SitesBLAST
Comparing Pf6N2E2_2193 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_2193 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)
6p5uE Structure of an enoyl-coa hydratase/aldolase isolated from a lignin- degrading consortium (see paper)
35% identity, 81% coverage: 1:220/272 of query aligns to 2:223/246 of 6p5uE
- active site: M67 (≠ A67), Y72 (= Y80), D77 (= D85), R89 (vs. gap), A93 (≠ M94), G117 (= G115), T120 (≠ G118), E140 (= E138), I145 (≠ L143), P147 (= P145), A148 (= A146)
- binding coenzyme a: D25 (≠ S25), K26 (= K26), R27 (≠ N27), A29 (= A29), A65 (= A65), M67 (≠ A67), D68 (= D68), L69 (= L69), W113 (≠ A111), F115 (= F113), S139 (= S137), W143 (≠ I141)
Sites not aligning to the query:
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
30% identity, 96% coverage: 4:264/272 of query aligns to 3:259/259 of 5zaiC
- active site: A65 (= A67), F70 (≠ M72), S82 (≠ L84), R86 (= R88), G110 (= G115), E113 (≠ G118), P132 (≠ S137), E133 (= E138), I138 (≠ L143), P140 (= P145), G141 (≠ A146), A226 (≠ T233), F236 (≠ R241)
- binding coenzyme a: K24 (= K26), L25 (≠ N27), A63 (= A65), G64 (= G66), A65 (= A67), D66 (= D68), I67 (≠ L69), P132 (≠ S137), R166 (= R170), F248 (= F253), K251 (= K256)
2vssD Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
34% identity, 74% coverage: 15:214/272 of query aligns to 16:218/246 of 2vssD
- active site: M68 (≠ A67), Y73 (= Y80), D78 (= D85), R90 (= R88), Q94 (≠ E92), G118 (= G115), S121 (≠ G118), S140 (= S137), E141 (= E138), I146 (≠ L143), P148 (= P145), G149 (≠ A146)
- binding acetyl coenzyme *a: E26 (≠ S25), K27 (= K26), R28 (≠ N27), A30 (= A29), A66 (= A65), M68 (≠ A67), D69 (= D68), L70 (= L69), F74 (≠ H81), W114 (≠ A111), F116 (= F113), S140 (= S137)
- binding 4-hydroxy-3-methoxybenzaldehyde: M68 (≠ A67), Y73 (= Y80), F74 (≠ H81), Q96 (≠ M94), E141 (= E138), G149 (≠ A146), 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)
34% identity, 74% coverage: 15:214/272 of query aligns to 15:217/247 of 2vssB
- active site: M67 (≠ A67), Y72 (= Y80), D77 (= D85), R89 (= R88), Q93 (≠ E92), G117 (= G115), S120 (≠ G118), S139 (= S137), E140 (= E138), I145 (≠ L143), P147 (= P145), G148 (≠ A146)
- binding acetyl coenzyme *a: E25 (≠ S25), K26 (= K26), R27 (≠ N27), A29 (= A29), A65 (= A65), M67 (≠ A67), D68 (= D68), W113 (≠ A111), F115 (= F113), G117 (= G115), S139 (= S137), E140 (= E138)
Sites not aligning to the query:
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)
34% identity, 74% coverage: 15:214/272 of query aligns to 18:220/276 of O69762
- K29 (= K26) binding
- A68 (= A65) binding
- M70 (≠ A67) binding
- L72 (= L69) binding
- Y75 (= Y80) binding
- G120 (= G115) binding
- S123 (≠ G118) mutation to A: Reduced kcat compared to wild-type but not markerdly.
- S142 (= S137) binding
- E143 (= E138) mutation to A: Abolishes catalytic activity.
- W146 (≠ I141) binding
- G151 (≠ A146) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 239 binding ; Y→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.
6l3pA Crystal strcuture of feruloyl-coa hydratase lyase(fchl) complexed with coa
33% identity, 74% coverage: 15:214/272 of query aligns to 17:214/244 of 6l3pA
- active site: M69 (≠ A67), Y74 (≠ M72), R86 (= R88), Q90 (≠ E92), G114 (= G115), S117 (≠ G118), S136 (= S137), E137 (= E138), I142 (≠ L143), P144 (= P145), G145 (≠ A146)
- binding coenzyme a: K28 (= K26), R29 (≠ N27), A31 (= A29), A67 (= A65), M69 (≠ A67), D70 (= D68), L71 (= L69), G113 (= G114)
Sites not aligning to the query:
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
30% identity, 95% coverage: 3:261/272 of query aligns to 1:253/256 of 3h81A
- active site: A64 (= A67), M69 (= M72), T79 (= T82), F83 (≠ A91), G107 (= G115), E110 (≠ G118), P129 (≠ S137), E130 (= E138), V135 (≠ L143), P137 (= P145), G138 (≠ A146), L223 (vs. gap), F233 (≠ I237)
- binding calcium ion: F233 (≠ I237), Q238 (≠ G246)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
30% identity, 95% coverage: 3:261/272 of query aligns to 2:254/255 of 3q0jC
- active site: A65 (= A67), M70 (= M72), T80 (= T82), F84 (≠ A91), G108 (= G115), E111 (≠ G118), P130 (≠ S137), E131 (= E138), V136 (≠ L143), P138 (= P145), G139 (≠ A146), L224 (vs. gap), F234 (≠ I237)
- binding acetoacetyl-coenzyme a: Q23 (≠ S25), A24 (≠ K26), L25 (≠ N27), A27 (= A29), A63 (= A65), G64 (= G66), A65 (= A67), D66 (= D68), I67 (≠ L69), K68 (≠ A70), M70 (= M72), F84 (≠ A91), G107 (= G114), G108 (= G115), E111 (≠ G118), P130 (≠ S137), E131 (= E138), P138 (= P145), G139 (≠ A146), M140 (≠ V147)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
30% identity, 95% coverage: 3:261/272 of query aligns to 2:254/255 of 3q0gC
- active site: A65 (= A67), M70 (= M72), T80 (= T82), F84 (≠ A91), G108 (= G115), E111 (≠ G118), P130 (≠ S137), E131 (= E138), V136 (≠ L143), P138 (= P145), G139 (≠ A146), L224 (vs. gap), F234 (≠ I237)
- binding coenzyme a: L25 (≠ N27), A63 (= A65), I67 (≠ L69), K68 (≠ A70), Y104 (≠ A111), P130 (≠ S137), E131 (= E138), L134 (≠ I141)
Q7CQ56 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
27% identity, 98% coverage: 2:267/272 of query aligns to 20:284/285 of Q7CQ56
4i42A E.Coli. 1,4-dihydroxy-2-naphthoyl coenzyme a synthase (ecmenb) in complex with 1-hydroxy-2-naphthoyl-coa (see paper)
27% identity, 98% coverage: 2:267/272 of query aligns to 20:284/285 of 4i42A
- active site: G86 (≠ A67), R91 (≠ E77), Y97 (≠ N83), H105 (vs. gap), L109 (≠ A91), G133 (= G115), V136 (≠ G118), G156 (≠ E138), S161 (vs. gap), D163 (≠ A144), G164 (≠ P145), A250 (≠ T233), Y258 (≠ R241)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (≠ K26), R45 (≠ N27), S84 (≠ A65), G85 (= G66), G86 (≠ A67), D87 (= D68), Q88 (= Q74), K89 (≠ S75), Y97 (≠ N83), V108 (≠ L90), Y129 (≠ A111), G133 (= G115), T155 (≠ S137), S161 (vs. gap), T254 (≠ I237), F270 (= F253), K273 (= K256)
P0ABU0 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Escherichia coli (strain K12) (see 4 papers)
27% identity, 98% coverage: 2:267/272 of query aligns to 20:284/285 of P0ABU0
- R45 (≠ N27) binding in other chain
- SGGD-----QK 84:89 (≠ AGADLAWMQQS 65:75) binding in other chain
- K89 (≠ S75) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- R91 (≠ E77) mutation to A: Loss of DHNA-CoA synthase activity.
- Y97 (≠ N83) binding in other chain; mutation to F: Loss of DHNA-CoA synthase activity.
- YSIGG 129:133 (≠ AAFGG 111:115) binding in other chain
- Q154 (≠ L136) 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 136:138) binding
- T155 (≠ S137) binding in other chain
- G156 (≠ E138) mutation to D: Loss of DHNA-CoA synthase activity.
- S161 (vs. gap) binding in other chain
- W184 (≠ A165) mutation to F: Reduces the specific DHNA-CoA synthase activity by 530-fold, whereas its affinity for hydrogencarbonate is reduced by 20-fold.
- Y258 (≠ R241) binding
- R267 (≠ L250) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- F270 (= F253) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- K273 (= K256) binding ; mutation to A: Impairs protein folding.
3t88A Crystal structure of escherichia coli menb in complex with substrate analogue, osb-ncoa (see paper)
27% identity, 98% coverage: 2:267/272 of query aligns to 16:280/281 of 3t88A
- active site: G82 (≠ A67), R87 (≠ E77), Y93 (≠ N83), H101 (vs. gap), L105 (≠ A91), G129 (= G115), V132 (≠ G118), G152 (≠ E138), S157 (vs. gap), D159 (≠ A144), G160 (≠ P145), A246 (≠ T233), Y254 (≠ R241)
- binding o-succinylbenzoyl-N-coenzyme A: Q39 (≠ S25), V40 (≠ K26), R41 (≠ N27), A43 (= A29), S80 (≠ A65), G81 (= G66), G82 (≠ A67), D83 (= D68), Q84 (= Q74), K85 (≠ S75), Y93 (≠ N83), V104 (≠ L90), L105 (≠ A91), Y125 (≠ A111), G129 (= G115), T151 (≠ S137), V155 (≠ I141), F158 (≠ L143), D159 (≠ A144), T250 (≠ I237), Y254 (≠ R241), F266 (= F253), K269 (= K256)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
30% identity, 95% coverage: 3:261/272 of query aligns to 1:249/250 of 3q0gD
- active site: A64 (= A67), M69 (= M72), T75 (≠ E77), F79 (≠ H81), G103 (= G115), E106 (≠ G118), P125 (≠ S137), E126 (= E138), V131 (≠ L143), P133 (= P145), G134 (≠ A146), L219 (vs. gap), F229 (≠ I237)
- binding Butyryl Coenzyme A: F225 (≠ T233), F241 (= F253)
3h02A 2.15 angstrom resolution crystal structure of naphthoate synthase from salmonella typhimurium.
26% identity, 98% coverage: 2:267/272 of query aligns to 16:265/266 of 3h02A
- active site: G82 (≠ A67), H86 (= H81), L90 (≠ D85), G114 (= G115), V117 (≠ G118), G137 (≠ E138), S142 (vs. gap), D144 (≠ A144), G145 (≠ P145), A231 (≠ T233), Y239 (≠ R241)
- binding bicarbonate ion: G113 (= G114), Q135 (≠ L136), G137 (≠ E138), W165 (≠ A165)
4elxA Structure of apo e.Coli. 1,4-dihydroxy-2- naphthoyl coa synthases with cl (see paper)
26% identity, 98% coverage: 2:267/272 of query aligns to 17:267/268 of 4elxA
- active site: G83 (≠ A67), H88 (= H81), L92 (≠ D85), G116 (= G115), V119 (≠ G118), G139 (≠ E138), S144 (vs. gap), D146 (≠ A144), G147 (≠ P145), A233 (≠ T233), Y241 (≠ R241)
- binding chloride ion: G115 (= G114), G139 (≠ E138), W167 (≠ A165)
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)
27% identity, 91% coverage: 15:262/272 of query aligns to 86:331/337 of Q8GYN9
Sites not aligning to the query:
- 20 H→V: Loss of peroxisomal targeting.
4elwA Structure of e. Coli. 1,4-dihydroxy-2- naphthoyl coenzyme a synthases (menb) in complex with nitrate (see paper)
26% identity, 98% coverage: 2:267/272 of query aligns to 17:266/267 of 4elwA
- active site: G83 (≠ A67), L91 (≠ D85), G115 (= G115), V118 (≠ G118), G138 (≠ E138), S143 (vs. gap), D145 (≠ A144), G146 (≠ P145), A232 (≠ T233), Y240 (≠ R241)
- binding nitrate ion: G114 (= G114), T137 (≠ S137), G138 (≠ E138), F144 (≠ L143), W166 (≠ A165)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
28% identity, 91% coverage: 16:262/272 of query aligns to 16:252/254 of 2dubA
- active site: A67 (= A67), M72 (= M72), S82 (≠ T82), G105 (= G115), E108 (≠ G118), P127 (≠ S137), E128 (= E138), T133 (≠ L143), P135 (= P145), G136 (vs. gap), K221 (≠ R231), F231 (≠ R241)
- binding octanoyl-coenzyme a: K25 (≠ S25), A26 (≠ K26), L27 (≠ N27), A29 (= A29), A65 (= A65), A67 (= A67), D68 (= D68), I69 (≠ L69), K70 (≠ A70), G105 (= G115), E108 (≠ G118), P127 (≠ S137), E128 (= E138), G136 (vs. gap), A137 (= A146)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
29% identity, 91% coverage: 16:262/272 of query aligns to 17:258/260 of 2hw5C
- active site: A68 (= A67), M73 (= M72), S83 (≠ T82), L87 (≠ A91), G111 (= G115), E114 (≠ G118), P133 (≠ S137), E134 (= E138), T139 (≠ L143), P141 (= P145), G142 (vs. gap), K227 (≠ R231), F237 (≠ R241)
- binding crotonyl coenzyme a: K26 (≠ S25), A27 (≠ K26), L28 (≠ N27), A30 (= A29), K62 (= K61), I70 (≠ L69), F109 (= F113)
Query Sequence
>Pf6N2E2_2193 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_2193
MDNFNTLELHSDPRGVATLWLSRESKNNAFNAEMIRELILALDHVSSDPNLRFLLIRGRG
KHFSAGADLAWMQQSAELDYHTNLDDARELAELMYNLAKLKIPTLAVVQGAAFGGALGLI
SACDMAIGADEAQFCLSEVRIGLAPAVISPFVVQAIGERAARRYALTAERFDGQRAKEIG
LLSESYPAEVLDQQVEQWIDNLLLNSPAAMRASKELLREVGNGALTPALRRYTENAIARI
RVSPEGQEGLRAFLQKRAPNWQAESNNKEPRR
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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