SitesBLAST
Comparing GFF1019 FitnessBrowser__Phaeo:GFF1019 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)
31% identity, 93% coverage: 17:259/260 of query aligns to 17:257/259 of 5zaiC
- active site: A65 (≠ G65), F70 (≠ M70), S82 (≠ G82), R86 (= R86), G110 (= G113), E113 (≠ G116), P132 (≠ T135), E133 (= E136), I138 (≠ L141), P140 (= P143), G141 (≠ A144), A226 (≠ V226), F236 (≠ W238)
- binding coenzyme a: K24 (= K24), L25 (≠ H25), A63 (= A63), G64 (= G64), A65 (≠ G65), D66 (= D66), I67 (≠ L67), P132 (≠ T135), R166 (≠ L168), F248 (= F250), K251 (= K253)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
34% identity, 99% coverage: 2:258/260 of query aligns to 3:254/255 of 3q0jC
- active site: A65 (≠ G65), M70 (= M70), T80 (= T80), F84 (≠ L88), G108 (= G113), E111 (≠ G116), P130 (≠ T135), E131 (= E136), V136 (≠ L141), P138 (= P143), G139 (≠ A144), L224 (≠ I227), F234 (≠ W238)
- binding acetoacetyl-coenzyme a: Q23 (≠ E23), A24 (≠ K24), L25 (≠ H25), A27 (= A27), A63 (= A63), G64 (= G64), A65 (≠ G65), D66 (= D66), I67 (≠ L67), K68 (≠ G68), M70 (= M70), F84 (≠ L88), G107 (= G112), G108 (= G113), E111 (≠ G116), P130 (≠ T135), E131 (= E136), P138 (= P143), G139 (≠ A144), M140 (≠ T145)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
34% identity, 99% coverage: 2:258/260 of query aligns to 3:254/255 of 3q0gC
- active site: A65 (≠ G65), M70 (= M70), T80 (= T80), F84 (≠ L88), G108 (= G113), E111 (≠ G116), P130 (≠ T135), E131 (= E136), V136 (≠ L141), P138 (= P143), G139 (≠ A144), L224 (≠ I227), F234 (≠ W238)
- binding coenzyme a: L25 (≠ H25), A63 (= A63), I67 (≠ L67), K68 (≠ G68), Y104 (≠ N109), P130 (≠ T135), E131 (= E136), L134 (= L139)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
34% identity, 99% coverage: 2:258/260 of query aligns to 2:253/256 of 3h81A
- active site: A64 (≠ G65), M69 (= M70), T79 (= T80), F83 (≠ L88), G107 (= G113), E110 (≠ G116), P129 (≠ T135), E130 (= E136), V135 (≠ L141), P137 (= P143), G138 (≠ A144), L223 (≠ I227), F233 (≠ W238)
- binding calcium ion: F233 (≠ W238), Q238 (≠ A243)
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)
36% identity, 78% coverage: 11:213/260 of query aligns to 84:286/337 of Q8GYN9
Sites not aligning to the query:
- 20 H→V: Loss of peroxisomal targeting.
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
35% identity, 99% coverage: 2:258/260 of query aligns to 2:249/250 of 3q0gD
- active site: A64 (≠ G65), M69 (= M74), T75 (= T80), F79 (≠ L88), G103 (= G113), E106 (≠ G116), P125 (≠ T135), E126 (= E136), V131 (≠ L141), P133 (= P143), G134 (≠ A144), L219 (≠ I227), F229 (≠ A232)
- binding Butyryl Coenzyme A: F225 (vs. gap), F241 (= F250)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
34% identity, 97% coverage: 7:259/260 of query aligns to 7:259/261 of 5jbxB
- active site: A67 (≠ G65), R72 (≠ Q71), L84 (vs. gap), R88 (≠ A89), G112 (= G113), E115 (≠ G116), T134 (= T135), E135 (= E136), I140 (≠ L141), P142 (= P143), G143 (≠ A144), A228 (= A232), L238 (vs. gap)
- binding coenzyme a: S24 (≠ E23), R25 (≠ K24), R26 (≠ H25), A28 (= A27), A65 (= A63), D68 (= D66), L69 (= L67), K70 (≠ W69), L110 (≠ F111), G111 (= G112), T134 (= T135), E135 (= E136), L138 (= L139), R168 (≠ L168)
3t88A Crystal structure of escherichia coli menb in complex with substrate analogue, osb-ncoa (see paper)
30% identity, 95% coverage: 13:260/260 of query aligns to 29:276/281 of 3t88A
- active site: G82 (= G65), R87 (≠ Q71), Y93 (≠ D77), H101 (≠ A85), L105 (≠ A89), G129 (= G113), V132 (≠ G116), G152 (≠ E136), S157 (≠ L141), D159 (≠ P143), G160 (≠ A144), A246 (= A232), Y254 (≠ W238)
- binding o-succinylbenzoyl-N-coenzyme A: Q39 (≠ E23), V40 (≠ K24), R41 (≠ H25), A43 (= A27), S80 (≠ A63), G81 (= G64), G82 (= G65), D83 (= D66), Q84 (≠ L67), K85 (≠ G68), Y93 (≠ D77), V104 (≠ L88), L105 (≠ A89), Y125 (≠ N109), G129 (= G113), T151 (= T135), V155 (≠ L139), F158 (≠ I142), D159 (≠ P143), T250 (≠ L234), Y254 (≠ W238), F266 (= F250), K269 (= K253)
4i42A E.Coli. 1,4-dihydroxy-2-naphthoyl coenzyme a synthase (ecmenb) in complex with 1-hydroxy-2-naphthoyl-coa (see paper)
30% identity, 95% coverage: 13:260/260 of query aligns to 33:280/285 of 4i42A
- active site: G86 (= G65), R91 (≠ Q71), Y97 (≠ D77), H105 (≠ A85), L109 (≠ A89), G133 (= G113), V136 (≠ G116), G156 (≠ E136), S161 (≠ L141), D163 (≠ P143), G164 (≠ A144), A250 (= A232), Y258 (≠ W238)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (≠ K24), R45 (≠ H25), S84 (≠ A63), G85 (= G64), G86 (= G65), D87 (= D66), Q88 (≠ L67), K89 (≠ G68), Y97 (≠ D77), V108 (≠ L88), Y129 (≠ N109), G133 (= G113), T155 (= T135), S161 (≠ L141), T254 (≠ L234), F270 (= F250), K273 (= K253)
P0ABU0 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Escherichia coli (strain K12) (see 4 papers)
30% identity, 95% coverage: 13:260/260 of query aligns to 33:280/285 of P0ABU0
- R45 (≠ H25) binding in other chain
- SGGDQK 84:89 (≠ AGGDLG 63:68) binding in other chain
- K89 (≠ G68) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- R91 (≠ Q71) mutation to A: Loss of DHNA-CoA synthase activity.
- Y97 (≠ D77) binding in other chain; mutation to F: Loss of DHNA-CoA synthase activity.
- YSIGG 129:133 (≠ NAFGG 109:113) binding in other chain
- Q154 (≠ L134) 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 134:136) binding hydrogencarbonate
- T155 (= T135) binding in other chain
- G156 (≠ E136) mutation to D: Loss of DHNA-CoA synthase activity.
- S161 (≠ L141) binding in other chain
- W184 (≠ F163) mutation to F: Reduces the specific DHNA-CoA synthase activity by 530-fold, whereas its affinity for hydrogencarbonate is reduced by 20-fold.
- Y258 (≠ W238) binding substrate
- R267 (≠ I247) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- F270 (= F250) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- K273 (= K253) binding substrate; mutation to A: Impairs protein folding.
Q7CQ56 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
29% identity, 100% coverage: 2:260/260 of query aligns to 22:280/285 of Q7CQ56
4elxA Structure of apo e.Coli. 1,4-dihydroxy-2- naphthoyl coa synthases with cl (see paper)
30% identity, 95% coverage: 13:260/260 of query aligns to 30:263/268 of 4elxA
- active site: G83 (= G65), H88 (≠ E84), L92 (= L88), G116 (= G113), V119 (≠ G116), G139 (≠ E136), S144 (≠ L141), D146 (≠ P143), G147 (≠ A144), A233 (= A232), Y241 (≠ W238)
- binding chloride ion: G115 (= G112), G139 (≠ E136), W167 (≠ F163)
4elwA Structure of e. Coli. 1,4-dihydroxy-2- naphthoyl coenzyme a synthases (menb) in complex with nitrate (see paper)
30% identity, 95% coverage: 13:260/260 of query aligns to 30:262/267 of 4elwA
- active site: G83 (= G65), L91 (= L88), G115 (= G113), V118 (≠ G116), G138 (≠ E136), S143 (≠ L141), D145 (≠ P143), G146 (≠ A144), A232 (= A232), Y240 (≠ W238)
- binding nitrate ion: G114 (= G112), T137 (= T135), G138 (≠ E136), F144 (≠ I142), W166 (≠ F163)
Q5HH38 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Staphylococcus aureus (strain COL) (see paper)
30% identity, 95% coverage: 13:260/260 of query aligns to 22:268/273 of Q5HH38
3h02A 2.15 angstrom resolution crystal structure of naphthoate synthase from salmonella typhimurium.
29% identity, 100% coverage: 2:260/260 of query aligns to 18:261/266 of 3h02A
- active site: G82 (= G65), H86 (≠ W69), L90 (≠ A89), G114 (= G113), V117 (≠ G116), G137 (≠ E136), S142 (≠ L141), D144 (≠ P143), G145 (≠ A144), A231 (= A232), Y239 (≠ W238)
- binding bicarbonate ion: G113 (= G112), Q135 (≠ L134), G137 (≠ E136), W165 (≠ F163)
2uzfA Crystal structure of staphylococcus aureus 1,4-dihydroxy-2-naphthoyl coa synthase (menb) in complex with acetoacetyl coa (see paper)
35% identity, 67% coverage: 13:185/260 of query aligns to 17:181/260 of 2uzfA
- active site: G70 (= G65), R80 (≠ E84), L84 (= L88), G108 (= G113), V111 (≠ G116), T130 (= T135), G131 (≠ E136), S136 (≠ L141), D138 (≠ P143), A139 (= A144)
- binding acetoacetyl-coenzyme a: V28 (≠ K24), R29 (≠ H25), S68 (≠ A63), G69 (= G64), G70 (= G65), D71 (= D66), Y104 (≠ N109), G108 (= G113)
Sites not aligning to the query:
Q4WF54 Mevalonyl-coenzyme A hydratase sidH; Siderophore biosynthesis protein H; EC 4.2.1.- from Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata) (see paper)
31% identity, 93% coverage: 17:259/260 of query aligns to 24:266/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
2vssD Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
32% identity, 72% coverage: 2:189/260 of query aligns to 6:195/246 of 2vssD
- active site: M68 (≠ G65), Y73 (≠ M70), D78 (≠ E75), R90 (≠ V87), Q94 (≠ M91), G118 (= G113), S121 (≠ G116), S140 (≠ T135), E141 (= E136), I146 (≠ L141), P148 (= P143), G149 (≠ A144)
- binding acetyl coenzyme *a: E26 (= E23), K27 (= K24), R28 (≠ H25), A30 (= A27), A66 (= A63), M68 (≠ G65), D69 (= D66), L70 (= L67), F74 (≠ Q71), W114 (≠ N109), F116 (= F111), S140 (≠ T135)
- binding 4-hydroxy-3-methoxybenzaldehyde: M68 (≠ G65), Y73 (≠ M70), F74 (≠ Q71), Q96 (≠ M93), E141 (= E136), G149 (≠ A144), N150 (≠ T145)
Sites not aligning to the query:
2vssB Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
32% identity, 72% coverage: 2:189/260 of query aligns to 5:194/247 of 2vssB
- active site: M67 (≠ G65), Y72 (≠ M70), D77 (≠ E75), R89 (≠ V87), Q93 (≠ M91), G117 (= G113), S120 (≠ G116), S139 (≠ T135), E140 (= E136), I145 (≠ L141), P147 (= P143), G148 (≠ A144)
- binding acetyl coenzyme *a: E25 (= E23), K26 (= K24), R27 (≠ H25), A29 (= A27), A65 (= A63), M67 (≠ G65), D68 (= D66), W113 (≠ N109), F115 (= F111), G117 (= G113), S139 (≠ T135), E140 (= E136)
Sites not aligning to the query:
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
37% identity, 68% coverage: 13:189/260 of query aligns to 12:185/257 of 6slbAAA
- active site: Q64 (≠ G65), F69 (≠ M70), L80 (≠ G82), N84 (≠ R86), A108 (≠ G113), S111 (≠ G116), A130 (≠ T135), F131 (≠ E136), L136 (= L141), P138 (= P143), D139 (≠ A144)
- 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 (≠ K59), A62 (= A63), Q64 (≠ G65), D65 (= D66), L66 (= L67), Y76 (≠ A78), A108 (≠ G113), F131 (≠ E136), D139 (≠ A144)
Sites not aligning to the query:
Query Sequence
>GFF1019 FitnessBrowser__Phaeo:GFF1019
MYNTITLAIDDRGVATLTLNRPEKHNAMSGEMLQELKAAAAALAKDRTVRVVVLTGAGKS
FCAGGDLGWMQAQMEADAETRGREARVLAEMLMAINTLPQPVIGAIQGNAFGGGVGMASV
CDVAIGADHIKMGLTETRLGLIPATIGPYVVARMGEARARRVFMSARLFGAAEAVDLGIL
ARVVPAADLDAAIEAEVIPYLSCAPEAVGAAKALVRDLGPKIDDAVIDHTIAALVDRWEG
SEAPEGIAAFFAKEKPSWQR
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