SitesBLAST
Comparing 642684568 IMG__ChlphaBS1_FD:642684568 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)
Q7CQ56 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
76% identity, 100% coverage: 2:273/273 of query aligns to 11:285/285 of Q7CQ56
4i42A E.Coli. 1,4-dihydroxy-2-naphthoyl coenzyme a synthase (ecmenb) in complex with 1-hydroxy-2-naphthoyl-coa (see paper)
76% identity, 100% coverage: 2:273/273 of query aligns to 11:285/285 of 4i42A
- active site: G86 (= G75), R91 (= R80), Y97 (= Y85), H105 (≠ R93), L109 (= L97), G133 (= G121), V136 (= V124), G156 (= G144), S161 (= S149), D163 (= D151), G164 (= G152), A250 (= A238), Y258 (= Y246)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (≠ R33), R45 (= R34), S84 (= S73), G85 (= G74), G86 (= G75), D87 (= D76), Q88 (= Q77), K89 (= K78), Y97 (= Y85), V108 (= V96), Y129 (= Y117), G133 (= G121), T155 (= T143), S161 (= S149), T254 (= T242), F270 (= F258), K273 (= K261)
P0ABU0 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Escherichia coli (strain K12) (see 4 papers)
76% identity, 100% coverage: 2:273/273 of query aligns to 11:285/285 of P0ABU0
- R45 (= R34) binding in other chain
- SGGDQK 84:89 (= SGGDQK 73:78) binding in other chain
- K89 (= K78) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- R91 (= R80) mutation to A: Loss of DHNA-CoA synthase activity.
- Y97 (= Y85) binding in other chain; mutation to F: Loss of DHNA-CoA synthase activity.
- YSIGG 129:133 (≠ YAIGG 117:121) binding in other chain
- Q154 (= Q142) 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 (= QTG 142:144) binding hydrogencarbonate
- T155 (= T143) binding in other chain
- G156 (= G144) mutation to D: Loss of DHNA-CoA synthase activity.
- S161 (= S149) binding in other chain
- W184 (= W172) mutation to F: Reduces the specific DHNA-CoA synthase activity by 530-fold, whereas its affinity for hydrogencarbonate is reduced by 20-fold.
- Y258 (= Y246) binding substrate
- R267 (≠ K255) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- F270 (= F258) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- K273 (= K261) binding substrate; mutation to A: Impairs protein folding.
3t88A Crystal structure of escherichia coli menb in complex with substrate analogue, osb-ncoa (see paper)
76% identity, 100% coverage: 2:273/273 of query aligns to 7:281/281 of 3t88A
- active site: G82 (= G75), R87 (= R80), Y93 (= Y85), H101 (≠ R93), L105 (= L97), G129 (= G121), V132 (= V124), G152 (= G144), S157 (= S149), D159 (= D151), G160 (= G152), A246 (= A238), Y254 (= Y246)
- binding o-succinylbenzoyl-N-coenzyme A: Q39 (≠ E32), V40 (≠ R33), R41 (= R34), A43 (= A36), S80 (= S73), G81 (= G74), G82 (= G75), D83 (= D76), Q84 (= Q77), K85 (= K78), Y93 (= Y85), V104 (= V96), L105 (= L97), Y125 (= Y117), G129 (= G121), T151 (= T143), V155 (= V147), F158 (= F150), D159 (= D151), T250 (= T242), Y254 (= Y246), F266 (= F258), K269 (= K261)
3h02A 2.15 angstrom resolution crystal structure of naphthoate synthase from salmonella typhimurium.
73% identity, 100% coverage: 2:273/273 of query aligns to 7:266/266 of 3h02A
- active site: G82 (= G75), H86 (≠ R93), L90 (= L97), G114 (= G121), V117 (= V124), G137 (= G144), S142 (= S149), D144 (= D151), G145 (= G152), A231 (= A238), Y239 (= Y246)
- binding bicarbonate ion: G113 (= G120), Q135 (= Q142), G137 (= G144), W165 (= W172)
4elxA Structure of apo e.Coli. 1,4-dihydroxy-2- naphthoyl coa synthases with cl (see paper)
74% identity, 100% coverage: 2:273/273 of query aligns to 8:268/268 of 4elxA
- active site: G83 (= G75), H88 (≠ R93), L92 (= L97), G116 (= G121), V119 (= V124), G139 (= G144), S144 (= S149), D146 (= D151), G147 (= G152), A233 (= A238), Y241 (= Y246)
- binding chloride ion: G115 (= G120), G139 (= G144), W167 (= W172)
4elwA Structure of e. Coli. 1,4-dihydroxy-2- naphthoyl coenzyme a synthases (menb) in complex with nitrate (see paper)
74% identity, 100% coverage: 2:273/273 of query aligns to 8:267/267 of 4elwA
- active site: G83 (= G75), L91 (= L97), G115 (= G121), V118 (= V124), G138 (= G144), S143 (= S149), D145 (= D151), G146 (= G152), A232 (= A238), Y240 (= Y246)
- binding nitrate ion: G114 (= G120), T137 (= T143), G138 (= G144), F144 (= F150), W166 (= W172)
4i52A Scmenb im complex with 1-hydroxy-2-naphthoyl-coa (see paper)
71% identity, 99% coverage: 4:273/273 of query aligns to 1:275/275 of 4i52A
- active site: G77 (= G75), R82 (= R80), Y87 (= Y85), R95 (= R93), L99 (= L97), G123 (= G121), V126 (= V124), G146 (= G144), S151 (= S149), D153 (= D151), G154 (= G152), A240 (= A238), Y248 (= Y246)
- binding 1-hydroxy-2-naphthoyl-CoA: H29 (≠ E32), K30 (≠ R33), R31 (= R34), A33 (= A36), S75 (= S73), G76 (= G74), G77 (= G75), D78 (= D76), Q79 (= Q77), L96 (= L94), V98 (= V96), Y119 (= Y117), I121 (= I119), G123 (= G121), T145 (= T143), V149 (= V147), S151 (= S149), F152 (= F150)
4i4zA Synechocystis sp. Pcc 6803 1,4-dihydroxy-2-naphthoyl-coenzyme a synthase (menb) in complex with salicylyl-coa (see paper)
71% identity, 99% coverage: 4:273/273 of query aligns to 1:275/275 of 4i4zA
- active site: G77 (= G75), R82 (= R80), Y87 (= Y85), R95 (= R93), L99 (= L97), G123 (= G121), V126 (= V124), G146 (= G144), S151 (= S149), D153 (= D151), G154 (= G152), A240 (= A238), Y248 (= Y246)
- binding Salicylyl CoA: H29 (≠ E32), K30 (≠ R33), R31 (= R34), S75 (= S73), G76 (= G74), G77 (= G75), D78 (= D76), Q79 (= Q77), Y87 (= Y85), V98 (= V96), G123 (= G121), T145 (= T143), V149 (= V147), S151 (= S149), F260 (= F258), K263 (= K261)
- binding bicarbonate ion: G122 (= G120), Q144 (= Q142), T145 (= T143), G146 (= G144), W174 (= W172)
Q5HH38 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Staphylococcus aureus (strain COL) (see paper)
67% identity, 100% coverage: 1:273/273 of query aligns to 1:273/273 of Q5HH38
- R34 (= R34) binding in other chain
- SGGDQ 73:77 (= SGGDQ 73:77) binding in other chain
- S149 (= S149) binding in other chain
4emlA Synechocystis sp. Pcc 6803 1,4-dihydroxy-2-naphthoyl-coenzyme a synthase (menb) in complex with bicarbonate (see paper)
69% identity, 99% coverage: 4:273/273 of query aligns to 1:261/261 of 4emlA
- active site: G77 (= G75), R81 (= R93), L85 (= L97), G109 (= G121), V112 (= V124), G132 (= G144), S137 (= S149), D139 (= D151), G140 (= G152), A226 (= A238), Y234 (= Y246)
- binding bicarbonate ion: G108 (= G120), Q130 (= Q142), G132 (= G144), W160 (= W172)
- binding chloride ion: D184 (= D196), R185 (= R197), E187 (= E199), E188 (= E200)
2uzfA Crystal structure of staphylococcus aureus 1,4-dihydroxy-2-naphthoyl coa synthase (menb) in complex with acetoacetyl coa (see paper)
67% identity, 98% coverage: 6:273/273 of query aligns to 1:260/260 of 2uzfA
- active site: G70 (= G75), R80 (= R93), L84 (= L97), G108 (= G121), V111 (= V124), T130 (= T143), G131 (= G144), S136 (= S149), D138 (= D151), A139 (≠ G152), A225 (= A238), Y233 (= Y246)
- binding acetoacetyl-coenzyme a: V28 (≠ R33), R29 (= R34), S68 (= S73), G69 (= G74), G70 (= G75), D71 (= D76), Y104 (= Y117), G108 (= G121)
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)
68% identity, 96% coverage: 11:273/273 of query aligns to 73:337/337 of Q8GYN9
Sites not aligning to the query:
- 20 H→V: Loss of peroxisomal targeting.
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)
50% identity, 96% coverage: 11:271/273 of query aligns to 33:312/314 of P9WNP5
- R58 (= R34) binding in other chain
- K95 (vs. gap) binding in other chain
- SGGDQ 103:107 (= SGGDQ 73:77) binding in other chain
- R133 (= R93) mutation to A: Loss of DHNA-CoA synthase activity.
- WAAGG 157:161 (≠ YAIGG 117:121) binding in other chain
- T184 (= T143) binding in other chain
- D185 (≠ G144) mutation to E: Nearly abolishes DHNA-CoA synthase activity.; mutation D->G,N: Loss of DHNA-CoA synthase activity.
- S190 (= S149) mutation to A: Reduces affinity for substrate. Nearly abolishes DHNA-CoA synthase activity.
- D192 (= D151) mutation to N: Loss of DHNA-CoA synthase activity.
- Y287 (= Y246) 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)
50% identity, 96% coverage: 11:271/273 of query aligns to 20:299/301 of 4qijA
- active site: G92 (= G75), R97 (= R80), Y102 (= Y85), R117 (vs. gap), H122 (≠ N95), G148 (= G121), S151 (≠ V124), D172 (≠ G144), S177 (= S149), D179 (= D151), G180 (= G152), A266 (= A238), Y274 (= Y246)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (≠ R33), R45 (= R34), A47 (= A36), F48 (= F37), K82 (vs. gap), S90 (= S73), G91 (= G74), G92 (= G75), D93 (= D76), Q94 (= Q77), Y102 (= Y85), L121 (= L94), I123 (≠ V96), W144 (≠ Y117), G148 (= G121), T171 (= T143), D172 (≠ G144), S177 (= S149), F286 (= F258), K289 (= K261)
4qiiB Crystal structure of type ii menb from mycobacteria tuberculosis (see paper)
50% identity, 96% coverage: 11:271/273 of query aligns to 20:299/301 of 4qiiB
- active site: G92 (= G75), R97 (= R80), Y102 (= Y85), R117 (vs. gap), H122 (≠ N95), G148 (= G121), S151 (≠ V124), D172 (≠ G144), S177 (= S149), D179 (= D151), G180 (= G152), A266 (= A238), Y274 (= Y246)
- binding Salicylyl CoA: V44 (≠ R33), R45 (= R34), A47 (= A36), K82 (vs. gap), S90 (= S73), G92 (= G75), D93 (= D76), Q94 (= Q77), Y102 (= Y85), W144 (≠ Y117), G147 (= G120), G148 (= G121), T171 (= T143), D172 (≠ G144), V175 (= V147), S177 (= S149), Y274 (= Y246), F286 (= F258), K289 (= K261)
1q51B Crystal structure of mycobacterium tuberculosis menb in complex with acetoacetyl-coenzyme a, a key enzyme in vitamin k2 biosynthesis (see paper)
50% identity, 96% coverage: 11:271/273 of query aligns to 16:278/280 of 1q51B
- active site: G88 (= G75), H101 (≠ N95), G127 (= G121), S130 (≠ V124), D151 (≠ G144), S156 (= S149), D158 (= D151), G159 (= G152), A245 (= A238), Y253 (= Y246)
- binding acetoacetyl-coenzyme a: V40 (≠ R33), R41 (= R34), A43 (= A36), S86 (= S73), G88 (= G75), D89 (= D76), Q90 (= Q77), W123 (≠ Y117), G126 (= G120), G127 (= G121), T150 (= T143)
1q51A Crystal structure of mycobacterium tuberculosis menb in complex with acetoacetyl-coenzyme a, a key enzyme in vitamin k2 biosynthesis (see paper)
49% identity, 96% coverage: 11:271/273 of query aligns to 16:269/271 of 1q51A
- active site: G88 (= G75), H92 (≠ N95), G118 (= G121), S121 (≠ V124), D142 (≠ G144), S147 (= S149), D149 (= D151), G150 (= G152), A236 (= A238), Y244 (= Y246)
- binding acetoacetyl-coenzyme a: V40 (≠ R33), R41 (= R34), K78 (vs. gap), S86 (= S73), G88 (= G75), D89 (= D76), Q90 (= Q77), W114 (≠ Y117), G117 (= G120), G118 (= G121), T141 (= T143)
1rjnB The crystal structure of menb (rv0548c) from mycobacterium tuberculosis in complex with the coa portion of naphthoyl coa (see paper)
49% identity, 96% coverage: 11:271/273 of query aligns to 20:273/275 of 1rjnB
- active site: G92 (= G75), H96 (≠ N95), G122 (= G121), S125 (≠ V124), D146 (≠ G144), S151 (= S149), D153 (= D151), G154 (= G152), A240 (= A238)
- binding coenzyme a: V44 (≠ R33), R45 (= R34), K82 (vs. gap), S90 (= S73), G92 (= G75), D93 (= D76), Q94 (= Q77), W118 (≠ Y117)
- binding 3-[4-(2-hydroxyethyl)piperazin-1-yl]propane-1-sulfonic acid: R163 (= R161), Q164 (≠ L162), V165 (= V163), M188 (= M186)
3t8aB Crystal structure of mycobacterium tuberculosis menb in complex with substrate analogue, osb-ncoa (see paper)
49% identity, 96% coverage: 11:271/273 of query aligns to 19:272/274 of 3t8aB
- active site: G91 (= G75), H97 (≠ N95), G123 (= G121), S126 (≠ V124), D147 (≠ G144), S152 (= S149), D154 (= D151), G155 (= G152), A241 (= A238), Y249 (= Y246)
- binding o-succinylbenzoyl-N-coenzyme A: V43 (≠ R33), R44 (= R34), K81 (vs. gap), S89 (= S73), G91 (= G75), D92 (= D76), Q93 (= Q77), W119 (≠ Y117)
Query Sequence
>642684568 IMG__ChlphaBS1_FD:642684568
MSTVNWIQSGDFTDIFYHKADGIAKITINRPERRNAFRPQTVVEMIQALENARNDENIGV
IILTGQGPLAFCSGGDQKIRGDAGYADEKGVNRLNVLDFQRNIRTCPKPVIAMVAGYAIG
GGHVLHMLCDLTIAAENAVFGQTGPKVGSFDGGWGASYMARLVGQKKAREIWYLCRQYNA
QEALDMGLVNTVVPLDRLEEETVQWCREILQHSPLAIRCLKSALNADCDGQAGLQELAGN
ATLLYYMSEEAQEGKNAFVEKRKPDFGKFPKRP
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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