SitesBLAST
Comparing Ac3H11_2732 3-oxoacyl-[acyl-carrier protein] reductase (EC 1.1.1.100) 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)
4nbuB Crystal structure of fabg from bacillus sp (see paper)
38% identity, 90% coverage: 10:259/278 of query aligns to 1:243/244 of 4nbuB
- active site: G18 (= G27), N111 (= N127), S139 (= S155), Q149 (≠ R165), Y152 (= Y168), K156 (= K172)
- binding acetoacetyl-coenzyme a: D93 (≠ P103), K98 (= K108), S139 (= S155), N146 (≠ D162), V147 (≠ I163), Q149 (≠ R165), Y152 (= Y168), F184 (≠ L200), M189 (≠ G205), K200 (≠ V216)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G23), N17 (≠ S26), G18 (= G27), I19 (= I28), D38 (= D47), F39 (≠ V48), V59 (≠ F69), D60 (= D70), V61 (≠ A71), N87 (= N97), A88 (= A98), G89 (≠ A99), I90 (≠ L100), T137 (= T153), S139 (= S155), Y152 (= Y168), K156 (= K172), P182 (= P198), F184 (≠ L200), T185 (≠ V201), T187 (= T203), M189 (≠ G205)
6vspB Structure of serratia marcescens 2,3-butanediol dehydrogenase mutant q247a (see paper)
37% identity, 90% coverage: 12:262/278 of query aligns to 3:247/252 of 6vspB
6vspA Structure of serratia marcescens 2,3-butanediol dehydrogenase mutant q247a (see paper)
37% identity, 90% coverage: 12:262/278 of query aligns to 1:245/251 of 6vspA
- active site: G16 (= G27), S138 (= S155), Y151 (= Y168)
- binding nicotinamide-adenine-dinucleotide: G12 (= G23), N15 (≠ S26), G16 (= G27), M17 (≠ I28), D36 (= D47), W37 (≠ V48), W37 (≠ V48), A38 (≠ N49), I59 (≠ F69), D60 (= D70), V61 (≠ A71), N87 (= N97), A88 (= A98), G89 (≠ A99), V90 (≠ L100), V110 (= V126), T136 (= T153), S138 (= S155), Y151 (= Y168), K155 (= K172), P181 (= P198), S182 (≠ G199), L183 (= L200), V184 (= V201), T186 (= T203), N187 (≠ P204), M188 (≠ G205), T189 (= T206)
6xewA Structure of serratia marcescens 2,3-butanediol dehydrogenase (see paper)
37% identity, 90% coverage: 12:262/278 of query aligns to 1:245/251 of 6xewA
- active site: G16 (= G27), S138 (= S155), Y151 (= Y168)
- binding r,3-hydroxybutan-2-one: S138 (= S155), S140 (≠ G157), Y151 (= Y168)
- binding s,3-hydroxybutan-2-one: S138 (= S155), Y151 (= Y168), S182 (≠ G199)
- binding nicotinamide-adenine-dinucleotide: G12 (= G23), N15 (≠ S26), G16 (= G27), M17 (≠ I28), D36 (= D47), W37 (≠ V48), W37 (≠ V48), A38 (≠ N49), I59 (≠ F69), D60 (= D70), V61 (≠ A71), N87 (= N97), A88 (= A98), G89 (≠ A99), V110 (= V126), T136 (= T153), S138 (= S155), Y151 (= Y168), K155 (= K172), S182 (≠ G199), L183 (= L200), V184 (= V201), T186 (= T203), N187 (≠ P204), M188 (≠ G205), T189 (= T206)
4wecA Crystal structure of a short chain dehydrogenase from mycobacterium smegmatis
37% identity, 88% coverage: 13:258/278 of query aligns to 7:250/258 of 4wecA
- active site: G21 (= G27), S143 (= S155), Q154 (≠ R165), Y157 (= Y168), K161 (= K172)
- binding nicotinamide-adenine-dinucleotide: G17 (= G23), A19 (= A25), S20 (= S26), G21 (= G27), I22 (= I28), D41 (= D47), I42 (≠ V48), V61 (≠ F69), D62 (= D70), V63 (≠ A71), N89 (= N97), T141 (= T153), Y157 (= Y168), K161 (= K172), P187 (= P198), P189 (≠ L200), V190 (= V201)
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)
37% identity, 90% coverage: 13:262/278 of query aligns to 2:245/251 of H9XP47
- N15 (≠ S26) binding
- M17 (≠ I28) binding
- D36 (= D47) binding
- D60 (= D70) binding
- V61 (≠ A71) binding
- N87 (= N97) binding
- S138 (= S155) binding ; binding
- V139 (≠ T156) mutation to Q: Retains 50% of activity with acetoin as substrate; when associated with A-247.
- S140 (≠ G157) binding
- Y151 (= Y168) binding ; binding ; binding
- K155 (= K172) binding
- V184 (= V201) binding
- T186 (= T203) binding
- RDK 197:199 (≠ IDV 214:216) 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.
6ixmC Crystal structure of the ketone reductase chkred20 from the genome of chryseobacterium sp. Ca49 complexed with NAD (see paper)
35% identity, 90% coverage: 12:260/278 of query aligns to 1:247/248 of 6ixmC
- active site: G16 (= G27), S142 (= S155), Y155 (= Y168), K159 (= K172)
- binding nicotinamide-adenine-dinucleotide: G12 (= G23), S15 (= S26), G16 (= G27), I17 (= I28), D36 (= D47), I37 (≠ V48), A61 (≠ F69), D62 (= D70), T63 (≠ A71), N89 (= N97), A90 (= A98), M140 (≠ T153), S142 (= S155), Y155 (= Y168), K159 (= K172), P185 (= P198), A186 (≠ G199), Y187 (≠ L200), I188 (≠ V201), L192 (≠ G205)
Q9LBG2 Levodione reductase; (6R)-2,2,6-trimethyl-1,4-cyclohexanedione reductase; EC 1.1.1.- from Leifsonia aquatica (Corynebacterium aquaticum) (see paper)
37% identity, 89% coverage: 13:260/278 of query aligns to 10:265/267 of Q9LBG2
- 17:42 (vs. 20:45, 54% identical) binding
- E103 (≠ H106) 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)
37% identity, 89% coverage: 13:260/278 of query aligns to 1:256/258 of 1iy8A
- active site: G15 (= G27), S143 (= S155), Q153 (≠ R165), Y156 (= Y168), K160 (= K172)
- binding nicotinamide-adenine-dinucleotide: G11 (= G23), S14 (= S26), G15 (= G27), L16 (≠ I28), D35 (= D47), V36 (= V48), A62 (≠ F69), D63 (= D70), V64 (≠ A71), N90 (= N97), G92 (≠ A99), I93 (= I105), T141 (= T153), S143 (= S155), Y156 (= Y168), K160 (= K172), P186 (= P198), G187 (= G199), T191 (= T203), P192 (= P204), M193 (vs. gap)
4fn4A Short-chain NAD(h)-dependent dehydrogenase/reductase from sulfolobus acidocaldarius (see paper)
36% identity, 88% coverage: 14:258/278 of query aligns to 5:251/254 of 4fn4A
- active site: G18 (= G27), S144 (= S155), Y157 (= Y168), K161 (= K172), S202 (≠ V213)
- binding nicotinamide-adenine-dinucleotide: G14 (= G23), S17 (= S26), G18 (= G27), I19 (= I28), E38 (≠ D47), L39 (≠ V48), R43 (= R52), A63 (≠ F69), D64 (= D70), V65 (≠ A71), N91 (= N97), G93 (≠ A99), I94 (≠ L100), T142 (= T153), S144 (= S155), Y157 (= Y168), K161 (= K172), P187 (= P198), V190 (= V201), T192 (= T203), N193 (≠ P204), I194 (≠ G205)
4nbtA Crystal structure of fabg from acholeplasma laidlawii (see paper)
32% identity, 88% coverage: 13:258/278 of query aligns to 2:237/239 of 4nbtA
- active site: G16 (= G27), S132 (= S155), Y145 (= Y168), K149 (= K172)
- binding nicotinamide-adenine-dinucleotide: G12 (= G23), K15 (≠ S26), G16 (= G27), L17 (≠ I28), D36 (= D47), L37 (≠ V48), L52 (≠ F69), N53 (≠ D70), V54 (≠ A71), N80 (= N97), A81 (= A98), G82 (≠ A99), I130 (≠ T153), S132 (= S155), Y145 (= Y168), K149 (= K172), P177 (= P198), G178 (= G199), I180 (≠ V201), T182 (= T203)
4jroC Crystal structure of 3-oxoacyl-[acyl-carrier protein]reductase (fabg) from listeria monocytogenes in complex with NADP+
35% identity, 87% coverage: 17:259/278 of query aligns to 6:246/247 of 4jroC
- active site: G16 (= G27), S142 (= S155), Q152 (≠ R165), Y155 (= Y168), K159 (= K172)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G23), S14 (≠ A25), R15 (≠ S26), G16 (= G27), I17 (= I28), N35 (≠ D47), Y36 (≠ V48), N37 (= N49), G38 (vs. gap), S39 (vs. gap), N63 (≠ D70), V64 (≠ A71), N90 (= N97), A91 (= A98), I93 (≠ L100), I113 (≠ V126), S142 (= S155), Y155 (= Y168), K159 (= K172), P185 (= P198), I188 (≠ V201), T190 (= T203)
8cxaA Crystal structure of 3-oxoacyl-[acyl-carrier-protein] reductase from mycobacterium smegmatis with bound NAD
36% identity, 88% coverage: 13:258/278 of query aligns to 2:248/251 of 8cxaA
- binding nicotinamide-adenine-dinucleotide: G12 (= G23), Q15 (≠ S26), G16 (= G27), I17 (= I28), D36 (= D47), V63 (≠ A71), N89 (= N97), A91 (= A99), S94 (= S102), I142 (≠ T153), S143 (≠ A154), S144 (= S155), Y157 (= Y168), K161 (= K172), P187 (= P198), H188 (≠ G199), I190 (≠ V201), I194 (≠ G205)
Q5P5I4 (S)-1-Phenylethanol dehydrogenase; EC 1.1.1.311 from Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)) (see 2 papers)
36% identity, 90% coverage: 13:261/278 of query aligns to 4:249/249 of Q5P5I4
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2ewmB Crystal structure of the (s)-specific 1-phenylethanol dehydrogenase of the denitrifying bacterium strain ebn1 (see paper)
36% identity, 90% coverage: 13:261/278 of query aligns to 2:247/247 of 2ewmB
- active site: G16 (= G27), S139 (= S155), Y149 (≠ R165), Y152 (= Y168), K156 (= K172)
- binding nicotinamide-adenine-dinucleotide: G12 (= G23), N15 (≠ S26), G16 (= G27), I17 (= I28), D36 (= D47), L37 (vs. gap), C59 (≠ F69), D60 (= D70), V61 (≠ A71), N87 (= N97), S139 (= S155), Y152 (= Y168), K156 (= K172), P182 (= P198), S183 (≠ G199), L184 (= L200), V185 (= V201), T189 (≠ G205)
2cfcA Structural basis for stereo selectivity in the (r)- and (s)-hydroxypropylethane thiosulfonate dehydrogenases (see paper)
36% identity, 88% coverage: 17:260/278 of query aligns to 3:249/250 of 2cfcA
- active site: G13 (= G27), S142 (= S155), Y155 (= Y168), K159 (= K172)
- binding (2-[2-ketopropylthio]ethanesulfonate: F149 (≠ D162), R152 (= R165), Y155 (= Y168), W195 (vs. gap), R196 (= R207)
- binding nicotinamide-adenine-dinucleotide: G9 (= G23), S12 (= S26), G13 (= G27), N14 (≠ I28), D33 (= D47), L34 (≠ V48), A59 (vs. gap), D60 (= D70), V61 (≠ A71), N87 (= N97), A88 (= A98), G89 (≠ A99), I140 (≠ T153), P185 (= P198), G186 (= G199), M187 (≠ L200), I188 (≠ V201), T190 (= T203), P191 (= P204), M192 (≠ G205), T193 (= T206)
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)
36% identity, 88% coverage: 17:260/278 of query aligns to 3:249/250 of Q56840
- SGN 12:14 (≠ SGI 26:28) binding
- D33 (= D47) binding
- DV 60:61 (≠ DA 70:71) binding
- N87 (= N97) binding
- S142 (= S155) mutation to A: Retains weak activity. 120-fold decrease in kcat.; mutation to C: Loss of activity.
- R152 (= R165) 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 (= Y168) mutation Y->E,F: Loss of activity.
- K159 (= K172) mutation to A: Loss of activity.
- R179 (= R192) mutation to A: Loss of activity.
- IETPM 188:192 (≠ VLTPG 201:205) binding
- WR 195:196 (≠ -R 207) binding
- R196 (= R207) mutation to A: Almost loss of activity with the natural substrate 2-KPC, but does not affect activity with 2-butanone as substrate.
- R203 (≠ I214) mutation to A: Slight decrease in catalytic efficiency.
- R209 (≠ H220) mutation to A: Does not affect catalytic efficiency.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
3osuA Crystal structure of the 3-oxoacyl-acyl carrier protein reductase, fabg, from staphylococcus aureus
34% identity, 86% coverage: 19:258/278 of query aligns to 7:244/246 of 3osuA
4cqmA Crystal structure of heterotetrameric human ketoacyl reductase complexed with NAD and NADP (see paper)
34% identity, 89% coverage: 13:259/278 of query aligns to 3:247/248 of 4cqmA
- active site: G17 (= G27), S143 (= S155), Y156 (= Y168), K160 (= K172)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G23), S16 (= S26), G17 (= G27), I18 (= I28), D37 (= D47), L38 (≠ V48), A61 (vs. gap), V63 (≠ A71), C90 (≠ P103), A91 (= A104), G92 (≠ I105), I93 (≠ H106), V113 (= V126), I141 (≠ T153), S143 (= S155), Y156 (= Y168), K160 (= K172), P186 (= P198), G187 (= G199), I189 (≠ V201), T191 (= T203), P192 (= P204), M193 (≠ G205), T194 (= T206)
6f9qC Binary complex of a 7s-cis-cis-nepetalactol cyclase from nepeta mussinii with NAD+ (see paper)
36% identity, 89% coverage: 13:259/278 of query aligns to 5:255/260 of 6f9qC
- active site: G19 (= G27), Y159 (= Y168)
- binding nicotinamide-adenine-dinucleotide: G15 (= G23), S18 (= S26), G19 (= G27), I20 (= I28), D40 (= D47), I41 (≠ V48), Q42 (≠ N49), C63 (≠ F69), D64 (= D70), V65 (≠ A71), N91 (= N97), A92 (= A98), G93 (≠ A99), N144 (≠ T153), Y159 (= Y168), K163 (= K172), P189 (= P198), M190 (≠ G199), V192 (= V201), T194 (= T203), P195 (= P204), L196 (≠ G205), T197 (= T206)
Query Sequence
>Ac3H11_2732 3-oxoacyl-[acyl-carrier protein] reductase (EC 1.1.1.100)
MSKPALPGPHVGRFKDQVAIVTGGASGIGEATCRRLVAEGATVVVADVNAERAAALASEL
GPRASAQVFDAADVRSIERLVQGTVERFGRLDVLHNNAALSSPAIHAKDKNAIDIEFEVW
DQVMAVNLRGYLAGCKYALPTMIAQGGGAIVNTASTGGFSGDITRMAYSVSKAAIIGLTR
QIATHHGAQGVRCNAVAPGLVLTPGTRGAAASVIDVMQRHLLVPEFGEPEDIAALVCFLA
SGEARYINGQTYIADGGMLAHNPTMADLVDMAKSRKSS
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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