SitesBLAST
Comparing PfGW456L13_3262 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_3262 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)
4iqgD Crystal structure of bpro0239 oxidoreductase from polaromonas sp. Js666 in NADP bound form
59% identity, 100% coverage: 1:248/248 of query aligns to 1:248/248 of 4iqgD
- active site: G13 (= G13), N112 (= N112), S143 (= S143), Y154 (= Y154), Y157 (= Y157), K161 (= K161)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G9 (= G9), S11 (= S11), R12 (= R12), G13 (= G13), I14 (= I14), N32 (= N32), A34 (≠ Q34), S35 (≠ A35), N36 (≠ D36), A59 (= A59), D60 (= D60), V61 (= V61), N87 (= N87), A88 (= A88), G89 (= G89), V141 (= V141), S143 (= S143), Y157 (= Y157), K161 (= K161), P187 (= P187), G188 (= G188), I190 (= I190), T192 (= T192), I194 (≠ F194), H195 (= H195)
8bcjB Crystal structure of short-chain dehydrogenase pa3128 from pseudomonas aeruginosa pao1 in complex with NADP+
55% identity, 100% coverage: 1:248/248 of query aligns to 3:250/250 of 8bcjB
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G11 (= G9), S13 (= S11), R14 (= R12), G15 (= G13), I16 (= I14), L36 (≠ Q34), R37 (≠ A35), N38 (≠ D36), A61 (= A59), D62 (= D60), V63 (= V61), N89 (= N87), A90 (= A88), G91 (= G89), T113 (= T111), V143 (= V141), S145 (= S143), Y159 (= Y157), K163 (= K161), P189 (= P187), G190 (= G188), I192 (= I190), T194 (= T192), I196 (≠ F194), H197 (= H195)
1g6kA Crystal structure of glucose dehydrogenase mutant e96a complexed with NAD+
38% identity, 99% coverage: 3:247/248 of query aligns to 8:249/261 of 1g6kA
- active site: G18 (= G13), S145 (= S143), Y158 (= Y157), K162 (= K161)
- binding nicotinamide-adenine-dinucleotide: T17 (≠ R12), G18 (= G13), L19 (≠ I14), R39 (≠ Q34), D65 (= D60), V66 (= V61), N92 (= N87), A93 (= A88), G94 (= G89), M143 (≠ V141), S145 (= S143), Y158 (= Y157), P188 (= P187), G189 (= G188), I191 (= I190), T193 (= T192)
P40288 Glucose 1-dehydrogenase; EC 1.1.1.47 from Priestia megaterium (Bacillus megaterium) (see 2 papers)
38% identity, 99% coverage: 3:247/248 of query aligns to 8:249/261 of P40288
- 11:35 (vs. 6:30, 36% identical) binding
- E96 (≠ V91) mutation E->A,G,K: Heat stable.
- D108 (≠ R104) mutation to N: Heat stable.
- V112 (≠ I108) mutation to A: Heat stable.
- E133 (≠ H131) mutation to K: Heat stable.
- V183 (= V182) mutation to I: Heat stable.
- P194 (≠ D193) mutation to Q: Heat stable.
- E210 (= E208) mutation to K: Heat stable.
- Y217 (≠ R215) mutation to H: Heat stable.
Sites not aligning to the query:
- 252 Q→L: Heat stable.
- 253 Y→C: Heat stable.
- 258 A→G: Heat stable.
3osuA Crystal structure of the 3-oxoacyl-acyl carrier protein reductase, fabg, from staphylococcus aureus
35% identity, 100% coverage: 1:247/248 of query aligns to 3:243/246 of 3osuA
3sj7A Structure of beta-ketoacetyl-coa reductase (fabg) from staphylococcus aureus complex with NADPH (see paper)
34% identity, 99% coverage: 3:247/248 of query aligns to 2:236/239 of 3sj7A
- active site: G12 (= G13), S138 (= S143), Q148 (≠ E153), Y151 (= Y157), K155 (= K161)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G9), S10 (= S11), R11 (= R12), I13 (= I14), N31 (= N32), Y32 (= Y33), A33 (≠ Q34), G34 (≠ A35), S35 (≠ D36), A58 (= A59), N59 (≠ D60), V60 (= V61), N86 (= N87), A87 (= A88), T109 (= T111), S138 (= S143), Y151 (= Y157), K155 (= K161), P181 (= P187), G182 (= G188)
3ay6B Crystal structure of bacillus megaterium glucose dehydrogenase 4 a258f mutant in complex with nadh and d-glucose (see paper)
37% identity, 99% coverage: 2:247/248 of query aligns to 13:255/267 of 3ay6B
- active site: G24 (= G13), S151 (= S143), Y164 (= Y157), K168 (= K161)
- binding beta-D-glucopyranose: E102 (≠ G92), S151 (= S143), H153 (≠ A145), W158 (≠ S150), Y164 (= Y157), N202 (≠ H195), K205 (≠ S198)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G20 (= G9), T23 (≠ R12), G24 (= G13), L25 (≠ I14), Y45 (≠ Q34), D71 (= D60), V72 (= V61), N98 (= N87), A99 (= A88), G100 (= G89), V101 (= V91), M149 (≠ V141), S151 (= S143), Y164 (= Y157), K168 (= K161), P194 (= P187), G195 (= G188), M197 (≠ I190), T199 (= T192), P200 (≠ D193), I201 (≠ F194), N202 (≠ H195)
4cqmF Crystal structure of heterotetrameric human ketoacyl reductase complexed with NAD and NADP (see paper)
39% identity, 100% coverage: 1:247/248 of query aligns to 5:236/241 of 4cqmF
- active site: G17 (= G13), S139 (= S143), Q149 (≠ E153), Y152 (= Y157), K156 (= K161)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G9), R16 (= R12), G17 (= G13), I18 (= I14), A37 (≠ Y33), R38 (≠ Q34), N39 (≠ A35), D60 (= D60), V61 (= V61), A87 (≠ N87), A88 (= A88), G89 (= G89), V137 (= V141), S139 (= S143), Y152 (= Y157), K156 (= K161), V185 (≠ I190), T187 (= T192), M189 (≠ L197)
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)
39% identity, 100% coverage: 1:247/248 of query aligns to 1:232/237 of Q8N4T8
- G9 (= G9) mutation to S: Unable to restore growth of an OAR1-deficient yeast mutant.
- SRGI 11:14 (= SRGI 11:14) binding
- R12 (= R12) mutation to A: Strongly reduced ability to restore growth of an OAR1-deficient yeast mutant.
- R34 (≠ Q34) 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 (≠ QA 34:35) binding
- D56 (= D60) binding
- L70 (≠ V74) to M: in dbSNP:rs2877380
- AAG 83:85 (≠ NAG 87:89) binding
- S135 (= S143) mutation to A: Unable to restore growth of an OAR1-deficient yeast mutant.
- Y148 (= Y157) binding ; mutation to A: Unable to restore growth of an OAR1-deficient yeast mutant.
- K152 (= K161) 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 (≠ G177) 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 (≠ E178) 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 (≠ IYT 190:192) binding
3ijrF 2.05 angstrom resolution crystal structure of a short chain dehydrogenase from bacillus anthracis str. 'Ames ancestor' in complex with NAD+
33% identity, 99% coverage: 3:247/248 of query aligns to 47:285/290 of 3ijrF
- active site: G57 (= G13), S182 (= S143), L192 (≠ Y154), Y195 (= Y157), K199 (= K161), K240 (≠ D202)
- binding magnesium ion: D55 (≠ S11), S56 (≠ R12), E80 (≠ D36)
- binding nicotinamide-adenine-dinucleotide: D55 (≠ S11), S56 (≠ R12), G57 (= G13), I58 (= I14), Y77 (= Y33), L78 (≠ Q34), E80 (≠ D36), G103 (≠ A59), D104 (= D60), L105 (≠ V61), N131 (= N87), V132 (≠ A88), A133 (≠ G89), Q134 (≠ T90), I155 (≠ T111), T180 (≠ V141), S182 (= S143), Y195 (= Y157), K199 (= K161), P225 (= P187), G226 (= G188), P227 (≠ Y189), I228 (= I190), T230 (= T192), L232 (≠ F194)
Sites not aligning to the query:
3i3oA 2.06 angstrom resolution crystal structure of a short chain dehydrogenase from bacillus anthracis str. 'Ames ancestor' in complex with NAD-acetone
33% identity, 99% coverage: 3:247/248 of query aligns to 39:277/282 of 3i3oA
- active site: G49 (= G13), S174 (= S143), L184 (≠ Y154), Y187 (= Y157), K191 (= K161), K232 (≠ D202)
- binding magnesium ion: D47 (≠ S11), S48 (≠ R12), E72 (≠ D36)
- binding nicotinamide adenine dinucleotide acetone adduct: G45 (= G9), D47 (≠ S11), S48 (≠ R12), G49 (= G13), I50 (= I14), Y69 (= Y33), L70 (≠ Q34), E72 (≠ D36), G95 (≠ A59), D96 (= D60), L97 (≠ V61), N123 (= N87), V124 (≠ A88), A125 (≠ G89), Q126 (≠ T90), Q127 (≠ V91), I147 (≠ T111), T172 (≠ V141), S174 (= S143), Y187 (= Y157), K191 (= K161), P217 (= P187), G218 (= G188), I220 (= I190), T222 (= T192), L224 (≠ F194)
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)
36% identity, 99% coverage: 3:247/248 of query aligns to 7:243/247 of P73574
- A14 (≠ G10) mutation to G: 4.2-fold increase in activity on acetoacetyl-CoA.
- P151 (= P151) 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 (≠ Y189) mutation to Y: 3.3-fold increase in activity on acetoacetyl-CoA.
- N198 (≠ S198) mutation to R: 3.5-fold increase in activity on acetoacetyl-CoA.
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)
34% identity, 99% coverage: 3:247/248 of query aligns to 4:242/246 of P14697
- GGI 13:15 (≠ RGI 12:14) binding
- G35 (≠ Q34) binding
- R40 (≠ S39) binding
- Q47 (= Q46) 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 (≠ ADV 59:61) binding
- NAG-IT 88:92 (≠ NAGTVG 87:92) binding
- D94 (≠ K94) mutation to A: About 6% of wild-type activity.
- K99 (≠ E99) mutation to A: Nearly loss of activity.
- Q147 (≠ S150) mutation to A: About 30% of wild-type activity.
- F148 (≠ P151) mutation to A: About 30% of wild-type activity.
- Q150 (≠ E153) mutation to A: About 20% of wild-type activity.
- T173 (≠ G177) 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 (= PGYI 187:190) binding
- Y185 (= Y189) mutation to A: Nearly loss of activity.
- R195 (≠ S198) mutation to A: Nearly loss of activity.
3vzsB Crystal structure of phab from ralstonia eutropha in complex with acetoacetyl-coa and NADP (see paper)
34% identity, 99% coverage: 3:247/248 of query aligns to 7:245/249 of 3vzsB
- active site: N115 (= N112), S143 (= S143), Y156 (= Y157), K160 (= K161)
- binding acetoacetyl-coenzyme a: D97 (≠ K94), Q150 (≠ S150), F151 (≠ P151), Q153 (≠ E153), Y156 (= Y157), G187 (= G188), Y188 (= Y189), R198 (≠ S198)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G9), I18 (= I14), G38 (≠ Q34), R43 (≠ S39), G63 (≠ A59), N64 (≠ D60), V65 (= V61), G93 (= G89), I94 (≠ V91), T95 (≠ G92), P186 (= P187), I189 (= I190), M193 (≠ F194), V194 (vs. gap)
7v0hG Crystal structure of putative glucose 1-dehydrogenase from burkholderia cenocepacia in complex with NADP and a potential reaction product
33% identity, 99% coverage: 3:247/248 of query aligns to 12:251/253 of 7v0hG
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G18 (= G9), S20 (= S11), K21 (≠ R12), G22 (= G13), I23 (= I14), A43 (≠ Q34), S44 (≠ A35), S45 (≠ D36), G68 (≠ A59), D69 (= D60), V70 (= V61), N96 (= N87), S97 (≠ A88), G98 (= G89), Y100 (≠ G92), I144 (≠ V141), S146 (= S143), Y159 (= Y157), K163 (= K161), P189 (= P187), G190 (= G188), M191 (≠ Y189), I192 (= I190), T194 (= T192), G196 (≠ F194), T197 (≠ H195)
- binding (2R)-2-(hydroxymethyl)pentanedioic acid: S146 (= S143), Y159 (= Y157), M191 (≠ Y189), I202 (vs. gap)
4fj0D Crystal structure of the ternary complex between a fungal 17beta- hydroxysteroid dehydrogenase (holo form) and 3,7-dihydroxy flavone (see paper)
32% identity, 99% coverage: 3:247/248 of query aligns to 10:259/261 of 4fj0D
- active site: G20 (= G13), S144 (= S143), N145 (≠ V144), H155 (≠ Y154), Y158 (= Y157), K162 (= K161), Y203 (vs. gap)
- binding 3,7-dihydroxy-2-phenyl-4H-chromen-4-one: S144 (= S143), N145 (≠ V144), G190 (≠ Y189), F196 (= F194), S200 (= S198), Y203 (vs. gap), A219 (≠ L207)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G16 (= G9), R19 (= R12), G20 (= G13), I21 (= I14), A41 (≠ Q34), N42 (≠ A35), S43 (≠ D36), I68 (≠ V61), N94 (= N87), S95 (≠ A88), G96 (= G89), L117 (≠ T111), T142 (≠ V141), Y158 (= Y157), K162 (= K161), P188 (= P187), G189 (= G188), G190 (≠ Y189), T191 (≠ I190), T193 (= T192), M195 (vs. gap)
4fj1B Crystal structure of the ternary complex between a fungal 17beta- hydroxysteroid dehydrogenase (holo form) and genistein (see paper)
32% identity, 99% coverage: 3:247/248 of query aligns to 8:257/259 of 4fj1B
- active site: G18 (= G13), S142 (= S143), N143 (≠ V144), H153 (≠ Y154), Y156 (= Y157), K160 (= K161), Y201 (vs. gap)
- binding genistein: G188 (≠ Y189), F194 (= F194), S198 (= S198), Y201 (vs. gap), I202 (vs. gap), M216 (≠ K206), A217 (≠ L207)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G14 (= G9), R17 (= R12), G18 (= G13), I19 (= I14), A39 (≠ Q34), N40 (≠ A35), S41 (≠ D36), I66 (≠ V61), N92 (= N87), S93 (≠ A88), G94 (= G89), L115 (≠ T111), T140 (≠ V141), S142 (= S143), Y156 (= Y157), K160 (= K161), G187 (= G188), T189 (≠ I190), T191 (= T192), M193 (vs. gap)
4fj2B Crystal structure of the ternary complex between a fungal 17beta- hydroxysteroid dehydrogenase (holo form) and biochanin a (see paper)
32% identity, 99% coverage: 3:247/248 of query aligns to 9:258/260 of 4fj2B
- active site: G19 (= G13), S143 (= S143), N144 (≠ V144), H154 (≠ Y154), Y157 (= Y157), K161 (= K161), Y202 (vs. gap)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G9), R18 (= R12), G19 (= G13), I20 (= I14), A40 (≠ Q34), N41 (≠ A35), S42 (≠ D36), I67 (≠ V61), N93 (= N87), S94 (≠ A88), G95 (= G89), L116 (≠ T111), T141 (≠ V141), Y157 (= Y157), K161 (= K161), G188 (= G188), G189 (≠ Y189), T190 (≠ I190), T192 (= T192), M194 (vs. gap)
- binding 5,7-dihydroxy-3-(4-methoxyphenyl)-4H-chromen-4-one: G189 (≠ Y189), F195 (= F194), V198 (≠ L197), S199 (= S198), Y202 (vs. gap), I203 (vs. gap), M217 (≠ K206), A218 (≠ L207)
3qwiA Crystal structure of a 17beta-hydroxysteroid dehydrogenase (holo form) from fungus cochliobolus lunatus in complex with NADPH and coumestrol (see paper)
32% identity, 99% coverage: 3:247/248 of query aligns to 9:258/260 of 3qwiA
- active site: G19 (= G13), S143 (= S143), N144 (≠ V144), H154 (≠ Y154), Y157 (= Y157), K161 (= K161), Y202 (vs. gap)
- binding Coumestrol: F149 (≠ G149), G189 (≠ Y189), M194 (vs. gap), Y202 (vs. gap), I203 (vs. gap), A218 (≠ L207)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G9), R18 (= R12), I20 (= I14), A40 (≠ Q34), N41 (≠ A35), S42 (≠ D36), I67 (≠ V61), N93 (= N87), S94 (≠ A88), G95 (= G89), L116 (≠ T111), T141 (≠ V141), Y157 (= Y157), K161 (= K161), P187 (= P187), G188 (= G188), G189 (≠ Y189), T190 (≠ I190), T192 (= T192), M194 (vs. gap)
3qwhA Crystal structure of the 17beta-hydroxysteroid dehydrogenase from cochliobolus lunatus in complex with NADPH and kaempferol (see paper)
32% identity, 99% coverage: 3:247/248 of query aligns to 9:258/260 of 3qwhA
- active site: G19 (= G13), S143 (= S143), N144 (≠ V144), H154 (≠ Y154), Y157 (= Y157), K161 (= K161), Y202 (vs. gap)
- binding 3,5,7-trihydroxy-2-(4-hydroxyphenyl)-4h-chromen-4-one: N144 (≠ V144), F149 (≠ G149), G189 (≠ Y189), F195 (= F194), S199 (= S198), Y202 (vs. gap), I203 (vs. gap), A218 (≠ L207)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G9), R18 (= R12), G19 (= G13), I20 (= I14), A40 (≠ Q34), N41 (≠ A35), S42 (≠ D36), D66 (= D60), I67 (≠ V61), N93 (= N87), S94 (≠ A88), G95 (= G89), L116 (≠ T111), T141 (≠ V141), Y157 (= Y157), K161 (= K161), P187 (= P187), G188 (= G188), G189 (≠ Y189), T190 (≠ I190), T192 (= T192), M194 (vs. gap)
Query Sequence
>PfGW456L13_3262 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_3262
MDKVIVITGGSRGIGAATALLAAAQGYRICINYQADEQSAFGVLEQVRALGAQAIAVRAD
VSIEDEVIALFNRVDSELGRVTALVNNAGTVGQKSRVDEMSEFRILKIMKTNVLAPMLCA
KHAILRMSPRHGGQGGSIVNVSSVASRLGSPNEYVDYAASKGALDTFTIGLSKEVAGEGI
RVNAVRPGYIYTDFHALSGDPDRVSKLESAIPMARGGRPDEVAEAIVWLLSDKASYATGT
FVDLGGGR
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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