SitesBLAST
Comparing 3607896 FitnessBrowser__Dino:3607896 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)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
30% identity, 97% coverage: 4:257/262 of query aligns to 3:253/259 of 5zaiC
- active site: A65 (≠ G67), F70 (≠ M72), S82 (= S84), R86 (= R88), G110 (= G115), E113 (≠ G118), P132 (≠ T137), E133 (= E138), I138 (≠ L143), P140 (= P145), G141 (≠ A146), A226 (= A234), F236 (vs. gap)
- binding coenzyme a: K24 (= K26), L25 (≠ H27), A63 (= A65), G64 (= G66), A65 (≠ G67), D66 (= D68), I67 (≠ L69), P132 (≠ T137), R166 (≠ L170), F248 (= F252), K251 (= K255)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
31% identity, 98% coverage: 4:260/262 of query aligns to 3:254/255 of 3q0jC
- active site: A65 (≠ G67), M70 (= M72), T80 (= T82), F84 (≠ L94), G108 (= G115), E111 (≠ G118), P130 (≠ T137), E131 (= E138), V136 (≠ L143), P138 (= P145), G139 (≠ A146), L224 (= L236), F234 (≠ W240)
- binding acetoacetyl-coenzyme a: Q23 (≠ D25), A24 (≠ K26), L25 (≠ H27), A27 (= A29), A63 (= A65), G64 (= G66), A65 (≠ G67), D66 (= D68), I67 (≠ L69), K68 (≠ G70), M70 (= M72), F84 (≠ L94), G107 (= G114), G108 (= G115), E111 (≠ G118), P130 (≠ T137), E131 (= E138), P138 (= P145), G139 (≠ A146), M140 (≠ T147)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
31% identity, 98% coverage: 4:260/262 of query aligns to 3:254/255 of 3q0gC
- active site: A65 (≠ G67), M70 (= M72), T80 (= T82), F84 (≠ L94), G108 (= G115), E111 (≠ G118), P130 (≠ T137), E131 (= E138), V136 (≠ L143), P138 (= P145), G139 (≠ A146), L224 (= L236), F234 (≠ W240)
- binding coenzyme a: L25 (≠ H27), A63 (= A65), I67 (≠ L69), K68 (≠ G70), Y104 (≠ Q111), P130 (≠ T137), E131 (= E138), L134 (= L141)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
31% identity, 98% coverage: 4:260/262 of query aligns to 2:253/256 of 3h81A
- active site: A64 (≠ G67), M69 (= M72), T79 (= T82), F83 (≠ L94), G107 (= G115), E110 (≠ G118), P129 (≠ T137), E130 (= E138), V135 (≠ L143), P137 (= P145), G138 (≠ A146), L223 (= L236), F233 (≠ W240)
- binding calcium ion: F233 (≠ W240), Q238 (≠ A245)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
31% identity, 98% coverage: 4:260/262 of query aligns to 2:249/250 of 3q0gD
- active site: A64 (≠ G67), M69 (= M76), T75 (= T82), F79 (≠ L94), G103 (= G115), E106 (≠ G118), P125 (≠ T137), E126 (= E138), V131 (≠ L143), P133 (= P145), G134 (≠ A146), L219 (= L236), F229 (≠ W240)
- binding Butyryl Coenzyme A: F225 (vs. gap), F241 (= F252)
6l3pA Crystal strcuture of feruloyl-coa hydratase lyase(fchl) complexed with coa
32% identity, 88% coverage: 3:232/262 of query aligns to 6:239/244 of 6l3pA
- active site: M69 (≠ G67), Y74 (≠ W71), R86 (≠ E86), Q90 (≠ L90), G114 (= G115), S117 (≠ G118), S136 (≠ T137), E137 (= E138), I142 (≠ L143), P144 (= P145), G145 (≠ A146), Y233 (≠ E226)
- binding coenzyme a: K28 (= K26), R29 (≠ H27), A31 (= A29), A67 (= A65), M69 (≠ G67), D70 (= D68), L71 (= L69), G113 (= G114)
Sites not aligning to the query:
Q8GYN9 1,4-dihydroxy-2-naphthoyl-CoA synthase, peroxisomal; DHNS; Enoyl-CoA hydratase/isomerase D; ECHID; Naphthoate synthase; EC 4.1.3.36 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
31% identity, 77% coverage: 15:215/262 of query aligns to 86:286/337 of Q8GYN9
Sites not aligning to the query:
- 20 H→V: Loss of peroxisomal targeting.
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
34% identity, 95% coverage: 8:256/262 of query aligns to 6:254/261 of 5jbxB
- active site: A67 (≠ G67), R72 (= R73), L84 (vs. gap), R88 (≠ A91), G112 (= G115), E115 (≠ G118), T134 (= T137), E135 (= E138), I140 (≠ L143), P142 (= P145), G143 (≠ A146), A228 (≠ D230), L238 (≠ W240)
- binding coenzyme a: S24 (≠ D25), R25 (≠ K26), R26 (≠ H27), A28 (= A29), A65 (= A65), D68 (= D68), L69 (= L69), K70 (≠ G70), L110 (≠ F113), G111 (= G114), T134 (= T137), E135 (= E138), L138 (= L141), R168 (≠ L170)
Q62651 Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial; EC 5.3.3.- from Rattus norvegicus (Rat) (see paper)
32% identity, 81% coverage: 3:214/262 of query aligns to 53:275/327 of Q62651
- D176 (≠ G118) mutation D->A,D: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- E196 (= E138) mutation E->D,Q: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- D204 (vs. gap) mutation D->A,N: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
2vssB Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
30% identity, 88% coverage: 3:232/262 of query aligns to 4:242/247 of 2vssB
- active site: M67 (≠ G67), Y72 (≠ M72), D77 (≠ A77), R89 (≠ S89), Q93 (≠ M93), G117 (= G115), S120 (≠ G118), S139 (≠ T137), E140 (= E138), I145 (≠ L143), P147 (= P145), G148 (≠ A146), Y236 (≠ E226)
- binding acetyl coenzyme *a: E25 (≠ D25), K26 (= K26), R27 (≠ H27), A29 (= A29), A65 (= A65), M67 (≠ G67), D68 (= D68), W113 (≠ Q111), F115 (= F113), G117 (= G115), S139 (≠ T137), E140 (= E138)
Sites not aligning to the query:
3t88A Crystal structure of escherichia coli menb in complex with substrate analogue, osb-ncoa (see paper)
27% identity, 99% coverage: 4:262/262 of query aligns to 18:276/281 of 3t88A
- active site: G82 (= G67), R87 (= R73), Y93 (≠ D79), H101 (≠ A87), L105 (≠ A91), G129 (= G115), V132 (≠ G118), G152 (≠ E138), S157 (≠ L143), D159 (≠ P145), G160 (≠ A146), A246 (≠ D230), Y254 (≠ W240)
- binding o-succinylbenzoyl-N-coenzyme A: Q39 (≠ D25), V40 (≠ K26), R41 (≠ H27), A43 (= A29), S80 (≠ A65), G81 (= G66), G82 (= G67), D83 (= D68), Q84 (≠ L69), K85 (≠ G70), Y93 (≠ D79), V104 (≠ L90), L105 (≠ A91), Y125 (≠ Q111), G129 (= G115), T151 (= T137), V155 (≠ L141), F158 (≠ I144), D159 (≠ P145), T250 (≠ A234), Y254 (≠ W240), F266 (= F252), K269 (= K255)
2vssD Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
30% identity, 88% coverage: 3:232/262 of query aligns to 5:243/246 of 2vssD
- active site: M68 (≠ G67), Y73 (≠ M72), D78 (≠ A77), R90 (≠ S89), Q94 (≠ M93), G118 (= G115), S121 (≠ G118), S140 (≠ T137), E141 (= E138), I146 (≠ L143), P148 (= P145), G149 (≠ A146), Y237 (≠ E226)
- binding acetyl coenzyme *a: E26 (≠ D25), K27 (= K26), R28 (≠ H27), A30 (= A29), A66 (= A65), M68 (≠ G67), D69 (= D68), L70 (= L69), F74 (≠ R73), W114 (≠ Q111), F116 (= F113), S140 (≠ T137)
- binding 4-hydroxy-3-methoxybenzaldehyde: M68 (≠ G67), Y73 (≠ M72), F74 (≠ R73), Q96 (≠ A96), E141 (= E138), G149 (≠ A146), N150 (≠ T147)
4i42A E.Coli. 1,4-dihydroxy-2-naphthoyl coenzyme a synthase (ecmenb) in complex with 1-hydroxy-2-naphthoyl-coa (see paper)
27% identity, 99% coverage: 4:262/262 of query aligns to 22:280/285 of 4i42A
- active site: G86 (= G67), R91 (= R73), Y97 (≠ D79), H105 (≠ A87), L109 (≠ A91), G133 (= G115), V136 (≠ G118), G156 (≠ E138), S161 (≠ L143), D163 (≠ P145), G164 (≠ A146), A250 (≠ D230), Y258 (≠ W240)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (≠ K26), R45 (≠ H27), S84 (≠ A65), G85 (= G66), G86 (= G67), D87 (= D68), Q88 (≠ L69), K89 (≠ G70), Y97 (≠ D79), V108 (≠ L90), Y129 (≠ Q111), G133 (= G115), T155 (= T137), S161 (≠ L143), T254 (≠ A234), F270 (= F252), K273 (= K255)
P0ABU0 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Escherichia coli (strain K12) (see 4 papers)
27% identity, 99% coverage: 4:262/262 of query aligns to 22:280/285 of P0ABU0
- R45 (≠ H27) binding in other chain
- SGGDQK 84:89 (≠ AGGDLG 65:70) binding in other chain
- K89 (≠ G70) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- R91 (= R73) mutation to A: Loss of DHNA-CoA synthase activity.
- Y97 (≠ D79) binding in other chain; mutation to F: Loss of DHNA-CoA synthase activity.
- YSIGG 129:133 (≠ QAFGG 111:115) binding in other chain
- Q154 (≠ L136) mutation to A: Reduces the specific DHNA-CoA synthase activity by 15-fold, whereas its affinity for hydrogencarbonate is reduced by 36-fold.
- QTG 154:156 (≠ LTE 136:138) binding
- T155 (= T137) binding in other chain
- G156 (≠ E138) mutation to D: Loss of DHNA-CoA synthase activity.
- S161 (≠ L143) binding in other chain
- W184 (≠ F165) mutation to F: Reduces the specific DHNA-CoA synthase activity by 530-fold, whereas its affinity for hydrogencarbonate is reduced by 20-fold.
- Y258 (≠ W240) binding
- R267 (≠ I249) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- F270 (= F252) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- K273 (= K255) binding ; mutation to A: Impairs protein folding.
O69762 Hydroxycinnamoyl-CoA hydratase-lyase; HCHL; P-hydroxycinnamoyl CoA hydratase/lyase; Trans-feruloyl-CoA hydratase/vanillin synthase; EC 4.1.2.61 from Pseudomonas fluorescens (see 2 papers)
30% identity, 88% coverage: 3:232/262 of query aligns to 7:245/276 of O69762
- K29 (= K26) binding
- A68 (= A65) binding
- M70 (≠ G67) binding
- L72 (= L69) binding
- Y75 (≠ M72) binding
- G120 (= G115) binding
- S123 (≠ G118) mutation to A: Reduced kcat compared to wild-type but not markerdly.
- S142 (≠ T137) binding
- E143 (= E138) mutation to A: Abolishes catalytic activity.
- W146 (≠ L141) binding
- G151 (≠ A146) binding
- Y239 (≠ E226) binding ; mutation to F: Increased KM for feruloyl-CoA but retains a significant amount of catalytic activity with a kcat 10 times less than that of the wild-type.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
28% identity, 98% coverage: 3:260/262 of query aligns to 2:257/260 of 1dubA
- active site: A68 (≠ G67), M73 (= M72), S83 (≠ T82), L87 (= L94), G111 (= G115), E114 (≠ G118), P133 (≠ T137), E134 (= E138), T139 (≠ L143), P141 (= P145), G142 (≠ A146), K227 (≠ T223), F237 (≠ V233)
- binding acetoacetyl-coenzyme a: K26 (≠ D25), A27 (≠ K26), L28 (≠ H27), A30 (= A29), A66 (= A65), A68 (≠ G67), D69 (= D68), I70 (≠ L69), Y107 (≠ Q111), G110 (= G114), G111 (= G115), E114 (≠ G118), P133 (≠ T137), E134 (= E138), L137 (= L141), G142 (≠ A146), F233 (≠ I229), 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)
28% identity, 98% coverage: 3:260/262 of query aligns to 32:287/290 of P14604
- E144 (≠ G118) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E138) 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)
28% identity, 98% coverage: 4:260/262 of query aligns to 1:255/258 of 1ey3A
- active site: A66 (≠ G67), M71 (= M72), S81 (≠ T82), L85 (= L94), G109 (= G115), E112 (≠ G118), P131 (≠ T137), E132 (= E138), T137 (≠ L143), P139 (= P145), G140 (≠ A146), K225 (≠ T223), F235 (≠ V233)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ D25), L26 (≠ H27), A28 (= A29), A64 (= A65), G65 (= G66), A66 (≠ G67), D67 (= D68), I68 (≠ L69), L85 (= L94), W88 (= W97), G109 (= G115), P131 (≠ T137), L135 (= L141), G140 (≠ A146)
3p85A Crystal structure enoyl-coa hydratase from mycobacterium avium (see paper)
34% identity, 75% coverage: 16:212/262 of query aligns to 11:190/224 of 3p85A
- active site: L62 (≠ G67), L67 (≠ M72), P68 (= P80), G92 (= G115), E95 (≠ G118), T114 (= T137), H115 (≠ E138), L120 (= L143), P122 (= P145), T123 (≠ A146)
- binding calcium ion: D43 (= D48), D45 (≠ A50)
Sites not aligning to the query:
2uzfA Crystal structure of staphylococcus aureus 1,4-dihydroxy-2-naphthoyl coa synthase (menb) in complex with acetoacetyl coa (see paper)
31% identity, 92% coverage: 15:256/262 of query aligns to 17:249/260 of 2uzfA
- active site: G70 (= G67), R80 (= R83), L84 (≠ R88), G108 (= G115), V111 (≠ G118), T130 (= T137), G131 (≠ E138), S136 (≠ L143), D138 (≠ P145), A139 (= A146), A225 (vs. gap), Y233 (≠ W240)
- binding acetoacetyl-coenzyme a: V28 (≠ K26), R29 (≠ H27), S68 (≠ A65), G69 (= G66), G70 (= G67), D71 (= D68), Y104 (≠ Q111), G108 (= G115)
Query Sequence
>3607896 FitnessBrowser__Dino:3607896
MTRFETLEVARDGRGVVTVTLARPDKHNAMNAAMIAELHGLARSLAADAAVRVVVLTGAG
RSFCAGGDLGWMRAQMAADPDTRSREARSLAQMLGAWNTLPKPVIGRIQGQAFGGGVGLM
AVCDVAVGVQDARFGLTETRLGLIPATIGPYVVARMGQACARRVFMSARLFDGAEAVRLG
LLARAVPEAELDAAVEAEVAPYLAVAPGAVAAAKALTLELGGTVTEAQIDATVAALRERW
ESDEAAEGIAAFFDKRKARWAS
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