SitesBLAST
Comparing GFF2642 FitnessBrowser__Phaeo:GFF2642 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)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
44% identity, 98% coverage: 5:261/261 of query aligns to 5:257/257 of 6slbAAA
- active site: Q64 (= Q63), F69 (≠ R68), L80 (≠ V83), N84 (≠ A88), A108 (= A112), S111 (≠ N115), A130 (≠ S134), F131 (= F135), L136 (= L140), P138 (= P142), D139 (= D143), A224 (≠ E228), G234 (= G238)
- 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 (= R57), A62 (= A61), Q64 (= Q63), D65 (= D64), L66 (= L65), Y76 (≠ L79), A108 (= A112), F131 (= F135), D139 (= D143)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
42% identity, 98% coverage: 5:261/261 of query aligns to 2:245/245 of 6slaAAA
- active site: Q61 (= Q63), L68 (≠ P70), N72 (≠ A88), A96 (= A112), S99 (≠ N115), A118 (≠ S134), F119 (= F135), L124 (= L140), P126 (= P142), N127 (≠ D143), A212 (≠ E228), G222 (= G238)
- 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 (= L24), A59 (= A61), Q61 (= Q63), D62 (= D64), L63 (= L65), L68 (≠ P70), Y71 (= Y87), A94 (= A110), G95 (= G111), A96 (= A112), F119 (= F135), I122 (≠ V138), L124 (= L140), N127 (≠ D143), F234 (= F250), K237 (= K253)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
35% identity, 99% coverage: 3:261/261 of query aligns to 4:259/259 of 5zaiC
- active site: A65 (≠ Q63), F70 (≠ R68), S82 (≠ R84), R86 (≠ A88), G110 (≠ A112), E113 (≠ N115), P132 (≠ S134), E133 (≠ F135), I138 (≠ L140), P140 (= P142), G141 (≠ D143), A226 (≠ E228), F236 (≠ G238)
- binding coenzyme a: K24 (≠ R23), L25 (= L24), A63 (= A61), G64 (= G62), A65 (≠ Q63), D66 (= D64), I67 (≠ L65), P132 (≠ S134), R166 (≠ P168), F248 (= F250), K251 (= K253)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
36% identity, 98% coverage: 3:258/261 of query aligns to 3:253/256 of 3h81A
- active site: A64 (≠ Q63), M69 (= M73), T79 (≠ V83), F83 (≠ Y87), G107 (≠ A112), E110 (≠ N115), P129 (≠ S134), E130 (≠ F135), V135 (≠ L140), P137 (= P142), G138 (≠ D143), L223 (≠ E228), F233 (≠ G238)
- binding calcium ion: F233 (≠ G238), Q238 (≠ Y243)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
36% identity, 98% coverage: 3:258/261 of query aligns to 4:254/255 of 3q0jC
- active site: A65 (≠ Q63), M70 (= M73), T80 (≠ V83), F84 (≠ Y87), G108 (≠ A112), E111 (≠ N115), P130 (≠ S134), E131 (≠ F135), V136 (≠ L140), P138 (= P142), G139 (≠ D143), L224 (≠ E228), F234 (≠ G238)
- binding acetoacetyl-coenzyme a: Q23 (≠ D22), A24 (≠ R23), L25 (= L24), A27 (≠ S26), A63 (= A61), G64 (= G62), A65 (≠ Q63), D66 (= D64), I67 (≠ L65), K68 (≠ R71), M70 (= M73), F84 (≠ Y87), G107 (= G111), G108 (≠ A112), E111 (≠ N115), P130 (≠ S134), E131 (≠ F135), P138 (= P142), G139 (≠ D143), M140 (≠ T144)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
36% identity, 98% coverage: 3:258/261 of query aligns to 4:254/255 of 3q0gC
- active site: A65 (≠ Q63), M70 (= M73), T80 (≠ V83), F84 (≠ Y87), G108 (≠ A112), E111 (≠ N115), P130 (≠ S134), E131 (≠ F135), V136 (≠ L140), P138 (= P142), G139 (≠ D143), L224 (≠ E228), F234 (≠ G238)
- binding coenzyme a: L25 (= L24), A63 (= A61), I67 (≠ L65), K68 (≠ R71), Y104 (≠ V108), P130 (≠ S134), E131 (≠ F135), L134 (≠ V138)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
36% identity, 98% coverage: 3:258/261 of query aligns to 3:249/250 of 3q0gD
- active site: A64 (≠ Q63), M69 (≠ R68), T75 (≠ K72), F79 (≠ Y87), G103 (≠ A112), E106 (≠ N115), P125 (≠ S134), E126 (≠ F135), V131 (≠ L140), P133 (= P142), G134 (≠ D143), L219 (≠ E228), F229 (≠ G238)
- binding Butyryl Coenzyme A: F225 (≠ M234), F241 (= F250)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
34% identity, 93% coverage: 16:259/261 of query aligns to 19:252/254 of 2dubA
- active site: A67 (≠ Q63), M72 (≠ R68), S82 (≠ A88), G105 (≠ A112), E108 (≠ N115), P127 (≠ S134), E128 (≠ F135), T133 (≠ L140), P135 (= P142), G136 (≠ D143), K221 (≠ E228), F231 (≠ G238)
- binding octanoyl-coenzyme a: K25 (≠ D22), A26 (≠ R23), L27 (= L24), A29 (≠ S26), A65 (= A61), A67 (≠ Q63), D68 (= D64), I69 (≠ L65), K70 (≠ G66), G105 (≠ A112), E108 (≠ N115), P127 (≠ S134), E128 (≠ F135), G136 (≠ D143), A137 (≠ T144)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
34% identity, 93% coverage: 16:259/261 of query aligns to 20:256/258 of 1mj3A
- active site: A68 (≠ Q63), M73 (≠ R68), S83 (≠ A88), L85 (= L90), G109 (≠ A112), E112 (≠ N115), P131 (≠ S134), E132 (≠ F135), T137 (≠ L140), P139 (= P142), G140 (≠ D143), K225 (≠ E228), F235 (≠ G238)
- binding hexanoyl-coenzyme a: K26 (≠ D22), A27 (≠ R23), L28 (= L24), A30 (≠ S26), A66 (= A61), G67 (= G62), A68 (≠ Q63), D69 (= D64), I70 (≠ L65), G109 (≠ A112), P131 (≠ S134), E132 (≠ F135), L135 (≠ V138), G140 (≠ D143)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
34% identity, 93% coverage: 16:259/261 of query aligns to 18:256/258 of 1ey3A
- active site: A66 (≠ Q63), M71 (≠ R68), S81 (≠ A88), L85 (vs. gap), G109 (≠ A112), E112 (≠ N115), P131 (≠ S134), E132 (≠ F135), T137 (≠ L140), P139 (= P142), G140 (≠ D143), K225 (≠ E228), F235 (≠ G238)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ D22), L26 (= L24), A28 (≠ S26), A64 (= A61), G65 (= G62), A66 (≠ Q63), D67 (= D64), I68 (≠ L65), L85 (vs. gap), W88 (vs. gap), G109 (≠ A112), P131 (≠ S134), L135 (≠ V138), G140 (≠ D143)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
34% identity, 93% coverage: 16:259/261 of query aligns to 20:258/260 of 1dubA
- active site: A68 (≠ Q63), M73 (≠ R68), S83 (≠ A88), L87 (vs. gap), G111 (≠ A112), E114 (≠ N115), P133 (≠ S134), E134 (≠ F135), T139 (≠ L140), P141 (= P142), G142 (≠ D143), K227 (≠ E228), F237 (≠ G238)
- binding acetoacetyl-coenzyme a: K26 (≠ D22), A27 (≠ R23), L28 (= L24), A30 (≠ S26), A66 (= A61), A68 (≠ Q63), D69 (= D64), I70 (≠ L65), Y107 (≠ V108), G110 (= G111), G111 (≠ A112), E114 (≠ N115), P133 (≠ S134), E134 (≠ F135), L137 (≠ V138), G142 (≠ D143), F233 (≠ M234), F249 (= F250)
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)
34% identity, 93% coverage: 16:259/261 of query aligns to 50:288/290 of P14604
- E144 (≠ N115) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (≠ F135) 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
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
32% identity, 93% coverage: 16:259/261 of query aligns to 20:258/260 of 2hw5C
- active site: A68 (≠ Q63), M73 (≠ P70), S83 (≠ G80), L87 (≠ R84), G111 (≠ A112), E114 (≠ N115), P133 (≠ S134), E134 (≠ F135), T139 (≠ L140), P141 (= P142), G142 (≠ D143), K227 (≠ E228), F237 (≠ G238)
- binding crotonyl coenzyme a: K26 (≠ D22), A27 (≠ R23), L28 (= L24), A30 (≠ S26), K62 (≠ R57), I70 (≠ L65), F109 (≠ A110)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
35% identity, 95% coverage: 14:261/261 of query aligns to 15:261/261 of 5jbxB
- active site: A67 (≠ Q63), R72 (= R68), L84 (≠ Y87), R88 (≠ V91), G112 (≠ A112), E115 (≠ N115), T134 (≠ S134), E135 (≠ F135), I140 (≠ L140), P142 (= P142), G143 (≠ D143), A228 (≠ E228), L238 (≠ G238)
- binding coenzyme a: S24 (≠ D22), R25 (= R23), R26 (≠ L24), A28 (≠ S26), A65 (= A61), D68 (= D64), L69 (= L65), K70 (≠ G66), L110 (≠ A110), G111 (= G111), T134 (≠ S134), E135 (≠ F135), L138 (≠ V138), R168 (≠ P168)
1jxzB Structure of the h90q mutant of 4-chlorobenzoyl-coenzyme a dehalogenase complexed with 4-hydroxybenzoyl-coenzyme a (product) (see paper)
30% identity, 91% coverage: 15:252/261 of query aligns to 15:254/269 of 1jxzB
- active site: C61 (= C60), F64 (≠ Q63), I69 (≠ R68), A86 (≠ R84), Q90 (≠ A88), G113 (= G111), G114 (≠ A112), G117 (≠ N115), A136 (≠ S134), W137 (≠ F135), I142 (≠ L140), N144 (≠ P142), D145 (= D143), E230 (= E228)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ D22), H23 (≠ R23), R24 (≠ L24), A62 (= A61), F64 (≠ Q63), Y65 (≠ D64), L66 (= L65), R67 (≠ G66), W89 (≠ Y87), G113 (= G111), A136 (≠ S134), W137 (≠ F135), I142 (≠ L140), D145 (= D143), T146 (= T144), F252 (= F250)
- binding calcium ion: G49 (≠ R48), L202 (≠ F200), A203 (= A201), A205 (≠ G203), T207 (= T205), Q210 (≠ L208)
Sites not aligning to the query:
1nzyB 4-chlorobenzoyl coenzyme a dehalogenase from pseudomonas sp. Strain cbs-3 (see paper)
30% identity, 91% coverage: 15:252/261 of query aligns to 15:254/269 of 1nzyB
- active site: C61 (= C60), F64 (≠ Q63), I69 (≠ R68), A86 (≠ R84), H90 (≠ A88), G114 (≠ A112), G117 (≠ N115), A136 (≠ S134), W137 (≠ F135), I142 (≠ L140), N144 (≠ P142), D145 (= D143), E230 (= E228)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ D22), H23 (≠ R23), R24 (≠ L24), A62 (= A61), F64 (≠ Q63), Y65 (≠ D64), L66 (= L65), R67 (≠ G66), W89 (≠ Y87), G113 (= G111), G114 (≠ A112), A136 (≠ S134), W137 (≠ F135), D145 (= D143), T146 (= T144), F252 (= F250)
- binding calcium ion: G49 (≠ R48), L202 (≠ F200), A203 (= A201), A205 (≠ G203), T207 (= T205), Q210 (≠ L208)
- binding phosphate ion: E57 (≠ G56), N108 (= N106), K188 (≠ D186), R192 (≠ M190)
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)
30% identity, 91% coverage: 15:252/261 of query aligns to 15:254/269 of A5JTM5
- R24 (≠ L24) binding in other chain; mutation R->K,L: Does not strongly affect catalytic activity, but reduces substrate CoA binding.
- E34 (≠ H33) mutation to T: Forms inclusion bodies.
- E43 (≠ A42) mutation to A: No effect on catalytic activity.
- D45 (= D44) mutation to A: No effect on catalytic activity.
- D46 (≠ G45) mutation to A: No effect on catalytic activity.
- G63 (= G62) mutation G->A,I,P: Yields insoluble protein.
- F64 (≠ Q63) 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 (≠ D64) mutation to D: Catalytic activity is almost as efficient as wild type.
- R67 (≠ G66) mutation to K: Reduces substrate CoA binding.; mutation to L: Forms inclusion bodies.
- E68 (≠ D67) mutation to T: No effect on catalytic activity.
- H81 (≠ L79) mutation to Q: Loss of catalytic activity, substrate benzoyl group binding is not affected.
- F82 (≠ G80) mutation to L: Retains catalytic activity, but substrate benzoyl group binding is decreased.
- W89 (≠ Y87) mutation to F: Retains catalytic activity, but substrate benzoyl group binding is decreased.; mutation to Y: Reduced activity and substrate benzoyl group binding.
- H90 (≠ A88) 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 (≠ N92) mutation to Q: No effect on catalytic activity.
- A112 (= A110) 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 (= G111) 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 (≠ A112) mutation to A: Strongly reduced catalytic activity and substrate benzoyl group binding.; mutation to P: Unstable.
- G115 (= G113) mutation G->L,N,S,V: Yields insoluble protein.
- D123 (= D121) mutation to T: No effect on catalytic activity.
- D129 (≠ E127) mutation to T: No effect on catalytic activity.
- W137 (≠ F135) mutation to F: Low catalytic activity, but KM unaffected (PubMed:8718880). Retains catalytic activity, but substrate benzoyl group binding is decreased (PubMed:9063883).
- D145 (= D143) active site, Nucleophile; mutation to A: Complete loss of catalytic activity, but not substrate binding.
- E163 (≠ G161) mutation to T: No effect on catalytic activity.
- E175 (≠ K173) mutation to D: No effect on catalytic activity.
- W179 (= W177) mutation to F: No effect on catalytic activity.
- H208 (≠ L206) mutation to Q: No effect on catalytic activity.
- R216 (≠ T214) mutation R->E,K,L: Yields insoluble protein.
- E232 (= E230) mutation E->A,N,Q,R: Yields insoluble protein.; mutation to D: Reduced catalytic activity, increased substrate binding.
Sites not aligning to the query:
- 257 R→K: Retains catalytic activity and substrate CoA binding.; R→L: Significantly reduces catalytic activity and substrate CoA binding.
7borA Structure of pseudomonas aeruginosa coa-bound odaa (see paper)
31% identity, 97% coverage: 2:253/261 of query aligns to 1:247/247 of 7borA
- active site: N63 (≠ Q63), F68 (≠ K72), D77 (≠ H81), G81 (≠ R84), I105 (≠ A112), T108 (≠ N115), F128 (= F135), L133 (= L140), P135 (= P142), E136 (≠ D143), A222 (≠ E228), L232 (≠ G238)
- binding coenzyme a: D21 (= D22), K22 (≠ R23), A25 (≠ S26), S61 (≠ A61), I65 (≠ L65), V103 (≠ A110), F128 (= F135), L131 (≠ V138), F244 (= F250), R247 (≠ K253)
Q9P4U9 Enoyl-CoA hydratase AKT3-1; AF-toxin biosynthesis protein 3-1; EC 4.2.1.17 from Alternaria alternata (Alternaria rot fungus) (Torula alternata) (see paper)
32% identity, 93% coverage: 16:259/261 of query aligns to 28:269/296 of Q9P4U9
Sites not aligning to the query:
- 294:296 Peroxisomal targeting signal type 1
5ducA Crystal structure of m. Tuberculosis echa6 bound to ligand gsk951a (see paper)
32% identity, 94% coverage: 16:260/261 of query aligns to 14:243/244 of 5ducA
- active site: A61 (≠ Q63), D66 (= D69), P73 (= P76), I77 (≠ V91), A101 (= A112), Q104 (≠ N115), P123 (≠ S134), T124 (≠ F135), L129 (= L140), L131 (≠ P142), D132 (= D143), P211 (≠ E228), W221 (≠ G238)
- binding (5R,7S)-N-(1,3-benzodioxol-5-ylmethyl)-5-(4-ethylphenyl)-7-(trifluoromethyl)-4,5,6,7-tetrahydropyrazolo[1,5-a]pyrimidine-3-carboxamide: L76 (= L79), H80 (≠ I94), D84 (= D98), Q104 (≠ N115), D132 (= D143), W134 (≠ G145), F217 (≠ M234)
Query Sequence
>GFF2642 FitnessBrowser__Phaeo:GFF2642
MSETLLVEDHGTWVEITLNRPDRLNSFTEEMHHALRAALEAARDGGARAVLLTGAGRGFC
AGQDLGDRDPRKMDGPPDLGHTVRTFYAPLVNLIRALDFPVICAVNGVAAGAGANLALAC
DVVLAAESAKFIQSFSKVGLIPDTGGSWHLPRLLGEARAKGLALTAEPLPAKKAEDWGLI
WKAVPDEELMAEARAMAEKFANGPTLGLGLTKQTIQAAAVTTLSDQLEIEADAMKTCGES
ADYAEGVASFLEKRVPAFKGK
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