structure of putative glucose 1-dehydrogenase from burkholderia cenocepacia in complex with NADP and a potential reaction product
39% identity, 98% coverage: 5:246/248 of query aligns to 8:252/253 of 7v0hG
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G18 (= G15), S20 (= S17), K21 (≠ R18), G22 (= G19), I23 (= I20), A43 (≠ V40), S44 (= S41), S45 (= S42), G68 (≠ A65), D69 (= D66), V70 (≠ S67), N96 (= N93), S97 (≠ A94), G98 (= G95), Y100 (≠ L97), I144 (= I141), S146 (= S143), Y159 (= Y157), K163 (= K161), P189 (= P187), G190 (= G188), M191 (≠ P189), I192 (≠ V190), T194 (= T192), G196 (≠ M194), T197 (≠ N195)
- binding (2R)-2-(hydroxymethyl)pentanedioic acid: S146 (= S143), Y159 (= Y157), M191 (≠ P189), I202 (vs. gap)
3sj7A Structure of beta-ketoacetyl-coa reductase (fabg) from staphylococcus aureus complex with NADPH (see paper)
38% identity, 96% coverage: 9:246/248 of query aligns to 2:237/239 of 3sj7A
- active site: G12 (= G19), S138 (= S143), Q148 (≠ G154), Y151 (= Y157), K155 (= K161)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G15), S10 (= S17), R11 (= R18), I13 (= I20), N31 (≠ T38), Y32 (= Y39), A33 (≠ V40), G34 (≠ S41), S35 (= S42), A58 (= A65), N59 (≠ D66), V60 (≠ S67), N86 (= N93), A87 (= A94), T109 (≠ I116), S138 (= S143), Y151 (= Y157), K155 (= K161), P181 (= P187), G182 (= G188)
4i08A Crystal structure of beta-ketoacyl-acyl carrier protein reductase (fabg) from vibrio cholerae in complex with NADPH (see paper)
40% identity, 98% coverage: 5:246/248 of query aligns to 5:240/243 of 4i08A
- active site: G19 (= G19), N113 (= N117), S141 (= S143), Q151 (≠ G154), Y154 (= Y157), K158 (= K161)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G15 (= G15), S17 (= S17), R18 (= R18), I20 (= I20), T40 (≠ V40), N62 (≠ D66), V63 (≠ S67), N89 (= N93), A90 (= A94), G140 (= G142), S141 (= S143), Y154 (= Y157), K158 (= K161), P184 (= P187), G185 (= G188), T189 (= T192)
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: 5:246/248 of query aligns to 5:244/247 of 3op4A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G15), S17 (= S17), R18 (= R18), I20 (= I20), T40 (≠ V40), N62 (≠ D66), V63 (≠ S67), N89 (= N93), A90 (= A94), I92 (≠ V96), V139 (≠ I141), S141 (= S143), Y154 (= Y157), K158 (= K161), P184 (= P187), G185 (= G188), I187 (≠ V190), T189 (= T192), M191 (= M194)
4dmmB 3-oxoacyl-[acyl-carrier-protein] reductase from synechococcus elongatus pcc 7942 in complex with NADP
42% identity, 97% coverage: 6:246/248 of query aligns to 3:237/240 of 4dmmB
- active site: G16 (= G19), S142 (= S143), Q152 (≠ G154), Y155 (= Y157), K159 (= K161)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G15), S14 (= S17), R15 (= R18), G16 (= G19), I17 (= I20), A37 (≠ V40), S38 (= S41), S39 (= S42), A62 (= A65), D63 (= D66), V64 (≠ S67), N90 (= N93), A91 (= A94), L113 (≠ I116), I140 (= I141), S142 (= S143), Y155 (= Y157), K159 (= K161), P185 (= P187), G186 (= G188), I188 (≠ V190), T190 (= T192), M192 (= M194)
7nm8AAA Antimycin pathway standalone ketoreductase, AntM (see paper)
39% identity, 99% coverage: 3:247/248 of query aligns to 1:249/251 of 7nm8AAA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G13 (= G15), S15 (= S17), R16 (= R18), G17 (= G19), I18 (= I20), H36 (≠ T38), Y37 (= Y39), G38 (≠ V40), H39 (≠ S41), L65 (vs. gap), N97 (= N93), G99 (= G95), S147 (≠ T144), Y160 (= Y157), K164 (= K161), G191 (= G188), T193 (≠ V190), T195 (= T192)
1q7bA The structure of betaketoacyl-[acp] reductase from e. Coli in complex with NADP+ (see paper)
41% identity, 98% coverage: 5:246/248 of query aligns to 1:240/243 of 1q7bA
- active site: G15 (= G19), E101 (≠ D109), S137 (= S143), Q147 (≠ G154), Y150 (= Y157), K154 (= K161)
- binding calcium ion: E232 (≠ A238), T233 (≠ S239)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G11 (= G15), S13 (= S17), R14 (= R18), T36 (≠ V40), N58 (≠ D66), V59 (≠ S67), N85 (= N93), A86 (= A94), G87 (= G95), I88 (≠ V96), S137 (= S143), Y150 (= Y157), K154 (= K161), P180 (= P187), G181 (= G188), I183 (≠ V190)
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)
41% identity, 98% coverage: 5:246/248 of query aligns to 2:241/244 of P0AEK2
- GASR 12:15 (≠ GGSR 15:18) binding
- T37 (≠ V40) binding
- NV 59:60 (≠ DS 66:67) binding
- N86 (= N93) binding
- Y151 (= Y157) mutation to F: Defect in the affinity for NADPH.
- YAAAK 151:155 (≠ YAMSK 157:161) binding
- A154 (≠ S160) mutation to T: Decreases in the thermolability of the reductase; when associated with K-233.
- K155 (= K161) mutation to A: Defect in the affinity for NADPH.
- I184 (≠ V190) binding
- E233 (≠ A238) mutation to K: Decreases in the thermolability of the reductase; when associated with T-154.
1q7cA The structure of betaketoacyl-[acp] reductase y151f mutant in complex with NADPH fragment (see paper)
40% identity, 98% coverage: 5:246/248 of query aligns to 1:240/243 of 1q7cA
- active site: G15 (= G19), S137 (= S143), Q147 (≠ G154), F150 (≠ Y157), K154 (= K161)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G11 (= G15), S13 (= S17), R14 (= R18), A35 (≠ Y39), T36 (≠ V40), L57 (≠ I63), N58 (≠ D66), V59 (≠ S67), G87 (= G95), I88 (≠ V96)
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)
40% identity, 98% coverage: 5:246/248 of query aligns to 2:241/244 of P0A2C9
- M125 (= M132) mutation to I: Loss of the temperature-sensitive phenotype; when associated with T-223.
- A223 (≠ V228) mutation to T: Loss of the temperature-sensitive phenotype; when associated with I-125.
- S224 (= S229) 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.
4fj1B Crystal structure of the ternary complex between a fungal 17beta- hydroxysteroid dehydrogenase (holo form) and genistein (see paper)
36% identity, 97% coverage: 6:245/248 of query aligns to 5:257/259 of 4fj1B
- active site: G18 (= G19), S142 (= S143), N143 (≠ T144), H153 (≠ G154), Y156 (= Y157), K160 (= K161), Y201 (≠ L205)
- binding genistein: G188 (≠ P189), F194 (≠ N195), S198 (≠ A202), Y201 (≠ L205), I202 (= I206), M216 (= M209), A217 (= A210)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G14 (= G15), R17 (= R18), G18 (= G19), I19 (= I20), A39 (≠ V40), N40 (≠ S41), S41 (= S42), I66 (≠ S67), N92 (= N93), S93 (≠ A94), G94 (= G95), L115 (≠ I116), T140 (≠ I141), S142 (= S143), Y156 (= Y157), K160 (= K161), G187 (= G188), T189 (≠ V190), T191 (= T192), M193 (= M194)
4fj2B Crystal structure of the ternary complex between a fungal 17beta- hydroxysteroid dehydrogenase (holo form) and biochanin a (see paper)
36% identity, 97% coverage: 6:245/248 of query aligns to 6:258/260 of 4fj2B
- active site: G19 (= G19), S143 (= S143), N144 (≠ T144), H154 (≠ G154), Y157 (= Y157), K161 (= K161), Y202 (≠ L205)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G15), R18 (= R18), G19 (= G19), I20 (= I20), A40 (≠ V40), N41 (≠ S41), S42 (= S42), I67 (≠ S67), N93 (= N93), S94 (≠ A94), G95 (= G95), L116 (≠ I116), T141 (≠ I141), Y157 (= Y157), K161 (= K161), G188 (= G188), G189 (≠ P189), T190 (≠ V190), T192 (= T192), M194 (= M194)
- binding 5,7-dihydroxy-3-(4-methoxyphenyl)-4H-chromen-4-one: G189 (≠ P189), F195 (≠ N195), V198 (≠ F201), S199 (≠ A202), Y202 (≠ L205), I203 (= I206), M217 (= M209), A218 (= A210)
Query Sequence
>PfGW456L13_4129 Oxidoreductase, short chain dehydrogenase/reductase family
MTTQNLSGKVALIQGGSRGIGAAIVKRLAAEGATVAFTYVSSTAKAEELQDSITAKGGKA
LAIKADSADADAIRSAVSATVEAFGRLDILVNNAGVLAVAPLAEFKLEDFDQTLAINVRS
VFIATQAAARHMTEGGRIINIGSTNADRMPFAGGGPYAMSKSALVGLTKGLARDLGPQGI
TINNVQPGPVDTDMNPAEGDFAESLIPLMAVGRYGKAEEIASFVAYLVSPEAGYITGASL
TIDGGFGA
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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