SitesBLAST
Comparing GFF1676 FitnessBrowser__Phaeo:GFF1676 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)
43% identity, 98% coverage: 6:258/258 of query aligns to 5:257/257 of 6slbAAA
- active site: Q64 (= Q63), F69 (≠ A68), L80 (= L80), N84 (≠ T85), A108 (= A109), S111 (≠ N112), A130 (= A131), F131 (= F132), L136 (= L137), P138 (= P139), D139 (= D140), A224 (≠ S225), G234 (= G235)
- 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 (≠ V57), A62 (≠ S61), Q64 (= Q63), D65 (= D64), L66 (= L65), Y76 (≠ L76), A108 (= A109), F131 (= F132), D139 (= D140)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
42% identity, 98% coverage: 6:258/258 of query aligns to 2:245/245 of 6slaAAA
- active site: Q61 (= Q63), L68 (= L76), N72 (≠ T85), A96 (= A109), S99 (≠ N112), A118 (= A131), F119 (= F132), L124 (= L137), P126 (= P139), N127 (≠ D140), A212 (≠ S225), G222 (= G235)
- 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 (≠ M25), A59 (≠ S61), Q61 (= Q63), D62 (= D64), L63 (= L65), L68 (= L76), Y71 (= Y84), A94 (= A107), G95 (= G108), A96 (= A109), F119 (= F132), I122 (= I135), L124 (= L137), N127 (≠ D140), F234 (= F247), K237 (= K250)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
31% identity, 100% coverage: 1:258/258 of query aligns to 1:259/259 of 5zaiC
- active site: A65 (≠ Q63), F70 (≠ A68), S82 (≠ R81), R86 (≠ T85), G110 (≠ A109), E113 (≠ N112), P132 (≠ A131), E133 (≠ F132), I138 (≠ L137), P140 (= P139), G141 (≠ D140), A226 (≠ S225), F236 (≠ G235)
- binding coenzyme a: K24 (= K24), L25 (≠ M25), A63 (≠ S61), G64 (= G62), A65 (≠ Q63), D66 (= D64), I67 (≠ L65), P132 (≠ A131), R166 (≠ K165), F248 (= F247), K251 (= K250)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
33% identity, 99% coverage: 1:255/258 of query aligns to 1:254/255 of 3q0jC
- active site: A65 (≠ Q63), M70 (≠ A68), T80 (= T85), F84 (≠ E89), G108 (≠ A109), E111 (≠ N112), P130 (≠ A131), E131 (≠ F132), V136 (≠ L137), P138 (= P139), G139 (≠ D140), L224 (≠ S225), F234 (≠ G235)
- binding acetoacetyl-coenzyme a: Q23 (≠ A23), A24 (≠ K24), L25 (≠ M25), A27 (= A27), A63 (≠ S61), G64 (= G62), A65 (≠ Q63), D66 (= D64), I67 (≠ L65), K68 (≠ S66), M70 (≠ A68), F84 (≠ E89), G107 (= G108), G108 (≠ A109), E111 (≠ N112), P130 (≠ A131), E131 (≠ F132), P138 (= P139), G139 (≠ D140), M140 (≠ A141)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
33% identity, 99% coverage: 1:255/258 of query aligns to 1:254/255 of 3q0gC
- active site: A65 (≠ Q63), M70 (≠ A68), T80 (= T85), F84 (≠ E89), G108 (≠ A109), E111 (≠ N112), P130 (≠ A131), E131 (≠ F132), V136 (≠ L137), P138 (= P139), G139 (≠ D140), L224 (≠ S225), F234 (≠ G235)
- binding coenzyme a: L25 (≠ M25), A63 (≠ S61), I67 (≠ L65), K68 (≠ S66), Y104 (≠ P105), P130 (≠ A131), E131 (≠ F132), L134 (≠ I135)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
32% identity, 99% coverage: 3:258/258 of query aligns to 2:256/256 of 3h81A
- active site: A64 (≠ Q63), M69 (≠ A68), T79 (= T85), F83 (≠ E89), G107 (≠ A109), E110 (≠ N112), P129 (≠ A131), E130 (≠ F132), V135 (≠ L137), P137 (= P139), G138 (≠ D140), L223 (≠ S225), F233 (≠ G235)
- binding calcium ion: F233 (≠ G235), Q238 (≠ F240)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
31% identity, 98% coverage: 3:255/258 of query aligns to 2:249/250 of 3q0gD
- active site: A64 (≠ Q63), M69 (≠ A68), T75 (vs. gap), F79 (vs. gap), G103 (≠ A109), E106 (≠ N112), P125 (≠ A131), E126 (≠ F132), V131 (≠ L137), P133 (= P139), G134 (≠ D140), L219 (≠ S225), F229 (≠ G235)
- binding Butyryl Coenzyme A: F225 (≠ Q231), F241 (= F247)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
30% identity, 95% coverage: 12:256/258 of query aligns to 15:258/260 of 2hw5C
- active site: A68 (≠ Q63), M73 (≠ A68), S83 (≠ R81), L87 (≠ T85), G111 (≠ A109), E114 (≠ N112), P133 (≠ A131), E134 (≠ F132), T139 (≠ L137), P141 (= P139), G142 (≠ D140), K227 (≠ S225), F237 (≠ G235)
- binding crotonyl coenzyme a: K26 (≠ A23), A27 (≠ K24), L28 (≠ M25), A30 (= A27), K62 (≠ V57), I70 (≠ L65), F109 (≠ A107)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
31% identity, 94% coverage: 14:256/258 of query aligns to 17:256/258 of 1mj3A
- active site: A68 (≠ Q63), M73 (≠ A68), S83 (≠ T85), L85 (≠ M87), G109 (≠ A109), E112 (≠ N112), P131 (≠ A131), E132 (≠ F132), T137 (≠ L137), P139 (= P139), G140 (≠ D140), K225 (≠ S225), F235 (≠ G235)
- binding hexanoyl-coenzyme a: K26 (≠ A23), A27 (≠ K24), L28 (≠ M25), A30 (= A27), A66 (≠ S61), G67 (= G62), A68 (≠ Q63), D69 (= D64), I70 (≠ L65), G109 (≠ A109), P131 (≠ A131), E132 (≠ F132), L135 (≠ I135), G140 (≠ D140)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
31% identity, 94% coverage: 14:256/258 of query aligns to 16:252/254 of 2dubA
- active site: A67 (≠ Q63), M72 (≠ A68), S82 (≠ T85), G105 (≠ A109), E108 (≠ N112), P127 (≠ A131), E128 (≠ F132), T133 (≠ L137), P135 (= P139), G136 (≠ D140), K221 (≠ S225), F231 (≠ G235)
- binding octanoyl-coenzyme a: K25 (≠ A23), A26 (≠ K24), L27 (≠ M25), A29 (= A27), A65 (≠ S61), A67 (≠ Q63), D68 (= D64), I69 (≠ L65), K70 (≠ S66), G105 (≠ A109), E108 (≠ N112), P127 (≠ A131), E128 (≠ F132), G136 (≠ D140), A137 (= A141)
1jxzB Structure of the h90q mutant of 4-chlorobenzoyl-coenzyme a dehalogenase complexed with 4-hydroxybenzoyl-coenzyme a (product) (see paper)
30% identity, 96% coverage: 3:249/258 of query aligns to 2:254/269 of 1jxzB
- active site: C61 (= C60), F64 (≠ Q63), I69 (vs. gap), A86 (≠ R81), Q90 (≠ T85), G113 (= G108), G114 (≠ A109), G117 (≠ N112), A136 (= A131), W137 (≠ F132), I142 (≠ L137), N144 (≠ P139), D145 (= D140), E230 (≠ S225)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ A23), H23 (≠ K24), R24 (≠ M25), A62 (≠ S61), F64 (≠ Q63), Y65 (≠ D64), L66 (= L65), R67 (≠ S66), W89 (≠ Y84), G113 (= G108), A136 (= A131), W137 (≠ F132), I142 (≠ L137), D145 (= D140), T146 (≠ A141), F252 (= F247)
- binding calcium ion: G49 (≠ R48), L202 (= L197), A203 (= A198), A205 (≠ G200), T207 (= T202), Q210 (≠ F205)
Sites not aligning to the query:
1nzyB 4-chlorobenzoyl coenzyme a dehalogenase from pseudomonas sp. Strain cbs-3 (see paper)
30% identity, 96% coverage: 3:249/258 of query aligns to 2:254/269 of 1nzyB
- active site: C61 (= C60), F64 (≠ Q63), I69 (vs. gap), A86 (≠ R81), H90 (≠ T85), G114 (≠ A109), G117 (≠ N112), A136 (= A131), W137 (≠ F132), I142 (≠ L137), N144 (≠ P139), D145 (= D140), E230 (≠ S225)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ A23), H23 (≠ K24), R24 (≠ M25), A62 (≠ S61), F64 (≠ Q63), Y65 (≠ D64), L66 (= L65), R67 (≠ S66), W89 (≠ Y84), G113 (= G108), G114 (≠ A109), A136 (= A131), W137 (≠ F132), D145 (= D140), T146 (≠ A141), F252 (= F247)
- binding calcium ion: G49 (vs. gap), L202 (= L197), A203 (= A198), A205 (≠ G200), T207 (= T202), Q210 (≠ F205)
- binding phosphate ion: E57 (≠ G56), N108 (= N103), K188 (≠ D183), R192 (vs. gap)
Sites not aligning to the query:
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
31% identity, 94% coverage: 14:256/258 of query aligns to 15:256/258 of 1ey3A
- active site: A66 (≠ Q63), M71 (≠ A68), S81 (≠ T85), L85 (vs. gap), G109 (≠ A109), E112 (≠ N112), P131 (≠ A131), E132 (≠ F132), T137 (≠ L137), P139 (= P139), G140 (≠ D140), K225 (≠ S225), F235 (≠ G235)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ A23), L26 (≠ M25), A28 (= A27), A64 (≠ S61), G65 (= G62), A66 (≠ Q63), D67 (= D64), I68 (≠ L65), L85 (vs. gap), W88 (vs. gap), G109 (≠ A109), P131 (≠ A131), L135 (≠ I135), G140 (≠ D140)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
31% identity, 94% coverage: 14:256/258 of query aligns to 17:258/260 of 1dubA
- active site: A68 (≠ Q63), M73 (≠ A68), S83 (≠ T85), L87 (vs. gap), G111 (≠ A109), E114 (≠ N112), P133 (≠ A131), E134 (≠ F132), T139 (≠ L137), P141 (= P139), G142 (≠ D140), K227 (≠ S225), F237 (≠ G235)
- binding acetoacetyl-coenzyme a: K26 (≠ A23), A27 (≠ K24), L28 (≠ M25), A30 (= A27), A66 (≠ S61), A68 (≠ Q63), D69 (= D64), I70 (≠ L65), Y107 (≠ P105), G110 (= G108), G111 (≠ A109), E114 (≠ N112), P133 (≠ A131), E134 (≠ F132), L137 (≠ I135), G142 (≠ D140), F233 (≠ Q231), F249 (= F247)
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)
31% identity, 94% coverage: 14:256/258 of query aligns to 47:288/290 of P14604
- E144 (≠ N112) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (≠ F132) 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
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, 96% coverage: 3:249/258 of query aligns to 2:254/269 of A5JTM5
- R24 (≠ M25) binding in other chain; mutation R->K,L: Does not strongly affect catalytic activity, but reduces substrate CoA binding.
- E34 (= E35) mutation to T: Forms inclusion bodies.
- E43 (≠ G44) mutation to A: No effect on catalytic activity.
- D45 (≠ E46) mutation to A: No effect on catalytic activity.
- D46 (vs. gap) 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 (≠ S66) mutation to K: Reduces substrate CoA binding.; mutation to L: Forms inclusion bodies.
- E68 (vs. gap) mutation to T: No effect on catalytic activity.
- H81 (≠ L76) mutation to Q: Loss of catalytic activity, substrate benzoyl group binding is not affected.
- F82 (≠ E77) mutation to L: Retains catalytic activity, but substrate benzoyl group binding is decreased.
- W89 (≠ Y84) mutation to F: Retains catalytic activity, but substrate benzoyl group binding is decreased.; mutation to Y: Reduced activity and substrate benzoyl group binding.
- H90 (≠ T85) 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 (≠ E89) mutation to Q: No effect on catalytic activity.
- A112 (= A107) 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 (= G108) 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 (≠ A109) mutation to A: Strongly reduced catalytic activity and substrate benzoyl group binding.; mutation to P: Unstable.
- G115 (= G110) mutation G->L,N,S,V: Yields insoluble protein.
- D123 (= D118) mutation to T: No effect on catalytic activity.
- D129 (≠ E124) mutation to T: No effect on catalytic activity.
- W137 (≠ F132) mutation to F: Low catalytic activity, but KM unaffected (PubMed:8718880). Retains catalytic activity, but substrate benzoyl group binding is decreased (PubMed:9063883).
- D145 (= D140) active site, Nucleophile; mutation to A: Complete loss of catalytic activity, but not substrate binding.
- E163 (≠ G158) mutation to T: No effect on catalytic activity.
- E175 (≠ Q170) mutation to D: No effect on catalytic activity.
- W179 (= W174) mutation to F: No effect on catalytic activity.
- H208 (≠ R203) mutation to Q: No effect on catalytic activity.
- R216 (≠ A211) mutation R->E,K,L: Yields insoluble protein.
- E232 (= E227) 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.
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
31% identity, 93% coverage: 18:258/258 of query aligns to 19:261/261 of 5jbxB
- active site: A67 (≠ Q63), R72 (≠ A68), L84 (≠ R81), R88 (≠ T85), G112 (≠ A109), E115 (≠ N112), T134 (≠ A131), E135 (≠ F132), I140 (≠ L137), P142 (= P139), G143 (≠ D140), A228 (≠ S225), L238 (≠ G235)
- binding coenzyme a: S24 (≠ A23), R25 (≠ K24), R26 (≠ M25), A28 (= A27), A65 (≠ S61), D68 (= D64), L69 (= L65), K70 (≠ S66), L110 (≠ A107), G111 (= G108), T134 (≠ A131), E135 (≠ F132), L138 (≠ I135), R168 (≠ K165)
5du6A Crystal structure of m. Tuberculosis echa6 bound to ligand gsk059a. (see paper)
32% identity, 95% coverage: 12:257/258 of query aligns to 9:241/242 of 5du6A
- active site: A61 (≠ Q63), P71 (≠ R81), I75 (≠ T85), A99 (= A109), Q102 (≠ N112), P121 (≠ A131), T122 (≠ F132), L127 (= L137), L129 (≠ P139), D130 (= D140), P209 (≠ S225), W219 (≠ G235)
- binding (5R,7R)-5-(4-ethylphenyl)-N-(4-fluorobenzyl)-7-methyl-4,5,6,7-tetrahydropyrazolo[1,5-a]pyrimidine-3-carboxamide: L74 (≠ Y84), D82 (≠ Y92), D130 (= D140), W132 (≠ G142), A207 (≠ Q223), K212 (≠ A228), F215 (≠ Q231)
Q62651 Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial; EC 5.3.3.- from Rattus norvegicus (Rat) (see paper)
31% identity, 98% coverage: 2:254/258 of query aligns to 53:320/327 of Q62651
- D176 (≠ N112) mutation D->A,D: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- E196 (≠ F132) mutation E->D,Q: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- D204 (= D140) mutation D->A,N: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
5ducA Crystal structure of m. Tuberculosis echa6 bound to ligand gsk951a (see paper)
32% identity, 95% coverage: 12:257/258 of query aligns to 9:243/244 of 5ducA
- active site: A61 (≠ Q63), D66 (≠ A68), P73 (≠ D75), I77 (≠ T85), A101 (= A109), Q104 (≠ N112), P123 (≠ A131), T124 (≠ F132), L129 (= L137), L131 (≠ P139), D132 (= D140), P211 (≠ S225), W221 (≠ G235)
- 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 (≠ Y84), H80 (≠ L88), D84 (≠ Y92), Q104 (≠ N112), D132 (= D140), W134 (≠ G142), F217 (≠ Q231)
Query Sequence
>GFF1676 FitnessBrowser__Phaeo:GFF1676
MDYQEILFSLEDGLAVVTLNRPAKMNALTGLTRAEITHAMQRAGKEARAVVLTGSGVSFC
SGQDLSDAASQGKLDLERTLRDEYTPMLEAIYNCPVPTIAAVNGPAAGAGANLALAADVV
IATESAYFMQAFARIGLMPDAGGTWFMPRQMGMAKAMGAALFADKISAKQASDWGMIWEA
IPDAEFDAHWRARAAYLASGPTRAFGAIKTAIRDGYGNSLPEQLSEEAHLQGQCGKTRDF
MEGVTAFMEKRPAKFEGR
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