SitesBLAST
Comparing Pf1N1B4_4790 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_4790 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)
3bptA Crystal structure of human beta-hydroxyisobutyryl-coa hydrolase in complex with quercetin
36% identity, 98% coverage: 7:354/356 of query aligns to 6:351/362 of 3bptA
- active site: G67 (= G68), P84 (≠ E85), R88 (≠ V89), G115 (= G116), G118 (= G119), E138 (= E139), D146 (= D147)
- binding (2r)-3-hydroxy-2-methylpropanoic acid: G66 (= G67), G67 (= G68), I69 (= I70), F87 (= F88), E90 (= E91), G114 (= G115), G115 (= G116), E138 (= E139), L143 (≠ Y144), D146 (= D147), V147 (= V148)
- binding 3,5,7,3',4'-pentahydroxyflavone: F25 (≠ G26), L26 (= L27), A28 (= A29), A65 (= A66), G66 (= G67), G67 (= G68), I69 (= I70), P137 (= P138), E138 (= E139), I141 (= I142), V318 (≠ L321), L319 (= L322)
4hdtA Crystal structure of a carnitinyl-coa dehydratase from mycobacterium thermoresistibile (see paper)
38% identity, 98% coverage: 5:353/356 of query aligns to 1:333/340 of 4hdtA
- active site: G64 (= G68), I69 (≠ L73), W84 (≠ F88), Y88 (= Y92), G112 (= G116), G115 (= G119), E135 (= E139), P142 (= P146), D143 (= D147), R283 (≠ A299)
- binding zinc ion: H28 (≠ L32), E42 (≠ A46), E57 (= E61), E79 (≠ L83), H93 (≠ A97), H185 (≠ S189)
Sites not aligning to the query:
Q9LKJ1 3-hydroxyisobutyryl-CoA hydrolase 1; CoA-thioester hydrolase CHY1; EC 3.1.2.-; EC 3.1.2.4 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
34% identity, 97% coverage: 3:348/356 of query aligns to 6:353/378 of Q9LKJ1
- G70 (= G68) mutation to S: Loss of activity.
- E142 (= E139) mutation to A: Loss of activity.
- D150 (= D147) mutation to G: Reduced activity.
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
35% identity, 49% coverage: 8:182/356 of query aligns to 6:178/260 of 2hw5C
- active site: A68 (≠ G68), M73 (vs. gap), S83 (≠ K78), L87 (≠ T82), G111 (= G116), E114 (≠ G119), P133 (= P138), E134 (= E139), T139 (≠ Y144), P141 (= P146), G142 (≠ D147)
- binding crotonyl coenzyme a: K26 (≠ A25), A27 (≠ G26), L28 (= L27), A30 (= A29), K62 (= K62), A66 (= A66), A68 (≠ G68), D69 (= D69), I70 (= I70), K71 (≠ R71), Y107 (≠ F112), F109 (≠ L114)
Sites not aligning to the query:
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)
35% identity, 47% coverage: 14:182/356 of query aligns to 45:208/290 of P14604
- E144 (≠ G119) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E139) 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
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
35% identity, 48% coverage: 13:182/356 of query aligns to 12:176/258 of 1ey3A
- active site: A66 (≠ G68), M71 (vs. gap), S81 (≠ K78), L85 (≠ T82), G109 (= G116), E112 (≠ G119), P131 (= P138), E132 (= E139), T137 (≠ Y144), P139 (= P146), G140 (≠ D147)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ A25), A25 (≠ G26), L26 (= L27), A28 (= A29), A64 (= A66), G65 (= G67), A66 (≠ G68), D67 (= D69), I68 (= I70), K69 (vs. gap), L85 (≠ T82), W88 (≠ E85), Y105 (≠ F112), L107 (= L114), G108 (= G115), G109 (= G116), P131 (= P138), E132 (= E139), L135 (≠ I142), G140 (≠ D147), A141 (≠ V148), R165 (≠ Q171)
Sites not aligning to the query:
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
35% identity, 48% coverage: 13:182/356 of query aligns to 14:178/260 of 1dubA
- active site: A68 (≠ G68), M73 (vs. gap), S83 (≠ K78), L87 (≠ T82), G111 (= G116), E114 (≠ G119), P133 (= P138), E134 (= E139), T139 (≠ Y144), P141 (= P146), G142 (≠ D147)
- binding acetoacetyl-coenzyme a: K26 (≠ A25), A27 (≠ G26), L28 (= L27), A30 (= A29), K62 (= K62), A66 (= A66), G67 (= G67), A68 (≠ G68), D69 (= D69), I70 (= I70), K71 (vs. gap), M73 (vs. gap), Y107 (≠ F112), L109 (= L114), G110 (= G115), G111 (= G116), E114 (≠ G119), P133 (= P138), E134 (= E139), L137 (≠ I142), G142 (≠ D147)
Sites not aligning to the query:
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
35% identity, 48% coverage: 13:182/356 of query aligns to 13:172/254 of 2dubA
- active site: A67 (≠ G68), M72 (≠ L73), S82 (≠ L83), G105 (= G116), E108 (≠ G119), P127 (= P138), E128 (= E139), T133 (≠ Y144), P135 (= P146), G136 (≠ D147)
- binding octanoyl-coenzyme a: K25 (≠ A25), A26 (≠ G26), L27 (= L27), A29 (= A29), K61 (= K62), A65 (= A66), G66 (= G67), A67 (≠ G68), D68 (= D69), I69 (= I70), K70 (≠ R71), Y101 (≠ F112), G104 (= G115), G105 (= G116), E108 (≠ G119), P127 (= P138), E128 (= E139), L131 (≠ I142), P135 (= P146), G136 (≠ D147), A137 (≠ V148)
Sites not aligning to the query:
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
35% identity, 48% coverage: 13:182/356 of query aligns to 14:176/258 of 1mj3A
- active site: A68 (≠ G68), M73 (≠ L73), S83 (≠ V89), L85 (≠ E91), G109 (= G116), E112 (≠ G119), P131 (= P138), E132 (= E139), T137 (≠ Y144), P139 (= P146), G140 (≠ D147)
- binding hexanoyl-coenzyme a: K26 (≠ A25), A27 (≠ G26), L28 (= L27), A30 (= A29), K62 (= K62), A66 (= A66), G67 (= G67), A68 (≠ G68), D69 (= D69), I70 (= I70), K71 (≠ R71), M73 (≠ L73), W88 (≠ L94), Y105 (≠ F112), L107 (= L114), G108 (= G115), G109 (= G116), E112 (≠ G119), P131 (= P138), E132 (= E139), L135 (≠ I142), G140 (≠ D147), A141 (≠ V148)
Sites not aligning to the query:
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
26% identity, 74% coverage: 19:280/356 of query aligns to 17:258/259 of 5zaiC
- active site: A65 (≠ G68), F70 (≠ Y74), S82 (≠ F88), R86 (≠ Y92), G110 (= G116), E113 (≠ G119), P132 (= P138), E133 (= E139), I138 (≠ Y144), P140 (= P146), G141 (≠ D147), A226 (vs. gap), F236 (≠ A258)
- binding coenzyme a: D23 (≠ A25), K24 (≠ G26), L25 (= L27), A27 (= A29), A63 (= A66), G64 (= G67), A65 (≠ G68), D66 (= D69), I67 (= I70), L108 (= L114), G109 (= G115), P132 (= P138), E133 (= E139), R166 (≠ Q171), F248 (≠ L270), K251 (≠ S273)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
29% identity, 62% coverage: 4:224/356 of query aligns to 1:210/256 of 3h81A
- active site: A64 (≠ G68), M69 (≠ L73), T79 (≠ H84), F83 (= F88), G107 (= G116), E110 (≠ G119), P129 (= P138), E130 (= E139), V135 (≠ Y144), P137 (= P146), G138 (≠ D147)
- binding calcium ion: R171 (≠ Y179), S172 (≠ C180)
Sites not aligning to the query:
3q0jA Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
29% identity, 62% coverage: 4:224/356 of query aligns to 2:211/255 of 3q0jA
- active site: A65 (≠ G68), M70 (≠ L73), T80 (≠ H84), F84 (= F88), G108 (= G116), E111 (≠ G119), P130 (= P138), E131 (= E139), V136 (≠ Y144), P138 (= P146), G139 (≠ D147)
Sites not aligning to the query:
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
29% identity, 62% coverage: 4:224/356 of query aligns to 2:211/255 of 3q0gC
- active site: A65 (≠ G68), M70 (≠ L73), T80 (≠ H84), F84 (= F88), G108 (= G116), E111 (≠ G119), P130 (= P138), E131 (= E139), V136 (≠ Y144), P138 (= P146), G139 (≠ D147)
- binding coenzyme a: A24 (≠ G26), L25 (= L27), A27 (= A29), A63 (= A66), A65 (≠ G68), D66 (= D69), I67 (= I70), K68 (≠ R71), Y104 (≠ F112), P130 (= P138), E131 (= E139), L134 (≠ I142)
Sites not aligning to the query:
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
28% identity, 62% coverage: 4:224/356 of query aligns to 1:206/250 of 3q0gD
- active site: A64 (≠ G68), M69 (≠ L73), T75 (≠ H84), F79 (= F88), G103 (= G116), E106 (≠ G119), P125 (= P138), E126 (= E139), V131 (≠ Y144), P133 (= P146), G134 (≠ D147)
Sites not aligning to the query:
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
32% identity, 49% coverage: 7:182/356 of query aligns to 9:184/266 of O53561
- K135 (≠ R134) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 134:141, 13% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (≠ A141) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
1wdmA Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form i (native3) (see paper)
31% identity, 47% coverage: 27:193/356 of query aligns to 32:195/707 of 1wdmA
Sites not aligning to the query:
- active site: 430, 451, 463, 501
- binding acetyl coenzyme *a: 297, 459, 501, 534, 535, 544, 651, 652, 655, 658
- binding nicotinamide-adenine-dinucleotide: 321, 322, 324, 325, 343, 344, 345, 400, 401, 403, 408, 428, 429, 430, 452, 454
1wdlA Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form ii (native4) (see paper)
31% identity, 47% coverage: 27:193/356 of query aligns to 32:195/715 of 1wdlA
Sites not aligning to the query:
- active site: 430, 451, 463, 501
- binding nicotinamide-adenine-dinucleotide: 321, 322, 324, 325, 344, 345, 400, 401, 402, 403, 408, 411, 428, 429, 430
P28793 Fatty acid oxidation complex subunit alpha; EC 4.2.1.17; EC 5.1.2.3; EC 5.3.3.8; EC 1.1.1.35 from Pseudomonas fragi (see paper)
31% identity, 47% coverage: 27:193/356 of query aligns to 32:195/715 of P28793
Sites not aligning to the query:
- 297 binding
- 325 binding
- 344 binding
- 401:403 binding
- 408 binding
- 430 binding
- 454 binding
- 501 binding
- 660 binding
5wydA Structural of pseudomonas aeruginosa dspi (see paper)
27% identity, 52% coverage: 6:191/356 of query aligns to 9:191/262 of 5wydA