SitesBLAST
Comparing N515DRAFT_0930 N515DRAFT_0930 methylglutaconyl-CoA hydratase 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)
6l3pA Crystal strcuture of feruloyl-coa hydratase lyase(fchl) complexed with coa
34% identity, 80% coverage: 2:211/264 of query aligns to 7:214/244 of 6l3pA
- active site: M69 (≠ A64), Y74 (≠ M69), R86 (= R81), Q90 (≠ L85), G114 (= G112), S117 (≠ G115), S136 (≠ T134), E137 (= E135), I142 (≠ L140), P144 (= P142), G145 (≠ A143)
- binding coenzyme a: K28 (≠ V23), R29 (≠ H24), A31 (= A26), A67 (= A62), M69 (≠ A64), D70 (= D65), L71 (= L66), G113 (= G111)
Sites not aligning to the query:
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
35% identity, 95% coverage: 10:261/264 of query aligns to 12:250/250 of 3q0gD
- active site: A64 (= A64), M69 (= M69), T75 (≠ E77), F79 (≠ R81), G103 (= G112), E106 (≠ G115), P125 (≠ T134), E126 (= E135), V131 (≠ L140), P133 (= P142), G134 (≠ A143), L219 (≠ D229), F229 (≠ R240)
- binding Butyryl Coenzyme A: F225 (≠ I236), F241 (= F252)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
34% identity, 95% coverage: 10:261/264 of query aligns to 13:255/255 of 3q0jC
- active site: A65 (= A64), M70 (= M69), T80 (≠ E77), F84 (≠ R81), G108 (= G112), E111 (≠ G115), P130 (≠ T134), E131 (= E135), V136 (≠ L140), P138 (= P142), G139 (≠ A143), L224 (≠ D229), F234 (≠ R240)
- binding acetoacetyl-coenzyme a: Q23 (= Q22), A24 (≠ V23), L25 (≠ H24), A27 (= A26), A63 (= A62), G64 (= G63), A65 (= A64), D66 (= D65), I67 (≠ L66), K68 (≠ N67), M70 (= M69), F84 (≠ R81), G107 (= G111), G108 (= G112), E111 (≠ G115), P130 (≠ T134), E131 (= E135), P138 (= P142), G139 (≠ A143), M140 (≠ V144)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
34% identity, 95% coverage: 10:261/264 of query aligns to 13:255/255 of 3q0gC
- active site: A65 (= A64), M70 (= M69), T80 (≠ E77), F84 (≠ R81), G108 (= G112), E111 (≠ G115), P130 (≠ T134), E131 (= E135), V136 (≠ L140), P138 (= P142), G139 (≠ A143), L224 (≠ D229), F234 (≠ R240)
- binding coenzyme a: L25 (≠ H24), A63 (= A62), I67 (≠ L66), K68 (≠ N67), Y104 (≠ A108), P130 (≠ T134), E131 (= E135), L134 (= L138)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
28% identity, 99% coverage: 2:263/264 of query aligns to 3:259/259 of 5zaiC
- active site: A65 (= A64), F70 (≠ M69), S82 (= S84), R86 (≠ A88), G110 (= G112), E113 (≠ G115), P132 (≠ T134), E133 (= E135), I138 (≠ L140), P140 (= P142), G141 (≠ A143), A226 (≠ D229), F236 (≠ R240)
- binding coenzyme a: K24 (≠ V23), L25 (≠ H24), A63 (= A62), G64 (= G63), A65 (= A64), D66 (= D65), I67 (≠ L66), P132 (≠ T134), R166 (≠ L167), F248 (= F252), K251 (= K255)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
34% identity, 95% coverage: 10:261/264 of query aligns to 12:254/256 of 3h81A
- active site: A64 (= A64), M69 (= M69), T79 (≠ E77), F83 (≠ R81), G107 (= G112), E110 (≠ G115), P129 (≠ T134), E130 (= E135), V135 (≠ L140), P137 (= P142), G138 (≠ A143), L223 (≠ D229), F233 (≠ R240)
- binding calcium ion: F233 (≠ R240), Q238 (≠ G245)
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: 2:257/264 of query aligns to 8:266/276 of O69762
- K29 (≠ V23) binding
- A68 (= A62) binding
- M70 (≠ A64) binding
- L72 (= L66) binding
- Y75 (≠ W68) binding
- G120 (= G112) binding
- S123 (≠ G115) mutation to A: Reduced kcat compared to wild-type but not markerdly.
- S142 (≠ T134) binding
- E143 (= E135) mutation to A: Abolishes catalytic activity.
- W146 (≠ L138) binding
- G151 (≠ A143) binding
- Y239 (≠ N232) 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
2uzfA Crystal structure of staphylococcus aureus 1,4-dihydroxy-2-naphthoyl coa synthase (menb) in complex with acetoacetyl coa (see paper)
32% identity, 78% coverage: 2:206/264 of query aligns to 7:203/260 of 2uzfA
- active site: G70 (≠ A64), R80 (≠ S84), L84 (≠ A88), G108 (= G112), V111 (≠ G115), T130 (= T134), G131 (≠ E135), S136 (≠ L140), D138 (≠ P142), A139 (= A143)
- binding acetoacetyl-coenzyme a: V28 (= V23), R29 (≠ H24), S68 (≠ A62), G69 (= G63), G70 (≠ A64), D71 (= D65), Y104 (≠ A108), G108 (= G112)
Sites not aligning to the query:
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, 78% coverage: 2:206/264 of query aligns to 12:216/273 of Q5HH38
- R34 (≠ H24) binding in other chain
- SGGDQ 73:77 (≠ AGADL 62:66) binding in other chain
- S149 (≠ L140) binding in other chain
6p5uE Structure of an enoyl-coa hydratase/aldolase isolated from a lignin- degrading consortium (see paper)
33% identity, 85% coverage: 3:226/264 of query aligns to 6:232/246 of 6p5uE
- active site: M67 (≠ A64), Y72 (≠ W68), D77 (≠ A73), R89 (≠ L87), A93 (vs. gap), G117 (= G112), T120 (≠ G115), E140 (= E135), I145 (≠ L140), P147 (= P142), A148 (= A143)
- binding coenzyme a: D25 (≠ Q22), K26 (≠ V23), R27 (≠ H24), A29 (= A26), A65 (= A62), M67 (≠ A64), D68 (= D65), L69 (= L66), W113 (≠ A108), F115 (≠ Y110), S139 (≠ T134), W143 (≠ L138)
Sites not aligning to the query:
2vssB Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
32% identity, 80% coverage: 2:212/264 of query aligns to 5:218/247 of 2vssB
- active site: M67 (≠ A64), Y72 (≠ W68), D77 (vs. gap), R89 (= R81), Q93 (≠ L85), G117 (= G112), S120 (≠ G115), S139 (≠ T134), E140 (= E135), I145 (≠ L140), P147 (= P142), G148 (≠ A143)
- binding acetyl coenzyme *a: E25 (≠ Q22), K26 (≠ V23), R27 (≠ H24), A29 (= A26), A65 (= A62), M67 (≠ A64), D68 (= D65), W113 (≠ A108), F115 (≠ Y110), G117 (= G112), S139 (≠ T134), E140 (= E135)
Sites not aligning to the query:
2vssD Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
32% identity, 80% coverage: 2:212/264 of query aligns to 6:219/246 of 2vssD
- active site: M68 (≠ A64), Y73 (≠ W68), D78 (vs. gap), R90 (= R81), Q94 (≠ L85), G118 (= G112), S121 (≠ G115), S140 (≠ T134), E141 (= E135), I146 (≠ L140), P148 (= P142), G149 (≠ A143)
- binding acetyl coenzyme *a: E26 (≠ Q22), K27 (≠ V23), R28 (≠ H24), A30 (= A26), A66 (= A62), M68 (≠ A64), D69 (= D65), L70 (= L66), F74 (≠ M69), W114 (≠ A108), F116 (≠ Y110), S140 (≠ T134)
- binding 4-hydroxy-3-methoxybenzaldehyde: M68 (≠ A64), Y73 (≠ W68), F74 (≠ M69), Q96 (≠ L87), E141 (= E135), G149 (≠ A143), N150 (vs. gap)
Sites not aligning to the query:
4i42A E.Coli. 1,4-dihydroxy-2-naphthoyl coenzyme a synthase (ecmenb) in complex with 1-hydroxy-2-naphthoyl-coa (see paper)
31% identity, 93% coverage: 12:256/264 of query aligns to 33:274/285 of 4i42A
- active site: G86 (≠ A64), R91 (= R70), Y97 (≠ S76), H105 (≠ S84), L109 (≠ A88), G133 (= G112), V136 (≠ G115), G156 (≠ E135), S161 (≠ L140), D163 (≠ P142), G164 (≠ A143), A250 (≠ R230), Y258 (≠ R240)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (= V23), R45 (≠ H24), S84 (≠ A62), G85 (= G63), G86 (≠ A64), D87 (= D65), Q88 (≠ L66), K89 (≠ N67), Y97 (≠ S76), V108 (≠ L87), Y129 (≠ A108), G133 (= G112), T155 (= T134), S161 (≠ L140), T254 (≠ E234), F270 (= F252), K273 (= K255)
P0ABU0 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Escherichia coli (strain K12) (see 4 papers)
31% identity, 93% coverage: 12:256/264 of query aligns to 33:274/285 of P0ABU0
- R45 (≠ H24) binding in other chain
- SGGDQK 84:89 (≠ AGADLN 62:67) binding in other chain
- K89 (≠ N67) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- R91 (= R70) mutation to A: Loss of DHNA-CoA synthase activity.
- Y97 (≠ S76) binding in other chain; mutation to F: Loss of DHNA-CoA synthase activity.
- YSIGG 129:133 (≠ AAYGG 108:112) binding in other chain
- Q154 (≠ L133) 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 (≠ LTE 133:135) binding
- T155 (= T134) binding in other chain
- G156 (≠ E135) mutation to D: Loss of DHNA-CoA synthase activity.
- S161 (≠ L140) binding in other chain
- W184 (≠ F162) mutation to F: Reduces the specific DHNA-CoA synthase activity by 530-fold, whereas its affinity for hydrogencarbonate is reduced by 20-fold.
- Y258 (≠ R240) binding
- R267 (≠ L249) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- F270 (= F252) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- K273 (= K255) binding ; mutation to A: Impairs protein folding.
3t88A Crystal structure of escherichia coli menb in complex with substrate analogue, osb-ncoa (see paper)
31% identity, 93% coverage: 12:256/264 of query aligns to 29:270/281 of 3t88A
- active site: G82 (≠ A64), R87 (= R70), Y93 (≠ S76), H101 (≠ S84), L105 (≠ A88), G129 (= G112), V132 (≠ G115), G152 (≠ E135), S157 (≠ L140), D159 (≠ P142), G160 (≠ A143), A246 (≠ R230), Y254 (≠ R240)
- binding o-succinylbenzoyl-N-coenzyme A: Q39 (= Q22), V40 (= V23), R41 (≠ H24), A43 (= A26), S80 (≠ A62), G81 (= G63), G82 (≠ A64), D83 (= D65), Q84 (≠ L66), K85 (≠ N67), Y93 (≠ S76), V104 (≠ L87), L105 (≠ A88), Y125 (≠ A108), G129 (= G112), T151 (= T134), V155 (≠ L138), F158 (≠ V141), D159 (≠ P142), T250 (≠ E234), Y254 (≠ R240), F266 (= F252), K269 (= K255)
Q7CQ56 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
31% identity, 97% coverage: 2:256/264 of query aligns to 22:274/285 of Q7CQ56
4elxA Structure of apo e.Coli. 1,4-dihydroxy-2- naphthoyl coa synthases with cl (see paper)
30% identity, 93% coverage: 12:256/264 of query aligns to 30:257/268 of 4elxA
- active site: G83 (≠ A64), H88 (≠ S84), L92 (≠ A88), G116 (= G112), V119 (≠ G115), G139 (≠ E135), S144 (≠ L140), D146 (≠ P142), G147 (≠ A143), A233 (≠ R230), Y241 (≠ R240)
- binding chloride ion: G115 (= G111), G139 (≠ E135), W167 (≠ F162)
4elwA Structure of e. Coli. 1,4-dihydroxy-2- naphthoyl coenzyme a synthases (menb) in complex with nitrate (see paper)
30% identity, 93% coverage: 12:256/264 of query aligns to 30:256/267 of 4elwA
- active site: G83 (≠ A64), L91 (≠ A88), G115 (= G112), V118 (≠ G115), G138 (≠ E135), S143 (≠ L140), D145 (≠ P142), G146 (≠ A143), A232 (≠ R230), Y240 (≠ R240)
- binding nitrate ion: G114 (= G111), T137 (= T134), G138 (≠ E135), F144 (≠ V141), W166 (≠ F162)
3h02A 2.15 angstrom resolution crystal structure of naphthoate synthase from salmonella typhimurium.
30% identity, 97% coverage: 2:256/264 of query aligns to 18:255/266 of 3h02A
- active site: G82 (≠ A64), H86 (≠ S84), L90 (≠ A88), G114 (= G112), V117 (≠ G115), G137 (≠ E135), S142 (≠ L140), D144 (≠ P142), G145 (≠ A143), A231 (≠ R230), Y239 (≠ R240)
- binding bicarbonate ion: G113 (= G111), Q135 (≠ L133), G137 (≠ E135), W165 (≠ F162)
3p85A Crystal structure enoyl-coa hydratase from mycobacterium avium (see paper)
36% identity, 67% coverage: 13:188/264 of query aligns to 11:169/224 of 3p85A
- active site: L62 (≠ A64), L67 (≠ N80), P68 (≠ R81), G92 (= G112), E95 (≠ G115), T114 (= T134), H115 (≠ E135), L120 (= L140), P122 (= P142), T123 (≠ A143)
- binding calcium ion: D43 (= D45), D45 (≠ N47)
Sites not aligning to the query:
Query Sequence
>N515DRAFT_0930 N515DRAFT_0930 methylglutaconyl-CoA hydratase
MYTSLQLADRAGVRTVTMNRPQVHNAFDDSLIAELTDALAAAGRDENVRAVVLTGAGASF
SAGADLNWMRGMAKASEAENREDSLRLAALMRTLQFLPKPTVARVNGAAYGGGVGLIACC
DIAIGVDSAKFGLTEVKLGLVPAVISPYVIAAIGLRQSRRLFLTGELFDASTAQRIGLLH
QCVRAEELDDALAGVLAAFAKAGPVAQAQAKRLALRVAGQDQAQAERIDRENAELIARLR
VSAEGQEGLGAFLDKRAAAWTAQA
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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