SitesBLAST
Comparing Dsui_0981 FitnessBrowser__PS:Dsui_0981 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, 99% coverage: 1:260/263 of query aligns to 1:256/259 of 5zaiC
- active site: A65 (= A65), F70 (≠ M70), S82 (≠ A85), R86 (≠ A89), G110 (= G113), E113 (≠ G116), P132 (≠ T135), E133 (= E136), I138 (≠ L141), P140 (= P143), G141 (≠ A144), A226 (= A233), F236 (≠ R240)
- binding coenzyme a: K24 (≠ R24), L25 (≠ H25), A63 (= A63), G64 (= G64), A65 (= A65), D66 (= D66), I67 (≠ L67), P132 (≠ T135), R166 (= R168), F248 (= F252), K251 (= K255)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
33% identity, 99% coverage: 1:260/263 of query aligns to 1:254/255 of 3q0jC
- active site: A65 (= A65), M70 (= M70), T80 (≠ N87), F84 (≠ L92), G108 (= G113), E111 (≠ G116), P130 (≠ T135), E131 (= E136), V136 (≠ L141), P138 (= P143), G139 (≠ A144), L224 (≠ I229), F234 (≠ R240)
- binding acetoacetyl-coenzyme a: Q23 (≠ D23), A24 (≠ R24), L25 (≠ H25), A27 (= A27), A63 (= A63), G64 (= G64), A65 (= A65), D66 (= D66), I67 (≠ L67), K68 (≠ N68), M70 (= M70), F84 (≠ L92), G107 (= G112), G108 (= G113), E111 (≠ G116), P130 (≠ T135), E131 (= E136), P138 (= P143), G139 (≠ A144), M140 (≠ V145)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
33% identity, 99% coverage: 1:260/263 of query aligns to 1:254/255 of 3q0gC
- active site: A65 (= A65), M70 (= M70), T80 (≠ N87), F84 (≠ L92), G108 (= G113), E111 (≠ G116), P130 (≠ T135), E131 (= E136), V136 (≠ L141), P138 (= P143), G139 (≠ A144), L224 (≠ I229), F234 (≠ R240)
- binding coenzyme a: L25 (≠ H25), A63 (= A63), I67 (≠ L67), K68 (≠ N68), Y104 (≠ P109), P130 (≠ T135), E131 (= E136), L134 (= L139)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
33% identity, 98% coverage: 2:260/263 of query aligns to 1:253/256 of 3h81A
- active site: A64 (= A65), M69 (= M70), T79 (≠ N87), F83 (≠ L92), G107 (= G113), E110 (≠ G116), P129 (≠ T135), E130 (= E136), V135 (≠ L141), P137 (= P143), G138 (≠ A144), L223 (≠ I229), F233 (≠ R240)
- binding calcium ion: F233 (≠ R240), Q238 (≠ G245)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
33% identity, 98% coverage: 2:260/263 of query aligns to 1:249/250 of 3q0gD
- active site: A64 (= A65), M69 (= M70), T75 (≠ N87), F79 (≠ L92), G103 (= G113), E106 (≠ G116), P125 (≠ T135), E126 (= E136), V131 (≠ L141), P133 (= P143), G134 (≠ A144), L219 (≠ I229), F229 (≠ R240)
- binding Butyryl Coenzyme A: F225 (≠ I236), F241 (= F252)
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, 98% coverage: 2:260/263 of query aligns to 8:265/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
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, 97% coverage: 3:256/263 of query aligns to 8:265/276 of O69762
- K29 (≠ R24) binding
- A68 (= A63) binding
- M70 (≠ A65) binding
- L72 (= L67) binding
- Y75 (≠ M70) binding
- G120 (= G113) binding
- S123 (≠ G116) mutation to A: Reduced kcat compared to wild-type but not markerdly.
- S142 (≠ T135) binding
- E143 (= E136) mutation to A: Abolishes catalytic activity.
- W146 (≠ L139) binding
- G151 (≠ A144) binding
- Y239 (≠ I229) 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
2vssD Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
32% identity, 81% coverage: 3:214/263 of query aligns to 6:219/246 of 2vssD
- active site: M68 (≠ A65), Y73 (≠ M70), D78 (≠ G75), R90 (≠ A85), Q94 (≠ A89), G118 (= G113), S121 (≠ G116), S140 (≠ T135), E141 (= E136), I146 (≠ L141), P148 (= P143), G149 (≠ A144)
- binding acetyl coenzyme *a: E26 (≠ D23), K27 (≠ R24), R28 (≠ H25), A30 (= A27), A66 (= A63), M68 (≠ A65), D69 (= D66), L70 (= L67), F74 (≠ K71), W114 (≠ P109), F116 (≠ Y111), S140 (≠ T135)
- binding 4-hydroxy-3-methoxybenzaldehyde: M68 (≠ A65), Y73 (≠ M70), F74 (≠ K71), Q96 (≠ L91), E141 (= E136), G149 (≠ A144), N150 (vs. gap)
Sites not aligning to the query:
2vssB Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
32% identity, 81% coverage: 3:214/263 of query aligns to 5:218/247 of 2vssB
- active site: M67 (≠ A65), Y72 (≠ M70), D77 (≠ G75), R89 (≠ A85), Q93 (≠ A89), G117 (= G113), S120 (≠ G116), S139 (≠ T135), E140 (= E136), I145 (≠ L141), P147 (= P143), G148 (≠ A144)
- binding acetyl coenzyme *a: E25 (≠ D23), K26 (≠ R24), R27 (≠ H25), A29 (= A27), A65 (= A63), M67 (≠ A65), D68 (= D66), W113 (≠ P109), F115 (≠ Y111), G117 (= G113), S139 (≠ T135), E140 (= E136)
Sites not aligning to the query:
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
31% identity, 98% coverage: 2:260/263 of query aligns to 2:257/260 of 2hw5C
- active site: A68 (= A65), M73 (= M70), S83 (≠ A85), L87 (≠ A89), G111 (= G113), E114 (≠ G116), P133 (≠ T135), E134 (= E136), T139 (≠ L141), P141 (= P143), G142 (vs. gap), K227 (≠ I229), F237 (≠ R240)
- binding crotonyl coenzyme a: K26 (≠ D23), A27 (≠ R24), L28 (≠ H25), A30 (= A27), K62 (= K59), I70 (≠ L67), F109 (≠ Y111)
6p5uE Structure of an enoyl-coa hydratase/aldolase isolated from a lignin- degrading consortium (see paper)
35% identity, 85% coverage: 3:225/263 of query aligns to 5:227/246 of 6p5uE
- active site: M67 (≠ A65), Y72 (≠ M70), D77 (≠ G75), R89 (≠ A83), A93 (= A89), G117 (= G113), T120 (≠ G116), E140 (= E136), I145 (≠ L141), P147 (= P143), A148 (= A144)
- binding coenzyme a: D25 (= D23), K26 (≠ R24), R27 (≠ H25), A29 (= A27), A65 (= A63), M67 (≠ A65), D68 (= D66), L69 (= L67), W113 (≠ P109), F115 (≠ Y111), S139 (≠ T135), W143 (≠ L139)
Sites not aligning to the query:
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
31% identity, 98% coverage: 2:260/263 of query aligns to 2:257/260 of 1dubA
- active site: A68 (= A65), M73 (= M70), S83 (≠ A85), L87 (≠ A89), G111 (= G113), E114 (≠ G116), P133 (≠ T135), E134 (= E136), T139 (≠ L141), P141 (= P143), G142 (vs. gap), K227 (≠ I229), F237 (≠ R240)
- binding acetoacetyl-coenzyme a: K26 (≠ D23), A27 (≠ R24), L28 (≠ H25), A30 (= A27), A66 (= A63), A68 (= A65), D69 (= D66), I70 (≠ L67), Y107 (≠ P109), G110 (= G112), G111 (= G113), E114 (≠ G116), P133 (≠ T135), E134 (= E136), L137 (= L139), G142 (vs. gap), F233 (≠ I236), F249 (= F252)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
31% identity, 98% coverage: 3:260/263 of query aligns to 1:255/258 of 1ey3A
- active site: A66 (= A65), M71 (= M70), S81 (≠ A85), L85 (≠ A89), G109 (= G113), E112 (≠ G116), P131 (≠ T135), E132 (= E136), T137 (≠ L141), P139 (= P143), G140 (vs. gap), K225 (≠ I229), F235 (≠ R240)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ D23), L26 (≠ H25), A28 (= A27), A64 (= A63), G65 (= G64), A66 (= A65), D67 (= D66), I68 (≠ L67), L85 (≠ A89), W88 (≠ L92), G109 (= G113), P131 (≠ T135), L135 (= L139), G140 (vs. gap)
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)
31% identity, 98% coverage: 2:260/263 of query aligns to 32:287/290 of P14604
- E144 (≠ G116) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E136) 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)
30% identity, 98% coverage: 2:260/263 of query aligns to 2:255/258 of 1mj3A
- active site: A68 (= A65), M73 (= M70), S83 (≠ N87), L85 (≠ A89), G109 (= G113), E112 (≠ G116), P131 (≠ T135), E132 (= E136), T137 (≠ L141), P139 (= P143), G140 (vs. gap), K225 (≠ I229), F235 (≠ R240)
- binding hexanoyl-coenzyme a: K26 (≠ D23), A27 (≠ R24), L28 (≠ H25), A30 (= A27), A66 (= A63), G67 (= G64), A68 (= A65), D69 (= D66), I70 (≠ L67), G109 (= G113), P131 (≠ T135), E132 (= E136), L135 (= L139), G140 (vs. gap)
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
31% identity, 97% coverage: 7:260/263 of query aligns to 11:263/266 of O53561
- K135 (≠ M131) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 131:138, 38% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (= K138) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
30% identity, 98% coverage: 2:260/263 of query aligns to 1:251/254 of 2dubA
- active site: A67 (= A65), M72 (= M70), S82 (≠ N87), G105 (= G113), E108 (≠ G116), P127 (≠ T135), E128 (= E136), T133 (≠ L141), P135 (= P143), G136 (vs. gap), K221 (≠ I229), F231 (≠ R240)
- binding octanoyl-coenzyme a: K25 (≠ D23), A26 (≠ R24), L27 (≠ H25), A29 (= A27), A65 (= A63), A67 (= A65), D68 (= D66), I69 (≠ L67), K70 (≠ N68), G105 (= G113), E108 (≠ G116), P127 (≠ T135), E128 (= E136), G136 (vs. gap), A137 (= A144)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
33% identity, 96% coverage: 8:260/263 of query aligns to 9:258/261 of 5jbxB
- active site: A67 (= A65), R72 (≠ A73), L84 (≠ A85), R88 (≠ A89), G112 (= G113), E115 (≠ G116), T134 (= T135), E135 (= E136), I140 (≠ L141), P142 (= P143), G143 (≠ A144), A228 (= A230), L238 (≠ R240)
- binding coenzyme a: S24 (≠ D23), R25 (= R24), R26 (≠ H25), A28 (= A27), A65 (= A63), D68 (= D66), L69 (= L67), K70 (= K71), L110 (≠ Y111), G111 (= G112), T134 (= T135), E135 (= E136), L138 (= L139), R168 (= R168)
6l3pA Crystal strcuture of feruloyl-coa hydratase lyase(fchl) complexed with coa
32% identity, 80% coverage: 3:213/263 of query aligns to 7:214/244 of 6l3pA
- active site: M69 (≠ A65), Y74 (≠ M70), R86 (≠ L82), Q90 (≠ G86), G114 (= G113), S117 (≠ G116), S136 (≠ T135), E137 (= E136), I142 (≠ L141), P144 (= P143), G145 (≠ A144)
- binding coenzyme a: K28 (≠ R24), R29 (≠ H25), A31 (= A27), A67 (= A63), M69 (≠ A65), D70 (= D66), L71 (= L67), G113 (= G112)
Sites not aligning to the query:
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
33% identity, 97% coverage: 6:260/263 of query aligns to 5:254/257 of 6slbAAA
- active site: Q64 (≠ A65), F69 (≠ W69), L80 (= L82), N84 (≠ G86), A108 (≠ G113), S111 (≠ G116), A130 (≠ T135), F131 (≠ E136), L136 (= L141), P138 (= P143), D139 (≠ A144), A224 (≠ I229), G234 (≠ M239)
- 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 (≠ K59), A62 (= A63), Q64 (≠ A65), D65 (= D66), L66 (= L67), Y76 (= Y76), A108 (≠ G113), F131 (≠ E136), D139 (≠ A144)
Query Sequence
>Dsui_0981 FitnessBrowser__PS:Dsui_0981
MTFSSILIEVDGPVGILTLNKPDRHNAFDETLMAEITAGLKQLEADPAVRVVVLSATGKS
FCAGADLNWMKRAAGYTPEQNLADAGNLAELLRTLNTLAKPTVARVQGPAYGGGVGLVAA
CDVAVASYDAMFALTEVKLGLIPAVISPYVIAALGERQCRRYFLTAERFSAAEGYRLGLL
HEIVPSEEQLDEAVGEIVDKLLKNGPAAQAASKELIRAVANQPIDDAVIADTARRITAMR
ASAEGREGIAAFLEKRKPHWITD
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