SitesBLAST
Comparing SM_b20752 FitnessBrowser__Smeli:SM_b20752 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)
3bptA Crystal structure of human beta-hydroxyisobutyryl-coa hydrolase in complex with quercetin
41% identity, 96% coverage: 9:349/356 of query aligns to 6:350/362 of 3bptA
- active site: G67 (= G70), P84 (≠ A87), R88 (= R91), G115 (= G118), G118 (= G121), E138 (= E141), D146 (= D149)
- binding (2r)-3-hydroxy-2-methylpropanoic acid: G66 (= G69), G67 (= G70), I69 (= I72), E90 (= E93), G114 (= G117), G115 (= G118), E138 (= E141), D146 (= D149), V147 (= V150)
- binding 3,5,7,3',4'-pentahydroxyflavone: F25 (≠ A28), L26 (= L29), A28 (≠ S31), G66 (= G69), G67 (= G70), I69 (= I72), P137 (= P140), I141 (= I144), L319 (≠ V319)
4hdtA Crystal structure of a carnitinyl-coa dehydratase from mycobacterium thermoresistibile (see paper)
44% identity, 90% coverage: 9:328/356 of query aligns to 3:311/340 of 4hdtA
- active site: G64 (= G70), I69 (= I75), W84 (= W90), Y88 (≠ F94), G112 (= G118), G115 (= G121), E135 (= E141), P142 (≠ T148), D143 (= D149), R283 (≠ E296)
- binding zinc ion: H28 (≠ R34), E42 (= E48), E57 (= E63), E79 (= E85), H93 (≠ R99), H185 (≠ S191)
Sites not aligning to the query:
Q9LKJ1 3-hydroxyisobutyryl-CoA hydrolase 1; CoA-thioester hydrolase CHY1; EC 3.1.2.-; EC 3.1.2.4 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
40% identity, 90% coverage: 9:328/356 of query aligns to 10:336/378 of Q9LKJ1
- G70 (= G70) mutation to S: Loss of activity.
- E142 (= E141) mutation to A: Loss of activity.
- D150 (= D149) mutation to G: Reduced activity.
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
29% identity, 53% coverage: 6:192/356 of query aligns to 1:178/250 of 3q0gD
- active site: A64 (≠ G70), M69 (≠ I75), T75 (≠ W90), F79 (= F94), G103 (= G118), E106 (≠ G121), P125 (= P140), E126 (= E141), V131 (≠ Y146), P133 (≠ T148), G134 (≠ D149)
Sites not aligning to the query:
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
31% identity, 53% coverage: 10:196/356 of query aligns to 6:188/258 of 1mj3A
- active site: A68 (≠ G70), M73 (≠ I75), S83 (≠ E85), L85 (≠ A87), G109 (= G118), E112 (≠ G121), P131 (= P140), E132 (= E141), T137 (≠ Y146), P139 (≠ T148), G140 (≠ D149)
- binding hexanoyl-coenzyme a: K26 (≠ R27), A27 (= A28), L28 (= L29), A30 (≠ S31), A66 (= A68), G67 (= G69), A68 (≠ G70), D69 (= D71), I70 (= I72), G109 (= G118), P131 (= P140), E132 (= E141), L135 (≠ I144), G140 (≠ D149)
Sites not aligning to the query:
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
30% identity, 46% coverage: 1:162/356 of query aligns to 1:154/259 of 5zaiC
- active site: A65 (≠ G70), F70 (≠ I75), S82 (≠ W90), R86 (≠ F94), G110 (= G118), E113 (≠ G121), P132 (= P140), E133 (= E141), I138 (≠ Y146), P140 (≠ T148), G141 (≠ D149)
- binding coenzyme a: K24 (≠ A28), L25 (= L29), A63 (= A68), G64 (= G69), A65 (≠ G70), D66 (= D71), I67 (= I72), P132 (= P140)
Sites not aligning to the query:
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
29% identity, 53% coverage: 6:192/356 of query aligns to 2:183/255 of 3q0jC
- active site: A65 (≠ G70), M70 (≠ I75), T80 (≠ W90), F84 (= F94), G108 (= G118), E111 (≠ G121), P130 (= P140), E131 (= E141), V136 (≠ Y146), P138 (≠ T148), G139 (≠ D149)
- binding acetoacetyl-coenzyme a: Q23 (≠ R27), A24 (= A28), L25 (= L29), A27 (≠ S31), A63 (= A68), G64 (= G69), A65 (≠ G70), D66 (= D71), I67 (= I72), K68 (≠ R73), M70 (≠ I75), F84 (= F94), G107 (= G117), G108 (= G118), E111 (≠ G121), P130 (= P140), E131 (= E141), P138 (≠ T148), G139 (≠ D149), M140 (≠ V150)
Sites not aligning to the query:
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
29% identity, 53% coverage: 6:192/356 of query aligns to 2:183/255 of 3q0gC
- active site: A65 (≠ G70), M70 (≠ I75), T80 (≠ W90), F84 (= F94), G108 (= G118), E111 (≠ G121), P130 (= P140), E131 (= E141), V136 (≠ Y146), P138 (≠ T148), G139 (≠ D149)
- binding coenzyme a: L25 (= L29), A63 (= A68), I67 (= I72), K68 (≠ R73), Y104 (≠ I114), P130 (= P140), E131 (= E141), L134 (≠ I144)
Sites not aligning to the query:
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
29% identity, 53% coverage: 6:192/356 of query aligns to 1:182/256 of 3h81A
- active site: A64 (≠ G70), M69 (≠ I75), T79 (≠ W90), F83 (= F94), G107 (= G118), E110 (≠ G121), P129 (= P140), E130 (= E141), V135 (≠ Y146), P137 (≠ T148), G138 (≠ D149)
Sites not aligning to the query:
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, 53% coverage: 10:196/356 of query aligns to 36:220/290 of P14604
- E144 (≠ G121) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E141) 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)
31% identity, 53% coverage: 10:196/356 of query aligns to 4:188/258 of 1ey3A
- active site: A66 (≠ G70), M71 (≠ I75), S81 (≠ P83), L85 (≠ A87), G109 (= G118), E112 (≠ G121), P131 (= P140), E132 (= E141), T137 (≠ Y146), P139 (≠ T148), G140 (≠ D149)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ R27), L26 (= L29), A28 (≠ S31), A64 (= A68), G65 (= G69), A66 (≠ G70), D67 (= D71), I68 (= I72), L85 (≠ A87), W88 (= W90), G109 (= G118), P131 (= P140), L135 (≠ I144), G140 (≠ D149)
Sites not aligning to the query:
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
31% identity, 53% coverage: 10:196/356 of query aligns to 6:190/260 of 1dubA
- active site: A68 (≠ G70), M73 (≠ I75), S83 (≠ P83), L87 (≠ A87), G111 (= G118), E114 (≠ G121), P133 (= P140), E134 (= E141), T139 (≠ Y146), P141 (≠ T148), G142 (≠ D149)
- binding acetoacetyl-coenzyme a: K26 (≠ R27), A27 (= A28), L28 (= L29), A30 (≠ S31), A66 (= A68), A68 (≠ G70), D69 (= D71), I70 (= I72), Y107 (≠ I114), G110 (= G117), G111 (= G118), E114 (≠ G121), P133 (= P140), E134 (= E141), L137 (≠ I144), G142 (≠ D149)
Sites not aligning to the query:
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
31% identity, 53% coverage: 10:196/356 of query aligns to 5:184/254 of 2dubA
- active site: A67 (≠ G70), M72 (≠ S78), S82 (≠ Q88), G105 (= G118), E108 (≠ G121), P127 (= P140), E128 (= E141), T133 (≠ Y146), P135 (≠ T148), G136 (≠ D149)
- binding octanoyl-coenzyme a: K25 (≠ R27), A26 (= A28), L27 (= L29), A29 (≠ S31), A65 (= A68), A67 (≠ G70), D68 (= D71), I69 (= I72), K70 (≠ R73), G105 (= G118), E108 (≠ G121), P127 (= P140), E128 (= E141), G136 (≠ D149), A137 (≠ V150)
Sites not aligning to the query:
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
30% identity, 53% coverage: 10:196/356 of query aligns to 6:190/260 of 2hw5C
- active site: A68 (≠ G70), M73 (≠ I75), S83 (≠ R91), L87 (≠ I95), G111 (= G118), E114 (≠ G121), P133 (= P140), E134 (= E141), T139 (≠ Y146), P141 (≠ T148), G142 (≠ D149)
- binding crotonyl coenzyme a: K26 (≠ R27), A27 (= A28), L28 (= L29), A30 (≠ S31), K62 (≠ R64), I70 (= I72), F109 (≠ M116)
Sites not aligning to the query:
6z1pBI mS93 (see paper)
28% identity, 48% coverage: 4:174/356 of query aligns to 18:190/1413 of 6z1pBI
- active site: T85 (vs. gap), S134 (≠ G118), E157 (= E141), D165 (= D149)
- binding : Y41 (≠ R27), K42 (≠ A28), Q43 (≠ L29), T45 (≠ S31), D47 (≠ N33), H49 (≠ T35), K83 (≠ G69), T85 (vs. gap), D86 (= D71), F87 (≠ I72), K88 (≠ R73), K92 (≠ E77), L130 (≠ I114), K152 (≠ R136)
Sites not aligning to the query:
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
33% identity, 43% coverage: 10:161/356 of query aligns to 5:151/257 of 6slbAAA
- active site: Q64 (≠ G70), F69 (≠ S78), L80 (≠ F89), N84 (≠ E93), A108 (≠ G118), S111 (≠ G121), A130 (≠ P140), F131 (≠ E141), L136 (≠ Y146), P138 (≠ T148), D139 (= D149)
- 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 (= R64), A62 (= A68), Q64 (≠ G70), D65 (= D71), L66 (≠ I75), Y76 (≠ E85), A108 (≠ G118), F131 (≠ E141), D139 (= D149)
Sites not aligning to the query:
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
29% identity, 51% coverage: 8:190/356 of query aligns to 8:190/266 of O53561
- K135 (≠ R136) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 136:143, 25% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (≠ G143) 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, 43% coverage: 10:161/356 of query aligns to 2:139/245 of 6slaAAA
- active site: Q61 (≠ G70), L68 (≠ F89), N72 (≠ E93), A96 (≠ G118), S99 (≠ G121), A118 (≠ P140), F119 (≠ E141), L124 (≠ Y146), P126 (≠ T148), N127 (≠ D149)
- 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 (= L29), A59 (= A68), Q61 (≠ G70), D62 (= D71), L63 (≠ I72), L68 (≠ F89), Y71 (≠ E92), A94 (≠ M116), G95 (= G117), A96 (≠ G118), F119 (≠ E141), I122 (= I144), L124 (≠ Y146), N127 (≠ D149)
Sites not aligning to the query:
Q62651 Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial; EC 5.3.3.- from Rattus norvegicus (Rat) (see paper)
25% identity, 51% coverage: 11:192/356 of query aligns to 59:249/327 of Q62651
- D176 (≠ G121) mutation D->A,D: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- E196 (= E141) mutation E->D,Q: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- D204 (= D149) mutation D->A,N: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
4izdA Crystal structure of dmdd e121a in complex with mmpa-coa (see paper)
30% identity, 45% coverage: 14:172/356 of query aligns to 16:172/253 of 4izdA
- active site: L70 (≠ G70), H75 (≠ I75), C89 (≠ A87), H93 (≠ R91), G117 (= G118), A120 (≠ G121), E140 (= E141), G148 (≠ D149)
- binding 3-methylmercaptopropionate-CoA (MMPA-CoA): D29 (≠ R27), K30 (≠ A28), R31 (≠ L29), A33 (≠ S31), A68 (= A68), L70 (≠ G70), D71 (= D71), L72 (≠ I72)
Sites not aligning to the query:
Query Sequence
>SM_b20752 FitnessBrowser__Smeli:SM_b20752
MEMQTTLPEVIVERQGAIGRLRLNRPRALNSLNRTMIRAIAAALTEFERNPEIAAVLVTG
EGERGLCAGGDIRMIYESGRERPGEGAQFWREEFIVNSRISAYSKPYIAIMDGIVMGGGV
GVSSHGSHRVVTERTRFAMPETGIGYFTDVGATWLLPRAPGEFGTYLGLTGRDIGAAAVI
HARLADSFVPSEMIGELLGALSSLSGSATADDVSAAIRAVSSEPPASALLDHLSVIDRCF
AFNAVEEIFAALEKDESDFARETLELLKTRSAISLKLTLSLLREGRSSATLNECLEREYA
ATLGMLSNPDFYEGVRAAVIDKDRNPKWSVGLSEATPELLARFGRNDGAPLFAGKE
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