SitesBLAST
Comparing GFF1024 FitnessBrowser__Marino:GFF1024 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)
32% identity, 82% coverage: 14:234/268 of query aligns to 13:233/246 of 6p5uE
- active site: M67 (≠ A68), Y72 (≠ M73), D77 (≠ E78), R89 (≠ E90), A93 (≠ L94), G117 (= G116), T120 (≠ G119), E140 (= E139), I145 (≠ L144), P147 (= P146), A148 (= A147)
- binding coenzyme a: D25 (= D26), K26 (= K27), R27 (= R28), A29 (= A30), A65 (≠ P66), M67 (≠ A68), D68 (= D69), L69 (= L70), W113 (≠ A112), F115 (= F114), S139 (= S138), W143 (≠ L142)
Sites not aligning to the query:
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
27% identity, 91% coverage: 20:263/268 of query aligns to 17:256/259 of 5zaiC
- active site: A65 (= A68), F70 (≠ M73), S82 (≠ L85), R86 (= R89), G110 (= G116), E113 (≠ G119), P132 (≠ S138), E133 (= E139), I138 (≠ L144), P140 (= P146), G141 (≠ A147), A226 (≠ I232), F236 (≠ R243)
- binding coenzyme a: K24 (= K27), L25 (≠ R28), A63 (≠ P66), G64 (= G67), A65 (= A68), D66 (= D69), I67 (≠ L70), P132 (≠ S138), R166 (≠ V171), F248 (= F255), K251 (= K258)
6l3pA Crystal strcuture of feruloyl-coa hydratase lyase(fchl) complexed with coa
31% identity, 75% coverage: 16:217/268 of query aligns to 17:215/244 of 6l3pA
- active site: M69 (≠ A68), Y74 (≠ N79), R86 (= R89), Q90 (≠ R93), G114 (= G116), S117 (≠ G119), S136 (= S138), E137 (= E139), I142 (≠ L144), P144 (= P146), G145 (≠ A147)
- binding coenzyme a: K28 (= K27), R29 (= R28), A31 (= A30), A67 (≠ P66), M69 (≠ A68), D70 (= D69), L71 (= L70), G113 (= G115)
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)
28% identity, 94% coverage: 11:263/268 of query aligns to 81:330/337 of Q8GYN9
Sites not aligning to the query:
- 20 H→V: Loss of peroxisomal targeting.
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)
28% identity, 93% coverage: 20:267/268 of query aligns to 24:269/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
2vssB Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
29% identity, 76% coverage: 14:216/268 of query aligns to 13:217/247 of 2vssB
- active site: M67 (≠ A68), Y72 (≠ M73), D77 (vs. gap), R89 (≠ Q82), Q93 (≠ D86), G117 (= G116), S120 (≠ G119), S139 (= S138), E140 (= E139), I145 (≠ L144), P147 (= P146), G148 (≠ A147)
- binding acetyl coenzyme *a: E25 (≠ D26), K26 (= K27), R27 (= R28), A29 (= A30), A65 (≠ P66), M67 (≠ A68), D68 (= D69), W113 (≠ A112), F115 (= F114), G117 (= G116), S139 (= S138), E140 (= E139)
Sites not aligning to the query:
2vssD Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
29% identity, 76% coverage: 14:216/268 of query aligns to 14:218/246 of 2vssD
- active site: M68 (≠ A68), Y73 (≠ M73), D78 (vs. gap), R90 (≠ Q82), Q94 (≠ D86), G118 (= G116), S121 (≠ G119), S140 (= S138), E141 (= E139), I146 (≠ L144), P148 (= P146), G149 (≠ A147)
- binding acetyl coenzyme *a: E26 (≠ D26), K27 (= K27), R28 (= R28), A30 (= A30), A66 (≠ P66), M68 (≠ A68), D69 (= D69), L70 (= L70), F74 (≠ R74), W114 (≠ A112), F116 (= F114), S140 (= S138)
- binding 4-hydroxy-3-methoxybenzaldehyde: M68 (≠ A68), Y73 (≠ M73), F74 (≠ R74), Q96 (≠ S88), E141 (= E139), G149 (≠ A147), 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)
29% identity, 76% coverage: 14:216/268 of query aligns to 16:220/276 of O69762
- K29 (= K27) binding
- A68 (≠ P66) binding
- M70 (≠ A68) binding
- L72 (= L70) binding
- Y75 (≠ M73) binding
- G120 (= G116) binding
- S123 (≠ G119) mutation to A: Reduced kcat compared to wild-type but not markerdly.
- S142 (= S138) binding
- E143 (= E139) mutation to A: Abolishes catalytic activity.
- W146 (≠ L142) binding
- G151 (≠ A147) 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.
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
28% identity, 94% coverage: 13:263/268 of query aligns to 13:257/260 of 2hw5C
- active site: A68 (= A68), M73 (= M73), S83 (= S88), L87 (≠ A92), G111 (= G116), E114 (≠ G119), P133 (≠ S138), E134 (= E139), T139 (≠ L144), P141 (= P146), G142 (vs. gap), K227 (≠ I232), F237 (≠ I242)
- binding crotonyl coenzyme a: K26 (≠ D26), A27 (≠ K27), L28 (≠ R28), A30 (= A30), K62 (≠ S62), I70 (≠ L70), F109 (= F114)
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: 2:263/268 of query aligns to 19:278/285 of Q7CQ56
3h02A 2.15 angstrom resolution crystal structure of naphthoate synthase from salmonella typhimurium.
26% identity, 98% coverage: 2:263/268 of query aligns to 15:259/266 of 3h02A
- active site: G82 (≠ S80), H86 (≠ N84), L90 (≠ A92), G114 (= G116), V117 (≠ G119), G137 (≠ E139), S142 (≠ L144), D144 (≠ P146), G145 (≠ A147), A231 (≠ D233), Y239 (≠ R243)
- binding bicarbonate ion: G113 (= G115), Q135 (≠ L137), G137 (≠ E139), W165 (≠ F166)
4elxA Structure of apo e.Coli. 1,4-dihydroxy-2- naphthoyl coa synthases with cl (see paper)
28% identity, 96% coverage: 8:263/268 of query aligns to 22:261/268 of 4elxA
- active site: G83 (≠ A68), H88 (≠ R81), L92 (= L85), G116 (= G116), V119 (≠ G119), G139 (≠ E139), S144 (≠ L144), D146 (≠ P146), G147 (≠ A147), A233 (≠ D233), Y241 (≠ R243)
- binding chloride ion: G115 (= G115), G139 (≠ E139), W167 (≠ F166)
4i42A E.Coli. 1,4-dihydroxy-2-naphthoyl coenzyme a synthase (ecmenb) in complex with 1-hydroxy-2-naphthoyl-coa (see paper)
29% identity, 96% coverage: 8:263/268 of query aligns to 25:278/285 of 4i42A
- active site: G86 (≠ A68), R91 (≠ E78), Y97 (≠ N84), H105 (≠ L94), L109 (= L98), G133 (= G116), V136 (≠ G119), G156 (≠ E139), S161 (≠ L144), D163 (≠ P146), G164 (≠ A147), A250 (≠ D233), Y258 (≠ R243)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (≠ K27), R45 (= R28), S84 (= S64), G85 (= G67), G86 (≠ A68), D87 (= D69), Q88 (≠ R75), K89 (≠ M76), Y97 (≠ N84), V108 (= V97), Y129 (≠ A112), G133 (= G116), T155 (≠ S138), S161 (≠ L144), T254 (≠ H237), F270 (= F255), K273 (= K258)
P0ABU0 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Escherichia coli (strain K12) (see 4 papers)
29% identity, 96% coverage: 8:263/268 of query aligns to 25:278/285 of P0ABU0
- R45 (= R28) binding in other chain
- S--GGD-----QK 84:89 (≠ SPPGADLGWMRRM 64:76) binding in other chain
- K89 (≠ M76) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- R91 (≠ E78) mutation to A: Loss of DHNA-CoA synthase activity.
- Y97 (≠ N84) binding in other chain; mutation to F: Loss of DHNA-CoA synthase activity.
- YSIGG 129:133 (≠ AAFGG 112:116) binding in other chain
- Q154 (≠ L137) 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 137:139) binding
- T155 (≠ S138) binding in other chain
- G156 (≠ E139) mutation to D: Loss of DHNA-CoA synthase activity.
- S161 (≠ L144) binding in other chain
- W184 (≠ F166) mutation to F: Reduces the specific DHNA-CoA synthase activity by 530-fold, whereas its affinity for hydrogencarbonate is reduced by 20-fold.
- Y258 (≠ R243) binding
- R267 (≠ L252) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- F270 (= F255) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- K273 (= K258) binding ; mutation to A: Impairs protein folding.
3t88A Crystal structure of escherichia coli menb in complex with substrate analogue, osb-ncoa (see paper)
29% identity, 96% coverage: 8:263/268 of query aligns to 21:274/281 of 3t88A
- active site: G82 (≠ A68), R87 (≠ E78), Y93 (≠ N84), H101 (≠ L94), L105 (= L98), G129 (= G116), V132 (≠ G119), G152 (≠ E139), S157 (≠ L144), D159 (≠ P146), G160 (≠ A147), A246 (≠ D233), Y254 (≠ R243)
- binding o-succinylbenzoyl-N-coenzyme A: Q39 (≠ D26), V40 (≠ K27), R41 (= R28), A43 (= A30), S80 (= S64), G81 (= G67), G82 (≠ A68), D83 (= D69), Q84 (≠ R75), K85 (≠ M76), Y93 (≠ N84), V104 (= V97), L105 (= L98), Y125 (≠ A112), G129 (= G116), T151 (≠ S138), V155 (≠ L142), F158 (≠ I145), D159 (≠ P146), T250 (≠ H237), Y254 (≠ R243), F266 (= F255), K269 (= K258)
4elwA Structure of e. Coli. 1,4-dihydroxy-2- naphthoyl coenzyme a synthases (menb) in complex with nitrate (see paper)
26% identity, 96% coverage: 8:263/268 of query aligns to 22:260/267 of 4elwA
- active site: G83 (≠ S80), L91 (≠ A92), G115 (= G116), V118 (≠ G119), G138 (≠ E139), S143 (≠ L144), D145 (≠ P146), G146 (≠ A147), A232 (≠ D233), Y240 (≠ R243)
- binding nitrate ion: G114 (= G115), T137 (≠ S138), G138 (≠ E139), F144 (≠ I145), W166 (≠ F166)
4emlA Synechocystis sp. Pcc 6803 1,4-dihydroxy-2-naphthoyl-coenzyme a synthase (menb) in complex with bicarbonate (see paper)
28% identity, 96% coverage: 9:265/268 of query aligns to 12:261/261 of 4emlA
- active site: G77 (≠ E78), R81 (≠ Q82), L85 (≠ D86), G109 (= G116), V112 (≠ G119), G132 (≠ E139), S137 (≠ L144), D139 (≠ P146), G140 (≠ A147), A226 (≠ D233), Y234 (≠ R243)
- binding bicarbonate ion: G108 (= G115), Q130 (≠ L137), G132 (≠ E139), W160 (≠ F166)
- binding chloride ion: D184 (= D191), R185 (≠ A192), E187 (= E194), E188 (≠ A195)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
27% identity, 96% coverage: 8:264/268 of query aligns to 4:254/256 of 3h81A
- active site: A64 (= A68), M69 (= M76), T79 (≠ S88), F83 (≠ A92), G107 (= G116), E110 (≠ G119), P129 (≠ S138), E130 (= E139), V135 (≠ L144), P137 (= P146), G138 (≠ A147), L223 (≠ I232), F233 (≠ V244)
- binding calcium ion: F233 (≠ V244), Q238 (= Q249)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
27% identity, 96% coverage: 8:264/268 of query aligns to 5:255/255 of 3q0jC
- active site: A65 (= A68), M70 (= M76), T80 (≠ S88), F84 (≠ A92), G108 (= G116), E111 (≠ G119), P130 (≠ S138), E131 (= E139), V136 (≠ L144), P138 (= P146), G139 (≠ A147), L224 (≠ I232), F234 (≠ V244)
- binding acetoacetyl-coenzyme a: Q23 (≠ D26), A24 (≠ K27), L25 (≠ R28), A27 (= A30), A63 (≠ P66), G64 (= G67), A65 (= A68), D66 (= D69), I67 (≠ L70), K68 (≠ R74), M70 (= M76), F84 (≠ A92), G107 (= G115), G108 (= G116), E111 (≠ G119), P130 (≠ S138), E131 (= E139), P138 (= P146), G139 (≠ A147), M140 (≠ V148)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
27% identity, 96% coverage: 8:264/268 of query aligns to 5:255/255 of 3q0gC
- active site: A65 (= A68), M70 (= M76), T80 (≠ S88), F84 (≠ A92), G108 (= G116), E111 (≠ G119), P130 (≠ S138), E131 (= E139), V136 (≠ L144), P138 (= P146), G139 (≠ A147), L224 (≠ I232), F234 (≠ V244)
- binding coenzyme a: L25 (≠ R28), A63 (≠ P66), I67 (≠ L70), K68 (≠ R74), Y104 (≠ A112), P130 (≠ S138), E131 (= E139), L134 (= L142)
Query Sequence
>GFF1024 FitnessBrowser__Marino:GFF1024
MTDNESAVLLKRRDEGIAEVVLNRPDKRNAFDDVIIQQLISTLTEVNADNSVKVVICAPK
ASTSPPGADLGWMRRMAENSRQENLDDSRELARLMNVLNHLSKPVIGLVQGAAFGGAVGL
AACCDIVIATEKSSFCLSEVKLGLIPAVISPYVVRAIGERQARRYFISAEVFTAKQAQEY
GLVHIVCDDVDAMEARCNEMLQQLAMNGPEAMKAAKDLVFAVSHKPINDDVIDDTAHRIA
DIRVGEEGQEGLSAFLNKRKANWVPEEE
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