SitesBLAST
Comparing Pf6N2E2_1322 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_1322 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
5t5qC Crystal structure of short-chain dehydrogenase/reductase sdr:glucose/ribitol dehydrogenase from brucella melitensis
36% identity, 92% coverage: 3:247/266 of query aligns to 6:241/245 of 5t5qC
- active site: G18 (= G15), S140 (= S134), N150 (≠ V144), Y153 (= Y147), K157 (= K151)
- binding nicotinamide-adenine-dinucleotide: N16 (≠ G13), G17 (≠ T14), G18 (= G15), I19 (= I16), D38 (≠ G35), L39 (≠ R36), D63 (= D56), A64 (= A57), S90 (≠ C83), I113 (≠ S106), Y153 (= Y147), K157 (= K151), P182 (= P177), I185 (≠ V180), T187 (= T182), M189 (= M184)
4fn4A Short-chain NAD(h)-dependent dehydrogenase/reductase from sulfolobus acidocaldarius (see paper)
34% identity, 94% coverage: 3:251/266 of query aligns to 6:254/254 of 4fn4A
- active site: G18 (= G15), S144 (= S134), Y157 (= Y147), K161 (= K151), S202 (≠ A185)
- binding nicotinamide-adenine-dinucleotide: G14 (= G11), S17 (≠ T14), G18 (= G15), I19 (= I16), E38 (≠ G35), L39 (≠ R36), R43 (≠ P40), A63 (≠ G55), D64 (= D56), V65 (≠ A57), N91 (≠ C83), G93 (= G85), I94 (≠ G86), T142 (≠ I132), S144 (= S134), Y157 (= Y147), K161 (= K151), P187 (= P177), V190 (= V180), T192 (= T182), N193 (≠ P183), I194 (≠ M184)
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: 5:249/266 of query aligns to 14:264/267 of Q9LBG2
- 17:42 (vs. 8:33, 58% identical) binding
- E103 (≠ M87) mutation E->A,D,N,Q: 26-fold increase in Km and a much lower enantiomeric excess of the reaction products.
1iy8A Crystal structure of levodione reductase (see paper)
35% identity, 92% coverage: 5:249/266 of query aligns to 5:255/258 of 1iy8A
- active site: G15 (= G15), S143 (= S134), Q153 (≠ V144), Y156 (= Y147), K160 (= K151)
- binding nicotinamide-adenine-dinucleotide: G11 (= G11), S14 (≠ T14), G15 (= G15), L16 (≠ I16), D35 (≠ G35), V36 (≠ R36), A62 (≠ G55), D63 (= D56), V64 (≠ A57), N90 (≠ C83), G92 (= G85), I93 (≠ G86), T141 (≠ I132), S143 (= S134), Y156 (= Y147), K160 (= K151), P186 (= P177), G187 (= G178), T191 (= T182), P192 (= P183), M193 (= M184)
4urfB Molecular genetic and crystal structural analysis of 1-(4- hydroxyphenyl)-ethanol dehydrogenase from aromatoleum aromaticum ebn1 (see paper)
35% identity, 93% coverage: 1:247/266 of query aligns to 2:244/248 of 4urfB
- active site: G16 (= G15), S142 (= S134), I152 (≠ V144), Y155 (= Y147), K159 (= K151)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: L210 (= L213), R211 (= R214), R212 (= R215)
- binding bicarbonate ion: I92 (≠ G86), G94 (= G88), R109 (≠ A102), R179 (= R171), S228 (= S231)
- binding nicotinamide-adenine-dinucleotide: G12 (= G11), G14 (= G13), N15 (≠ T14), G16 (= G15), I17 (= I16), D36 (≠ G35), I37 (≠ R36), D62 (= D56), T63 (≠ A57), N89 (≠ C83), A90 (= A84), G91 (= G85), I140 (= I132), Y155 (= Y147), K159 (= K151), P185 (= P177), A186 (≠ G178), I188 (≠ V180), T190 (= T182)
4urfA Molecular genetic and crystal structural analysis of 1-(4- hydroxyphenyl)-ethanol dehydrogenase from aromatoleum aromaticum ebn1 (see paper)
35% identity, 93% coverage: 1:247/266 of query aligns to 2:244/248 of 4urfA
- active site: G16 (= G15), S142 (= S134), I152 (≠ V144), Y155 (= Y147), K159 (= K151)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: I92 (≠ G86), S93 (≠ M87), G94 (= G88), E95 (≠ M89), T97 (≠ S91), E101 (= E94), T103 (≠ H96), Q106 (≠ A99), R109 (≠ A102), S175 (≠ P167), G177 (= G169)
- binding magnesium ion: S237 (≠ A240), Y238 (≠ T241)
- binding nicotinamide-adenine-dinucleotide: G12 (= G11), G14 (= G13), N15 (≠ T14), G16 (= G15), I17 (= I16), D36 (≠ G35), I37 (≠ R36), W41 (vs. gap), D62 (= D56), T63 (≠ A57), N89 (≠ C83), A90 (= A84), G91 (= G85), I140 (= I132), Y155 (= Y147), K159 (= K151), P185 (= P177), I188 (≠ V180), T190 (= T182)
4ureB Molecular genetic and crystal structural analysis of 1-(4- hydroxyphenyl)-ethanol dehydrogenase from aromatoleum aromaticum ebn1 (see paper)
35% identity, 93% coverage: 1:247/266 of query aligns to 2:244/248 of 4ureB
- active site: G16 (= G15), S142 (= S134), I152 (≠ V144), Y155 (= Y147), K159 (= K151)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: N15 (≠ T14), G16 (= G15), I17 (= I16), N89 (≠ C83), G91 (= G85), Y155 (= Y147), P185 (= P177), A186 (≠ G178)
6vspA Structure of serratia marcescens 2,3-butanediol dehydrogenase mutant q247a (see paper)
34% identity, 94% coverage: 3:252/266 of query aligns to 4:245/251 of 6vspA
- active site: G16 (= G15), S138 (= S134), Y151 (= Y147)
- binding nicotinamide-adenine-dinucleotide: G12 (= G11), N15 (≠ T14), G16 (= G15), M17 (≠ I16), D36 (≠ G35), W37 (≠ R36), W37 (≠ R36), A38 (≠ R37), I59 (≠ G55), D60 (= D56), V61 (≠ A57), N87 (≠ C83), A88 (= A84), G89 (= G85), V90 (≠ G86), V110 (≠ S106), T136 (≠ I132), S138 (= S134), Y151 (= Y147), K155 (= K151), P181 (= P177), S182 (≠ G178), L183 (≠ W179), V184 (= V180), T186 (= T182), N187 (≠ P183), M188 (= M184), T189 (≠ A185)
6vspB Structure of serratia marcescens 2,3-butanediol dehydrogenase mutant q247a (see paper)
34% identity, 94% coverage: 3:252/266 of query aligns to 6:247/252 of 6vspB
H9XP47 Meso-2,3-butanediol dehydrogenase; BDH; meso-2,3-BDH; (R,S)-butane-2,3-diol dehydrogenase; NAD(H)-dependent meso-2,3-BDH; SmBdh; EC 1.1.1.- from Serratia marcescens (see paper)
34% identity, 94% coverage: 3:252/266 of query aligns to 4:245/251 of H9XP47
- N15 (≠ T14) binding
- M17 (≠ I16) binding
- D36 (≠ G35) binding
- D60 (= D56) binding
- V61 (≠ A57) binding
- N87 (≠ C83) binding
- S138 (= S134) binding ; binding
- V139 (≠ I135) mutation to Q: Retains 50% of activity with acetoin as substrate; when associated with A-247.
- S140 (≠ A136) binding
- Y151 (= Y147) binding ; binding ; binding
- K155 (= K151) binding
- V184 (= V180) binding
- T186 (= T182) binding
- RDK 197:199 (≠ YDR 204:206) mutation to SEAAGKPLGYGTET: Mimics longer alpha6 helix. Retains 3% of activity with acetoin as substrate.
Sites not aligning to the query:
- 247 Q→A: Retains 10% of activity with acetoin as substrate. Retains 50% of activity with acetoin as substrate; when associated with Q-139.
6xewA Structure of serratia marcescens 2,3-butanediol dehydrogenase (see paper)
34% identity, 94% coverage: 3:252/266 of query aligns to 4:245/251 of 6xewA
- active site: G16 (= G15), S138 (= S134), Y151 (= Y147)
- binding r,3-hydroxybutan-2-one: S138 (= S134), S140 (≠ A136), Y151 (= Y147)
- binding s,3-hydroxybutan-2-one: S138 (= S134), Y151 (= Y147), S182 (≠ G178)
- binding nicotinamide-adenine-dinucleotide: G12 (= G11), N15 (≠ T14), G16 (= G15), M17 (≠ I16), D36 (≠ G35), W37 (≠ R36), W37 (≠ R36), A38 (≠ R37), I59 (≠ G55), D60 (= D56), V61 (≠ A57), N87 (≠ C83), A88 (= A84), G89 (= G85), V110 (≠ S106), T136 (≠ I132), S138 (= S134), Y151 (= Y147), K155 (= K151), S182 (≠ G178), L183 (≠ W179), V184 (= V180), T186 (= T182), N187 (≠ P183), M188 (= M184), T189 (≠ A185)
Q8JZV9 Dehydrogenase/reductase SDR family member 6; (R)-beta-hydroxybutyrate dehydrogenase; 3-hydroxybutyrate dehydrogenase type 2; 4-oxo-L-proline reductase; Oxidoreductase UCPA; Short chain dehydrogenase/reductase family 15C member 1; EC 1.1.1.-; EC 1.1.1.30; EC 1.1.1.104 from Mus musculus (Mouse) (see paper)
32% identity, 93% coverage: 3:250/266 of query aligns to 5:245/245 of Q8JZV9
- Y147 (= Y147) active site, Proton acceptor; mutation to F: Loss of function.
4bmsF Short chain alcohol dehydrogenase from ralstonia sp. Dsm 6428 in complex with NADPH
33% identity, 92% coverage: 4:247/266 of query aligns to 6:245/249 of 4bmsF
- active site: S137 (= S134), H147 (≠ V144), Y150 (= Y147), K154 (= K151), Q195 (= Q194)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G11), N15 (≠ G13), S16 (≠ T14), I18 (= I16), R38 (= R36), R39 (= R37), A59 (≠ G55), D60 (= D56), V61 (≠ A57), N87 (≠ C83), S88 (≠ A84), G89 (= G85), V110 (≠ S106), S137 (= S134), Y150 (= Y147), K154 (= K151), G181 (= G178), I183 (≠ V180), T185 (= T182), I187 (≠ M184)
D4A1J4 Dehydrogenase/reductase SDR family member 6; (R)-beta-hydroxybutyrate dehydrogenase; 3-hydroxybutyrate dehydrogenase type 2; 4-oxo-L-proline reductase; Oxidoreductase UCPA; Short chain dehydrogenase/reductase family 15C member 1; EC 1.1.1.-; EC 1.1.1.30; EC 1.1.1.104 from Rattus norvegicus (Rat) (see paper)
34% identity, 93% coverage: 3:250/266 of query aligns to 5:245/245 of D4A1J4
- Y147 (= Y147) mutation to F: Loss of function.
6ixmC Crystal structure of the ketone reductase chkred20 from the genome of chryseobacterium sp. Ca49 complexed with NAD (see paper)
30% identity, 94% coverage: 3:251/266 of query aligns to 4:248/248 of 6ixmC
- active site: G16 (= G15), S142 (= S134), Y155 (= Y147), K159 (= K151)
- binding nicotinamide-adenine-dinucleotide: G12 (= G11), S15 (≠ T14), G16 (= G15), I17 (= I16), D36 (≠ G35), I37 (≠ R36), A61 (≠ G55), D62 (= D56), T63 (≠ A57), N89 (≠ C83), A90 (= A84), M140 (≠ I132), S142 (= S134), Y155 (= Y147), K159 (= K151), P185 (= P177), A186 (≠ G178), Y187 (≠ W179), I188 (≠ V180), L192 (≠ M184)
6ihhA Crystal structure of rasadh f12 from ralstonia.Sp in complex with NADPH and a6o
32% identity, 92% coverage: 4:247/266 of query aligns to 6:245/249 of 6ihhA
- binding (2R,3S)-2-ethyl-2-[(2E)-2-(6-methoxy-3,4-dihydro-2H-naphthalen-1-ylidene)ethyl]-3-oxidanyl-cyclopentan-1-one: S137 (= S134), H147 (≠ V144), Y150 (= Y147), L188 (≠ A185)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G11), N15 (≠ G13), S16 (≠ T14), G17 (= G15), I18 (= I16), R38 (= R36), R39 (= R37), D60 (= D56), V61 (≠ A57), N87 (≠ C83), S88 (≠ A84), G89 (= G85), V110 (≠ S106), T135 (≠ I132), S137 (= S134), Y150 (= Y147), K154 (= K151), P180 (= P177), G181 (= G178), A182 (≠ W179), I183 (≠ V180), T185 (= T182), S187 (≠ M184)
Sites not aligning to the query:
5itvA Crystal structure of bacillus subtilis bacc dihydroanticapsin 7- dehydrogenase in complex with nadh (see paper)
33% identity, 92% coverage: 5:249/266 of query aligns to 8:253/255 of 5itvA
- active site: G18 (= G15), S141 (= S134), Y154 (= Y147), K158 (= K151)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G11), S17 (≠ T14), G18 (= G15), I19 (= I16), D38 (≠ G35), I39 (≠ R36), T61 (vs. gap), I63 (vs. gap), N89 (≠ C83), G91 (= G85), T139 (≠ I132), S141 (= S134), Y154 (= Y147), K158 (= K151), P184 (= P177), G185 (= G178), I186 (≠ W179), I187 (≠ V180)
2ztlA Closed conformation of d-3-hydroxybutyrate dehydrogenase complexed with NAD+ and l-3-hydroxybutyrate (see paper)
33% identity, 93% coverage: 1:247/266 of query aligns to 1:256/260 of 2ztlA
- active site: G15 (= G15), N114 (= N107), S142 (= S134), Y155 (= Y147), K159 (= K151), L200 (= L192)
- binding (3s)-3-hydroxybutanoic acid: Q94 (≠ G88), S142 (= S134), H144 (≠ A136), K152 (≠ V144), Y155 (= Y147), Q196 (≠ E188)
- binding nicotinamide-adenine-dinucleotide: G11 (= G11), G15 (= G15), I16 (= I16), F36 (vs. gap), L64 (≠ A57), N90 (≠ C83), A91 (= A84), G92 (= G85), L113 (≠ S106), Y155 (= Y147), K159 (= K151), P185 (= P177), W187 (= W179), V188 (= V180), T190 (= T182), V193 (≠ A185)
1wmbA Crystal structure of NAD dependent d-3-hydroxybutylate dehydrogenase (see paper)
33% identity, 93% coverage: 1:247/266 of query aligns to 1:256/260 of 1wmbA
Sites not aligning to the query:
5t2uA Short chain dehydrogenase/reductase family protein (see paper)
35% identity, 94% coverage: 3:251/266 of query aligns to 5:241/241 of 5t2uA
- active site: G17 (= G15), T135 (≠ S134), T145 (≠ V144), Y148 (= Y147), K152 (= K151)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G11), G17 (= G15), R38 (= R36), D39 (≠ R37), R42 (≠ P40), D60 (≠ C59), L61 (≠ P60), N83 (≠ C83), A84 (= A84), Y87 (≠ M87), I133 (= I132), T135 (≠ S134), Y148 (= Y147), K152 (= K151), P178 (= P177), P180 (≠ W179), T181 (≠ V180), T183 (= T182), T185 (≠ M184), T186 (≠ A185)
Query Sequence
>Pf6N2E2_1322 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_1322
MPESRTVVITGAGTGIGAACARLYAAEGANLVLIGRRREPLEALAEDIGGLVLVGDAACP
NTWDGFVEQIRKRHGRLDVLLACAGGMGMGSATETHPSAWEAALRSNLDSAFYSARACLP
LLKESAGNIVLIASIASLAAGPHVCGYTTAKHALLGLNRSLARDYGPHGVRVNAICPGWV
RTPMADEEMQALMQFHGETLQQAYDRVCADVPLRRPASAEEIANVCRFLASPDASIITGA
TLVADGGSSIVDVPTLAFSRMEASDV
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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