SitesBLAST
Comparing Pf6N2E2_1840 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_1840 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)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
38% identity, 96% coverage: 11:270/270 of query aligns to 3:257/257 of 6slbAAA
- active site: Q64 (≠ G72), F69 (= F77), L80 (≠ A91), N84 (≠ Q96), A108 (≠ G120), S111 (≠ G124), A130 (≠ G143), F131 (≠ A144), L136 (≠ M149), P138 (= P151), D139 (= D152), A224 (≠ P237), G234 (≠ C247)
- binding (~{E})-6-[2-[3-[[(2~{R})-4-[[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-4-oxidanyl-3-phosphonooxy-oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxy-3,3-dimethyl-2-oxidanyl-butanoyl]amino]propanoylamino]ethylsulfanyl]-6-oxidanylidene-hex-3-enoic acid: R58 (≠ A66), A62 (= A70), Q64 (≠ G72), D65 (= D73), L66 (≠ V74), Y76 (= Y87), A108 (≠ G120), F131 (≠ A144), D139 (= D152)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
37% identity, 91% coverage: 24:270/270 of query aligns to 13:245/245 of 6slaAAA
- active site: Q61 (≠ G72), L68 (= L84), N72 (≠ I88), A96 (≠ G120), S99 (≠ G124), A118 (≠ G143), F119 (≠ A144), L124 (≠ M149), P126 (= P151), N127 (≠ D152), A212 (≠ P237), G222 (≠ C247)
- binding ~{S}-[2-[3-[[(2~{R})-4-[[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-4-oxidanyl-3-phosphonooxy-oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxy-3,3-dimethyl-2-oxidanyl-butanoyl]amino]propanoylamino]ethyl] 2-(2,5-dihydrooxepin-7-yl)ethanethioate: L21 (≠ A32), A59 (= A70), Q61 (≠ G72), D62 (= D73), L63 (≠ V74), L68 (= L84), Y71 (= Y87), A94 (= A118), G95 (= G119), A96 (≠ G120), F119 (≠ A144), I122 (≠ V147), L124 (≠ M149), N127 (≠ D152), F234 (≠ V259), K237 (= K262)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
29% identity, 94% coverage: 18:270/270 of query aligns to 11:259/259 of 5zaiC
- active site: A65 (≠ G72), F70 (= F77), S82 (≠ T92), R86 (≠ Q96), G110 (= G120), E113 (≠ G124), P132 (≠ G143), E133 (≠ A144), I138 (≠ M149), P140 (= P151), G141 (≠ D152), A226 (≠ P237), F236 (≠ C247)
- binding coenzyme a: K24 (≠ A31), L25 (≠ A32), A63 (= A70), G64 (= G71), A65 (≠ G72), D66 (= D73), I67 (≠ V74), P132 (≠ G143), R166 (≠ V177), F248 (≠ V259), K251 (= K262)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
33% identity, 88% coverage: 33:270/270 of query aligns to 27:261/261 of 5jbxB
- active site: A67 (≠ G72), R72 (≠ K80), L84 (≠ T92), R88 (≠ Q96), G112 (= G121), E115 (≠ G124), T134 (≠ G143), E135 (≠ A144), I140 (≠ M149), P142 (= P151), G143 (≠ D152), A228 (≠ P237), L238 (≠ C247)
- binding coenzyme a: A28 (≠ G34), A65 (= A70), D68 (= D73), L69 (≠ V74), K70 (≠ H75), L110 (≠ G119), G111 (= G120), T134 (≠ G143), E135 (≠ A144), L138 (≠ V147), R168 (≠ V177)
Sites not aligning to the query:
Q5HH38 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Staphylococcus aureus (strain COL) (see paper)
32% identity, 99% coverage: 3:268/270 of query aligns to 5:267/273 of Q5HH38
- R34 (≠ A32) binding in other chain
- SGGDQ 73:77 (≠ AGGDV 70:74) binding in other chain
- S149 (≠ A150) binding in other chain
1jxzB Structure of the h90q mutant of 4-chlorobenzoyl-coenzyme a dehalogenase complexed with 4-hydroxybenzoyl-coenzyme a (product) (see paper)
33% identity, 73% coverage: 21:217/270 of query aligns to 13:209/269 of 1jxzB
- active site: C61 (= C69), F64 (≠ G72), I69 (≠ F77), A86 (≠ T92), Q90 (= Q96), G113 (= G119), G114 (= G120), G117 (= G124), A136 (≠ G143), W137 (≠ A144), I142 (≠ M149), N144 (≠ P151), D145 (= D152)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ D30), H23 (≠ A31), R24 (≠ A32), A62 (= A70), F64 (≠ G72), Y65 (≠ D73), L66 (≠ V74), R67 (≠ H75), W89 (≠ L95), G113 (= G119), A136 (≠ G143), W137 (≠ A144), I142 (≠ M149), D145 (= D152), T146 (≠ A153)
- binding calcium ion: G49 (≠ R57), L202 (≠ M209), A203 (≠ T210), A205 (= A213), T207 (≠ L215)
Sites not aligning to the query:
2uzfA Crystal structure of staphylococcus aureus 1,4-dihydroxy-2-naphthoyl coa synthase (menb) in complex with acetoacetyl coa (see paper)
32% identity, 95% coverage: 13:268/270 of query aligns to 10:254/260 of 2uzfA
- active site: G70 (= G72), R80 (= R89), L84 (≠ V93), G108 (= G120), V111 (vs. gap), T130 (≠ G143), G131 (≠ A144), S136 (≠ A150), D138 (= D152), A139 (= A153), A225 (≠ S240), Y233 (≠ R248)
- binding acetoacetyl-coenzyme a: V28 (≠ A31), R29 (≠ A32), S68 (≠ A70), G69 (= G71), G70 (= G72), D71 (= D73), Y104 (≠ F116), G108 (= G120)
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
31% identity, 95% coverage: 14:270/270 of query aligns to 11:266/266 of O53561
- K135 (= K139) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 139:146, 25% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (≠ R146) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
Q8GYN9 1,4-dihydroxy-2-naphthoyl-CoA synthase, peroxisomal; DHNS; Enoyl-CoA hydratase/isomerase D; ECHID; Naphthoate synthase; EC 4.1.3.36 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
33% identity, 93% coverage: 16:267/270 of query aligns to 82:330/337 of Q8GYN9
Sites not aligning to the query:
- 20 H→V: Loss of peroxisomal targeting.
1nzyB 4-chlorobenzoyl coenzyme a dehalogenase from pseudomonas sp. Strain cbs-3 (see paper)
32% identity, 73% coverage: 21:217/270 of query aligns to 13:209/269 of 1nzyB
- active site: C61 (= C69), F64 (≠ G72), I69 (≠ F77), A86 (≠ T92), H90 (≠ Q96), G114 (= G120), G117 (= G124), A136 (≠ G143), W137 (≠ A144), I142 (≠ M149), N144 (≠ P151), D145 (= D152)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ D30), H23 (≠ A31), R24 (≠ A32), A62 (= A70), F64 (≠ G72), Y65 (≠ D73), L66 (≠ V74), R67 (≠ H75), W89 (≠ L95), G113 (= G119), G114 (= G120), A136 (≠ G143), W137 (≠ A144), D145 (= D152), T146 (≠ A153)
- binding calcium ion: G49 (≠ R57), L202 (≠ M209), A203 (≠ T210), A205 (= A213), T207 (≠ L215)
- binding phosphate ion: E57 (≠ G65), N108 (≠ Q114), K188 (≠ D195), R192 (≠ Q199)
Sites not aligning to the query:
A5JTM5 4-chlorobenzoyl coenzyme A dehalogenase; 4-CBA-CoA dehalogenase; 4-CBCoA dehalogenase; 4-chlorobenzoyl-CoA dehalogenase; EC 3.8.1.7 from Pseudomonas sp. (strain CBS-3) (see 7 papers)
32% identity, 73% coverage: 21:217/270 of query aligns to 13:209/269 of A5JTM5
- R24 (≠ A32) binding in other chain; mutation R->K,L: Does not strongly affect catalytic activity, but reduces substrate CoA binding.
- E34 (≠ D42) mutation to T: Forms inclusion bodies.
- E43 (≠ H51) mutation to A: No effect on catalytic activity.
- D45 (≠ E53) mutation to A: No effect on catalytic activity.
- D46 (≠ R54) mutation to A: No effect on catalytic activity.
- G63 (= G71) mutation G->A,I,P: Yields insoluble protein.
- F64 (≠ G72) mutation to A: 30-fold reduction in catalytic activity, substrate benzoyl group binding is unaffected.; mutation to L: Retains catalytic activity, but substrate benzoyl group binding is decreased.; mutation to P: Severely reduces catalytic activity. Arylated intermediate does not accumulate.
- Y65 (≠ D73) mutation to D: Catalytic activity is almost as efficient as wild type.
- R67 (≠ H75) mutation to K: Reduces substrate CoA binding.; mutation to L: Forms inclusion bodies.
- E68 (≠ T76) mutation to T: No effect on catalytic activity.
- H81 (≠ Y87) mutation to Q: Loss of catalytic activity, substrate benzoyl group binding is not affected.
- F82 (≠ I88) mutation to L: Retains catalytic activity, but substrate benzoyl group binding is decreased.
- W89 (≠ L95) mutation to F: Retains catalytic activity, but substrate benzoyl group binding is decreased.; mutation to Y: Reduced activity and substrate benzoyl group binding.
- H90 (≠ Q96) active site, Proton acceptor; mutation to Q: Complete loss of catalytic activity (PubMed:8718880, PubMed:9063883). Significantly reduced activity (PubMed:11695894). Substrate binding is not significantly affected. Reduced arylated intermediate formation.
- H94 (≠ S100) mutation to Q: No effect on catalytic activity.
- A112 (= A118) mutation to G: Yields insoluble protein.; mutation to S: Protein precipitates upon purification.; mutation to V: Catalytic activity is almost as efficient as wild type.
- G113 (= G119) mutation to A: Strongly reduced catalytic activity and substrate benzoyl group binding. Arylated intermediate does not accumulate.; mutation G->N,S: Strongly reduced catalytic activity. Arylated intermediate does not accumulate.; mutation to V: Protein precipitates upon purification.
- G114 (= G120) mutation to A: Strongly reduced catalytic activity and substrate benzoyl group binding.; mutation to P: Unstable.
- G115 (= G121) mutation G->L,N,S,V: Yields insoluble protein.
- D123 (= D130) mutation to T: No effect on catalytic activity.
- D129 (≠ E136) mutation to T: No effect on catalytic activity.
- W137 (≠ A144) mutation to F: Low catalytic activity, but KM unaffected (PubMed:8718880). Retains catalytic activity, but substrate benzoyl group binding is decreased (PubMed:9063883).
- D145 (= D152) active site, Nucleophile; mutation to A: Complete loss of catalytic activity, but not substrate binding.
- E163 (= E170) mutation to T: No effect on catalytic activity.
- E175 (= E182) mutation to D: No effect on catalytic activity.
- W179 (≠ M186) mutation to F: No effect on catalytic activity.
- H208 (≠ A216) mutation to Q: No effect on catalytic activity.
Sites not aligning to the query:
- 216 mutation R->E,K,L: Yields insoluble protein.
- 232 mutation E->A,N,Q,R: Yields insoluble protein.; E→D: Reduced catalytic activity, increased substrate binding.
- 257 R→K: Retains catalytic activity and substrate CoA binding.; R→L: Significantly reduces catalytic activity and substrate CoA binding.
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
29% identity, 93% coverage: 18:268/270 of query aligns to 14:256/258 of 1mj3A
- active site: A68 (≠ G72), M73 (≠ F77), S83 (= S100), L85 (≠ M102), G109 (= G120), E112 (≠ G122), P131 (≠ G143), E132 (≠ A144), T137 (≠ M149), P139 (= P151), G140 (≠ D152), K225 (≠ P237), F235 (≠ C247)
- binding hexanoyl-coenzyme a: K26 (≠ D30), A27 (= A31), L28 (≠ A32), A30 (≠ G34), A66 (= A70), G67 (= G71), A68 (≠ G72), D69 (= D73), I70 (≠ V74), G109 (= G120), P131 (≠ G143), E132 (≠ A144), L135 (≠ V147), G140 (≠ D152)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
30% identity, 94% coverage: 13:267/270 of query aligns to 5:249/250 of 3q0gD
- active site: A64 (≠ G72), M69 (≠ F77), T75 (= T92), F79 (≠ Q96), G103 (= G120), E106 (≠ G122), P125 (≠ G143), E126 (≠ A144), V131 (≠ M149), P133 (= P151), G134 (≠ D152), L219 (≠ P237), F229 (≠ C247)
- binding Butyryl Coenzyme A: F225 (≠ V243), F241 (≠ V259)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
30% identity, 93% coverage: 18:268/270 of query aligns to 12:256/258 of 1ey3A
- active site: A66 (≠ G72), M71 (≠ L84), S81 (≠ L95), L85 (≠ I99), G109 (= G120), E112 (≠ G122), P131 (≠ G143), E132 (≠ A144), T137 (≠ M149), P139 (= P151), G140 (≠ D152), K225 (≠ P237), F235 (≠ C247)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ D30), L26 (≠ A32), A28 (≠ G34), A64 (= A70), G65 (= G71), A66 (≠ G72), D67 (= D73), I68 (≠ V74), L85 (≠ I99), W88 (≠ M102), G109 (= G120), P131 (≠ G143), L135 (≠ V147), G140 (≠ D152)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
30% identity, 93% coverage: 18:268/270 of query aligns to 14:258/260 of 1dubA
- active site: A68 (≠ G72), M73 (≠ L84), S83 (≠ L95), L87 (≠ I99), G111 (= G120), E114 (≠ G122), P133 (≠ G143), E134 (≠ A144), T139 (≠ M149), P141 (= P151), G142 (≠ D152), K227 (≠ P237), F237 (≠ C247)
- binding acetoacetyl-coenzyme a: K26 (≠ D30), A27 (= A31), L28 (≠ A32), A30 (≠ G34), A66 (= A70), A68 (≠ G72), D69 (= D73), I70 (≠ V74), Y107 (≠ F116), G110 (= G119), G111 (= G120), E114 (≠ G122), P133 (≠ G143), E134 (≠ A144), L137 (≠ V147), G142 (≠ D152), F233 (≠ V243), F249 (≠ V259)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
30% identity, 94% coverage: 13:267/270 of query aligns to 6:254/255 of 3q0jC
- active site: A65 (≠ G72), M70 (≠ L84), T80 (= T92), F84 (≠ Q96), G108 (= G120), E111 (≠ G122), P130 (≠ G143), E131 (≠ A144), V136 (≠ M149), P138 (= P151), G139 (≠ D152), L224 (≠ P237), F234 (≠ C247)
- binding acetoacetyl-coenzyme a: Q23 (≠ D30), A24 (= A31), L25 (≠ A32), A27 (≠ G34), A63 (= A70), G64 (= G71), A65 (≠ G72), D66 (= D73), I67 (≠ V74), K68 (≠ H75), M70 (≠ L84), F84 (≠ Q96), G107 (= G119), G108 (= G120), E111 (≠ G122), P130 (≠ G143), E131 (≠ A144), P138 (= P151), G139 (≠ D152), M140 (≠ A153)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
30% identity, 94% coverage: 13:267/270 of query aligns to 6:254/255 of 3q0gC
- active site: A65 (≠ G72), M70 (≠ L84), T80 (= T92), F84 (≠ Q96), G108 (= G120), E111 (≠ G122), P130 (≠ G143), E131 (≠ A144), V136 (≠ M149), P138 (= P151), G139 (≠ D152), L224 (≠ P237), F234 (≠ C247)
- binding coenzyme a: L25 (≠ A32), A63 (= A70), I67 (≠ V74), K68 (≠ H75), Y104 (≠ F116), P130 (≠ G143), E131 (≠ A144), L134 (≠ V147)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
30% identity, 94% coverage: 13:267/270 of query aligns to 5:253/256 of 3h81A
- active site: A64 (≠ G72), M69 (≠ L84), T79 (= T92), F83 (≠ Q96), G107 (= G120), E110 (≠ G122), P129 (≠ G143), E130 (≠ A144), V135 (≠ M149), P137 (= P151), G138 (≠ D152), L223 (≠ P237), F233 (≠ C247)
- binding calcium ion: F233 (≠ C247), Q238 (≠ V252)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
28% identity, 94% coverage: 18:270/270 of query aligns to 14:260/260 of 2hw5C
- active site: A68 (≠ G72), M73 (≠ F77), S83 (≠ L95), L87 (≠ I99), G111 (= G120), E114 (≠ G122), P133 (≠ G143), E134 (≠ A144), T139 (≠ M149), P141 (= P151), G142 (≠ D152), K227 (≠ P237), F237 (≠ C247)
- binding crotonyl coenzyme a: K26 (≠ D30), A27 (= A31), L28 (≠ A32), A30 (≠ G34), K62 (≠ A66), I70 (≠ V74), F109 (≠ A118)
P14604 Enoyl-CoA hydratase, mitochondrial; mECH; mECH1; Enoyl-CoA hydratase 1; ECHS1; Short-chain enoyl-CoA hydratase; SCEH; EC 4.2.1.17; EC 5.3.3.8 from Rattus norvegicus (Rat) (see 3 papers)
30% identity, 93% coverage: 18:268/270 of query aligns to 44:288/290 of P14604
- E144 (≠ G122) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (≠ A144) mutation to D: Reduces activity 1250-fold.; mutation to Q: Reduces activity 330000-fold.
Sites not aligning to the query:
- 1:29 modified: transit peptide, Mitochondrion
Query Sequence
>Pf6N2E2_1840 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_1840
MSQPELLITSGFVLLSLHGSVAHLHLNRPDAANGLDIPTLQDLIAALMRCHGERRVRVVL
LTGAGANFCAGGDVHTFVGKGDELPEYIRQATVYLQAVISAMIHLDAPVIAAVQGFAAGG
GGMGLVCAADVVIAGESAKFLAGATRVAMAPDAGLSVTLPRLVGPRKATEMLLMNPVVKA
PEALAMGLINQVVADAELQTTAMAYAQQMTEAAPLALAATKRLLWAGIGLGVDAAMPEES
RTVAELCRTRDVREGLAAVIEKRTAQFEGQ
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