SitesBLAST
Comparing H281DRAFT_01179 FitnessBrowser__Burk376:H281DRAFT_01179 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)
35% identity, 100% coverage: 1:257/257 of query aligns to 1:259/259 of 5zaiC
- active site: A65 (= A65), F70 (≠ R70), S82 (≠ H83), R86 (= R87), G110 (≠ A111), E113 (≠ G114), P132 (= P133), E133 (= E134), I138 (≠ L139), P140 (vs. gap), G141 (vs. gap), A226 (≠ R224), F236 (≠ S234)
- binding coenzyme a: K24 (= K24), L25 (≠ R25), A63 (= A63), G64 (= G64), A65 (= A65), D66 (= D66), I67 (≠ L67), P132 (= P133), R166 (≠ K164), F248 (= F246), K251 (= K249)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
34% identity, 99% coverage: 1:255/257 of query aligns to 1:255/255 of 3q0jC
- active site: A65 (= A65), M70 (≠ R70), T80 (≠ P80), F84 (≠ R84), G108 (≠ A111), E111 (≠ G114), P130 (= P133), E131 (= E134), V136 (≠ L139), P138 (vs. gap), G139 (vs. gap), L224 (≠ R224), F234 (≠ S234)
- binding acetoacetyl-coenzyme a: Q23 (≠ E23), A24 (≠ K24), L25 (≠ R25), A27 (= A27), A63 (= A63), G64 (= G64), A65 (= A65), D66 (= D66), I67 (≠ L67), K68 (≠ T68), M70 (≠ R70), F84 (≠ R84), G107 (= G110), G108 (≠ A111), E111 (≠ G114), P130 (= P133), E131 (= E134), P138 (vs. gap), G139 (vs. gap), M140 (≠ A140)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
34% identity, 99% coverage: 1:255/257 of query aligns to 1:255/255 of 3q0gC
- active site: A65 (= A65), M70 (≠ R70), T80 (≠ P80), F84 (≠ R84), G108 (≠ A111), E111 (≠ G114), P130 (= P133), E131 (= E134), V136 (≠ L139), P138 (vs. gap), G139 (vs. gap), L224 (≠ R224), F234 (≠ S234)
- binding coenzyme a: L25 (≠ R25), A63 (= A63), I67 (≠ L67), K68 (≠ T68), Y104 (≠ A107), P130 (= P133), E131 (= E134), L134 (≠ V137)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
34% identity, 99% coverage: 3:257/257 of query aligns to 2:256/256 of 3h81A
- active site: A64 (= A65), M69 (≠ R70), T79 (≠ P80), F83 (≠ R84), G107 (≠ A111), E110 (≠ G114), P129 (= P133), E130 (= E134), V135 (≠ L139), P137 (vs. gap), G138 (vs. gap), L223 (≠ R224), F233 (≠ S234)
- binding calcium ion: F233 (≠ S234), Q238 (≠ S239)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
34% identity, 98% coverage: 3:255/257 of query aligns to 2:250/250 of 3q0gD
- active site: A64 (= A65), M69 (≠ R70), T75 (≠ P80), F79 (≠ R84), G103 (≠ A111), E106 (≠ G114), P125 (= P133), E126 (= E134), V131 (≠ L139), P133 (vs. gap), G134 (vs. gap), L219 (≠ R224), F229 (≠ S234)
- binding Butyryl Coenzyme A: F225 (≠ T230), F241 (= F246)
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)
34% identity, 94% coverage: 13:254/257 of query aligns to 20:265/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
33% identity, 93% coverage: 11:250/257 of query aligns to 14:253/260 of 2hw5C
- active site: A68 (= A65), M73 (≠ R70), S83 (≠ P76), L87 (≠ P80), G111 (≠ A111), E114 (≠ G114), P133 (= P133), E134 (= E134), T139 (≠ L139), P141 (vs. gap), G142 (vs. gap), K227 (≠ R224), F237 (≠ S234)
- binding crotonyl coenzyme a: K26 (≠ E23), A27 (≠ K24), L28 (≠ R25), A30 (= A27), K62 (≠ S59), I70 (≠ L67), F109 (≠ M109)
Q62651 Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial; EC 5.3.3.- from Rattus norvegicus (Rat) (see paper)
33% identity, 91% coverage: 17:250/257 of query aligns to 69:317/327 of Q62651
- D176 (≠ G114) mutation D->A,D: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- E196 (= E134) mutation E->D,Q: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- D204 (≠ G142) mutation D->A,N: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
33% identity, 97% coverage: 8:257/257 of query aligns to 9:261/261 of 5jbxB
- active site: A67 (= A65), R72 (= R70), L84 (≠ P80), R88 (= R87), G112 (≠ A111), E115 (≠ G114), T134 (≠ P133), E135 (= E134), I140 (≠ L139), P142 (vs. gap), G143 (vs. gap), A228 (≠ R224), L238 (≠ S234)
- binding coenzyme a: S24 (≠ E23), R25 (≠ K24), R26 (= R25), A28 (= A27), A65 (= A63), D68 (= D66), L69 (= L67), K70 (≠ T68), L110 (≠ M109), G111 (= G110), T134 (≠ P133), E135 (= E134), L138 (≠ V137), R168 (≠ K164)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
32% identity, 99% coverage: 3:257/257 of query aligns to 2:257/257 of 6slbAAA
- active site: Q64 (≠ A65), F69 (≠ R70), L80 (≠ H83), N84 (≠ R87), A108 (= A111), S111 (≠ G114), A130 (≠ P133), F131 (≠ E134), L136 (= L139), P138 (vs. gap), D139 (vs. gap), A224 (≠ R224), G234 (≠ S234)
- 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 (≠ S59), A62 (= A63), Q64 (≠ A65), D65 (= D66), L66 (= L67), Y76 (≠ F79), A108 (= A111), F131 (≠ E134), D139 (vs. gap)
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)
31% identity, 97% coverage: 3:251/257 of query aligns to 8:266/276 of O69762
- K29 (= K24) binding acetyl-CoA
- A68 (= A63) binding acetyl-CoA
- M70 (≠ A65) binding acetyl-CoA
- L72 (= L67) binding acetyl-CoA
- Y75 (≠ R70) binding vanillin
- G120 (≠ A111) binding acetyl-CoA
- S123 (≠ G114) mutation to A: Reduced kcat compared to wild-type but not markerdly.
- S142 (≠ P133) binding acetyl-CoA
- E143 (= E134) mutation to A: Abolishes catalytic activity.
- W146 (≠ V137) binding acetyl-CoA
- G151 (= G142) binding vanillin
- Y239 (= Y225) binding vanillin; 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
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
31% identity, 93% coverage: 11:250/257 of query aligns to 13:247/254 of 2dubA
- active site: A67 (= A65), M72 (≠ R70), S82 (≠ P80), G105 (≠ A111), E108 (≠ G114), P127 (= P133), E128 (= E134), T133 (≠ L139), P135 (vs. gap), G136 (vs. gap), K221 (≠ R224), F231 (≠ S234)
- binding octanoyl-coenzyme a: K25 (≠ E23), A26 (≠ K24), L27 (≠ R25), A29 (= A27), A65 (= A63), A67 (= A65), D68 (= D66), I69 (≠ L67), K70 (≠ T68), G105 (≠ A111), E108 (≠ G114), P127 (= P133), E128 (= E134), G136 (vs. gap), A137 (= A140)
2vssD Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
33% identity, 81% coverage: 3:210/257 of query aligns to 6:220/246 of 2vssD
- active site: M68 (≠ A65), Y73 (≠ R70), D78 (≠ Q75), R90 (= R87), Q94 (≠ Y91), G118 (≠ A111), S121 (≠ G114), S140 (≠ P133), E141 (= E134), I146 (≠ L139), P148 (≠ G141), G149 (= G142)
- binding acetyl coenzyme *a: E26 (= E23), K27 (= K24), R28 (= R25), A30 (= A27), A66 (= A63), M68 (≠ A65), D69 (= D66), L70 (= L67), F74 (≠ K71), W114 (≠ A107), F116 (≠ M109), S140 (≠ P133)
- binding 4-hydroxy-3-methoxybenzaldehyde: M68 (≠ A65), Y73 (≠ R70), F74 (≠ K71), Q96 (vs. gap), E141 (= E134), G149 (= G142), N150 (≠ S144)
Sites not aligning to the query:
2vssB Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
33% identity, 81% coverage: 3:210/257 of query aligns to 5:219/247 of 2vssB
- active site: M67 (≠ A65), Y72 (≠ R70), D77 (≠ Q75), R89 (= R87), Q93 (≠ Y91), G117 (≠ A111), S120 (≠ G114), S139 (≠ P133), E140 (= E134), I145 (≠ L139), P147 (≠ G141), G148 (= G142)
- binding acetyl coenzyme *a: E25 (= E23), K26 (= K24), R27 (= R25), A29 (= A27), A65 (= A63), M67 (≠ A65), D68 (= D66), W113 (≠ A107), F115 (≠ M109), G117 (≠ A111), S139 (≠ P133), E140 (= E134)
Sites not aligning to the query:
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
32% identity, 98% coverage: 6:257/257 of query aligns to 2:245/245 of 6slaAAA
- active site: Q61 (≠ A65), L68 (≠ F79), N72 (≠ H83), A96 (= A111), S99 (≠ G114), A118 (≠ P133), F119 (≠ E134), L124 (= L139), P126 (vs. gap), N127 (vs. gap), A212 (≠ R224), G222 (≠ S234)
- 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 (≠ R25), A59 (= A63), Q61 (≠ A65), D62 (= D66), L63 (= L67), L68 (≠ F79), Y71 (≠ H82), A94 (≠ M109), G95 (= G110), A96 (= A111), F119 (≠ E134), I122 (≠ V137), L124 (= L139), N127 (vs. gap), F234 (= F246), K237 (= K249)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
32% identity, 93% coverage: 11:250/257 of query aligns to 12:251/258 of 1ey3A
- active site: A66 (= A65), M71 (≠ R70), S81 (≠ P76), L85 (≠ P80), G109 (≠ A111), E112 (≠ G114), P131 (= P133), E132 (= E134), T137 (≠ L139), P139 (vs. gap), G140 (vs. gap), K225 (≠ R224), F235 (≠ S234)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ E23), L26 (≠ R25), A28 (= A27), A64 (= A63), G65 (= G64), A66 (= A65), D67 (= D66), I68 (≠ L67), L85 (≠ P80), W88 (≠ H83), G109 (≠ A111), P131 (= P133), L135 (≠ V137), G140 (vs. gap)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
32% identity, 93% coverage: 11:250/257 of query aligns to 14:253/260 of 1dubA