SitesBLAST
Comparing Echvi_1820 FitnessBrowser__Cola:Echvi_1820 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)
3asvA The closed form of serine dehydrogenase complexed with NADP+ (see paper)
44% identity, 95% coverage: 4:242/252 of query aligns to 2:239/248 of 3asvA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G7 (= G9), T9 (= T11), G11 (= G13), F12 (≠ I14), R32 (= R34), R33 (= R35), D54 (= D58), V55 (= V59), N81 (= N85), G83 (= G87), I132 (= I136), S134 (= S138), Y147 (= Y151), K151 (= K155), G178 (= G182), V180 (= V184), T183 (= T186), E184 (= E187), F185 (= F188)
- binding phosphate ion: S134 (= S138), Y147 (= Y151), G178 (= G182), F185 (= F188)
Q9P7B4 NADP-dependent 3-hydroxy acid dehydrogenase; L-allo-threonine dehydrogenase; EC 1.1.1.381 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
42% identity, 99% coverage: 3:252/252 of query aligns to 7:259/259 of Q9P7B4
- S42 (vs. gap) modified: Phosphoserine
- T43 (vs. gap) modified: Phosphothreonine
Q05016 NADP-dependent 3-hydroxy acid dehydrogenase; L-allo-threonine dehydrogenase; EC 1.1.1.-; EC 1.1.1.381 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
39% identity, 98% coverage: 3:249/252 of query aligns to 14:266/267 of Q05016
- N102 (= N85) binding
- Y168 (= Y151) binding
- K172 (= K155) binding
3rkuA Substrate fingerprint and the structure of NADP+ dependent serine dehydrogenase from saccharomyces cerevisiae complexed with NADP+
39% identity, 98% coverage: 3:249/252 of query aligns to 15:267/268 of 3rkuA
- active site: A107 (= A89), N128 (= N110), S156 (= S138), Y169 (= Y151), K173 (= K155), N214 (≠ D196)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G21 (= G9), S23 (≠ T11), G25 (= G13), I26 (= I14), R49 (= R34), R50 (= R35), D76 (= D58), I77 (≠ V59), N103 (= N85), A104 (= A86), G105 (= G87), K106 (≠ N88), S156 (= S138), Y169 (= Y151), K173 (= K155), P199 (= P181), G200 (= G182), V202 (= V184), T204 (= T186), E205 (= E187), F206 (= F188)
6ixjA The crystal structure of sulfoacetaldehyde reductase from klebsiella oxytoca (see paper)
43% identity, 96% coverage: 2:242/252 of query aligns to 1:242/251 of 6ixjA
- binding 2-hydroxyethylsulfonic acid: S138 (= S138), Y145 (= Y145), Y151 (= Y151)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G9), T10 (= T11), S11 (= S12), G12 (= G13), F13 (≠ I14), R33 (= R34), R34 (= R35), D57 (= D58), V58 (= V59), N84 (= N85), A85 (= A86), G86 (= G87), T108 (≠ I109), I136 (= I136), S138 (= S138), Y151 (= Y151), K155 (= K155), P181 (= P181), G182 (= G182), A184 (≠ V184), T186 (= T186), E187 (= E187), F188 (= F188)
2japA Clavulanic acid dehydrogenase: structural and biochemical analysis of the final step in the biosynthesis of the beta- lactamase inhibitor clavulanic acid (see paper)
37% identity, 92% coverage: 3:234/252 of query aligns to 6:237/245 of 2japA
- active site: S140 (= S138), Y153 (= Y151), K157 (= K155), A198 (≠ R199)
- binding (2r,3z,5r)-3-(2-hydroxyethylidene)-7-oxo-4-oxa-1-azabicyclo[3.2.0]heptane-2-carboxylic acid: M93 (≠ A89), S140 (= S138), A142 (= A140), Y153 (= Y151), T185 (≠ L183), Y203 (= Y204), R206 (vs. gap)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G12 (= G9), S14 (≠ T11), S15 (= S12), G16 (= G13), I17 (= I14), A36 (≠ G33), R37 (= R34), R38 (= R35), L61 (≠ F57), D62 (= D58), V63 (= V59), N89 (= N85), A90 (= A86), G91 (= G87), T112 (≠ I109), M138 (≠ I136), S139 (≠ G137), S140 (= S138), Y153 (= Y151), K157 (= K155), P183 (= P181), T185 (≠ L183), T186 (≠ V184), T188 (= T186), E189 (= E187), L190 (≠ F188)
2jahC Biochemical and structural analysis of the clavulanic acid dehydeogenase (cad) from streptomyces clavuligerus (see paper)
37% identity, 92% coverage: 3:234/252 of query aligns to 7:238/246 of 2jahC
- active site: S141 (= S138), Y154 (= Y151), K158 (= K155), A199 (≠ R199)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G13 (= G9), S15 (≠ T11), S16 (= S12), G17 (= G13), I18 (= I14), A37 (≠ G33), R38 (= R34), R39 (= R35), D63 (= D58), V64 (= V59), N90 (= N85), A91 (= A86), G92 (= G87), T113 (≠ I109), M139 (≠ I136), S141 (= S138), Y154 (= Y151), K158 (= K155), P184 (= P181), G185 (= G182), T186 (≠ L183), T187 (≠ V184), T189 (= T186), E190 (= E187), L191 (≠ F188)
1xg5C Structure of human putative dehydrogenase mgc4172 in complex with nadp
33% identity, 93% coverage: 2:236/252 of query aligns to 10:252/257 of 1xg5C
- active site: S150 (= S138), Y165 (= Y151), K169 (= K155)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G17 (= G9), S19 (≠ T11), G21 (= G13), I22 (= I14), A41 (≠ G33), R42 (= R34), T43 (≠ R35), D69 (= D58), L70 (≠ V59), N96 (= N85), G98 (= G87), I148 (= I136), S150 (= S138), Y165 (= Y151), K169 (= K155), G198 (= G182), V200 (= V184), T202 (= T186), F204 (= F188), K207 (≠ V191)
A0A1U8QWA2 Glycine betaine reductase ATRR; Nonribosomal peptide synthetase-like protein ATRR; EC 1.2.1.-; EC 1.1.1.- from Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) (see paper)
33% identity, 93% coverage: 3:236/252 of query aligns to 1030:1263/1270 of A0A1U8QWA2
- G1036 (= G9) mutation to A: Compromises binding of the cosubstrate NADPH to aldehyde reductase domain R2. Decreases the aldehyde reductase activity by 4,000-fold; when associated with F-1178.
- Y1178 (= Y151) mutation to F: Does not substantially affect carboxylic acid reductase activity but results to a 150-fold loss of aldehyde reductase activity and the accumulation of glycine betaine aldehyde intermediate. Further decreases the aldehyde reductase activity by 4,000-fold; when associated with F-1178.
Sites not aligning to the query:
- 14:418 Adenylation (A) domain
- 643:937 Carboxylic acid reductase domain R1
- 812 Y→F: Abolishes overall carboxylic acid reductase activity but does nor affect aldehyde reductase activity.
- 1026:1256 Aldehyde reductase domain R2
3p19A Improved NADPH-dependent blue fluorescent protein (see paper)
33% identity, 96% coverage: 1:241/252 of query aligns to 1:237/239 of 3p19A
- active site: S132 (= S138), Y145 (= Y151), K149 (= K155)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G9 (= G9), S11 (≠ T11), S12 (= S12), G13 (= G13), I14 (= I14), A33 (≠ G33), R34 (= R34), R35 (= R35), D53 (= D51), V54 (= V59), N80 (= N85), A81 (= A86), G82 (= G87), I130 (= I136), S132 (= S138), Y145 (= Y151), K149 (= K155), P175 (= P181), A177 (≠ L183), V178 (= V184), T180 (= T186), E181 (= E187), L182 (≠ F188)
2ehdB Crystal structure analysis of oxidoreductase
31% identity, 94% coverage: 1:236/252 of query aligns to 3:210/213 of 2ehdB
5u9pB Crystal structure of a gluconate 5-dehydrogenase from burkholderia cenocepacia j2315 in complex with NADP and tartrate
36% identity, 74% coverage: 3:189/252 of query aligns to 17:203/261 of 5u9pB
- active site: G27 (= G13), S152 (= S138), Y165 (= Y151), K169 (= K155)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G23 (= G9), R26 (≠ S12), G27 (= G13), I28 (= I14), R48 (= R34), D73 (= D58), V74 (= V59), N100 (= N85), A101 (= A86), I150 (= I136), Y165 (= Y151), K169 (= K155), P195 (= P181), F198 (≠ V184), T200 (= T186), L202 (≠ F188), N203 (≠ S189)
1xkqA Crystal structure of short-chain dehydrogenase/reductase of unknown function from caenorhabditis elegans with cofactor
33% identity, 89% coverage: 2:225/252 of query aligns to 5:244/272 of 1xkqA
- active site: G16 (= G13), S147 (= S138), F158 (≠ G148), Y161 (= Y151), K165 (= K155), D206 (≠ E198)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G12 (= G9), S14 (≠ T11), G16 (= G13), I17 (= I14), R37 (= R34), S38 (≠ R35), R41 (= R38), D65 (= D58), V66 (= V59), N92 (= N85), A93 (= A86), G94 (= G87), L119 (≠ I109), S147 (= S138), Y161 (= Y151), K165 (= K155), P191 (= P181), G192 (= G182), M193 (≠ L183), V194 (= V184), T196 (= T186), G197 (≠ E187), F198 (= F188)
5itvA Crystal structure of bacillus subtilis bacc dihydroanticapsin 7- dehydrogenase in complex with nadh (see paper)
32% identity, 87% coverage: 2:221/252 of query aligns to 7:232/255 of 5itvA
- active site: G18 (= G13), S141 (= S138), Y154 (= Y151), K158 (= K155)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G9), S17 (= S12), G18 (= G13), I19 (= I14), D38 (≠ G33), I39 (≠ R34), T61 (≠ F57), I63 (≠ V59), N89 (= N85), G91 (= G87), T139 (≠ I136), S141 (= S138), Y154 (= Y151), K158 (= K155), P184 (= P181), G185 (= G182), I186 (≠ L183), I187 (≠ V184)
1w4zA Structure of actinorhodin polyketide (actiii) reductase (see paper)
35% identity, 73% coverage: 2:186/252 of query aligns to 4:190/259 of 1w4zA
- active site: G15 (= G13), N112 (= N110), S142 (= S138), Y155 (= Y151), K159 (= K155)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G11 (= G9), T13 (= T11), S14 (= S12), G15 (= G13), I16 (= I14), R36 (= R34), G37 (≠ R35), D61 (= D58), V62 (= V59), N88 (= N85), G90 (= G87), S142 (= S138), Y155 (= Y151), K159 (= K155), P185 (= P181), G186 (= G182), V188 (= V184), T190 (= T186)
Sites not aligning to the query:
P16544 Putative ketoacyl reductase; EC 1.3.1.- from Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) (see 2 papers)
35% identity, 73% coverage: 2:186/252 of query aligns to 6:192/261 of P16544
- 11:39 (vs. 7:35, 45% identical) binding
- D63 (= D58) binding
- K161 (= K155) binding
1xr3A Actinorhodin polyketide ketoreductase with NADP and the inhibitor isoniazid bound (see paper)
35% identity, 73% coverage: 2:186/252 of query aligns to 1:187/256 of 1xr3A
- active site: G12 (= G13), N109 (= N110), S139 (= S138), Y152 (= Y151), K156 (= K155)
- binding 4-(diazenylcarbonyl)pyridine: T140 (≠ I139), G141 (≠ A140), V146 (≠ Y145)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G9), T10 (= T11), S11 (= S12), G12 (= G13), I13 (= I14), A32 (≠ G33), R33 (= R34), G34 (≠ R35), C57 (≠ F57), D58 (= D58), V59 (= V59), N85 (= N85), A86 (= A86), G87 (= G87), S139 (= S138), Y152 (= Y151), K156 (= K155), G183 (= G182), V185 (= V184), T187 (= T186)
Sites not aligning to the query:
2rh4A Actinorhodin ketoreductase, actkr, with NADPH and inhibitor emodin (see paper)
35% identity, 73% coverage: 2:186/252 of query aligns to 2:188/257 of 2rh4A
- active site: G13 (= G13), N110 (= N110), S140 (= S138), Y153 (= Y151), K157 (= K155)
- binding 3-methyl-1,6,8-trihydroxyanthraquinone: T141 (≠ I139), Q145 (≠ E143), V147 (≠ Y145), Y153 (= Y151), F185 (≠ L183)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G9 (= G9), T11 (= T11), S12 (= S12), G13 (= G13), I14 (= I14), A33 (≠ G33), R34 (= R34), G35 (≠ R35), C58 (≠ F57), D59 (= D58), V60 (= V59), N86 (= N85), G88 (= G87), S140 (= S138), Y153 (= Y151), K157 (= K155), P183 (= P181), G184 (= G182), V186 (= V184), T188 (= T186)
Sites not aligning to the query:
2rh4B Actinorhodin ketoreductase, actkr, with NADPH and inhibitor emodin (see paper)
34% identity, 75% coverage: 2:189/252 of query aligns to 13:202/268 of 2rh4B
- active site: G24 (= G13), N121 (= N110), S151 (= S138), Y164 (= Y151), K168 (= K155)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G20 (= G9), T22 (= T11), S23 (= S12), I25 (= I14), A44 (≠ G33), R45 (= R34), G46 (≠ R35), C69 (≠ F57), D70 (= D58), V71 (= V59), N97 (= N85), S151 (= S138), Y164 (= Y151), K168 (= K155), G195 (= G182), V197 (= V184), T199 (= T186), M201 (≠ F188)
Sites not aligning to the query:
4qecA Elxo with NADP bound (see paper)
31% identity, 74% coverage: 1:187/252 of query aligns to 1:188/248 of 4qecA
- active site: G13 (= G13), N111 (= N110), S139 (= S138), Y152 (= Y151), K156 (= K155)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: K12 (≠ S12), G13 (= G13), I14 (= I14), S33 (≠ G33), R34 (= R34), K38 (≠ R35), D59 (= D58), V60 (= V59), N86 (= N85), A87 (= A86), G88 (= G87), I137 (= I136), Y152 (= Y151), K156 (= K155), P182 (= P181), I185 (≠ V184)
Query Sequence
>Echvi_1820 FitnessBrowser__Cola:Echvi_1820
MNKIALITGATSGIGRECAIALSNSGYNIIATGRREERLQALQSKLSPSVDYHYLVFDVR
DKAAVDAALDSLPKPWSDIDVLINNAGNAHGLDPIQEGDPADWDAMMDINVKGLLYVSKK
VMPGMIDKKAGHIVNIGSIAAKEVYPNGNVYCASKHAVDAITKGMRLDLTKYNIRVTGIH
PGLVETEFSLVRFKGDEERAKHVYEGFEPLKPEDIADIVHFAVTRPAHVVMTDITVLAGK
QANSNTVYKDQS
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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