SitesBLAST
Comparing Pf1N1B4_412 3-oxoacyl-[acyl-carrier protein] reductase (EC 1.1.1.100) 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)
4fn4A Short-chain NAD(h)-dependent dehydrogenase/reductase from sulfolobus acidocaldarius (see paper)
38% identity, 93% coverage: 17:269/272 of query aligns to 3:254/254 of 4fn4A
- active site: G18 (= G32), S144 (= S157), Y157 (= Y170), K161 (= K174), S202 (≠ H219)
- binding nicotinamide-adenine-dinucleotide: G14 (= G28), S17 (≠ Q31), G18 (= G32), I19 (= I33), E38 (≠ D52), L39 (≠ I53), R43 (≠ K57), A63 (= A77), D64 (= D78), V65 (= V79), N91 (≠ C105), G93 (= G107), I94 (≠ V108), T142 (≠ I155), S144 (= S157), Y157 (= Y170), K161 (= K174), P187 (= P200), V190 (≠ I203), T192 (= T205), N193 (≠ Q206), I194 (≠ L207)
6ixmC Crystal structure of the ketone reductase chkred20 from the genome of chryseobacterium sp. Ca49 complexed with NAD (see paper)
36% identity, 92% coverage: 19:269/272 of query aligns to 3:248/248 of 6ixmC
- active site: G16 (= G32), S142 (= S157), Y155 (= Y170), K159 (= K174)
- binding nicotinamide-adenine-dinucleotide: G12 (= G28), S15 (≠ Q31), G16 (= G32), I17 (= I33), D36 (= D52), I37 (= I53), A61 (= A77), D62 (= D78), T63 (≠ V79), N89 (≠ C105), A90 (= A106), M140 (≠ I155), S142 (= S157), Y155 (= Y170), K159 (= K174), P185 (= P200), A186 (≠ G201), Y187 (= Y202), I188 (= I203), L192 (= L207)
4urfB Molecular genetic and crystal structural analysis of 1-(4- hydroxyphenyl)-ethanol dehydrogenase from aromatoleum aromaticum ebn1 (see paper)
36% identity, 91% coverage: 19:265/272 of query aligns to 3:244/248 of 4urfB
- active site: G16 (= G32), S142 (= S157), I152 (≠ C167), Y155 (= Y170), K159 (= K174)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: L210 (≠ P231), R211 (= R232), R212 (= R233)
- binding bicarbonate ion: I92 (≠ V108), G94 (vs. gap), R109 (= R124), R179 (= R194), S228 (= S249)
- binding nicotinamide-adenine-dinucleotide: G12 (= G28), G14 (≠ A30), N15 (≠ Q31), G16 (= G32), I17 (= I33), D36 (= D52), I37 (= I53), D62 (= D78), T63 (≠ V79), N89 (≠ C105), A90 (= A106), G91 (= G107), I140 (= I155), Y155 (= Y170), K159 (= K174), P185 (= P200), A186 (≠ G201), I188 (= I203), T190 (= T205)
4urfA Molecular genetic and crystal structural analysis of 1-(4- hydroxyphenyl)-ethanol dehydrogenase from aromatoleum aromaticum ebn1 (see paper)
36% identity, 91% coverage: 19:265/272 of query aligns to 3:244/248 of 4urfA
- active site: G16 (= G32), S142 (= S157), I152 (≠ C167), Y155 (= Y170), K159 (= K174)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: I92 (≠ V108), S93 (≠ N109), G94 (vs. gap), E95 (≠ V110), T97 (≠ R112), E101 (≠ Q116), T103 (= T118), Q106 (≠ D121), R109 (= R124), S175 (≠ P190), G177 (= G192)
- binding magnesium ion: S237 (= S258), Y238 (≠ C259)
- binding nicotinamide-adenine-dinucleotide: G12 (= G28), G14 (≠ A30), N15 (≠ Q31), G16 (= G32), I17 (= I33), D36 (= D52), I37 (= I53), W41 (≠ K57), D62 (= D78), T63 (≠ V79), N89 (≠ C105), A90 (= A106), G91 (= G107), I140 (= I155), Y155 (= Y170), K159 (= K174), P185 (= P200), I188 (= I203), T190 (= T205)
4ureB Molecular genetic and crystal structural analysis of 1-(4- hydroxyphenyl)-ethanol dehydrogenase from aromatoleum aromaticum ebn1 (see paper)
36% identity, 91% coverage: 19:265/272 of query aligns to 3:244/248 of 4ureB
- active site: G16 (= G32), S142 (= S157), I152 (≠ C167), Y155 (= Y170), K159 (= K174)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: N15 (≠ Q31), G16 (= G32), I17 (= I33), N89 (≠ C105), G91 (= G107), Y155 (= Y170), P185 (= P200), A186 (≠ G201)
Q9LBG2 Levodione reductase; (6R)-2,2,6-trimethyl-1,4-cyclohexanedione reductase; EC 1.1.1.- from Leifsonia aquatica (Corynebacterium aquaticum) (see paper)
36% identity, 93% coverage: 18:270/272 of query aligns to 10:267/267 of Q9LBG2
- 17:42 (vs. 25:50, 35% identical) binding
- E103 (≠ N109) 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)
36% identity, 93% coverage: 18:270/272 of query aligns to 1:258/258 of 1iy8A
- active site: G15 (= G32), S143 (= S157), Q153 (≠ C167), Y156 (= Y170), K160 (= K174)
- binding nicotinamide-adenine-dinucleotide: G11 (= G28), S14 (≠ Q31), G15 (= G32), L16 (≠ I33), D35 (= D52), V36 (≠ I53), A62 (= A77), D63 (= D78), V64 (= V79), N90 (≠ C105), G92 (= G107), I93 (≠ V108), T141 (≠ I155), S143 (= S157), Y156 (= Y170), K160 (= K174), P186 (= P200), G187 (= G201), T191 (= T205), P192 (≠ Q206), M193 (≠ L207)
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)
35% identity, 92% coverage: 19:269/272 of query aligns to 3:246/248 of Q9KJF1
- S15 (≠ Q31) binding
- D36 (= D52) binding
- D62 (= D78) binding
- I63 (≠ V79) binding
- N89 (≠ C105) binding
- Y153 (= Y170) binding
- K157 (= K174) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
7pcsB Structure of the heterotetrameric sdr family member bbscd (see paper)
35% identity, 92% coverage: 19:269/272 of query aligns to 2:245/247 of 7pcsB
- binding nicotinamide-adenine-dinucleotide: G11 (= G28), M16 (≠ I33), D35 (= D52), I36 (= I53), I62 (≠ V79), N88 (≠ C105), G90 (= G107), I138 (= I155), S140 (= S157), Y152 (= Y170), K156 (= K174), I185 (= I203)
P40288 Glucose 1-dehydrogenase; EC 1.1.1.47 from Priestia megaterium (Bacillus megaterium) (see 2 papers)
33% identity, 92% coverage: 19:267/272 of query aligns to 5:251/261 of P40288
- 11:35 (vs. 25:49, 32% identical) binding
- E96 (≠ N109) mutation E->A,G,K: Heat stable.
- D108 (= D121) mutation to N: Heat stable.
- V112 (≠ C125) mutation to A: Heat stable.
- E133 (= E146) mutation to K: Heat stable.
- V183 (= V195) mutation to I: Heat stable.
- P194 (≠ Q206) mutation to Q: Heat stable.
- E210 (≠ F226) mutation to K: Heat stable.
- Y217 (≠ R233) 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.
1g6kA Crystal structure of glucose dehydrogenase mutant e96a complexed with NAD+
33% identity, 92% coverage: 19:267/272 of query aligns to 5:251/261 of 1g6kA
- active site: G18 (= G32), S145 (= S157), Y158 (= Y170), K162 (= K174)
- binding nicotinamide-adenine-dinucleotide: T17 (≠ Q31), G18 (= G32), L19 (≠ I33), R39 (≠ I53), D65 (= D78), V66 (= V79), N92 (≠ C105), A93 (= A106), G94 (= G107), M143 (≠ I155), S145 (= S157), Y158 (= Y170), P188 (= P200), G189 (= G201), I191 (= I203), T193 (= T205)
2zatA Crystal structure of a mammalian reductase (see paper)
34% identity, 91% coverage: 19:265/272 of query aligns to 3:246/251 of 2zatA
- active site: G16 (= G32), S142 (= S157), L152 (≠ C167), Y155 (= Y170), K159 (= K174), K200 (≠ H219)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: A12 (≠ G28), T14 (≠ A30), D15 (≠ Q31), G16 (= G32), I17 (= I33), S36 (≠ D52), R37 (≠ I53), K38 (≠ Q54), N41 (≠ K57), H62 (≠ D78), N89 (≠ C105), A91 (≠ G107), V140 (≠ I155), S142 (= S157), Y155 (= Y170), K159 (= K174), P185 (= P200), G186 (= G201), I188 (= I203), T190 (= T205), F192 (≠ L207), S193 (≠ N208)
Q8WNV7 Dehydrogenase/reductase SDR family member 4; NADPH-dependent carbonyl reductase; CR; PHCR; NADPH-dependent retinol dehydrogenase/reductase; NDRD; Peroxisomal carbonyl reductase; PerCR; Peroxisomal short-chain alcohol dehydrogenase; PSCD; Short chain dehydrogenase/reductase family 25C member 2; Protein SDR25C2; EC 1.1.1.184; EC 1.1.1.300 from Sus scrofa (Pig) (see 2 papers)
34% identity, 91% coverage: 19:265/272 of query aligns to 31:274/279 of Q8WNV7
- 37:61 (vs. 25:49, 40% identical) binding
- F177 (≠ I164) Responsible for the stereoselective reduction of 3-ketosteroids into 3alpha-hydroxysteroids and benzil into S-benzoin; mutation to S: Change in stereoselective activity by the reduction of 3-ketosteroids and benzil into 3beta-hydroxysteroid and R-benzoin, respectively; when associated with F-180.
- L180 (≠ C167) Responsible for the stereoselective reduction of 3-ketosteroids into 3alpha-hydroxysteroids and benzil into S-benzoin; mutation to F: Change in stereoselective activity by the reduction of 3-ketosteroids and benzil into 3beta-hydroxysteroid and R-benzoin, respectively; when associated with S-177.
- Y183 (= Y170) active site, Proton acceptor
- K187 (= K174) binding
- N196 (≠ A183) Important for the maintenance of the quaternary structure, the catalytic activity and cold stability
Sites not aligning to the query:
- 277:279 Peroxisomal targeting signal
3o4rA Crystal structure of human dehydrogenase/reductase (sdr family) member 4 (dhrs4)
35% identity, 91% coverage: 19:265/272 of query aligns to 6:249/254 of 3o4rA
- active site: G19 (= G32), S145 (= S157), F155 (≠ C167), Y158 (= Y170), K162 (= K174), K203 (≠ P218)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: A15 (≠ G28), T17 (≠ A30), D18 (≠ Q31), G19 (= G32), I20 (= I33), S39 (≠ D52), R40 (≠ I53), K41 (≠ Q54), N44 (≠ K57), H65 (≠ D78), V66 (= V79), N92 (≠ C105), A94 (≠ G107), S145 (= S157), Y158 (= Y170), K162 (= K174), P188 (= P200), G189 (= G201), L190 (≠ Y202), I191 (= I203), T193 (= T205), F195 (≠ L207), S196 (≠ N208)
Q9BTZ2 Dehydrogenase/reductase SDR family member 4; NADPH-dependent carbonyl reductase; CR; NADPH-dependent retinol dehydrogenase/reductase; NRDR; humNRDR; Peroxisomal short-chain alcohol dehydrogenase; PSCD; SCAD-SRL; Short chain dehydrogenase/reductase family 25C member 2; Protein SDR25C2; Short-chain dehydrogenase/reductase family member 4; EC 1.1.1.184 from Homo sapiens (Human) (see 2 papers)
35% identity, 91% coverage: 19:265/272 of query aligns to 30:273/278 of Q9BTZ2
- S176 (≠ I164) Responsible for the stereoselective reduction of 3-ketosteroids into 3beta-hydroxysteroids and benzil into R-benzoin; mutation to F: Decreased reduction activity for benzil, isatin and retinal and increased activity for 5beta-Pregnane-3,20-dione and 5beta-Dihydrotestosterone. No change of stereoselectivity in 3-ketosteroids reduction and no change in 3beta-hydroxysteroid oxidation. Decreased reduction activity for isatin and increased activity for 5beta-Pregnane-3,20-dione, 5beta-Dihydrotestosterone, benzil and retinal; when associated with L-179. Change in stereoselective activity by the reduction of 5beta-Pregnane-3,20-dione predominantly to the 3alpha-hydroxysteroid; when associated with L-179. Switch from 3beta-hydroxysteroid to 3alpha-hydroxysteroid oxidation; when associated with L-179. Loss of cold catalytic inactivation; when associated with L-179 and N-195. Increased reduction activity for renital and oxidation activity for retinol; when associated with L-179 and N-195.
- F179 (≠ C167) Responsible for the stereoselective reduction of 3-ketosteroids into 3beta-hydroxysteroids and benzil into R-benzoin; mutation to L: Decreased reduction activity for isatin and increased activity for 5beta-Pregnane-3,20-dione, 5beta-Dihydrotestosterone, benzil and retinal; when associated with F-176. Change in stereoselective activity by the reduction of 5beta-Pregnane-3,20-dione predominantly to the 3alpha-hydroxysteroid; when associated with F-176. Switch from 3beta-hydroxysteroid to 3alpha-hydroxysteroid oxidation; when associated with F-176. Loss of cold catalytic inactivation; when associated with F-176 and N-195. Increased reduction activity for renital and oxidation activity for retinol; when associated with F-176 and N-195.
- T195 (≠ A183) mutation to N: Loss of cold catalytic inactivation. Loss of cold catalytic inactivation; when associated with F-176 and L-179. Switch in stereoselective activity from 3beta-hydroxysteroid to 3alpha-hydroxysteroid oxidation; when associated with F-176 and L-179. Increased reduction activity for renital and oxidation activity for retinol; when associated with F-176 and L-179.
3ay6B Crystal structure of bacillus megaterium glucose dehydrogenase 4 a258f mutant in complex with nadh and d-glucose (see paper)
34% identity, 92% coverage: 19:267/272 of query aligns to 11:257/267 of 3ay6B
- active site: G24 (= G32), S151 (= S157), Y164 (= Y170), K168 (= K174)
- binding beta-D-glucopyranose: E102 (≠ N109), S151 (= S157), H153 (= H159), W158 (≠ I164), Y164 (= Y170), N202 (= N208), K205 (≠ Y211)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G20 (= G28), T23 (≠ Q31), G24 (= G32), L25 (≠ I33), Y45 (≠ I53), D71 (= D78), V72 (= V79), N98 (≠ C105), A99 (= A106), G100 (= G107), V101 (= V108), M149 (≠ I155), S151 (= S157), Y164 (= Y170), K168 (= K174), P194 (= P200), G195 (= G201), M197 (≠ I203), T199 (= T205), P200 (≠ Q206), I201 (≠ L207), N202 (= N208)
4nbuB Crystal structure of fabg from bacillus sp (see paper)
35% identity, 91% coverage: 18:265/272 of query aligns to 4:241/244 of 4nbuB
- active site: G18 (= G32), N111 (≠ D129), S139 (= S157), Q149 (≠ C167), Y152 (= Y170), K156 (= K174)
- binding acetoacetyl-coenzyme a: D93 (= D113), K98 (≠ Q116), S139 (= S157), N146 (≠ I164), V147 (≠ P165), Q149 (≠ C167), Y152 (= Y170), F184 (≠ Y202), M189 (≠ L207), K200 (≠ R224)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G28), N17 (≠ Q31), G18 (= G32), I19 (= I33), D38 (= D52), F39 (≠ I53), V59 (≠ A77), D60 (= D78), V61 (= V79), N87 (≠ C105), A88 (= A106), G89 (= G107), I90 (≠ V108), T137 (≠ I155), S139 (= S157), Y152 (= Y170), K156 (= K174), P182 (= P200), F184 (≠ Y202), T185 (≠ I203), T187 (= T205), M189 (≠ L207)
2cfcA Structural basis for stereo selectivity in the (r)- and (s)-hydroxypropylethane thiosulfonate dehydrogenases (see paper)
35% identity, 92% coverage: 21:269/272 of query aligns to 2:250/250 of 2cfcA
- active site: G13 (= G32), S142 (= S157), Y155 (= Y170), K159 (= K174)
- binding (2-[2-ketopropylthio]ethanesulfonate: F149 (≠ I164), R152 (≠ C167), Y155 (= Y170), W195 (= W212), R196 (≠ N213)
- binding nicotinamide-adenine-dinucleotide: G9 (= G28), S12 (≠ Q31), G13 (= G32), N14 (≠ I33), D33 (= D52), L34 (≠ I53), A59 (= A77), D60 (= D78), V61 (= V79), N87 (≠ C105), A88 (= A106), G89 (= G107), I140 (= I155), P185 (= P200), G186 (= G201), M187 (≠ Y202), I188 (= I203), T190 (= T205), P191 (≠ Q206), M192 (≠ L207), T193 (≠ N208)
Q56840 2-(R)-hydroxypropyl-CoM dehydrogenase; R-HPCDH; 2-[(R)-2-hydroxypropylthio]ethanesulfonate dehydrogenase; Aliphatic epoxide carboxylation component III; Epoxide carboxylase component III; RHPCDH1; EC 1.1.1.268 from Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2) (see 4 papers)
35% identity, 92% coverage: 21:269/272 of query aligns to 2:250/250 of Q56840
- SGN 12:14 (≠ QGI 31:33) binding
- D33 (= D52) binding
- DV 60:61 (= DV 78:79) binding
- N87 (≠ C105) binding
- S142 (= S157) mutation to A: Retains weak activity. 120-fold decrease in kcat.; mutation to C: Loss of activity.
- R152 (≠ C167) binding ; mutation to A: Almost loss of activity with the natural substrate 2-KPC, but does not affect activity with 2-butanone as substrate.
- Y155 (= Y170) mutation Y->E,F: Loss of activity.
- K159 (= K174) mutation to A: Loss of activity.
- R179 (= R194) mutation to A: Loss of activity.
- IETPM 188:192 (≠ IETQL 203:207) binding
- WR 195:196 (≠ WN 212:213) binding
- R196 (≠ N213) mutation to A: Almost loss of activity with the natural substrate 2-KPC, but does not affect activity with 2-butanone as substrate.
- R203 (= R222) mutation to A: Slight decrease in catalytic efficiency.
- R209 (≠ L228) mutation to A: Does not affect catalytic efficiency.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
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)
36% identity, 92% coverage: 18:267/272 of query aligns to 2:242/251 of H9XP47
- N15 (≠ Q31) binding
- M17 (≠ I33) binding
- D36 (= D52) binding
- D60 (= D78) binding
- V61 (= V79) binding
- N87 (≠ C105) binding
- S138 (= S157) binding ; binding
- V139 (≠ T158) mutation to Q: Retains 50% of activity with acetoin as substrate; when associated with A-247.
- S140 (≠ H159) binding
- Y151 (= Y170) binding ; binding ; binding
- K155 (= K174) binding
- V184 (≠ I203) binding
- T186 (= T205) binding
- RDK 197:199 (≠ RQR 222:224) 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.
Query Sequence
>Pf1N1B4_412 3-oxoacyl-[acyl-carrier protein] reductase (EC 1.1.1.100)
MAEPLSLPPVPEPPKGERLKNKVVLLTGAAQGIGEAIVATFASQQARLVISDIQGEKVEK
VAAHWREQGADVVAIKADVSRQQDLHAMARLAIELHGRIDVLVNCAGVNVFRDPLQMTEE
DWHRCFAIDLDGAWYGCKAVLPQMIEQGIGSIINIASTHSTHIIPGCFPYPVAKHGLLGL
TRALGIEYAPKGIRVNAIAPGYIETQLNVDYWNGFADPHAERQRAFDLHPPRRIGQPIEV
AMTAVFLASDEAPFINASCITIDGGRSVMYHD
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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