SitesBLAST
Comparing Echvi_2341 FitnessBrowser__Cola:Echvi_2341 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)
P9WNP5 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 4 papers)
64% identity, 97% coverage: 3:271/277 of query aligns to 25:308/314 of P9WNP5
- R58 (= R31) binding in other chain
- K95 (= K68) binding in other chain
- SGGDQ 103:107 (= SGGDQ 76:80) binding in other chain
- R133 (= R96) mutation to A: Loss of DHNA-CoA synthase activity.
- WAAGG 157:161 (≠ WAVGG 120:124) binding in other chain
- T184 (= T147) binding in other chain
- D185 (= D148) mutation to E: Nearly abolishes DHNA-CoA synthase activity.; mutation D->G,N: Loss of DHNA-CoA synthase activity.
- S190 (= S153) mutation to A: Reduces affinity for substrate. Nearly abolishes DHNA-CoA synthase activity.
- D192 (= D155) mutation to N: Loss of DHNA-CoA synthase activity.
- Y287 (= Y250) mutation to F: Loss of DHNA-CoA synthase activity.
4qijA Crystal structure of menb from mycobacteria tuberculosis in complex with 1-hna-coa (see paper)
64% identity, 97% coverage: 3:271/277 of query aligns to 12:295/301 of 4qijA
- active site: G92 (= G78), R97 (= R83), Y102 (= Y88), R117 (vs. gap), H122 (≠ N98), G148 (= G124), S151 (= S127), D172 (= D148), S177 (= S153), D179 (= D155), G180 (= G156), A266 (= A242), Y274 (= Y250)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (= V30), R45 (= R31), A47 (= A33), F48 (= F34), K82 (= K68), S90 (= S76), G91 (= G77), G92 (= G78), D93 (= D79), Q94 (= Q80), Y102 (= Y88), L121 (= L97), I123 (= I99), W144 (= W120), G148 (= G124), T171 (= T147), D172 (= D148), S177 (= S153), F286 (= F262), K289 (= K265)
4qiiB Crystal structure of type ii menb from mycobacteria tuberculosis (see paper)
64% identity, 97% coverage: 3:271/277 of query aligns to 12:295/301 of 4qiiB
- active site: G92 (= G78), R97 (= R83), Y102 (= Y88), R117 (vs. gap), H122 (≠ N98), G148 (= G124), S151 (= S127), D172 (= D148), S177 (= S153), D179 (= D155), G180 (= G156), A266 (= A242), Y274 (= Y250)
- binding Salicylyl CoA: V44 (= V30), R45 (= R31), A47 (= A33), K82 (= K68), S90 (= S76), G92 (= G78), D93 (= D79), Q94 (= Q80), Y102 (= Y88), W144 (= W120), G147 (= G123), G148 (= G124), T171 (= T147), D172 (= D148), V175 (= V151), S177 (= S153), Y274 (= Y250), F286 (= F262), K289 (= K265)
1q51B Crystal structure of mycobacterium tuberculosis menb in complex with acetoacetyl-coenzyme a, a key enzyme in vitamin k2 biosynthesis (see paper)
65% identity, 97% coverage: 3:271/277 of query aligns to 8:274/280 of 1q51B
- active site: G88 (= G78), H101 (≠ N98), G127 (= G124), S130 (= S127), D151 (= D148), S156 (= S153), D158 (= D155), G159 (= G156), A245 (= A242), Y253 (= Y250)
- binding acetoacetyl-coenzyme a: V40 (= V30), R41 (= R31), A43 (= A33), S86 (= S76), G88 (= G78), D89 (= D79), Q90 (= Q80), W123 (= W120), G126 (= G123), G127 (= G124), T150 (= T147)
1q51A Crystal structure of mycobacterium tuberculosis menb in complex with acetoacetyl-coenzyme a, a key enzyme in vitamin k2 biosynthesis (see paper)
64% identity, 97% coverage: 3:271/277 of query aligns to 8:265/271 of 1q51A
- active site: G88 (= G78), H92 (≠ N98), G118 (= G124), S121 (= S127), D142 (= D148), S147 (= S153), D149 (= D155), G150 (= G156), A236 (= A242), Y244 (= Y250)
- binding acetoacetyl-coenzyme a: V40 (= V30), R41 (= R31), K78 (= K68), S86 (= S76), G88 (= G78), D89 (= D79), Q90 (= Q80), W114 (= W120), G117 (= G123), G118 (= G124), T141 (= T147)
1rjnB The crystal structure of menb (rv0548c) from mycobacterium tuberculosis in complex with the coa portion of naphthoyl coa (see paper)
64% identity, 97% coverage: 3:271/277 of query aligns to 12:269/275 of 1rjnB
- active site: G92 (= G78), H96 (≠ N98), G122 (= G124), S125 (= S127), D146 (= D148), S151 (= S153), D153 (= D155), G154 (= G156), A240 (= A242)
- binding coenzyme a: V44 (= V30), R45 (= R31), K82 (= K68), S90 (= S76), G92 (= G78), D93 (= D79), Q94 (= Q80), W118 (= W120)
- binding 3-[4-(2-hydroxyethyl)piperazin-1-yl]propane-1-sulfonic acid: R163 (≠ K165), Q164 (≠ M166), V165 (= V167), M188 (= M190)
4i52A Scmenb im complex with 1-hydroxy-2-naphthoyl-coa (see paper)
60% identity, 100% coverage: 1:277/277 of query aligns to 1:275/275 of 4i52A
- active site: G77 (= G78), R82 (= R83), Y87 (= Y88), R95 (= R96), L99 (= L100), G123 (= G124), V126 (≠ S127), G146 (≠ D148), S151 (= S153), D153 (= D155), G154 (= G156), A240 (= A242), Y248 (= Y250)
- binding 1-hydroxy-2-naphthoyl-CoA: H29 (≠ E29), K30 (≠ V30), R31 (= R31), A33 (= A33), S75 (= S76), G76 (= G77), G77 (= G78), D78 (= D79), Q79 (= Q80), L96 (= L97), V98 (≠ I99), Y119 (≠ W120), I121 (≠ V122), G123 (= G124), T145 (= T147), V149 (= V151), S151 (= S153), F152 (= F154)
4i4zA Synechocystis sp. Pcc 6803 1,4-dihydroxy-2-naphthoyl-coenzyme a synthase (menb) in complex with salicylyl-coa (see paper)
60% identity, 100% coverage: 1:277/277 of query aligns to 1:275/275 of 4i4zA
- active site: G77 (= G78), R82 (= R83), Y87 (= Y88), R95 (= R96), L99 (= L100), G123 (= G124), V126 (≠ S127), G146 (≠ D148), S151 (= S153), D153 (= D155), G154 (= G156), A240 (= A242), Y248 (= Y250)
- binding Salicylyl CoA: H29 (≠ E29), K30 (≠ V30), R31 (= R31), S75 (= S76), G76 (= G77), G77 (= G78), D78 (= D79), Q79 (= Q80), Y87 (= Y88), V98 (≠ I99), G123 (= G124), T145 (= T147), V149 (= V151), S151 (= S153), F260 (= F262), K263 (= K265)
- binding bicarbonate ion: G122 (= G123), Q144 (= Q146), T145 (= T147), G146 (≠ D148), W174 (≠ F176)
3t8aB Crystal structure of mycobacterium tuberculosis menb in complex with substrate analogue, osb-ncoa (see paper)
64% identity, 97% coverage: 3:271/277 of query aligns to 11:268/274 of 3t8aB
- active site: G91 (= G78), H97 (≠ N98), G123 (= G124), S126 (= S127), D147 (= D148), S152 (= S153), D154 (= D155), G155 (= G156), A241 (= A242), Y249 (= Y250)
- binding o-succinylbenzoyl-N-coenzyme A: V43 (= V30), R44 (= R31), K81 (= K68), S89 (= S76), G91 (= G78), D92 (= D79), Q93 (= Q80), W119 (= W120)
4emlA Synechocystis sp. Pcc 6803 1,4-dihydroxy-2-naphthoyl-coenzyme a synthase (menb) in complex with bicarbonate (see paper)
57% identity, 100% coverage: 1:277/277 of query aligns to 1:261/261 of 4emlA
- active site: G77 (= G78), R81 (= R96), L85 (= L100), G109 (= G124), V112 (≠ S127), G132 (≠ D148), S137 (= S153), D139 (= D155), G140 (= G156), A226 (= A242), Y234 (= Y250)
- binding bicarbonate ion: G108 (= G123), Q130 (= Q146), G132 (≠ D148), W160 (≠ F176)
- binding chloride ion: D184 (≠ N200), R185 (≠ E201), E187 (= E203), E188 (≠ D204)
Q5HH38 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Staphylococcus aureus (strain COL) (see paper)
52% identity, 100% coverage: 2:277/277 of query aligns to 5:273/273 of Q5HH38
- R34 (= R31) binding in other chain
- SGGDQ 73:77 (= SGGDQ 76:80) binding in other chain
- S149 (= S153) binding in other chain
Q7CQ56 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
52% identity, 100% coverage: 1:277/277 of query aligns to 13:285/285 of Q7CQ56
3t88A Crystal structure of escherichia coli menb in complex with substrate analogue, osb-ncoa (see paper)
52% identity, 100% coverage: 1:277/277 of query aligns to 9:281/281 of 3t88A
- active site: G82 (= G78), R87 (= R83), Y93 (= Y88), H101 (≠ R96), L105 (= L100), G129 (= G124), V132 (≠ S127), G152 (≠ D148), S157 (= S153), D159 (= D155), G160 (= G156), A246 (= A242), Y254 (= Y250)
- binding o-succinylbenzoyl-N-coenzyme A: Q39 (≠ E29), V40 (= V30), R41 (= R31), A43 (= A33), S80 (= S76), G81 (= G77), G82 (= G78), D83 (= D79), Q84 (= Q80), K85 (= K81), Y93 (= Y88), V104 (≠ I99), L105 (= L100), Y125 (≠ W120), G129 (= G124), T151 (= T147), V155 (= V151), F158 (= F154), D159 (= D155), T250 (= T246), Y254 (= Y250), F266 (= F262), K269 (= K265)
4i42A E.Coli. 1,4-dihydroxy-2-naphthoyl coenzyme a synthase (ecmenb) in complex with 1-hydroxy-2-naphthoyl-coa (see paper)
52% identity, 100% coverage: 1:277/277 of query aligns to 13:285/285 of 4i42A
- active site: G86 (= G78), R91 (= R83), Y97 (= Y88), H105 (≠ R96), L109 (= L100), G133 (= G124), V136 (≠ S127), G156 (≠ D148), S161 (= S153), D163 (= D155), G164 (= G156), A250 (= A242), Y258 (= Y250)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (= V30), R45 (= R31), S84 (= S76), G85 (= G77), G86 (= G78), D87 (= D79), Q88 (= Q80), K89 (= K81), Y97 (= Y88), V108 (≠ I99), Y129 (≠ W120), G133 (= G124), T155 (= T147), S161 (= S153), T254 (= T246), F270 (= F262), K273 (= K265)
P0ABU0 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Escherichia coli (strain K12) (see 4 papers)
52% identity, 100% coverage: 1:277/277 of query aligns to 13:285/285 of P0ABU0
- R45 (= R31) binding in other chain
- SGGDQK 84:89 (= SGGDQK 76:81) binding in other chain
- K89 (= K81) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- R91 (= R83) mutation to A: Loss of DHNA-CoA synthase activity.
- Y97 (= Y88) binding in other chain; mutation to F: Loss of DHNA-CoA synthase activity.
- YSIGG 129:133 (≠ WAVGG 120:124) binding in other chain
- Q154 (= Q146) 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 (≠ QTD 146:148) binding
- T155 (= T147) binding in other chain
- G156 (≠ D148) mutation to D: Loss of DHNA-CoA synthase activity.
- S161 (= S153) binding in other chain
- W184 (≠ F176) mutation to F: Reduces the specific DHNA-CoA synthase activity by 530-fold, whereas its affinity for hydrogencarbonate is reduced by 20-fold.
- Y258 (= Y250) binding
- R267 (= R259) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- F270 (= F262) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- K273 (= K265) binding ; mutation to A: Impairs protein folding.
2uzfA Crystal structure of staphylococcus aureus 1,4-dihydroxy-2-naphthoyl coa synthase (menb) in complex with acetoacetyl coa (see paper)
50% identity, 99% coverage: 3:277/277 of query aligns to 1:260/260 of 2uzfA
- active site: G70 (= G78), R80 (= R96), L84 (= L100), G108 (= G124), V111 (≠ S127), T130 (= T147), G131 (≠ D148), S136 (= S153), D138 (= D155), A139 (≠ G156), A225 (= A242), Y233 (= Y250)
- binding acetoacetyl-coenzyme a: V28 (= V30), R29 (= R31), S68 (= S76), G69 (= G77), G70 (= G78), D71 (= D79), Y104 (≠ W120), G108 (= G124)
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)
51% identity, 98% coverage: 7:277/277 of query aligns to 72:337/337 of Q8GYN9
Sites not aligning to the query:
- 20 H→V: Loss of peroxisomal targeting.
4elxA Structure of apo e.Coli. 1,4-dihydroxy-2- naphthoyl coa synthases with cl (see paper)
50% identity, 100% coverage: 1:277/277 of query aligns to 10:268/268 of 4elxA
- active site: G83 (= G78), H88 (≠ R96), L92 (= L100), G116 (= G124), V119 (≠ S127), G139 (≠ D148), S144 (= S153), D146 (= D155), G147 (= G156), A233 (= A242), Y241 (= Y250)
- binding chloride ion: G115 (= G123), G139 (≠ D148), W167 (≠ F176)
3h02A 2.15 angstrom resolution crystal structure of naphthoate synthase from salmonella typhimurium.
49% identity, 100% coverage: 1:277/277 of query aligns to 9:266/266 of 3h02A
- active site: G82 (= G78), H86 (≠ R96), L90 (= L100), G114 (= G124), V117 (≠ S127), G137 (≠ D148), S142 (= S153), D144 (= D155), G145 (= G156), A231 (= A242), Y239 (= Y250)
- binding bicarbonate ion: G113 (= G123), Q135 (= Q146), G137 (≠ D148), W165 (≠ F176)
4elwA Structure of e. Coli. 1,4-dihydroxy-2- naphthoyl coenzyme a synthases (menb) in complex with nitrate (see paper)
49% identity, 100% coverage: 1:277/277 of query aligns to 10:267/267 of 4elwA
- active site: G83 (= G78), L91 (= L100), G115 (= G124), V118 (≠ S127), G138 (≠ D148), S143 (= S153), D145 (= D155), G146 (= G156), A232 (= A242), Y240 (= Y250)
- binding nitrate ion: G114 (= G123), T137 (= T147), G138 (≠ D148), F144 (= F154), W166 (≠ F176)
Query Sequence
>Echvi_2341 FitnessBrowser__Cola:Echvi_2341
MEWKVVKEFKDITYKKCDGVARIAFNRPEVRNAFRPQTTSELFEAFVDAREDTSIGVVLL
SAEGPSPKDGVYSFCSGGDQKARGHQGYVGDDGMHRLNILEVQRLIRFMPKVVIAVVPGW
AVGGGHSLHVVCDLTLASKEHAIFKQTDADVTSFDGGYGSAYLAKMVGQKRAREIFFLGR
NYSAQEAYEMGMVNAVIPHNELEDTAYEWAQEILAKSPTSIKMLKFAFNLTDDGMVGQQV
FAGEATRLTYMTEEAQEGRNAFLEKRKPNFKDIKWIP
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