SitesBLAST
Comparing Ac3H11_1922 FitnessBrowser__acidovorax_3H11:Ac3H11_1922 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)
Q9BY49 Peroxisomal trans-2-enoyl-CoA reductase; TERP; 2,4-dienoyl-CoA reductase-related protein; DCR-RP; HPDHase; Short chain dehydrogenase/reductase family 29C member 1; pVI-ARL; EC 1.3.1.38 from Homo sapiens (Human) (see paper)
49% identity, 82% coverage: 10:261/309 of query aligns to 8:265/303 of Q9BY49
Sites not aligning to the query:
- 303 mutation Missing: Abolishes localization to peroxisomes.
1yxmB Crystal structure of peroxisomal trans 2-enoyl coa reductase
49% identity, 82% coverage: 10:261/309 of query aligns to 1:250/283 of 1yxmB
- active site: G22 (= G31), V152 (≠ A156), G157 (≠ S161), H163 (= H167), S164 (= S168), R168 (= R172)
- binding adenine: S42 (≠ G51), R43 (= R52), C72 (= C76), N73 (≠ D77), I74 (= I78), T123 (= T127)
4fc7A Studies on dcr shed new light on peroxisomal beta-oxidation: crystal structure of the ternary complex of pdcr (see paper)
34% identity, 82% coverage: 8:259/309 of query aligns to 13:266/274 of 4fc7A
- active site: G36 (= G31), A162 (= A156), Q172 (≠ G166), H174 (= H167), A175 (≠ S168), K179 (≠ R172)
- binding coenzyme a: R57 (= R52), R85 (= R79), G113 (= G107), N114 (≠ Q108), F115 (= F109), S123 (= S117), N125 (≠ K119), A126 (≠ G120), T129 (≠ A123), R216 (≠ N208)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G32 (= G27), S35 (= S30), G36 (= G31), I37 (= I32), S56 (≠ G51), R57 (= R52), S58 (≠ K53), R61 (≠ K56), D83 (= D77), V84 (≠ I78), R85 (= R79), C110 (≠ N104), A111 (= A105), A112 (≠ G106), I160 (= I154), K179 (≠ R172), P205 (= P198), G206 (= G199), T211 (≠ S203), E212 (≠ S204), G213 (= G205)
Q9NUI1 Peroxisomal 2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing]; pDCR; 2,4-dienoyl-CoA reductase 2; Short chain dehydrogenase/reductase family 17C member 1; EC 1.3.1.124 from Homo sapiens (Human) (see paper)
34% identity, 82% coverage: 8:259/309 of query aligns to 16:269/292 of Q9NUI1
- GGGSGI 35:40 (= GGGSGI 27:32) binding NADP(+)
- RSLPR 60:64 (≠ RKPEK 52:56) binding NADP(+)
- D86 (= D77) binding NADP(+); mutation to A: Reduces enzyme activity by 98%.
- D137 (≠ N128) mutation to A: Reduces enzyme activity by 97%.
- K182 (≠ R172) binding NADP(+)
- D186 (≠ V176) mutation to A: Reduces enzyme activity by about 95%.
- 208:214 (vs. 198:203, 43% identical) binding NADP(+)
- D268 (= D258) mutation to A: Reduces enzyme activity by 97%.
4fc6B Studies on dcr shed new light on peroxisomal beta-oxidation: crystal structure of the ternary complex of pdcr (see paper)
34% identity, 82% coverage: 8:259/309 of query aligns to 14:267/276 of 4fc6B
- active site: G37 (= G31), A163 (= A156), Q173 (≠ G166), H175 (= H167), A176 (≠ S168), K180 (≠ R172)
- binding hexanoyl-coenzyme a: G114 (= G107), N115 (≠ Q108), F116 (= F109), S124 (= S117), N126 (≠ K119), A127 (≠ G120), T130 (≠ A123), L165 (≠ M158), R217 (≠ N208)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G33 (= G27), S36 (= S30), G37 (= G31), I38 (= I32), S57 (≠ G51), R58 (= R52), S59 (≠ K53), R62 (≠ K56), M83 (vs. gap), D84 (= D77), V85 (≠ I78), C111 (≠ N104), A112 (= A105), A113 (≠ G106), I134 (≠ T127), I161 (= I154), K180 (≠ R172), P206 (= P198), G207 (= G199), T212 (≠ S203), E213 (≠ S204), G214 (= G205)
4jroC Crystal structure of 3-oxoacyl-[acyl-carrier protein]reductase (fabg) from listeria monocytogenes in complex with NADP+
36% identity, 78% coverage: 18:259/309 of query aligns to 3:243/247 of 4jroC
- active site: G16 (= G31), S142 (vs. gap), Q152 (≠ M165), Y155 (≠ S168), K159 (≠ R172)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G27), S14 (≠ G29), R15 (≠ S30), G16 (= G31), I17 (= I32), N35 (vs. gap), Y36 (≠ V50), N37 (≠ G51), G38 (≠ R52), S39 (≠ K53), N63 (≠ D77), V64 (≠ I78), N90 (= N104), A91 (= A105), I93 (≠ G107), I113 (≠ T127), S142 (vs. gap), Y155 (≠ S168), K159 (≠ R172), P185 (= P198), I188 (= I201), T190 (≠ S203)
1zemA Crystal structure of NAD+-bound xylitol dehydrogenase (see paper)
34% identity, 78% coverage: 18:259/309 of query aligns to 3:259/260 of 1zemA
- active site: N16 (≠ G31), S142 (≠ D157), Y155 (≠ S168), K159 (≠ R172), D212 (≠ E212)
- binding nicotinamide-adenine-dinucleotide: G12 (= G27), G15 (≠ S30), N16 (≠ G31), I17 (= I32), D36 (≠ G51), M37 (≠ R52), D62 (= D77), V63 (≠ I78), N89 (= N104), A90 (= A105), G91 (= G106), T140 (≠ V155), S142 (≠ D157), Y155 (≠ S168), K159 (≠ R172), P185 (= P198), M188 (≠ I201)
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)
34% identity, 79% coverage: 18:261/309 of query aligns to 3:243/248 of Q9KJF1
- S15 (= S30) binding NAD(+)
- D36 (≠ G51) binding NAD(+)
- D62 (= D77) binding NAD(+)
- I63 (= I78) binding NAD(+)
- N89 (= N104) binding NAD(+)
- Y153 (≠ S168) binding NAD(+)
- K157 (≠ R172) binding NAD(+)
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
7pcsB Structure of the heterotetrameric sdr family member bbscd (see paper)
34% identity, 79% coverage: 18:261/309 of query aligns to 2:242/247 of 7pcsB
- binding nicotinamide-adenine-dinucleotide: G11 (= G27), M16 (≠ I32), D35 (≠ G51), I36 (≠ R52), I62 (= I78), N88 (= N104), G90 (= G106), I138 (= I154), S140 (≠ A156), Y152 (≠ S168), K156 (≠ R172), I185 (= I201)
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)
39% identity, 77% coverage: 21:259/309 of query aligns to 7:242/247 of P73574
- A14 (≠ G28) mutation to G: 4.2-fold increase in activity on acetoacetyl-CoA.
- P151 (= P163) 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 (≠ R172) mutation to A: Almost no activity on acetoacetyl-CoA.
- F188 (≠ Y200) mutation to Y: 3.3-fold increase in activity on acetoacetyl-CoA.
- N198 (≠ P210) mutation to R: 3.5-fold increase in activity on acetoacetyl-CoA.
3osuA Crystal structure of the 3-oxoacyl-acyl carrier protein reductase, fabg, from staphylococcus aureus
36% identity, 76% coverage: 24:259/309 of query aligns to 8:242/246 of 3osuA
3ay6B Crystal structure of bacillus megaterium glucose dehydrogenase 4 a258f mutant in complex with nadh and d-glucose (see paper)
35% identity, 78% coverage: 18:259/309 of query aligns to 11:254/267 of 3ay6B
- active site: G24 (= G31), S151 (vs. gap), Y164 (≠ S168), K168 (≠ R172)
- binding beta-D-glucopyranose: E102 (≠ Q108), S151 (vs. gap), H153 (≠ A156), W158 (= W159), Y164 (≠ S168), N202 (≠ E212), K205 (≠ D215)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G20 (= G27), T23 (≠ S30), G24 (= G31), L25 (≠ I32), Y45 (≠ G51), D71 (= D77), V72 (≠ I78), N98 (= N104), A99 (= A105), G100 (= G106), V101 (≠ G107), M149 (≠ I154), S151 (vs. gap), Y164 (≠ S168), K168 (≠ R172), P194 (= P198), G195 (= G199), M197 (≠ I201), T199 (≠ Y209), P200 (= P210), I201 (≠ P211), N202 (≠ E212)
7ucwB Structure of mouse decr1 in complex with 2'-5' oligoadenylate (see paper)
32% identity, 81% coverage: 9:259/309 of query aligns to 10:256/281 of 7ucwB
- binding [[(2R,3R,4R,5R)-5-(6-aminopurin-9-yl)-4-[[(2R,3R,4R,5R)-5-(6-aminopurin-9-yl)-4-[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxy-oxolan-2-yl]methoxy-hydroxy-phosphoryl]oxy-3-hydroxy-oxolan-2-yl]methoxy-hydroxy-phosphoryl]oxy-3-hydroxy-oxolan-2-yl]methoxy-hydroxy-phosphoryl] phosphono hydrogen phosphate: G32 (= G27), T35 (≠ S30), S56 (≠ G51), R57 (= R52), N58 (≠ K53), D83 (= D77), V84 (≠ I78), A111 (= A105), A112 (≠ G106), I133 (≠ T127)
3sj7A Structure of beta-ketoacetyl-coa reductase (fabg) from staphylococcus aureus complex with NADPH (see paper)
35% identity, 76% coverage: 24:259/309 of query aligns to 5:235/239 of 3sj7A
- active site: G12 (= G31), S138 (≠ D157), Q148 (≠ M165), Y151 (≠ S168), K155 (≠ R172)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G27), S10 (≠ G29), R11 (≠ S30), I13 (= I32), N31 (vs. gap), Y32 (vs. gap), A33 (≠ V50), G34 (= G51), S35 (≠ R52), A58 (≠ C76), N59 (≠ D77), V60 (≠ I78), N86 (= N104), A87 (= A105), T109 (= T127), S138 (≠ D157), Y151 (≠ S168), K155 (≠ R172), P181 (= P198), G182 (= G199)
3uf0A Crystal structure of a putative NAD(p) dependent gluconate 5- dehydrogenase from beutenbergia cavernae(efi target efi-502044) with bound NADP (low occupancy)
38% identity, 79% coverage: 15:259/309 of query aligns to 2:244/249 of 3uf0A
- active site: G18 (= G31), S141 (≠ A156), V151 (≠ M165), Y154 (≠ S168), K158 (≠ R172)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G14 (= G27), S17 (= S30), G18 (= G31), I19 (= I32), R39 (= R52), D63 (= D77), L64 (≠ I78), N89 (= N104), G91 (= G106), I92 (≠ G107), I139 (= I154), A140 (≠ V155), S141 (≠ A156), Y154 (≠ S168), K158 (≠ R172), P184 (= P198), G185 (= G199), V187 (≠ I201), T189 (≠ S203), N191 (= N208), T192 (≠ Y209)
P40288 Glucose 1-dehydrogenase; EC 1.1.1.47 from Priestia megaterium (Bacillus megaterium) (see 2 papers)
34% identity, 80% coverage: 18:263/309 of query aligns to 5:252/261 of P40288
- 11:35 (vs. 24:48, 40% identical) binding NADP(+)
- E96 (≠ Q108) mutation E->A,G,K: Heat stable.
- D108 (≠ G120) mutation to N: Heat stable.
- V112 (= V124) mutation to A: Heat stable.
- E133 (≠ A145) mutation to K: Heat stable.
- V183 (= V193) mutation to I: Heat stable.
- P194 (vs. gap) mutation to Q: Heat stable.
- E210 (≠ P221) mutation to K: Heat stable.
- Y217 (≠ R228) mutation to H: Heat stable.
- Q252 (= Q263) mutation to L: Heat stable.
Sites not aligning to the query:
- 253 Y→C: Heat stable.
- 258 A→G: Heat stable.
1edoA The x-ray structure of beta-keto acyl carrier protein reductase from brassica napus complexed with NADP+ (see paper)
36% identity, 77% coverage: 22:259/309 of query aligns to 3:240/244 of 1edoA
- active site: G12 (= G31), S138 (vs. gap), Y151 (≠ S168), K155 (≠ R172)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G27), S10 (≠ G29), R11 (≠ S30), I13 (= I32), N31 (vs. gap), Y32 (≠ V50), A33 (≠ G51), R34 (= R52), S35 (≠ K53), D59 (= D77), V60 (≠ I78), N86 (= N104), A87 (= A105), S138 (vs. gap), Y151 (≠ S168), K155 (≠ R172), P181 (= P198), G182 (= G199), I184 (= I201), S186 (= S203), M188 (≠ N208)
1g6kA Crystal structure of glucose dehydrogenase mutant e96a complexed with NAD+
34% identity, 80% coverage: 18:263/309 of query aligns to 5:252/261 of 1g6kA
- active site: G18 (= G31), S145 (≠ A156), Y158 (≠ S168), K162 (≠ R172)
- binding nicotinamide-adenine-dinucleotide: T17 (≠ S30), G18 (= G31), L19 (≠ I32), R39 (= R52), D65 (= D77), V66 (≠ I78), N92 (= N104), A93 (= A105), G94 (= G106), M143 (≠ I154), S145 (≠ A156), Y158 (≠ S168), P188 (= P198), G189 (= G199), I191 (= I201), T193 (vs. gap)
4dmmB 3-oxoacyl-[acyl-carrier-protein] reductase from synechococcus elongatus pcc 7942 in complex with NADP
37% identity, 78% coverage: 18:259/309 of query aligns to 3:235/240 of 4dmmB
- active site: G16 (= G31), S142 (≠ D157), Q152 (≠ M165), Y155 (≠ S168), K159 (≠ R172)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G27), S14 (≠ G29), R15 (≠ S30), G16 (= G31), I17 (= I32), A37 (≠ G51), S38 (≠ R52), S39 (≠ K53), A62 (≠ C76), D63 (= D77), V64 (≠ I78), N90 (= N104), A91 (= A105), L113 (≠ T127), I140 (= I154), S142 (≠ D157), Y155 (≠ S168), K159 (≠ R172), P185 (= P198), G186 (= G199), I188 (= I201), T190 (≠ S203), M192 (≠ L217)
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, 79% coverage: 18:261/309 of query aligns to 11:263/267 of Q9LBG2
- 17:42 (vs. 24:49, 58% identical) binding NAD(+)
- E103 (≠ Q108) mutation E->A,D,N,Q: 26-fold increase in Km and a much lower enantiomeric excess of the reaction products.
Query Sequence
>Ac3H11_1922 FitnessBrowser__acidovorax_3H11:Ac3H11_1922
MAPTARNAYQSVFAPGLFQGQVVVVTGGGSGIGRCTAHELAHLGAHVVLVGRKPEKLLAV
AEEITADGGRVSCQVCDIRSEEGVVALVQQIVAAQGRIDALVNNAGGQFMAPLESISAKG
WEAVLHTNLTGGFLMAREFYRQWMAQHGGSIVNIVADMWGSMPGMGHSGAARAGMVSLTE
TAALEWAHSGVRVNAVAPGYIASSGMDNYPPEAADMLRAMPRTVPLGRFGNEAEVSAAIT
FLLSPAASFISGTTLRVDGARPQVRMGWPQRPPGATAAAHPAVRPFDGFHRAQVPQVFAP
SHTPKTEAA
Or try a new SitesBLAST search
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