SitesBLAST
Comparing 6937190 FitnessBrowser__SB2B:6937190 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)
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)
29% identity, 91% coverage: 14:265/276 of query aligns to 8:266/276 of O69762
- K29 (≠ V35) binding
- A68 (= A74) binding
- M70 (≠ A76) binding
- L72 (= L78) binding
- Y75 (≠ W80) binding
- G120 (= G124) binding
- S123 (≠ G127) mutation to A: Reduced kcat compared to wild-type but not markerdly.
- S142 (= S146) binding
- E143 (= E147) mutation to A: Abolishes catalytic activity.
- W146 (≠ L150) binding
- G151 (≠ A155) binding
- Y239 (≠ S241) 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
6l3pA Crystal strcuture of feruloyl-coa hydratase lyase(fchl) complexed with coa
28% identity, 88% coverage: 8:249/276 of query aligns to 1:241/244 of 6l3pA
- active site: M69 (≠ A76), Y74 (≠ W80), R86 (= R97), Q90 (≠ N101), G114 (= G124), S117 (≠ G127), S136 (= S146), E137 (= E147), I142 (≠ L152), P144 (= P154), G145 (≠ A155), Y233 (≠ S241)
- binding coenzyme a: K28 (≠ V35), R29 (≠ H36), A31 (= A38), A67 (= A74), M69 (≠ A76), D70 (= D77), L71 (= L78), G113 (= G123)
Sites not aligning to the query:
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
27% identity, 92% coverage: 14:268/276 of query aligns to 3:256/259 of 5zaiC
- active site: A65 (= A76), F70 (≠ M81), S82 (≠ L93), R86 (= R97), G110 (= G124), E113 (≠ G127), P132 (≠ S146), E133 (= E147), I138 (≠ L152), P140 (= P154), G141 (≠ A155), A226 (≠ I232), F236 (≠ R248)
- binding coenzyme a: K24 (≠ V35), L25 (≠ H36), A63 (= A74), G64 (= G75), A65 (= A76), D66 (= D77), I67 (≠ L78), P132 (≠ S146), R166 (= R179), F248 (= F260), K251 (= K263)
2vssD Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
29% identity, 86% coverage: 14:249/276 of query aligns to 6:245/246 of 2vssD
- active site: M68 (≠ A76), Y73 (≠ W80), D78 (≠ A85), R90 (= R97), Q94 (≠ N101), G118 (= G124), S121 (≠ G127), S140 (= S146), E141 (= E147), I146 (≠ L152), P148 (= P154), G149 (≠ A155), Y237 (≠ S241)
- binding acetyl coenzyme *a: E26 (= E34), K27 (≠ V35), R28 (≠ H36), A30 (= A38), A66 (= A74), M68 (≠ A76), D69 (= D77), L70 (= L78), F74 (≠ M81), W114 (≠ A120), F116 (≠ Y122), S140 (= S146)
- binding 4-hydroxy-3-methoxybenzaldehyde: M68 (≠ A76), Y73 (≠ W80), F74 (≠ M81), Q96 (≠ M103), E141 (= E147), G149 (≠ A155), N150 (vs. gap)
2vssB Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
29% identity, 86% coverage: 14:249/276 of query aligns to 5:244/247 of 2vssB
- active site: M67 (≠ A76), Y72 (≠ W80), D77 (≠ A85), R89 (= R97), Q93 (≠ N101), G117 (= G124), S120 (≠ G127), S139 (= S146), E140 (= E147), I145 (≠ L152), P147 (= P154), G148 (≠ A155), Y236 (≠ S241)
- binding acetyl coenzyme *a: E25 (= E34), K26 (≠ V35), R27 (≠ H36), A29 (= A38), A65 (= A74), M67 (≠ A76), D68 (= D77), W113 (≠ A120), F115 (≠ Y122), G117 (= G124), S139 (= S146), E140 (= E147)
Sites not aligning to the query:
6p5uE Structure of an enoyl-coa hydratase/aldolase isolated from a lignin- degrading consortium (see paper)
29% identity, 78% coverage: 14:228/276 of query aligns to 5:224/246 of 6p5uE
- active site: M67 (≠ A76), Y72 (≠ W80), D77 (vs. gap), R89 (≠ D95), A93 (= A100), G117 (= G124), T120 (≠ G127), E140 (= E147), I145 (≠ L152), P147 (= P154), A148 (= A155)
- binding coenzyme a: D25 (≠ E34), K26 (≠ V35), R27 (≠ H36), A29 (= A38), A65 (= A74), M67 (≠ A76), D68 (= D77), L69 (= L78), W113 (≠ A120), F115 (≠ Y122), S139 (= S146), W143 (≠ L150)
Sites not aligning to the query:
7xwtB Crystal structure of feruoyl-coa hydratase/lyase complexed with coa from sphingomonas paucimobilis (see paper)
28% identity, 89% coverage: 17:263/276 of query aligns to 8:246/277 of 7xwtB
- binding acetyl coenzyme *a: T25 (≠ E34), K26 (≠ V35), R27 (≠ H36), A29 (= A38), A65 (= A74), G66 (= G75), M67 (≠ A76), D68 (= D77), L69 (= L78), F73 (≠ M81), F114 (≠ Y122), G116 (= G124), S138 (= S146), W142 (≠ L150)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
29% identity, 93% coverage: 13:270/276 of query aligns to 1:255/256 of 3h81A
- active site: A64 (= A76), M69 (= M81), T79 (≠ K94), F83 (≠ M103), G107 (= G124), E110 (≠ G127), P129 (≠ S146), E130 (= E147), V135 (≠ L152), P137 (= P154), G138 (≠ A155), L223 (≠ I232), F233 (≠ V249)
- binding calcium ion: F233 (≠ V249), Q238 (= Q254)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
29% identity, 93% coverage: 13:269/276 of query aligns to 2:255/255 of 3q0jC
- active site: A65 (= A76), M70 (= M81), T80 (≠ K94), F84 (≠ M103), G108 (= G124), E111 (≠ G127), P130 (≠ S146), E131 (= E147), V136 (≠ L152), P138 (= P154), G139 (≠ A155), L224 (≠ I232), F234 (≠ V249)
- binding acetoacetyl-coenzyme a: Q23 (≠ E34), A24 (≠ V35), L25 (≠ H36), A27 (= A38), A63 (= A74), G64 (= G75), A65 (= A76), D66 (= D77), I67 (≠ L78), K68 (≠ N79), M70 (= M81), F84 (≠ M103), G107 (= G123), G108 (= G124), E111 (≠ G127), P130 (≠ S146), E131 (= E147), P138 (= P154), G139 (≠ A155), M140 (≠ V156)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
29% identity, 93% coverage: 13:269/276 of query aligns to 2:255/255 of 3q0gC
- active site: A65 (= A76), M70 (= M81), T80 (≠ K94), F84 (≠ M103), G108 (= G124), E111 (≠ G127), P130 (≠ S146), E131 (= E147), V136 (≠ L152), P138 (= P154), G139 (≠ A155), L224 (≠ I232), F234 (≠ V249)
- binding coenzyme a: L25 (≠ H36), A63 (= A74), I67 (≠ L78), K68 (≠ N79), Y104 (≠ A120), P130 (≠ S146), E131 (= E147), L134 (= L150)
7xwvA Feruloyl-coa hydratase/lyase complexed with vanillin and coenzyme a (see paper)
27% identity, 88% coverage: 17:260/276 of query aligns to 7:243/244 of 7xwvA
- binding coenzyme a: T24 (≠ E34), K25 (≠ V35), R26 (≠ H36), A64 (= A74), G65 (= G75), M66 (≠ A76), D67 (= D77), L68 (= L78), W111 (≠ A120), F113 (≠ Y122), G114 (= G123), G115 (= G124), S137 (= S146)
- binding 4-hydroxy-3-methoxybenzaldehyde: M66 (≠ A76), Y71 (≠ W80), F72 (≠ M81), E138 (= E147), G146 (≠ A155), G147 (≠ V156)
Q7CQ56 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
28% identity, 93% coverage: 9:266/276 of query aligns to 17:276/285 of Q7CQ56
3h02A 2.15 angstrom resolution crystal structure of naphthoate synthase from salmonella typhimurium.
27% identity, 93% coverage: 9:266/276 of query aligns to 13:257/266 of 3h02A
- active site: G82 (≠ A76), H86 (≠ W80), L90 (≠ M87), G114 (= G124), V117 (≠ G127), G137 (≠ E147), S142 (≠ L152), D144 (≠ P154), G145 (≠ A155), A231 (≠ T240), Y239 (≠ R248)
- binding bicarbonate ion: G113 (= G123), Q135 (≠ L145), G137 (≠ E147), W165 (≠ M174)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
29% identity, 93% coverage: 13:269/276 of query aligns to 1:250/250 of 3q0gD
- active site: A64 (= A76), M69 (= M81), T75 (≠ K94), F79 (≠ M103), G103 (= G124), E106 (≠ G127), P125 (≠ S146), E126 (= E147), V131 (≠ L152), P133 (= P154), G134 (≠ A155), L219 (≠ I232), F229 (≠ V249)
- binding Butyryl Coenzyme A: F225 (≠ A245), F241 (= F260)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
35% identity, 66% coverage: 12:194/276 of query aligns to 1:180/258 of 1mj3A
- active site: A68 (= A76), M73 (= M81), S83 (≠ D91), L85 (= L93), G109 (= G124), E112 (≠ G127), P131 (≠ S146), E132 (= E147), T137 (≠ L152), P139 (= P154), G140 (vs. gap)
- binding hexanoyl-coenzyme a: K26 (≠ E34), A27 (≠ V35), L28 (≠ H36), A30 (= A38), A66 (= A74), G67 (= G75), A68 (= A76), D69 (= D77), I70 (≠ L78), G109 (= G124), P131 (≠ S146), E132 (= E147), L135 (= L150), G140 (vs. gap)
Sites not aligning to the query:
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
29% identity, 92% coverage: 12:264/276 of query aligns to 1:253/260 of 2hw5C
- active site: A68 (= A76), M73 (= M81), S83 (≠ A96), L87 (≠ A100), G111 (= G124), E114 (≠ G127), P133 (≠ S146), E134 (= E147), T139 (≠ L152), P141 (= P154), G142 (vs. gap), K227 (≠ R237), F237 (≠ R248)
- binding crotonyl coenzyme a: K26 (≠ E34), A27 (≠ V35), L28 (≠ H36), A30 (= A38), K62 (= K70), I70 (≠ L78), F109 (≠ Y122)
3t88A Crystal structure of escherichia coli menb in complex with substrate analogue, osb-ncoa (see paper)
28% identity, 93% coverage: 9:266/276 of query aligns to 13:272/281 of 3t88A
- active site: G82 (≠ A76), R87 (= R82), Y93 (≠ D88), H101 (≠ A96), L105 (≠ A100), G129 (= G124), V132 (≠ G127), G152 (≠ E147), S157 (≠ L152), D159 (≠ P154), G160 (≠ A155), A246 (≠ T240), Y254 (≠ R248)
- binding o-succinylbenzoyl-N-coenzyme A: Q39 (≠ E34), V40 (= V35), R41 (≠ H36), A43 (= A38), S80 (≠ A74), G81 (= G75), G82 (≠ A76), D83 (= D77), Q84 (≠ L78), K85 (≠ N79), Y93 (≠ D88), V104 (≠ L99), L105 (≠ A100), Y125 (≠ A120), G129 (= G124), T151 (≠ S146), V155 (≠ L150), F158 (≠ I153), D159 (≠ P154), T250 (≠ I244), Y254 (≠ R248), F266 (= F260), K269 (= K263)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
34% identity, 66% coverage: 12:194/276 of query aligns to 1:182/260 of 1dubA
- active site: A68 (= A76), M73 (= M81), S83 (≠ D91), L87 (≠ A100), G111 (= G124), E114 (≠ G127), P133 (≠ S146), E134 (= E147), T139 (≠ L152), P141 (= P154), G142 (vs. gap)
- binding acetoacetyl-coenzyme a: K26 (≠ E34), A27 (≠ V35), L28 (≠ H36), A30 (= A38), A66 (= A74), A68 (= A76), D69 (= D77), I70 (≠ L78), Y107 (≠ A120), G110 (= G123), G111 (= G124), E114 (≠ G127), P133 (≠ S146), E134 (= E147), L137 (= L150), G142 (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)
28% identity, 93% coverage: 9:266/276 of query aligns to 17:276/285 of 4i42A
- active site: G86 (≠ A76), R91 (= R82), Y97 (≠ D88), H105 (≠ A96), L109 (≠ A100), G133 (= G124), V136 (≠ G127), G156 (≠ E147), S161 (≠ L152), D163 (≠ P154), G164 (≠ A155), A250 (≠ T240), Y258 (≠ R248)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (= V35), R45 (≠ H36), S84 (≠ A74), G85 (= G75), G86 (≠ A76), D87 (= D77), Q88 (≠ L78), K89 (≠ N79), Y97 (≠ D88), V108 (≠ L99), Y129 (≠ A120), G133 (= G124), T155 (≠ S146), S161 (≠ L152), T254 (≠ I244), F270 (= F260), K273 (= K263)
P0ABU0 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Escherichia coli (strain K12) (see 4 papers)
28% identity, 93% coverage: 9:266/276 of query aligns to 17:276/285 of P0ABU0
- R45 (≠ H36) binding in other chain
- SGGDQK 84:89 (≠ AGADLN 74:79) binding in other chain
- K89 (≠ N79) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- R91 (= R82) mutation to A: Loss of DHNA-CoA synthase activity.
- Y97 (≠ D88) binding in other chain; mutation to F: Loss of DHNA-CoA synthase activity.
- YSIGG 129:133 (≠ AAYGG 120:124) binding in other chain
- Q154 (≠ L145) 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 (≠ LSE 145:147) binding
- T155 (≠ S146) binding in other chain
- G156 (≠ E147) mutation to D: Loss of DHNA-CoA synthase activity.
- S161 (≠ L152) binding in other chain
- W184 (≠ M174) mutation to F: Reduces the specific DHNA-CoA synthase activity by 530-fold, whereas its affinity for hydrogencarbonate is reduced by 20-fold.
- Y258 (≠ R248) binding
- R267 (≠ L257) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- F270 (= F260) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- K273 (= K263) binding ; mutation to A: Impairs protein folding.
Query Sequence
>6937190 FitnessBrowser__SB2B:6937190
MTTMTSIAELSASFSRIRLELNGRVGYLILNRPEVHNAFDEVMISEMTQAINAFAHESEC
AVMVLKSDGKHFSAGADLNWMRKQAAMDFDDNLKDARELANLMDTLDRFPKPSIALVNGA
AYGGALGLVCCCDIAISSHKASFCLSEVKLGLIPAVISPYVVRAMGPRQSRRYMLTAERF
DASMALALGVVHEIADDLDAAAAPIIQNLLSGSPQALGWCKSLIARLQSGVIDEHTRDYT
SERIARIRVSAEGQEGLNAFFDKRSPAWVNDTGSKD
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