SitesBLAST
Comparing Dsui_2041 FitnessBrowser__PS:Dsui_2041 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)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
33% identity, 92% coverage: 18:258/261 of query aligns to 17:256/259 of 5zaiC
- active site: A65 (≠ H66), F70 (≠ M71), S82 (≠ E86), R86 (= R90), G110 (≠ A113), E113 (≠ Q116), P132 (= P135), E133 (≠ G136), I138 (≠ L141), P140 (≠ C143), G141 (≠ S144), A226 (= A228), F236 (≠ L238)
- binding coenzyme a: K24 (≠ A25), L25 (≠ R26), A63 (= A64), G64 (= G65), A65 (≠ H66), D66 (= D67), I67 (≠ L68), P132 (= P135), R166 (≠ L168), F248 (= F250), K251 (= K253)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
32% identity, 99% coverage: 3:260/261 of query aligns to 3:255/256 of 3h81A
- active site: A64 (≠ H66), M69 (= M71), T79 (≠ A81), F83 (= F85), G107 (≠ A113), E110 (≠ Q116), P129 (= P135), E130 (≠ G136), V135 (≠ L141), P137 (= P146), G138 (≠ M147), L223 (≠ A228), F233 (≠ L238)
- binding calcium ion: F233 (≠ L238), Q238 (≠ A243)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
32% identity, 98% coverage: 3:259/261 of query aligns to 4:255/255 of 3q0jC
- active site: A65 (≠ H66), M70 (= M71), T80 (≠ A81), F84 (= F85), G108 (≠ A113), E111 (≠ Q116), P130 (= P135), E131 (≠ G136), V136 (≠ L141), P138 (= P146), G139 (≠ M147), L224 (≠ A228), F234 (≠ L238)
- binding acetoacetyl-coenzyme a: Q23 (≠ A24), A24 (= A25), L25 (≠ R26), A27 (= A28), A63 (= A64), G64 (= G65), A65 (≠ H66), D66 (= D67), I67 (≠ L68), K68 (= K69), M70 (= M71), F84 (= F85), G107 (≠ A112), G108 (≠ A113), E111 (≠ Q116), P130 (= P135), E131 (≠ G136), P138 (= P146), G139 (≠ M147), M140 (≠ V148)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
32% identity, 98% coverage: 3:259/261 of query aligns to 4:255/255 of 3q0gC
- active site: A65 (≠ H66), M70 (= M71), T80 (≠ A81), F84 (= F85), G108 (≠ A113), E111 (≠ Q116), P130 (= P135), E131 (≠ G136), V136 (≠ L141), P138 (= P146), G139 (≠ M147), L224 (≠ A228), F234 (≠ L238)
- binding coenzyme a: L25 (≠ R26), A63 (= A64), I67 (≠ L68), K68 (= K69), Y104 (≠ I109), P130 (= P135), E131 (≠ G136), L134 (≠ I139)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
32% identity, 98% coverage: 3:259/261 of query aligns to 3:250/250 of 3q0gD
- active site: A64 (≠ H66), M69 (= M71), T75 (≠ A81), F79 (= F85), G103 (≠ A113), E106 (≠ Q116), P125 (= P135), E126 (≠ G136), V131 (≠ L141), P133 (= P146), G134 (≠ M147), L219 (≠ A228), F229 (≠ L238)
- binding Butyryl Coenzyme A: F225 (≠ M234), F241 (= F250)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
31% identity, 96% coverage: 9:258/261 of query aligns to 11:257/260 of 2hw5C
- active site: A68 (≠ H66), M73 (= M71), S83 (≠ A81), L87 (≠ F85), G111 (≠ A113), E114 (≠ Q116), P133 (= P135), E134 (≠ G136), T139 (≠ S144), P141 (= P146), G142 (≠ M147), K227 (≠ A228), F237 (≠ L238)
- binding crotonyl coenzyme a: K26 (≠ A24), A27 (= A25), L28 (≠ R26), A30 (= A28), K62 (≠ P60), I70 (≠ L68), F109 (≠ T111)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
31% identity, 93% coverage: 15:258/261 of query aligns to 16:251/254 of 2dubA
- active site: A67 (≠ H66), M72 (= M71), S82 (≠ R90), G105 (≠ A113), E108 (≠ Q116), P127 (= P135), E128 (≠ G136), T133 (≠ L141), P135 (≠ C143), G136 (≠ S144), K221 (≠ A228), F231 (≠ L238)
- binding octanoyl-coenzyme a: K25 (≠ A24), A26 (= A25), L27 (≠ R26), A29 (= A28), A65 (= A64), A67 (≠ H66), D68 (= D67), I69 (≠ L68), K70 (= K69), G105 (≠ A113), E108 (≠ Q116), P127 (= P135), E128 (≠ G136), G136 (≠ S144), A137 (≠ T145)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
30% identity, 93% coverage: 15:258/261 of query aligns to 15:255/258 of 1ey3A
- active site: A66 (≠ H66), M71 (= M71), S81 (≠ A81), L85 (≠ F85), G109 (≠ A113), E112 (≠ Q116), P131 (= P135), E132 (≠ G136), T137 (≠ L141), P139 (≠ C143), G140 (≠ S144), K225 (≠ A228), F235 (≠ L238)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ A24), L26 (≠ R26), A28 (= A28), A64 (= A64), G65 (= G65), A66 (≠ H66), D67 (= D67), I68 (≠ L68), L85 (≠ F85), W88 (≠ M92), G109 (≠ A113), P131 (= P135), L135 (≠ I139), G140 (≠ S144)
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, 93% coverage: 15:258/261 of query aligns to 47:287/290 of P14604
- E144 (≠ Q116) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (≠ G136) 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
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
30% identity, 93% coverage: 15:258/261 of query aligns to 17:257/260 of 1dubA
- active site: A68 (≠ H66), M73 (= M71), S83 (≠ A81), L87 (≠ F85), G111 (≠ A113), E114 (≠ Q116), P133 (= P135), E134 (≠ G136), T139 (≠ L141), P141 (≠ C143), G142 (≠ S144), K227 (≠ A228), F237 (≠ L238)
- binding acetoacetyl-coenzyme a: K26 (≠ A24), A27 (= A25), L28 (≠ R26), A30 (= A28), A66 (= A64), A68 (≠ H66), D69 (= D67), I70 (≠ L68), Y107 (≠ I109), G110 (≠ A112), G111 (≠ A113), E114 (≠ Q116), P133 (= P135), E134 (≠ G136), L137 (≠ I139), G142 (≠ S144), F233 (≠ M234), F249 (= F250)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
31% identity, 93% coverage: 15:258/261 of query aligns to 17:255/258 of 1mj3A
- active site: A68 (≠ H66), M73 (= M71), S83 (≠ E86), L85 (≠ C88), G109 (≠ A113), E112 (≠ Q116), P131 (= P135), E132 (≠ G136), T137 (≠ L141), P139 (≠ C143), G140 (≠ S144), K225 (≠ A228), F235 (≠ L238)
- binding hexanoyl-coenzyme a: K26 (≠ A24), A27 (= A25), L28 (≠ R26), A30 (= A28), A66 (= A64), G67 (= G65), A68 (≠ H66), D69 (= D67), I70 (≠ L68), G109 (≠ A113), P131 (= P135), E132 (≠ G136), L135 (≠ I139), G140 (≠ S144)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
32% identity, 97% coverage: 6:258/261 of query aligns to 4:254/257 of 6slbAAA
- active site: Q64 (≠ H66), F69 (≠ Y76), L80 (≠ A89), N84 (≠ Q93), A108 (= A113), S111 (≠ Q116), A130 (≠ P135), F131 (≠ G136), L136 (= L141), P138 (≠ C143), D139 (≠ S144), A224 (= A228), G234 (≠ L238)
- 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 (≠ P60), A62 (= A64), Q64 (≠ H66), D65 (= D67), L66 (= L68), Y76 (≠ F85), A108 (= A113), F131 (≠ G136), D139 (≠ S144)
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)
32% identity, 93% coverage: 12:254/261 of query aligns to 16:265/276 of O69762
- K29 (≠ A25) binding
- A68 (= A64) binding
- M70 (≠ H66) binding
- L72 (= L68) binding
- Y75 (vs. gap) binding
- G120 (≠ A113) binding
- S123 (≠ Q116) mutation to A: Reduced kcat compared to wild-type but not markerdly.
- S142 (≠ P135) binding
- E143 (≠ G136) mutation to A: Abolishes catalytic activity.
- W146 (≠ I139) binding
- G151 (≠ S144) binding
- Y239 (= Y229) 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
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
34% identity, 98% coverage: 4:258/261 of query aligns to 9:263/266 of O53561
- K135 (≠ R131) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 131:141, 18% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (≠ L141) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
30% identity, 97% coverage: 6:258/261 of query aligns to 1:242/245 of 6slaAAA
- active site: Q61 (≠ H66), L68 (≠ G73), N72 (≠ G77), A96 (= A113), S99 (≠ Q116), A118 (≠ P135), F119 (≠ G136), L124 (= L141), P126 (≠ C143), N127 (≠ S144), A212 (= A228), G222 (≠ L238)
- 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 (≠ R26), A59 (= A64), Q61 (≠ H66), D62 (= D67), L63 (= L68), L68 (≠ G73), Y71 (= Y76), A94 (≠ T111), G95 (≠ A112), A96 (= A113), F119 (≠ G136), I122 (= I139), L124 (= L141), N127 (≠ S144), F234 (= F250), K237 (= K253)
2vssB Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
33% identity, 84% coverage: 12:231/261 of query aligns to 13:238/247 of 2vssB
- active site: M67 (≠ H66), Y72 (vs. gap), D77 (= D75), R89 (≠ E86), Q93 (≠ R90), G117 (≠ A113), S120 (≠ Q116), S139 (≠ P135), E140 (≠ G136), I145 (≠ L141), P147 (≠ C143), G148 (≠ S144), Y236 (= Y229)
- binding acetyl coenzyme *a: E25 (≠ A24), K26 (≠ A25), R27 (= R26), A29 (= A28), A65 (= A64), M67 (≠ H66), D68 (= D67), W113 (≠ I109), F115 (≠ T111), G117 (≠ A113), S139 (≠ P135), E140 (≠ G136)
Sites not aligning to the query:
2vssD Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
33% identity, 84% coverage: 12:231/261 of query aligns to 14:239/246 of 2vssD
- active site: M68 (≠ H66), Y73 (vs. gap), D78 (= D75), R90 (≠ E86), Q94 (≠ R90), G118 (≠ A113), S121 (≠ Q116), S140 (≠ P135), E141 (≠ G136), I146 (≠ L141), P148 (≠ C143), G149 (≠ S144), Y237 (= Y229)
- binding acetyl coenzyme *a: E26 (≠ A24), K27 (≠ A25), R28 (= R26), A30 (= A28), A66 (= A64), M68 (≠ H66), D69 (= D67), L70 (= L68), F74 (≠ M71), W114 (≠ I109), F116 (≠ T111), S140 (≠ P135)
- binding 4-hydroxy-3-methoxybenzaldehyde: M68 (≠ H66), Y73 (vs. gap), F74 (≠ M71), Q96 (≠ M92), E141 (≠ G136), G149 (≠ S144), N150 (≠ T145)
Q4WF54 Mevalonyl-coenzyme A hydratase sidH; Siderophore biosynthesis protein H; EC 4.2.1.- from Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata) (see paper)
31% identity, 93% coverage: 15:258/261 of query aligns to 21:265/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
Q5HH38 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Staphylococcus aureus (strain COL) (see paper)
33% identity, 93% coverage: 13:256/261 of query aligns to 21:264/273 of Q5HH38
- R34 (= R26) binding in other chain
- SGGDQ 73:77 (≠ AGHDL 64:68) binding in other chain
- S149 (≠ L141) binding in other chain
3p85A Crystal structure enoyl-coa hydratase from mycobacterium avium (see paper)
33% identity, 93% coverage: 6:248/261 of query aligns to 2:222/224 of 3p85A
- active site: L62 (≠ H66), L67 (≠ M71), P68 (≠ A74), G92 (≠ A113), E95 (≠ Q116), T114 (≠ P135), H115 (≠ G136), L120 (= L141), P122 (≠ C143), T123 (≠ S144), W208 (≠ M234), T219 (≠ E245)
- binding calcium ion: D43 (vs. gap), D45 (vs. gap)
Query Sequence
>Dsui_2041 FitnessBrowser__PS:Dsui_2041
MSEEALVLRQDKDGIARLTLNRPAARNALSRPMIAALQAEFDRIAADPSIGVVILAGNGP
AFCAGHDLKEMRGADYGERYAEDLFEACARLMQRIVSLPQPVIARVHGIATAAGAQLVAS
ADLAIATDDARFATPGVNIGLFCSTPMVALSRNISHKHALQMLLTGDLIDAPTALRFGLI
NEHVSGEQLDVAVEALAVKIASKSRHTLAVGKAAYYRQAELPLDEAYAYAKGVMVHNLQA
RDAREGIDAFIDKRHPTWCHG
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