SitesBLAST
Comparing PfGW456L13_2589 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_2589 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)
6p5uE Structure of an enoyl-coa hydratase/aldolase isolated from a lignin- degrading consortium (see paper)
36% identity, 81% coverage: 1:220/270 of query aligns to 2:223/246 of 6p5uE
- active site: M67 (≠ A67), Y72 (≠ Q74), D77 (= D79), R89 (≠ L90), A93 (≠ M94), G117 (= G115), T120 (≠ G118), E140 (= E138), I145 (≠ L143), P147 (= P145), A148 (= A146)
- binding coenzyme a: D25 (≠ E25), 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:
2vssD Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
34% identity, 74% coverage: 15:214/270 of query aligns to 16:218/246 of 2vssD
- active site: M68 (≠ A67), Y73 (≠ Q74), D78 (= D79), R90 (= R88), Q94 (≠ E92), G118 (= G115), S121 (≠ G118), S140 (= S137), E141 (= E138), I146 (≠ L143), P148 (= P145), G149 (≠ A146)
- binding acetyl coenzyme *a: E26 (= E25), K27 (= K26), R28 (≠ N27), A30 (= A29), A66 (= A65), M68 (≠ A67), D69 (= D68), L70 (= L69), F74 (≠ S75), W114 (≠ A111), F116 (= F113), S140 (= S137)
- binding 4-hydroxy-3-methoxybenzaldehyde: M68 (≠ A67), Y73 (≠ Q74), F74 (≠ S75), Q96 (≠ M94), E141 (= E138), G149 (≠ A146), N150 (vs. gap)
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: 15:214/270 of query aligns to 18:220/276 of O69762
- K29 (= K26) binding
- A68 (= A65) binding
- M70 (≠ A67) binding
- L72 (= L69) binding
- Y75 (≠ Q74) 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.
2vssB Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
34% identity, 74% coverage: 15:214/270 of query aligns to 15:217/247 of 2vssB
- active site: M67 (≠ A67), Y72 (≠ Q74), D77 (= D79), R89 (= R88), Q93 (≠ E92), G117 (= G115), S120 (≠ G118), S139 (= S137), E140 (= E138), I145 (≠ L143), P147 (= P145), G148 (≠ A146)
- binding acetyl coenzyme *a: E25 (= E25), 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:
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
29% identity, 97% coverage: 3:264/270 of query aligns to 2:259/259 of 5zaiC
- active site: A65 (= A67), F70 (≠ M72), S82 (≠ A87), R86 (≠ A91), 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)
6l3pA Crystal strcuture of feruloyl-coa hydratase lyase(fchl) complexed with coa
33% identity, 74% coverage: 15:215/270 of query aligns to 17:215/244 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:
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)
29% identity, 91% coverage: 15:261/270 of query aligns to 86:330/337 of Q8GYN9
Sites not aligning to the query:
- 20 H→V: Loss of peroxisomal targeting.
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, 91% coverage: 15:261/270 of query aligns to 33:278/285 of Q7CQ56
3t88A Crystal structure of escherichia coli menb in complex with substrate analogue, osb-ncoa (see paper)
28% identity, 91% coverage: 15:261/270 of query aligns to 29:274/281 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 (≠ E25), 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)
4i42A E.Coli. 1,4-dihydroxy-2-naphthoyl coenzyme a synthase (ecmenb) in complex with 1-hydroxy-2-naphthoyl-coa (see paper)
28% identity, 91% coverage: 15:261/270 of query aligns to 33:278/285 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)
28% identity, 91% coverage: 15:261/270 of query aligns to 33:278/285 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.
4elxA Structure of apo e.Coli. 1,4-dihydroxy-2- naphthoyl coa synthases with cl (see paper)
29% identity, 91% coverage: 15:261/270 of query aligns to 30:261/268 of 4elxA
- active site: G83 (≠ A67), H88 (≠ E77), L92 (= L84), 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)
4i52A Scmenb im complex with 1-hydroxy-2-naphthoyl-coa (see paper)
27% identity, 91% coverage: 15:261/270 of query aligns to 19:268/275 of 4i52A
- active site: G77 (≠ A67), R82 (≠ M72), Y87 (≠ E77), R95 (≠ L84), L99 (≠ R88), G123 (= G115), V126 (≠ G118), G146 (≠ E138), S151 (vs. gap), D153 (≠ A144), G154 (≠ P145), A240 (≠ T233), Y248 (≠ R241)
- binding 1-hydroxy-2-naphthoyl-CoA: H29 (≠ E25), K30 (= K26), R31 (≠ N27), A33 (= A29), S75 (≠ A65), G76 (= G66), G77 (≠ A67), D78 (= D68), Q79 (≠ L69), L96 (≠ D85), V98 (≠ A87), Y119 (≠ A111), I121 (≠ F113), G123 (= G115), T145 (≠ S137), V149 (≠ I141), S151 (vs. gap), F152 (≠ L143)
4i4zA Synechocystis sp. Pcc 6803 1,4-dihydroxy-2-naphthoyl-coenzyme a synthase (menb) in complex with salicylyl-coa (see paper)
27% identity, 91% coverage: 15:261/270 of query aligns to 19:268/275 of 4i4zA
- active site: G77 (≠ A67), R82 (≠ M72), Y87 (≠ E77), R95 (≠ L84), L99 (≠ R88), G123 (= G115), V126 (≠ G118), G146 (≠ E138), S151 (vs. gap), D153 (≠ A144), G154 (≠ P145), A240 (≠ T233), Y248 (≠ R241)
- binding Salicylyl CoA: H29 (≠ E25), K30 (= K26), R31 (≠ N27), S75 (≠ A65), G76 (= G66), G77 (≠ A67), D78 (= D68), Q79 (≠ L69), Y87 (≠ E77), V98 (≠ A87), G123 (= G115), T145 (≠ S137), V149 (≠ I141), S151 (vs. gap), F260 (= F253), K263 (= K256)
- binding bicarbonate ion: G122 (= G114), Q144 (≠ L136), T145 (≠ S137), G146 (≠ E138), W174 (≠ A165)
3h02A 2.15 angstrom resolution crystal structure of naphthoate synthase from salmonella typhimurium.
28% identity, 91% coverage: 15:261/270 of query aligns to 29:259/266 of 3h02A
- active site: G82 (≠ A67), H86 (≠ Y80), L90 (= L84), 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)
4elwA Structure of e. Coli. 1,4-dihydroxy-2- naphthoyl coenzyme a synthases (menb) in complex with nitrate (see paper)
28% identity, 91% coverage: 15:261/270 of query aligns to 30:260/267 of 4elwA
- active site: G83 (≠ A67), L91 (= L84), 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)
7xwtB Crystal structure of feruoyl-coa hydratase/lyase complexed with coa from sphingomonas paucimobilis (see paper)
28% identity, 88% coverage: 17:253/270 of query aligns to 17:244/277 of 7xwtB
- binding acetyl coenzyme *a: T25 (≠ E25), K26 (= K26), R27 (≠ N27), A29 (= A29), A65 (= A65), G66 (= G66), M67 (≠ A67), D68 (= D68), L69 (= L69), F73 (≠ M72), F114 (= F113), G116 (= G115), S138 (= S137), W142 (≠ I141)
7xwvA Feruloyl-coa hydratase/lyase complexed with vanillin and coenzyme a (see paper)
28% identity, 88% coverage: 17:253/270 of query aligns to 16:243/244 of 7xwvA
- binding coenzyme a: T24 (≠ E25), K25 (= K26), R26 (≠ N27), A64 (= A65), G65 (= G66), M66 (≠ A67), D67 (= D68), L68 (= L69), W111 (≠ A111), F113 (= F113), G114 (= G114), G115 (= G115), S137 (= S137)
- binding 4-hydroxy-3-methoxybenzaldehyde: M66 (≠ A67), Y71 (≠ W71), F72 (≠ M72), E138 (= E138), G146 (vs. gap), G147 (≠ A146)
4emlA Synechocystis sp. Pcc 6803 1,4-dihydroxy-2-naphthoyl-coenzyme a synthase (menb) in complex with bicarbonate (see paper)
27% identity, 91% coverage: 15:261/270 of query aligns to 19:254/261 of 4emlA
- active site: G77 (≠ A67), R81 (≠ W71), L85 (≠ R88), G109 (= G115), V112 (≠ G118), G132 (≠ E138), S137 (vs. gap), D139 (≠ A144), G140 (≠ P145), A226 (≠ T233), Y234 (≠ R241)
- binding bicarbonate ion: G108 (= G114), Q130 (≠ L136), G132 (≠ E138), W160 (≠ A165)
- binding chloride ion: D184 (≠ A189), R185 (≠ E190), E187 (= E192), E188 (≠ Q193)
2uzfA Crystal structure of staphylococcus aureus 1,4-dihydroxy-2-naphthoyl coa synthase (menb) in complex with acetoacetyl coa (see paper)
26% identity, 91% coverage: 15:261/270 of query aligns to 17:253/260 of 2uzfA
- active site: G70 (≠ A67), R80 (≠ E77), L84 (≠ D85), G108 (= G115), V111 (≠ G118), T130 (≠ S137), G131 (≠ E138), S136 (≠ L143), D138 (≠ P145), A139 (= A146), A225 (≠ T233), Y233 (≠ R241)
- binding acetoacetyl-coenzyme a: V28 (≠ K26), R29 (≠ N27), S68 (≠ A65), G69 (= G66), G70 (≠ A67), D71 (= D68), Y104 (≠ A111), G108 (= G115)
Query Sequence
>PfGW456L13_2589 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_2589
MSDFNTLELLTDPRGFATLWLSREEKNNAFNAEMIRELILALDKVASDASLRFLIVRGRG
KHFSAGADLAWMQQSAELDYATNLDDARELAELMYNLAKLKIPSLAVVQGAAFGGALGLI
SCCDMAIGADDAQFCLSEVRIGLAPAVISPFVVQAIGERATRRYALTAERFGGQRAREIG
LLSESYAGAELEQKVDQWIDNLLLNSPAAMRASKDLLREVGDGSLTPALRRYTENAIARI
RVSPEGQEGLRAFLQKRPPSWQAETTKEPR
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