SitesBLAST
Comparing Dsui_0502 FitnessBrowser__PS:Dsui_0502 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)
41% identity, 99% coverage: 1:260/263 of query aligns to 2:254/257 of 6slbAAA
- active site: Q64 (≠ G62), F69 (= F67), L80 (≠ I86), N84 (≠ H90), A108 (≠ F114), S111 (= S117), A130 (= A136), F131 (≠ Y137), L136 (= L142), P138 (= P144), D139 (= D145), A224 (≠ F230), G234 (≠ S240)
- 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 (≠ E56), A62 (= A60), Q64 (≠ G62), D65 (= D63), L66 (= L64), Y76 (≠ F82), A108 (≠ F114), F131 (≠ Y137), D139 (= D145)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
41% identity, 98% coverage: 4:260/263 of query aligns to 2:242/245 of 6slaAAA
- active site: Q61 (≠ G62), L68 (≠ S69), N72 (≠ E83), A96 (≠ F114), S99 (= S117), A118 (= A136), F119 (≠ Y137), L124 (= L142), P126 (= P144), N127 (≠ D145), A212 (≠ F230), G222 (≠ S240)
- 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 (= L23), A59 (= A60), Q61 (≠ G62), D62 (= D63), L63 (= L64), L68 (≠ S69), Y71 (≠ F82), A94 (= A112), G95 (= G113), A96 (≠ F114), F119 (≠ Y137), I122 (= I140), L124 (= L142), N127 (≠ D145), F234 (= F252), K237 (= K255)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
35% identity, 99% coverage: 3:263/263 of query aligns to 5:259/259 of 5zaiC
- active site: A65 (≠ G62), F70 (= F67), S82 (≠ F82), R86 (≠ I86), G110 (≠ F114), E113 (≠ S117), P132 (≠ A136), E133 (≠ Y137), I138 (≠ L142), P140 (= P144), G141 (≠ D145), A226 (≠ F230), F236 (≠ S240)
- binding coenzyme a: K24 (≠ A22), L25 (= L23), A63 (= A60), G64 (= G61), A65 (≠ G62), D66 (= D63), I67 (≠ L64), P132 (≠ A136), R166 (= R170), F248 (= F252), K251 (= K255)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
36% identity, 94% coverage: 15:260/263 of query aligns to 19:251/254 of 2dubA
- active site: A67 (≠ G62), M72 (≠ F67), S82 (≠ A91), G105 (≠ F114), E108 (≠ S117), P127 (≠ A136), E128 (≠ Y137), T133 (≠ L142), P135 (= P144), G136 (≠ D145), K221 (≠ S224), F231 (= F236)
- binding octanoyl-coenzyme a: K25 (≠ E21), A26 (= A22), L27 (= L23), A29 (= A25), A65 (= A60), A67 (≠ G62), D68 (= D63), I69 (≠ L64), K70 (= K65), G105 (≠ F114), E108 (≠ S117), P127 (≠ A136), E128 (≠ Y137), G136 (≠ D145), A137 (≠ G146)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
36% identity, 94% coverage: 15:260/263 of query aligns to 20:255/258 of 1mj3A
- active site: A68 (≠ G62), M73 (≠ F67), S83 (≠ A87), L85 (≠ V89), G109 (≠ F114), E112 (≠ S117), P131 (≠ A136), E132 (≠ Y137), T137 (≠ L142), P139 (= P144), G140 (≠ D145), K225 (≠ S224), F235 (= F236)
- binding hexanoyl-coenzyme a: K26 (≠ E21), A27 (= A22), L28 (= L23), A30 (= A25), A66 (= A60), G67 (= G61), A68 (≠ G62), D69 (= D63), I70 (≠ L64), G109 (≠ F114), P131 (≠ A136), E132 (≠ Y137), L135 (≠ I140), G140 (≠ D145)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
35% identity, 94% coverage: 15:260/263 of query aligns to 18:255/258 of 1ey3A
- active site: A66 (≠ G62), M71 (≠ F67), S81 (≠ A87), L85 (≠ A91), G109 (≠ F114), E112 (≠ S117), P131 (≠ A136), E132 (≠ Y137), T137 (≠ L142), P139 (= P144), G140 (≠ D145), K225 (≠ S224), F235 (= F236)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ E21), L26 (= L23), A28 (= A25), A64 (= A60), G65 (= G61), A66 (≠ G62), D67 (= D63), I68 (≠ L64), L85 (≠ A91), W88 (≠ L94), G109 (≠ F114), P131 (≠ A136), L135 (≠ I140), G140 (≠ D145)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
35% identity, 94% coverage: 15:260/263 of query aligns to 20:257/260 of 1dubA
- active site: A68 (≠ G62), M73 (≠ F67), S83 (≠ A87), L87 (≠ A91), G111 (≠ F114), E114 (≠ S117), P133 (≠ A136), E134 (≠ Y137), T139 (≠ L142), P141 (= P144), G142 (≠ D145), K227 (≠ S224), F237 (= F236)
- binding acetoacetyl-coenzyme a: K26 (≠ E21), A27 (= A22), L28 (= L23), A30 (= A25), A66 (= A60), A68 (≠ G62), D69 (= D63), I70 (≠ L64), Y107 (≠ A110), G110 (= G113), G111 (≠ F114), E114 (≠ S117), P133 (≠ A136), E134 (≠ Y137), L137 (≠ I140), G142 (≠ D145), F233 (= F230), F249 (= F252)
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, 94% coverage: 15:260/263 of query aligns to 50:287/290 of P14604
- E144 (≠ S117) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (≠ Y137) 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
1nzyB 4-chlorobenzoyl coenzyme a dehalogenase from pseudomonas sp. Strain cbs-3 (see paper)
34% identity, 98% coverage: 1:257/263 of query aligns to 1:257/269 of 1nzyB
- active site: C61 (≠ M59), F64 (≠ G62), I69 (≠ L71), A86 (= A88), H90 (= H90), G114 (≠ F114), G117 (≠ S117), A136 (= A136), W137 (≠ Y137), I142 (≠ L142), N144 (≠ P144), D145 (= D145), E230 (≠ F230)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ E21), H23 (≠ A22), R24 (≠ L23), A62 (= A60), F64 (≠ G62), Y65 (≠ D63), L66 (= L64), R67 (≠ K65), W89 (vs. gap), G113 (= G113), G114 (≠ F114), A136 (= A136), W137 (≠ Y137), D145 (= D145), T146 (≠ G146), F252 (= F252), R257 (≠ K257)
- binding calcium ion: G49 (= G48), L202 (= L202), A203 (= A203), A205 (≠ G205), T207 (≠ R207), Q210 (≠ L210)
- binding phosphate ion: E57 (= E56), N108 (≠ S108), K188 (≠ A188), R192 (≠ E192)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
36% identity, 94% coverage: 15:260/263 of query aligns to 20:257/260 of 2hw5C
- active site: A68 (≠ G62), M73 (≠ F67), S83 (≠ R78), L87 (≠ F82), G111 (≠ F114), E114 (≠ S117), P133 (≠ A136), E134 (≠ Y137), T139 (≠ L142), P141 (= P144), G142 (≠ D145), K227 (≠ F230), F237 (≠ S240)
- binding crotonyl coenzyme a: K26 (≠ E21), A27 (= A22), L28 (= L23), A30 (= A25), K62 (≠ H57), I70 (≠ L64), F109 (≠ A112)
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, 98% coverage: 1:257/263 of query aligns to 1:257/269 of A5JTM5
- R24 (≠ L23) binding in other chain; mutation R->K,L: Does not strongly affect catalytic activity, but reduces substrate CoA binding.
- E34 (≠ D33) mutation to T: Forms inclusion bodies.
- E43 (= E42) mutation to A: No effect on catalytic activity.
- D45 (= D44) mutation to A: No effect on catalytic activity.
- D46 (≠ E45) mutation to A: No effect on catalytic activity.
- G63 (= G61) mutation G->A,I,P: Yields insoluble protein.
- F64 (≠ G62) 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 (≠ D63) mutation to D: Catalytic activity is almost as efficient as wild type.
- R67 (≠ K65) mutation to K: Reduces substrate CoA binding.; mutation to L: Forms inclusion bodies.
- E68 (≠ Q70) mutation to T: No effect on catalytic activity.
- H81 (≠ E83) mutation to Q: Loss of catalytic activity, substrate benzoyl group binding is not affected.
- F82 (≠ Q84) mutation to L: Retains catalytic activity, but substrate benzoyl group binding is decreased.
- W89 (vs. gap) mutation to F: Retains catalytic activity, but substrate benzoyl group binding is decreased.; mutation to Y: Reduced activity and substrate benzoyl group binding.
- H90 (= H90) 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 (≠ L94) mutation to Q: No effect on catalytic activity.
- A112 (= A112) 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 (= G113) 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 (≠ F114) mutation to A: Strongly reduced catalytic activity and substrate benzoyl group binding.; mutation to P: Unstable.
- G115 (= G115) mutation G->L,N,S,V: Yields insoluble protein.
- D123 (= D123) mutation to T: No effect on catalytic activity.
- D129 (= D129) mutation to T: No effect on catalytic activity.
- W137 (≠ Y137) mutation to F: Low catalytic activity, but KM unaffected (PubMed:8718880). Retains catalytic activity, but substrate benzoyl group binding is decreased (PubMed:9063883).
- D145 (= D145) active site, Nucleophile; mutation to A: Complete loss of catalytic activity, but not substrate binding.
- E163 (= E163) mutation to T: No effect on catalytic activity.
- E175 (≠ Q175) mutation to D: No effect on catalytic activity.
- W179 (= W179) mutation to F: No effect on catalytic activity.
- H208 (≠ Q208) mutation to Q: No effect on catalytic activity.
- R216 (≠ L216) mutation R->E,K,L: Yields insoluble protein.
- E232 (= E232) mutation E->A,N,Q,R: Yields insoluble protein.; mutation to D: Reduced catalytic activity, increased substrate binding.
- R257 (≠ K257) mutation to K: Retains catalytic activity and substrate CoA binding.; mutation to L: Significantly reduces catalytic activity and substrate CoA binding.
1jxzB Structure of the h90q mutant of 4-chlorobenzoyl-coenzyme a dehalogenase complexed with 4-hydroxybenzoyl-coenzyme a (product) (see paper)
33% identity, 98% coverage: 1:257/263 of query aligns to 1:257/269 of 1jxzB
- active site: C61 (≠ M59), F64 (≠ G62), I69 (≠ L71), A86 (= A88), Q90 (≠ T92), G113 (= G113), G114 (≠ F114), G117 (≠ S117), A136 (= A136), W137 (≠ Y137), I142 (≠ L142), N144 (≠ P144), D145 (= D145), E230 (≠ F230)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ E21), H23 (≠ A22), R24 (≠ L23), A62 (= A60), F64 (≠ G62), Y65 (≠ D63), L66 (= L64), R67 (≠ K65), W89 (≠ A91), G113 (= G113), A136 (= A136), W137 (≠ Y137), I142 (≠ L142), D145 (= D145), T146 (≠ G146), F252 (= F252), R257 (≠ K257)
- binding calcium ion: G49 (= G48), L202 (= L202), A203 (= A203), A205 (≠ G205), T207 (≠ R207), Q210 (≠ L210)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
33% identity, 99% coverage: 3:263/263 of query aligns to 4:256/256 of 3h81A
- active site: A64 (≠ G62), M69 (≠ F67), T79 (≠ R78), F83 (= F82), G107 (≠ F114), E110 (≠ S117), P129 (≠ A136), E130 (≠ Y137), V135 (≠ L142), P137 (= P144), G138 (≠ D145), L223 (≠ F230), F233 (≠ S240)
- binding calcium ion: F233 (≠ S240), Q238 (≠ F245)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
33% identity, 98% coverage: 3:260/263 of query aligns to 5:254/255 of 3q0jC
- active site: A65 (≠ G62), M70 (≠ F67), T80 (≠ R78), F84 (= F82), G108 (≠ F114), E111 (≠ S117), P130 (≠ A136), E131 (≠ Y137), V136 (≠ L142), P138 (= P144), G139 (≠ D145), L224 (≠ F230), F234 (≠ S240)
- binding acetoacetyl-coenzyme a: Q23 (≠ E21), A24 (= A22), L25 (= L23), A27 (= A25), A63 (= A60), G64 (= G61), A65 (≠ G62), D66 (= D63), I67 (≠ L64), K68 (= K65), M70 (≠ F67), F84 (= F82), G107 (= G113), G108 (≠ F114), E111 (≠ S117), P130 (≠ A136), E131 (≠ Y137), P138 (= P144), G139 (≠ D145), M140 (≠ G146)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
33% identity, 98% coverage: 3:260/263 of query aligns to 5:254/255 of 3q0gC
- active site: A65 (≠ G62), M70 (≠ F67), T80 (≠ R78), F84 (= F82), G108 (≠ F114), E111 (≠ S117), P130 (≠ A136), E131 (≠ Y137), V136 (≠ L142), P138 (= P144), G139 (≠ D145), L224 (≠ F230), F234 (≠ S240)
- binding coenzyme a: L25 (= L23), A63 (= A60), I67 (≠ L64), K68 (= K65), Y104 (≠ A110), P130 (≠ A136), E131 (≠ Y137), L134 (≠ I140)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
32% identity, 98% coverage: 3:260/263 of query aligns to 4:249/250 of 3q0gD
- active site: A64 (≠ G62), M69 (≠ F67), T75 (≠ I86), F79 (≠ H90), G103 (≠ F114), E106 (≠ S117), P125 (≠ A136), E126 (≠ Y137), V131 (≠ L142), P133 (= P144), G134 (≠ D145), L219 (≠ F230), F229 (≠ S240)
- binding Butyryl Coenzyme A: F225 (= F236), F241 (= F252)
Q7CQ56 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
33% identity, 96% coverage: 10:262/263 of query aligns to 32:280/285 of Q7CQ56
4elxA Structure of apo e.Coli. 1,4-dihydroxy-2- naphthoyl coa synthases with cl (see paper)
32% identity, 96% coverage: 10:262/263 of query aligns to 29:263/268 of 4elxA
- active site: G83 (= G62), H88 (≠ Q70), L92 (≠ P74), G116 (≠ F114), V119 (≠ S117), G139 (≠ Y137), S144 (≠ L142), D146 (≠ P144), G147 (≠ D145), A233 (≠ S221), Y241 (≠ L229)
- binding chloride ion: G115 (= G113), G139 (≠ Y137), W167 (≠ A165)
4elwA Structure of e. Coli. 1,4-dihydroxy-2- naphthoyl coenzyme a synthases (menb) in complex with nitrate (see paper)
32% identity, 96% coverage: 10:262/263 of query aligns to 29:262/267 of 4elwA
- active site: G83 (= G62), L91 (≠ H90), G115 (≠ F114), V118 (≠ S117), G138 (≠ Y137), S143 (≠ L142), D145 (≠ P144), G146 (≠ D145), A232 (≠ S221), Y240 (≠ L229)
- binding nitrate ion: G114 (= G113), T137 (≠ A136), G138 (≠ Y137), F144 (≠ S143), W166 (≠ A165)
4i42A E.Coli. 1,4-dihydroxy-2-naphthoyl coenzyme a synthase (ecmenb) in complex with 1-hydroxy-2-naphthoyl-coa (see paper)
32% identity, 96% coverage: 10:262/263 of query aligns to 32:280/285 of 4i42A
- active site: G86 (= G62), R91 (≠ A76), Y97 (≠ F82), H105 (= H90), L109 (= L94), G133 (≠ F114), V136 (≠ S117), G156 (≠ Y137), S161 (≠ L142), D163 (≠ P144), G164 (≠ D145), A250 (≠ S221), Y258 (≠ L229)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (≠ A22), R45 (≠ L23), S84 (≠ A60), G85 (= G61), G86 (= G62), D87 (= D63), Q88 (≠ L64), K89 (= K65), Y97 (≠ F82), V108 (≠ T93), Y129 (≠ A110), G133 (≠ F114), T155 (≠ A136), S161 (≠ L142), T254 (≠ L225), F270 (= F252), K273 (= K255)
Query Sequence
>Dsui_0502 FitnessBrowser__PS:Dsui_0502
MSTVLSHLEDGVLTLTLNRPEALNALNLAMIEDLRAATARAEHDEAVGAVVLRGGEHFMA
GGDLKWFHSQLALPPAERQALFEQTIAAVHATTLQVRRMGKPVVASVSGAAAGFGLSLML
ACDLAVAADNAYFTLAYCHIGLSPDGGATWFLPRAVGAKRAAEIALLGDRFDAAQAREWG
LINRVVPAAELEAESAKLARRLAAGPRQALARTKALLQASSGNSLPEQLFAEQGNFAACS
VHPDFAEGLGAFLEKRKPAFGQK
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