SitesBLAST
Comparing GFF4154 FitnessBrowser__Marino:GFF4154 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)
39% identity, 94% coverage: 15:263/264 of query aligns to 12:256/257 of 6slbAAA
- active site: Q64 (≠ G67), F69 (≠ M72), L80 (= L87), N84 (= N91), A108 (= A115), S111 (= S118), A130 (= A137), F131 (≠ Y138), L136 (≠ A143), P138 (= P145), D139 (= D146), A224 (≠ E231), G234 (≠ T241)
- 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 (= R61), A62 (= A65), Q64 (≠ G67), D65 (= D68), L66 (≠ V69), Y76 (≠ I83), A108 (= A115), F131 (≠ Y138), D139 (= D146)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
39% identity, 94% coverage: 15:263/264 of query aligns to 9:244/245 of 6slaAAA
- active site: Q61 (≠ G67), L68 (= L87), N72 (= N91), A96 (= A115), S99 (= S118), A118 (= A137), F119 (≠ Y138), L124 (≠ A143), P126 (= P145), N127 (≠ D146), A212 (≠ E231), G222 (≠ T241)
- 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 (= L27), A59 (= A65), Q61 (≠ G67), D62 (= D68), L63 (≠ V69), L68 (= L87), Y71 (≠ V90), A94 (= A113), G95 (= G114), A96 (= A115), F119 (≠ Y138), I122 (= I141), L124 (≠ A143), N127 (≠ D146), F234 (= F253), K237 (= K256)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
33% identity, 93% coverage: 19:263/264 of query aligns to 17:258/259 of 5zaiC
- active site: A65 (≠ G67), F70 (≠ M72), S82 (≠ G80), R86 (≠ G84), G110 (≠ A115), E113 (≠ S118), P132 (≠ A137), E133 (≠ Y138), I138 (≠ A143), P140 (= P145), G141 (≠ D146), A226 (≠ E231), F236 (≠ T241)
- binding coenzyme a: K24 (≠ A26), L25 (= L27), A63 (= A65), G64 (= G66), A65 (≠ G67), D66 (= D68), I67 (≠ V69), P132 (≠ A137), R166 (≠ T171), F248 (= F253), K251 (= K256)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
33% identity, 92% coverage: 19:261/264 of query aligns to 17:254/255 of 3q0jC
- active site: A65 (≠ G67), M70 (= M72), T80 (≠ G84), F84 (≠ D88), G108 (≠ A115), E111 (≠ S118), P130 (≠ A137), E131 (≠ Y138), V136 (≠ A143), P138 (= P145), G139 (≠ D146), L224 (≠ E231), F234 (≠ T241)
- binding acetoacetyl-coenzyme a: Q23 (≠ E25), A24 (= A26), L25 (= L27), A27 (= A29), A63 (= A65), G64 (= G66), A65 (≠ G67), D66 (= D68), I67 (≠ V69), K68 (≠ S70), M70 (= M72), F84 (≠ D88), G107 (= G114), G108 (≠ A115), E111 (≠ S118), P130 (≠ A137), E131 (≠ Y138), P138 (= P145), G139 (≠ D146), M140 (≠ C147)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
33% identity, 92% coverage: 19:261/264 of query aligns to 17:254/255 of 3q0gC
- active site: A65 (≠ G67), M70 (= M72), T80 (≠ G84), F84 (≠ D88), G108 (≠ A115), E111 (≠ S118), P130 (≠ A137), E131 (≠ Y138), V136 (≠ A143), P138 (= P145), G139 (≠ D146), L224 (≠ E231), F234 (≠ T241)
- binding coenzyme a: L25 (= L27), A63 (= A65), I67 (≠ V69), K68 (≠ S70), Y104 (≠ V111), P130 (≠ A137), E131 (≠ Y138), L134 (≠ I141)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
33% identity, 92% coverage: 19:261/264 of query aligns to 16:253/256 of 3h81A
- active site: A64 (≠ G67), M69 (= M72), T79 (≠ G84), F83 (≠ D88), G107 (≠ A115), E110 (≠ S118), P129 (≠ A137), E130 (≠ Y138), V135 (≠ A143), P137 (= P145), G138 (≠ D146), L223 (≠ E231), F233 (≠ T241)
- binding calcium ion: F233 (≠ T241), Q238 (≠ F246)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
33% identity, 92% coverage: 19:261/264 of query aligns to 16:249/250 of 3q0gD
- active site: A64 (≠ G67), M69 (= M72), T75 (≠ G84), F79 (≠ D88), G103 (≠ A115), E106 (≠ S118), P125 (≠ A137), E126 (≠ Y138), V131 (≠ A143), P133 (= P145), G134 (≠ D146), L219 (≠ E231), F229 (≠ T241)
- binding Butyryl Coenzyme A: F225 (= F237), F241 (= F253)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
30% identity, 98% coverage: 5:262/264 of query aligns to 4:256/258 of 1ey3A
- active site: A66 (≠ G67), M71 (= M72), S81 (≠ A82), L85 (= L87), G109 (≠ A115), E112 (≠ S118), P131 (≠ A137), E132 (≠ Y138), T137 (≠ A143), P139 (= P145), G140 (≠ D146), K225 (≠ E231), F235 (≠ T241)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ E25), L26 (= L27), A28 (= A29), A64 (= A65), G65 (= G66), A66 (≠ G67), D67 (= D68), I68 (≠ V69), L85 (= L87), W88 (≠ V90), G109 (≠ A115), P131 (≠ A137), L135 (≠ I141), G140 (≠ D146)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
30% identity, 98% coverage: 5:262/264 of query aligns to 6:258/260 of 1dubA
- active site: A68 (≠ G67), M73 (= M72), S83 (≠ A82), L87 (= L87), G111 (≠ A115), E114 (≠ S118), P133 (≠ A137), E134 (≠ Y138), T139 (≠ A143), P141 (= P145), G142 (≠ D146), K227 (≠ E231), F237 (≠ T241)
- binding acetoacetyl-coenzyme a: K26 (≠ E25), A27 (= A26), L28 (= L27), A30 (= A29), A66 (= A65), A68 (≠ G67), D69 (= D68), I70 (≠ V69), Y107 (≠ V111), G110 (= G114), G111 (≠ A115), E114 (≠ S118), P133 (≠ A137), E134 (≠ Y138), L137 (≠ I141), G142 (≠ D146), F233 (= F237), F249 (= F253)
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, 98% coverage: 5:262/264 of query aligns to 36:288/290 of P14604
- E144 (≠ S118) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (≠ Y138) 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
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
29% identity, 98% coverage: 5:262/264 of query aligns to 6:256/258 of 1mj3A
- active site: A68 (≠ G67), M73 (= M72), S83 (≠ A82), L85 (≠ G84), G109 (≠ A115), E112 (≠ S118), P131 (≠ A137), E132 (≠ Y138), T137 (≠ A143), P139 (= P145), G140 (≠ D146), K225 (≠ E231), F235 (≠ T241)
- binding hexanoyl-coenzyme a: K26 (≠ E25), A27 (= A26), L28 (= L27), A30 (= A29), A66 (= A65), G67 (= G66), A68 (≠ G67), D69 (= D68), I70 (≠ V69), G109 (≠ A115), P131 (≠ A137), E132 (≠ Y138), L135 (≠ I141), G140 (≠ D146)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
30% identity, 98% coverage: 5:262/264 of query aligns to 5:252/254 of 2dubA
- active site: A67 (≠ G67), M72 (= M72), S82 (≠ N91), G105 (≠ A115), E108 (≠ S118), P127 (≠ A137), E128 (≠ Y138), T133 (≠ A143), P135 (= P145), G136 (≠ D146), K221 (≠ E231), F231 (≠ T241)
- binding octanoyl-coenzyme a: K25 (≠ E25), A26 (= A26), L27 (= L27), A29 (= A29), A65 (= A65), A67 (≠ G67), D68 (= D68), I69 (≠ V69), K70 (≠ S70), G105 (≠ A115), E108 (≠ S118), P127 (≠ A137), E128 (≠ Y138), G136 (≠ D146), A137 (≠ C147)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
30% identity, 94% coverage: 16:262/264 of query aligns to 17:258/260 of 2hw5C
- active site: A68 (≠ G67), M73 (= M72), S83 (≠ N91), L87 (= L95), G111 (≠ A115), E114 (≠ S118), P133 (≠ A137), E134 (≠ Y138), T139 (≠ A143), P141 (= P145), G142 (≠ D146), K227 (≠ E231), F237 (≠ T241)
- binding crotonyl coenzyme a: K26 (≠ E25), A27 (= A26), L28 (= L27), A30 (= A29), K62 (≠ R61), I70 (≠ V69), F109 (≠ A113)
1jxzB Structure of the h90q mutant of 4-chlorobenzoyl-coenzyme a dehalogenase complexed with 4-hydroxybenzoyl-coenzyme a (product) (see paper)
34% identity, 74% coverage: 15:209/264 of query aligns to 12:208/269 of 1jxzB
- active site: C61 (≠ M64), F64 (≠ G67), I69 (≠ M72), A86 (≠ I94), Q90 (≠ R98), G113 (= G114), G114 (≠ A115), G117 (≠ S118), A136 (= A137), W137 (≠ Y138), I142 (≠ A143), N144 (≠ P145), D145 (= D146)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ E25), H23 (≠ A26), R24 (≠ L27), A62 (= A65), F64 (≠ G67), Y65 (≠ D68), L66 (≠ V69), R67 (≠ S70), W89 (≠ L97), G113 (= G114), A136 (= A137), W137 (≠ Y138), I142 (≠ A143), D145 (= D146), T146 (≠ C147)
- binding calcium ion: G49 (≠ R52), L202 (≠ V203), A203 (= A204), A205 (≠ G206), T207 (= T208)
Sites not aligning to the query:
1nzyB 4-chlorobenzoyl coenzyme a dehalogenase from pseudomonas sp. Strain cbs-3 (see paper)
34% identity, 74% coverage: 15:209/264 of query aligns to 12:208/269 of 1nzyB
- active site: C61 (≠ M64), F64 (≠ G67), I69 (≠ M72), A86 (≠ I94), H90 (≠ R98), G114 (≠ A115), G117 (≠ S118), A136 (= A137), W137 (≠ Y138), I142 (≠ A143), N144 (≠ P145), D145 (= D146)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ E25), H23 (≠ A26), R24 (≠ L27), A62 (= A65), F64 (≠ G67), Y65 (≠ D68), L66 (≠ V69), R67 (≠ S70), W89 (≠ L97), G113 (= G114), G114 (≠ A115), A136 (= A137), W137 (≠ Y138), D145 (= D146), T146 (≠ C147)
- binding calcium ion: G49 (≠ R52), L202 (≠ V203), A203 (= A204), A205 (≠ G206), T207 (= T208)
- binding phosphate ion: E57 (≠ G60), N108 (≠ R109), K188 (≠ A189), R192 (≠ E193)
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)
33% identity, 74% coverage: 15:209/264 of query aligns to 12:208/269 of A5JTM5
- R24 (≠ L27) binding in other chain; mutation R->K,L: Does not strongly affect catalytic activity, but reduces substrate CoA binding.
- E34 (≠ A37) mutation to T: Forms inclusion bodies.
- E43 (≠ N46) mutation to A: No effect on catalytic activity.
- D45 (≠ L48) mutation to A: No effect on catalytic activity.
- D46 (≠ S49) mutation to A: No effect on catalytic activity.
- G63 (= G66) mutation G->A,I,P: Yields insoluble protein.
- F64 (≠ G67) 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 (≠ D68) mutation to D: Catalytic activity is almost as efficient as wild type.
- R67 (≠ S70) mutation to K: Reduces substrate CoA binding.; mutation to L: Forms inclusion bodies.
- E68 (≠ S71) mutation to T: No effect on catalytic activity.
- H81 (≠ A89) mutation to Q: Loss of catalytic activity, substrate benzoyl group binding is not affected.
- F82 (≠ V90) mutation to L: Retains catalytic activity, but substrate benzoyl group binding is decreased.
- W89 (≠ L97) mutation to F: Retains catalytic activity, but substrate benzoyl group binding is decreased.; mutation to Y: Reduced activity and substrate benzoyl group binding.
- H90 (≠ R98) 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 (vs. gap) mutation to Q: No effect on catalytic activity.
- A112 (= A113) 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 (= G114) 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 (≠ A115) mutation to A: Strongly reduced catalytic activity and substrate benzoyl group binding.; mutation to P: Unstable.
- G115 (= G116) mutation G->L,N,S,V: Yields insoluble protein.
- D123 (= D124) mutation to T: No effect on catalytic activity.
- D129 (≠ E130) mutation to T: No effect on catalytic activity.
- W137 (≠ Y138) mutation to F: Low catalytic activity, but KM unaffected (PubMed:8718880). Retains catalytic activity, but substrate benzoyl group binding is decreased (PubMed:9063883).
- D145 (= D146) active site, Nucleophile; mutation to A: Complete loss of catalytic activity, but not substrate binding.
- E163 (= E164) mutation to T: No effect on catalytic activity.
- E175 (= E176) mutation to D: No effect on catalytic activity.
- W179 (= W180) mutation to F: No effect on catalytic activity.
- H208 (≠ R209) 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.
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
32% identity, 89% coverage: 28:263/264 of query aligns to 27:260/261 of 5jbxB
- active site: A67 (≠ G67), R72 (≠ M72), L84 (= L87), R88 (≠ N91), G112 (≠ A115), E115 (≠ S118), T134 (≠ A137), E135 (≠ Y138), I140 (≠ A143), P142 (= P145), G143 (≠ D146), A228 (≠ E231), L238 (≠ T241)
- binding coenzyme a: A28 (= A29), A65 (= A65), D68 (= D68), L69 (≠ V69), K70 (≠ S70), L110 (≠ A113), G111 (= G114), T134 (≠ A137), E135 (≠ Y138), L138 (≠ I141), R168 (≠ T171)
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, 95% coverage: 10:261/264 of query aligns to 17:266/273 of Q5HH38
- R34 (≠ L27) binding in other chain
- SGGD-Q 73:77 (≠ AGGDVS 65:70) binding in other chain
- S149 (≠ A143) binding in other chain
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: 10:261/264 of query aligns to 12:253/260 of 2uzfA
- active site: G70 (= G67), R80 (≠ I86), L84 (≠ V90), G108 (≠ A115), V111 (≠ S118), T130 (≠ A137), G131 (≠ Y138), S136 (≠ A143), D138 (≠ P145), A139 (≠ D146), A225 (≠ E233), Y233 (≠ T241)
- binding acetoacetyl-coenzyme a: V28 (≠ A26), R29 (≠ L27), S68 (≠ A65), G69 (= G66), G70 (= G67), D71 (= D68), Y104 (≠ V111), G108 (≠ A115)
3omeC Crystal structure of a probable enoyl-coa hydratase from mycobacterium smegmatis (see paper)
32% identity, 82% coverage: 4:220/264 of query aligns to 2:213/247 of 3omeC
- active site: H65 (≠ G67), E70 (vs. gap), A82 (≠ G80), L86 (= L87), G110 (≠ A115), L113 (≠ S118), V133 (= V136), I138 (= I141), G139 (= G142), E142 (≠ P145)
- binding zinc ion: E81 (≠ A79), E142 (≠ P145)
Sites not aligning to the query:
Query Sequence
>GFF4154 FitnessBrowser__Marino:GFF4154
MTDTLVTTAFDAGTGVARLTFNRPEALNAINVPLAEAFLAAVEHINSLSGVRCIVLAGAG
RAFMAGGDVSSMAGTSEQAGKAIGAILDAVNPAILLLRSMDAPVIAAVRGVAAGAGLSLT
LMADLVIAEEDAKFLVAYNGIGAVPDCGGSWALAHKLGAGRAAELMLLGRTLNAGEAKDW
GMVNEVVPASEFESRVNRMIEKVAKGPTRAFGAFRQLIDRANGDRLAAHLEAERVAFLEM
TRTEDFAEGVSAFLAKRPSGFRGC
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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