SitesBLAST
Comparing WP_009546068.1 NCBI__GCF_000017845.1:WP_009546068.1 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)
4i52A Scmenb im complex with 1-hydroxy-2-naphthoyl-coa (see paper)
85% identity, 99% coverage: 3:277/277 of query aligns to 1:275/275 of 4i52A
- active site: G77 (= G79), R82 (= R84), Y87 (= Y89), R95 (= R97), L99 (= L101), G123 (= G125), V126 (= V128), G146 (= G148), S151 (= S153), D153 (= D155), G154 (= G156), A240 (= A242), Y248 (= Y250)
- binding 1-hydroxy-2-naphthoyl-CoA: H29 (= H31), K30 (= K32), R31 (= R33), A33 (= A35), S75 (= S77), G76 (= G78), G77 (= G79), D78 (= D80), Q79 (= Q81), L96 (= L98), V98 (= V100), Y119 (= Y121), I121 (= I123), G123 (= G125), 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)
85% identity, 99% coverage: 3:277/277 of query aligns to 1:275/275 of 4i4zA
- active site: G77 (= G79), R82 (= R84), Y87 (= Y89), R95 (= R97), L99 (= L101), G123 (= G125), V126 (= V128), G146 (= G148), S151 (= S153), D153 (= D155), G154 (= G156), A240 (= A242), Y248 (= Y250)
- binding Salicylyl CoA: H29 (= H31), K30 (= K32), R31 (= R33), S75 (= S77), G76 (= G78), G77 (= G79), D78 (= D80), Q79 (= Q81), Y87 (= Y89), V98 (= V100), G123 (= G125), T145 (= T147), V149 (= V151), S151 (= S153), F260 (= F262), K263 (= K265)
- binding bicarbonate ion: G122 (= G124), Q144 (= Q146), T145 (= T147), G146 (= G148), W174 (= W176)
4emlA Synechocystis sp. Pcc 6803 1,4-dihydroxy-2-naphthoyl-coenzyme a synthase (menb) in complex with bicarbonate (see paper)
82% identity, 99% coverage: 3:277/277 of query aligns to 1:261/261 of 4emlA
- active site: G77 (= G79), R81 (= R97), L85 (= L101), G109 (= G125), V112 (= V128), G132 (= G148), S137 (= S153), D139 (= D155), G140 (= G156), A226 (= A242), Y234 (= Y250)
- binding bicarbonate ion: G108 (= G124), Q130 (= Q146), G132 (= G148), W160 (= W176)
- binding chloride ion: D184 (≠ E200), R185 (≠ Q201), E187 (= E203), E188 (≠ T204)
3t88A Crystal structure of escherichia coli menb in complex with substrate analogue, osb-ncoa (see paper)
68% identity, 99% coverage: 3:277/277 of query aligns to 9:281/281 of 3t88A
- active site: G82 (= G79), R87 (= R84), Y93 (= Y89), H101 (≠ R97), L105 (= L101), G129 (= G125), V132 (= V128), G152 (= G148), S157 (= S153), D159 (= D155), G160 (= G156), A246 (= A242), Y254 (= Y250)
- binding o-succinylbenzoyl-N-coenzyme A: Q39 (≠ H31), V40 (≠ K32), R41 (= R33), A43 (= A35), S80 (= S77), G81 (= G78), G82 (= G79), D83 (= D80), Q84 (= Q81), K85 (≠ S82), Y93 (= Y89), V104 (= V100), L105 (= L101), Y125 (= Y121), G129 (= G125), 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)
68% identity, 99% coverage: 3:277/277 of query aligns to 13:285/285 of 4i42A
- active site: G86 (= G79), R91 (= R84), Y97 (= Y89), H105 (≠ R97), L109 (= L101), G133 (= G125), V136 (= V128), G156 (= G148), S161 (= S153), D163 (= D155), G164 (= G156), A250 (= A242), Y258 (= Y250)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (≠ K32), R45 (= R33), S84 (= S77), G85 (= G78), G86 (= G79), D87 (= D80), Q88 (= Q81), K89 (≠ S82), Y97 (= Y89), V108 (= V100), Y129 (= Y121), G133 (= G125), 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)
68% identity, 99% coverage: 3:277/277 of query aligns to 13:285/285 of P0ABU0
- R45 (= R33) binding in other chain
- SGGDQK 84:89 (≠ SGGDQS 77:82) binding in other chain
- K89 (≠ S82) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- R91 (= R84) mutation to A: Loss of DHNA-CoA synthase activity.
- Y97 (= Y89) binding in other chain; mutation to F: Loss of DHNA-CoA synthase activity.
- YSIGG 129:133 (≠ YAIGG 121:125) 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 (= QTG 146:148) binding hydrogencarbonate
- T155 (= T147) binding in other chain
- G156 (= G148) mutation to D: Loss of DHNA-CoA synthase activity.
- S161 (= S153) binding in other chain
- W184 (= W176) 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 substrate
- R267 (≠ K259) 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 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)
67% identity, 99% coverage: 3:277/277 of query aligns to 13:285/285 of Q7CQ56
Q5HH38 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Staphylococcus aureus (strain COL) (see paper)
65% identity, 99% coverage: 5:277/277 of query aligns to 6:273/273 of Q5HH38
- R34 (= R33) binding in other chain
- SGGDQ 73:77 (= SGGDQ 77:81) binding in other chain
- S149 (= S153) binding in other chain
4elwA Structure of e. Coli. 1,4-dihydroxy-2- naphthoyl coenzyme a synthases (menb) in complex with nitrate (see paper)
65% identity, 99% coverage: 3:277/277 of query aligns to 10:267/267 of 4elwA
- active site: G83 (= G79), L91 (= L101), G115 (= G125), V118 (= V128), G138 (= G148), S143 (= S153), D145 (= D155), G146 (= G156), A232 (= A242), Y240 (= Y250)
- binding nitrate ion: G114 (= G124), T137 (= T147), G138 (= G148), F144 (= F154), W166 (= W176)
4elxA Structure of apo e.Coli. 1,4-dihydroxy-2- naphthoyl coa synthases with cl (see paper)
65% identity, 99% coverage: 3:277/277 of query aligns to 10:268/268 of 4elxA
- active site: G83 (= G79), H88 (≠ R97), L92 (= L101), G116 (= G125), V119 (= V128), G139 (= G148), S144 (= S153), D146 (= D155), G147 (= G156), A233 (= A242), Y241 (= Y250)
- binding chloride ion: G115 (= G124), G139 (= G148), W167 (= W176)
2uzfA Crystal structure of staphylococcus aureus 1,4-dihydroxy-2-naphthoyl coa synthase (menb) in complex with acetoacetyl coa (see paper)
64% identity, 99% coverage: 5:277/277 of query aligns to 1:260/260 of 2uzfA
- active site: G70 (= G79), R80 (= R97), L84 (= L101), G108 (= G125), V111 (= V128), T130 (= T147), G131 (= G148), S136 (= S153), D138 (= D155), A139 (≠ G156), A225 (= A242), Y233 (= Y250)
- binding acetoacetyl-coenzyme a: V28 (≠ K32), R29 (= R33), S68 (= S77), G69 (= G78), G70 (= G79), D71 (= D80), Y104 (= Y121), G108 (= G125)
3h02A 2.15 angstrom resolution crystal structure of naphthoate synthase from salmonella typhimurium.
64% identity, 99% coverage: 3:277/277 of query aligns to 9:266/266 of 3h02A
- active site: G82 (= G79), H86 (≠ R97), L90 (= L101), G114 (= G125), V117 (= V128), G137 (= G148), S142 (= S153), D144 (= D155), G145 (= G156), A231 (= A242), Y239 (= Y250)
- binding bicarbonate ion: G113 (= G124), Q135 (= Q146), G137 (= G148), W165 (= W176)
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)
62% identity, 97% coverage: 9:277/277 of query aligns to 72:337/337 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)
54% identity, 97% coverage: 5:274/277 of query aligns to 25:311/314 of P9WNP5
- R58 (= R33) binding in other chain
- K95 (≠ T69) binding in other chain
- SGGDQ 103:107 (= SGGDQ 77:81) binding in other chain
- R133 (= R97) mutation to A: Loss of DHNA-CoA synthase activity.
- WAAGG 157:161 (≠ YAIGG 121:125) binding in other chain
- T184 (= T147) binding in other chain
- D185 (≠ G148) 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)
54% identity, 97% coverage: 5:274/277 of query aligns to 12:298/301 of 4qijA
- active site: G92 (= G79), R97 (= R84), Y102 (= Y89), R117 (≠ G94), H122 (≠ N99), G148 (= G125), S151 (≠ V128), D172 (≠ G148), S177 (= S153), D179 (= D155), G180 (= G156), A266 (= A242), Y274 (= Y250)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (≠ K32), R45 (= R33), A47 (= A35), F48 (= F36), K82 (≠ T69), S90 (= S77), G91 (= G78), G92 (= G79), D93 (= D80), Q94 (= Q81), Y102 (= Y89), L121 (= L98), I123 (≠ V100), W144 (≠ Y121), G148 (= G125), T171 (= T147), D172 (≠ G148), S177 (= S153), F286 (= F262), K289 (= K265)
4qiiB Crystal structure of type ii menb from mycobacteria tuberculosis (see paper)
54% identity, 97% coverage: 5:274/277 of query aligns to 12:298/301 of 4qiiB