SitesBLAST
Comparing Dsui_2807 FitnessBrowser__PS:Dsui_2807 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: 20:261/262 of query aligns to 17:258/259 of 5zaiC
- active site: A65 (≠ H68), F70 (≠ M73), S82 (≠ F86), R86 (≠ A90), G110 (≠ A114), E113 (≠ Q117), P132 (≠ S136), E133 (≠ G137), I138 (≠ L142), P140 (= P147), G141 (≠ A148), A226 (≠ Q229), F236 (≠ M239)
- binding coenzyme a: K24 (≠ Q27), L25 (≠ F28), A63 (= A66), G64 (= G67), A65 (≠ H68), D66 (= D69), I67 (≠ L70), P132 (≠ S136), R166 (≠ F169), F248 (= F251), K251 (= K254)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
32% identity, 97% coverage: 5:257/262 of query aligns to 3:247/250 of 3q0gD
- active site: A64 (≠ H68), M69 (= M73), T75 (≠ M82), F79 (= F86), G103 (≠ A114), E106 (≠ Q117), P125 (≠ S136), E126 (≠ G137), V131 (≠ L142), P133 (= P147), G134 (≠ A148), L219 (≠ Q229), F229 (≠ M239)
- binding Butyryl Coenzyme A: F225 (≠ M235), F241 (= F251)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
32% identity, 97% coverage: 5:257/262 of query aligns to 3:251/256 of 3h81A
- active site: A64 (≠ H68), M69 (= M73), T79 (≠ M82), F83 (= F86), G107 (≠ A114), E110 (≠ Q117), P129 (≠ S136), E130 (≠ G137), V135 (≠ L142), P137 (= P147), G138 (≠ A148), L223 (≠ Q229), F233 (≠ M239)
- binding calcium ion: F233 (≠ M239), Q238 (≠ A244)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
32% identity, 97% coverage: 5:257/262 of query aligns to 4:252/255 of 3q0jC
- active site: A65 (≠ H68), M70 (= M73), T80 (≠ M82), F84 (= F86), G108 (≠ A114), E111 (≠ Q117), P130 (≠ S136), E131 (≠ G137), V136 (≠ L142), P138 (= P147), G139 (≠ A148), L224 (≠ Q229), F234 (≠ M239)
- binding acetoacetyl-coenzyme a: Q23 (≠ A26), A24 (≠ Q27), L25 (≠ F28), A27 (≠ S30), A63 (= A66), G64 (= G67), A65 (≠ H68), D66 (= D69), I67 (≠ L70), K68 (= K71), M70 (= M73), F84 (= F86), G107 (≠ A113), G108 (≠ A114), E111 (≠ Q117), P130 (≠ S136), E131 (≠ G137), P138 (= P147), G139 (≠ A148), M140 (≠ V149)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
32% identity, 97% coverage: 5:257/262 of query aligns to 4:252/255 of 3q0gC
- active site: A65 (≠ H68), M70 (= M73), T80 (≠ M82), F84 (= F86), G108 (≠ A114), E111 (≠ Q117), P130 (≠ S136), E131 (≠ G137), V136 (≠ L142), P138 (= P147), G139 (≠ A148), L224 (≠ Q229), F234 (≠ M239)
- binding coenzyme a: L25 (≠ F28), A63 (= A66), I67 (≠ L70), K68 (= K71), Y104 (≠ I110), P130 (≠ S136), E131 (≠ G137), L134 (≠ V140)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
33% identity, 91% coverage: 22:260/262 of query aligns to 21:252/254 of 2dubA
- active site: A67 (≠ H68), M72 (= M73), S82 (≠ K91), G105 (≠ A114), E108 (≠ Q117), P127 (≠ S136), E128 (≠ G137), T133 (≠ S145), P135 (= P147), G136 (≠ A148), K221 (≠ Q229), F231 (≠ M239)
- binding octanoyl-coenzyme a: K25 (≠ A26), A26 (≠ Q27), L27 (≠ F28), A29 (≠ S30), A65 (= A66), A67 (≠ H68), D68 (= D69), I69 (≠ L70), K70 (= K71), G105 (≠ A114), E108 (≠ Q117), P127 (≠ S136), E128 (≠ G137), G136 (≠ A148), A137 (≠ V149)
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)
33% identity, 90% coverage: 22:256/262 of query aligns to 52:284/290 of P14604
- E144 (≠ Q117) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (≠ G137) 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)
33% identity, 91% coverage: 22:260/262 of query aligns to 22:256/258 of 1mj3A
- active site: A68 (≠ H68), M73 (= M73), S83 (≠ F86), L85 (= L88), G109 (≠ A114), E112 (≠ Q117), P131 (≠ S136), E132 (≠ G137), T137 (≠ S145), P139 (= P147), G140 (≠ A148), K225 (≠ Q229), F235 (≠ M239)
- binding hexanoyl-coenzyme a: K26 (≠ A26), A27 (≠ Q27), L28 (≠ F28), A30 (≠ S30), A66 (= A66), G67 (= G67), A68 (≠ H68), D69 (= D69), I70 (≠ L70), G109 (≠ A114), P131 (≠ S136), E132 (≠ G137), L135 (≠ V140), G140 (≠ A148)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
32% identity, 91% coverage: 22:260/262 of query aligns to 22:258/260 of 1dubA
- active site: A68 (≠ H68), M73 (= M73), S83 (≠ F86), L87 (≠ A90), G111 (≠ A114), E114 (≠ Q117), P133 (≠ S136), E134 (≠ G137), T139 (≠ S145), P141 (= P147), G142 (≠ A148), K227 (≠ Q229), F237 (≠ M239)
- binding acetoacetyl-coenzyme a: K26 (≠ A26), A27 (≠ Q27), L28 (≠ F28), A30 (≠ S30), A66 (= A66), A68 (≠ H68), D69 (= D69), I70 (≠ L70), Y107 (≠ I110), G110 (≠ A113), G111 (≠ A114), E114 (≠ Q117), P133 (≠ S136), E134 (≠ G137), L137 (≠ V140), G142 (≠ A148), F233 (≠ M235), F249 (= F251)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
32% identity, 91% coverage: 22:260/262 of query aligns to 20:256/258 of 1ey3A
- active site: A66 (≠ H68), M71 (= M73), S81 (≠ F86), L85 (≠ A90), G109 (≠ A114), E112 (≠ Q117), P131 (≠ S136), E132 (≠ G137), T137 (≠ S145), P139 (= P147), G140 (≠ A148), K225 (≠ Q229), F235 (≠ M239)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ A26), L26 (≠ F28), A28 (≠ S30), A64 (= A66), G65 (= G67), A66 (≠ H68), D67 (= D69), I68 (≠ L70), L85 (≠ A90), W88 (≠ M93), G109 (≠ A114), P131 (≠ S136), L135 (≠ V140), G140 (≠ A148)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
31% identity, 95% coverage: 8:256/262 of query aligns to 6:254/260 of 2hw5C
- active site: A68 (≠ H68), M73 (= M73), S83 (≠ F86), L87 (≠ A90), G111 (≠ A114), E114 (≠ Q117), P133 (≠ S136), E134 (≠ G137), T139 (≠ S145), P141 (= P147), G142 (≠ A148), K227 (≠ Q229), F237 (≠ M239)
- binding crotonyl coenzyme a: K26 (≠ A26), A27 (≠ Q27), L28 (≠ F28), A30 (≠ S30), K62 (= K62), I70 (≠ L70), F109 (≠ T112)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
32% identity, 95% coverage: 11:260/262 of query aligns to 7:255/257 of 6slbAAA
- active site: Q64 (≠ H68), F69 (≠ M73), L80 (≠ F86), N84 (≠ A90), A108 (= A114), S111 (≠ Q117), A130 (≠ S136), F131 (≠ G137), L136 (= L142), P138 (= P147), D139 (≠ A148), A224 (≠ Q229), 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 (≠ K62), A62 (= A66), Q64 (≠ H68), D65 (= D69), L66 (= L70), Y76 (≠ M82), A108 (= A114), F131 (≠ G137), D139 (≠ A148)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
33% identity, 90% coverage: 26:260/262 of query aligns to 24:259/261 of 5jbxB
- active site: A67 (≠ H68), R72 (vs. gap), L84 (≠ M82), R88 (≠ A90), G112 (≠ A114), E115 (≠ Q117), T134 (≠ S136), E135 (≠ G137), I140 (≠ L142), P142 (= P147), G143 (≠ A148), A228 (≠ Q229), L238 (≠ M239)
- binding coenzyme a: S24 (≠ A26), R25 (≠ Q27), R26 (≠ F28), A28 (≠ S30), A65 (= A66), D68 (= D69), L69 (= L70), K70 (= K71), L110 (≠ T112), G111 (≠ A113), T134 (≠ S136), E135 (≠ G137), L138 (≠ V140), R168 (≠ F169)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
32% identity, 95% coverage: 11:260/262 of query aligns to 4:243/245 of 6slaAAA
- active site: Q61 (≠ H68), L68 (≠ F86), N72 (≠ A90), A96 (= A114), S99 (≠ Q117), A118 (≠ S136), F119 (≠ G137), L124 (= L142), P126 (= P147), N127 (≠ A148), A212 (≠ Q229), G222 (≠ M239)
- 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 (≠ F28), A59 (= A66), Q61 (≠ H68), D62 (= D69), L63 (= L70), L68 (≠ F86), Y71 (≠ C89), A94 (≠ T112), G95 (≠ A113), A96 (= A114), F119 (≠ G137), I122 (≠ V140), L124 (= L142), N127 (≠ A148), F234 (= F251), K237 (= K254)
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)
30% identity, 93% coverage: 15:257/262 of query aligns to 85:328/337 of Q8GYN9
Sites not aligning to the query:
- 20 H→V: Loss of peroxisomal targeting.
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
32% identity, 94% coverage: 16:260/262 of query aligns to 16:264/266 of O53561
- K135 (= K132) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 132:139, 38% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (≠ N139) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
4i42A E.Coli. 1,4-dihydroxy-2-naphthoyl coenzyme a synthase (ecmenb) in complex with 1-hydroxy-2-naphthoyl-coa (see paper)
32% identity, 94% coverage: 11:257/262 of query aligns to 28:276/285 of 4i42A
- active site: G86 (≠ H68), R91 (= R74), Y97 (vs. gap), H105 (≠ A84), L109 (= L88), G133 (≠ A114), V136 (≠ Q117), G156 (= G137), S161 (≠ L142), D163 (vs. gap), G164 (≠ C144), A250 (= A231), Y258 (≠ M239)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (≠ Q27), R45 (≠ F28), S84 (≠ A66), G85 (= G67), G86 (≠ H68), D87 (= D69), Q88 (≠ L70), K89 (= K71), Y97 (vs. gap), V108 (≠ K87), Y129 (≠ I110), G133 (≠ A114), T155 (≠ S136), S161 (≠ L142), T254 (≠ M235), F270 (= F251), K273 (= K254)
P0ABU0 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Escherichia coli (strain K12) (see 4 papers)
32% identity, 94% coverage: 11:257/262 of query aligns to 28:276/285 of P0ABU0
- R45 (≠ F28) binding in other chain
- SGGDQK 84:89 (≠ AGHDLK 66:71) binding in other chain
- K89 (= K71) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- R91 (= R74) mutation to A: Loss of DHNA-CoA synthase activity.
- Y97 (vs. gap) binding in other chain; mutation to F: Loss of DHNA-CoA synthase activity.
- YSIGG 129:133 (≠ IATAA 110:114) binding in other chain
- Q154 (≠ V135) 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 (≠ VSG 135:137) binding
- T155 (≠ S136) binding in other chain
- G156 (= G137) mutation to D: Loss of DHNA-CoA synthase activity.
- S161 (≠ L142) binding in other chain
- W184 (≠ L164) mutation to F: Reduces the specific DHNA-CoA synthase activity by 530-fold, whereas its affinity for hydrogencarbonate is reduced by 20-fold.
- Y258 (≠ M239) binding
- R267 (≠ I248) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- F270 (= F251) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- K273 (= K254) binding ; mutation to A: Impairs protein folding.
Q5HH38 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Staphylococcus aureus (strain COL) (see paper)
32% identity, 98% coverage: 1:257/262 of query aligns to 1:264/273 of Q5HH38
- R34 (≠ F28) binding in other chain
- SGGDQ 73:77 (≠ AGHDL 66:70) binding in other chain
- S149 (≠ L142) binding in other chain
3t88A Crystal structure of escherichia coli menb in complex with substrate analogue, osb-ncoa (see paper)
32% identity, 94% coverage: 11:257/262 of query aligns to 24:272/281 of 3t88A
- active site: G82 (≠ H68), R87 (= R74), Y93 (vs. gap), H101 (≠ A84), L105 (= L88), G129 (≠ A114), V132 (≠ Q117), G152 (= G137), S157 (≠ L142), D159 (vs. gap), G160 (≠ C144), A246 (= A231), Y254 (≠ M239)
- binding o-succinylbenzoyl-N-coenzyme A: Q39 (≠ A26), V40 (≠ Q27), R41 (≠ F28), A43 (≠ S30), S80 (≠ A66), G81 (= G67), G82 (≠ H68), D83 (= D69), Q84 (≠ L70), K85 (= K71), Y93 (vs. gap), V104 (≠ K87), L105 (= L88), Y125 (≠ I110), G129 (≠ A114), T151 (≠ S136), V155 (= V140), F158 (= F143), D159 (vs. gap), T250 (≠ M235), Y254 (≠ M239), F266 (= F251), K269 (= K254)
Query Sequence
>Dsui_2807 FitnessBrowser__PS:Dsui_2807
MTNQEPILLREDRPDGRTTLVLNRPAQFNSLSNAMLETLLAELQSIAADKTVRVVVLQGA
GKAFCAGHDLKEMRSNHDKAFMQALFKLCAKVMLTIQEMPQPVIARIHGIATAAGCQLVS
MCDLAVAADVAKFAVSGINVGLFCSTPAVGLARNMGRKEALEMLLTGEFIDAGEAQRRGL
VNRVVALGDLDEAVEHLVQSILAKSPVAVATGKQMFYKQLEMGIEAAYQYAGEVMACNMM
AGDAAEGIDAFIEKRKPVWQAA
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