SitesBLAST
Comparing WP_086511943.1 NCBI__GCF_002151265.1:WP_086511943.1 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)
Q5HH38 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Staphylococcus aureus (strain COL) (see paper)
55% identity, 97% coverage: 8:263/263 of query aligns to 12:269/273 of Q5HH38
- R34 (≠ Y30) binding in other chain
- SGGDQ 73:77 (≠ TGGDQ 69:73) binding in other chain
- S149 (= S143) binding in other chain
2uzfA Crystal structure of staphylococcus aureus 1,4-dihydroxy-2-naphthoyl coa synthase (menb) in complex with acetoacetyl coa (see paper)
55% identity, 97% coverage: 8:263/263 of query aligns to 7:256/260 of 2uzfA
- active site: G70 (= G71), R80 (≠ G87), L84 (≠ E91), G108 (= G115), V111 (= V118), T130 (≠ V137), G131 (= G138), S136 (= S143), D138 (= D145), A139 (≠ P146), A225 (≠ G232), Y233 (= Y240)
- binding acetoacetyl-coenzyme a: V28 (≠ R29), R29 (≠ Y30), S68 (≠ T69), G69 (= G70), G70 (= G71), D71 (= D72), Y104 (≠ F111), G108 (= G115)
4i52A Scmenb im complex with 1-hydroxy-2-naphthoyl-coa (see paper)
56% identity, 98% coverage: 5:263/263 of query aligns to 6:271/275 of 4i52A
- active site: G77 (= G71), R82 (≠ H76), Y87 (= Y80), R95 (≠ G87), L99 (≠ E91), G123 (= G115), V126 (= V118), G146 (= G138), S151 (= S143), D153 (= D145), G154 (≠ P146), A240 (≠ G232), Y248 (= Y240)
- binding 1-hydroxy-2-naphthoyl-CoA: H29 (≠ E28), K30 (≠ R29), R31 (≠ Y30), A33 (= A32), S75 (≠ T69), G76 (= G70), G77 (= G71), D78 (= D72), Q79 (= Q73), L96 (= L88), V98 (= V90), Y119 (≠ F111), I121 (= I113), G123 (= G115), T145 (≠ V137), V149 (= V141), S151 (= S143), F152 (≠ V144)
4i4zA Synechocystis sp. Pcc 6803 1,4-dihydroxy-2-naphthoyl-coenzyme a synthase (menb) in complex with salicylyl-coa (see paper)
56% identity, 98% coverage: 5:263/263 of query aligns to 6:271/275 of 4i4zA
- active site: G77 (= G71), R82 (≠ H76), Y87 (= Y80), R95 (≠ G87), L99 (≠ E91), G123 (= G115), V126 (= V118), G146 (= G138), S151 (= S143), D153 (= D145), G154 (≠ P146), A240 (≠ G232), Y248 (= Y240)
- binding Salicylyl CoA: H29 (≠ E28), K30 (≠ R29), R31 (≠ Y30), S75 (≠ T69), G76 (= G70), G77 (= G71), D78 (= D72), Q79 (= Q73), Y87 (= Y80), V98 (= V90), G123 (= G115), T145 (≠ V137), V149 (= V141), S151 (= S143), F260 (= F252), K263 (= K255)
- binding bicarbonate ion: G122 (= G114), Q144 (= Q136), T145 (≠ V137), G146 (= G138), W174 (= W166)
3t88A Crystal structure of escherichia coli menb in complex with substrate analogue, osb-ncoa (see paper)
53% identity, 97% coverage: 8:263/263 of query aligns to 18:277/281 of 3t88A
- active site: G82 (= G71), R87 (vs. gap), Y93 (≠ Q79), H101 (≠ G87), L105 (≠ E91), G129 (= G115), V132 (= V118), G152 (= G138), S157 (= S143), D159 (= D145), G160 (≠ P146), A246 (≠ G232), Y254 (= Y240)
- binding o-succinylbenzoyl-N-coenzyme A: Q39 (≠ E28), V40 (≠ R29), R41 (≠ Y30), A43 (= A32), S80 (≠ T69), G81 (= G70), G82 (= G71), D83 (= D72), Q84 (= Q73), K85 (≠ S74), Y93 (≠ Q79), V104 (= V90), L105 (≠ E91), Y125 (≠ F111), G129 (= G115), T151 (≠ V137), V155 (= V141), F158 (≠ V144), D159 (= D145), T250 (≠ L236), Y254 (= Y240), F266 (= F252), K269 (= K255)
4i42A E.Coli. 1,4-dihydroxy-2-naphthoyl coenzyme a synthase (ecmenb) in complex with 1-hydroxy-2-naphthoyl-coa (see paper)
53% identity, 97% coverage: 8:263/263 of query aligns to 22:281/285 of 4i42A
- active site: G86 (= G71), R91 (vs. gap), Y97 (≠ Q79), H105 (≠ G87), L109 (≠ E91), G133 (= G115), V136 (= V118), G156 (= G138), S161 (= S143), D163 (= D145), G164 (≠ P146), A250 (≠ G232), Y258 (= Y240)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (≠ R29), R45 (≠ Y30), S84 (≠ T69), G85 (= G70), G86 (= G71), D87 (= D72), Q88 (= Q73), K89 (≠ S74), Y97 (≠ Q79), V108 (= V90), Y129 (≠ F111), G133 (= G115), T155 (≠ V137), S161 (= S143), T254 (≠ L236), F270 (= F252), K273 (= K255)
P0ABU0 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Escherichia coli (strain K12) (see 4 papers)
53% identity, 97% coverage: 8:263/263 of query aligns to 22:281/285 of P0ABU0
- R45 (≠ Y30) binding in other chain
- SGGDQK 84:89 (≠ TGGDQS 69:74) binding in other chain
- K89 (≠ S74) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- R91 (vs. gap) mutation to A: Loss of DHNA-CoA synthase activity.
- Y97 (≠ Q79) binding in other chain; mutation to F: Loss of DHNA-CoA synthase activity.
- YSIGG 129:133 (≠ FAIGG 111:115) binding in other chain
- Q154 (= Q136) 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 (≠ QVG 136:138) binding
- T155 (≠ V137) binding in other chain
- G156 (= G138) mutation to D: Loss of DHNA-CoA synthase activity.
- S161 (= S143) binding in other chain
- W184 (= W166) mutation to F: Reduces the specific DHNA-CoA synthase activity by 530-fold, whereas its affinity for hydrogencarbonate is reduced by 20-fold.
- Y258 (= Y240) binding
- R267 (≠ V249) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- F270 (= F252) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- K273 (= K255) binding ; 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)
53% identity, 97% coverage: 8:263/263 of query aligns to 22:281/285 of Q7CQ56
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)
52% identity, 97% coverage: 8:263/263 of query aligns to 74:333/337 of Q8GYN9
Sites not aligning to the query:
- 20 H→V: Loss of peroxisomal targeting.
4emlA Synechocystis sp. Pcc 6803 1,4-dihydroxy-2-naphthoyl-coenzyme a synthase (menb) in complex with bicarbonate (see paper)
55% identity, 98% coverage: 5:263/263 of query aligns to 6:257/261 of 4emlA
- active site: G77 (= G71), R81 (≠ A75), L85 (≠ E91), G109 (= G115), V112 (= V118), G132 (= G138), S137 (= S143), D139 (= D145), G140 (≠ P146), A226 (≠ G232), Y234 (= Y240)
- binding bicarbonate ion: G108 (= G114), Q130 (= Q136), G132 (= G138), W160 (= W166)
- binding chloride ion: D184 (= D190), R185 (≠ K191), E187 (≠ D193), E188 (= E194)
4elxA Structure of apo e.Coli. 1,4-dihydroxy-2- naphthoyl coa synthases with cl (see paper)
53% identity, 97% coverage: 8:263/263 of query aligns to 19:264/268 of 4elxA
- active site: G83 (= G71), H88 (= H76), L92 (≠ E91), G116 (= G115), V119 (= V118), G139 (= G138), S144 (= S143), D146 (= D145), G147 (≠ P146), A233 (≠ G232), Y241 (= Y240)
- binding chloride ion: G115 (= G114), G139 (= G138), W167 (= W166)
4elwA Structure of e. Coli. 1,4-dihydroxy-2- naphthoyl coenzyme a synthases (menb) in complex with nitrate (see paper)
53% identity, 97% coverage: 8:263/263 of query aligns to 19:263/267 of 4elwA
- active site: G83 (= G71), L91 (≠ E91), G115 (= G115), V118 (= V118), G138 (= G138), S143 (= S143), D145 (= D145), G146 (≠ P146), A232 (≠ G232), Y240 (= Y240)
- binding nitrate ion: G114 (= G114), T137 (≠ V137), G138 (= G138), F144 (≠ V144), W166 (= W166)
3h02A 2.15 angstrom resolution crystal structure of naphthoate synthase from salmonella typhimurium.
53% identity, 97% coverage: 8:263/263 of query aligns to 18:262/266 of 3h02A
- active site: G82 (= G71), H86 (≠ A75), L90 (≠ E91), G114 (= G115), V117 (= V118), G137 (= G138), S142 (= S143), D144 (= D145), G145 (≠ P146), A231 (≠ G232), Y239 (= Y240)
- binding bicarbonate ion: G113 (= G114), Q135 (= Q136), G137 (= G138), W165 (= W166)
1q51B Crystal structure of mycobacterium tuberculosis menb in complex with acetoacetyl-coenzyme a, a key enzyme in vitamin k2 biosynthesis (see paper)
43% identity, 97% coverage: 10:263/263 of query aligns to 19:276/280 of 1q51B
- active site: G88 (= G71), H101 (≠ P89), G127 (= G115), S130 (≠ V118), D151 (≠ G138), S156 (= S143), D158 (= D145), G159 (≠ P146), A245 (≠ G232), Y253 (= Y240)
- binding acetoacetyl-coenzyme a: V40 (≠ R29), R41 (≠ Y30), A43 (= A32), S86 (≠ T69), G88 (= G71), D89 (= D72), Q90 (= Q73), W123 (≠ F111), G126 (= G114), G127 (= G115), T150 (≠ V137)
1q51A Crystal structure of mycobacterium tuberculosis menb in complex with acetoacetyl-coenzyme a, a key enzyme in vitamin k2 biosynthesis (see paper)
42% identity, 97% coverage: 10:263/263 of query aligns to 19:267/271 of 1q51A
- active site: G88 (= G71), H92 (≠ P89), G118 (= G115), S121 (≠ V118), D142 (≠ G138), S147 (= S143), D149 (= D145), G150 (≠ P146), A236 (≠ G232), Y244 (= Y240)
- binding acetoacetyl-coenzyme a: V40 (≠ R29), R41 (≠ Y30), K78 (vs. gap), S86 (≠ T69), G88 (= G71), D89 (= D72), Q90 (= Q73), W114 (≠ F111), G117 (= G114), G118 (= G115), T141 (≠ V137)
1rjnB The crystal structure of menb (rv0548c) from mycobacterium tuberculosis in complex with the coa portion of naphthoyl coa (see paper)
43% identity, 97% coverage: 10:263/263 of query aligns to 23:271/275 of 1rjnB
- active site: G92 (= G71), H96 (≠ G84), G122 (= G115), S125 (≠ V118), D146 (≠ G138), S151 (= S143), D153 (= D145), G154 (≠ P146), A240 (≠ G232)
- binding coenzyme a: V44 (≠ R29), R45 (≠ Y30), K82 (vs. gap), S90 (≠ T69), G92 (= G71), D93 (= D72), Q94 (= Q73), W118 (≠ F111)
- binding 3-[4-(2-hydroxyethyl)piperazin-1-yl]propane-1-sulfonic acid: R163 (= R155), Q164 (≠ V156), V165 (≠ I157), M188 (≠ W180)
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)
41% identity, 97% coverage: 10:263/263 of query aligns to 36:310/314 of P9WNP5
- R58 (≠ Y30) binding in other chain
- K95 (vs. gap) binding in other chain
- SGGDQ 103:107 (≠ TGGDQ 69:73) binding in other chain
- R133 (vs. gap) mutation to A: Loss of DHNA-CoA synthase activity.
- WAAGG 157:161 (≠ FAIGG 111:115) binding in other chain
- T184 (≠ V137) binding in other chain
- D185 (≠ G138) mutation to E: Nearly abolishes DHNA-CoA synthase activity.; mutation D->G,N: Loss of DHNA-CoA synthase activity.
- S190 (= S143) mutation to A: Reduces affinity for substrate. Nearly abolishes DHNA-CoA synthase activity.
- D192 (= D145) mutation to N: Loss of DHNA-CoA synthase activity.
- Y287 (= Y240) 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)
41% identity, 97% coverage: 10:263/263 of query aligns to 23:297/301 of 4qijA
- active site: G92 (= G71), R97 (vs. gap), Y102 (≠ Q79), R117 (vs. gap), H122 (≠ P89), G148 (= G115), S151 (≠ V118), D172 (≠ G138), S177 (= S143), D179 (= D145), G180 (≠ P146), A266 (≠ G232), Y274 (= Y240)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (≠ R29), R45 (≠ Y30), A47 (= A32), F48 (= F33), K82 (vs. gap), S90 (≠ T69), G91 (= G70), G92 (= G71), D93 (= D72), Q94 (= Q73), Y102 (≠ Q79), L121 (= L88), I123 (≠ V90), W144 (≠ F111), G148 (= G115), T171 (≠ V137), D172 (≠ G138), S177 (= S143), F286 (= F252), K289 (= K255)
4qiiB Crystal structure of type ii menb from mycobacteria tuberculosis (see paper)
41% identity, 97% coverage: 10:263/263 of query aligns to 23:297/301 of 4qiiB
- active site: G92 (= G71), R97 (vs. gap), Y102 (≠ Q79), R117 (vs. gap), H122 (≠ P89), G148 (= G115), S151 (≠ V118), D172 (≠ G138), S177 (= S143), D179 (= D145), G180 (≠ P146), A266 (≠ G232), Y274 (= Y240)
- binding Salicylyl CoA: V44 (≠ R29), R45 (≠ Y30), A47 (= A32), K82 (vs. gap), S90 (≠ T69), G92 (= G71), D93 (= D72), Q94 (= Q73), Y102 (≠ Q79), W144 (≠ F111), G147 (= G114), G148 (= G115), T171 (≠ V137), D172 (≠ G138), V175 (= V141), S177 (= S143), Y274 (= Y240), F286 (= F252), K289 (= K255)
3t8aB Crystal structure of mycobacterium tuberculosis menb in complex with substrate analogue, osb-ncoa (see paper)
42% identity, 97% coverage: 10:263/263 of query aligns to 22:270/274 of 3t8aB
- active site: G91 (= G71), H97 (≠ P89), G123 (= G115), S126 (≠ V118), D147 (≠ G138), S152 (= S143), D154 (= D145), G155 (≠ P146), A241 (≠ G232), Y249 (= Y240)
- binding o-succinylbenzoyl-N-coenzyme A: V43 (≠ R29), R44 (≠ Y30), K81 (vs. gap), S89 (≠ T69), G91 (= G71), D92 (= D72), Q93 (= Q73), W119 (≠ F111)
Query Sequence
>WP_086511943.1 NCBI__GCF_002151265.1:WP_086511943.1
MTLQAPNYEDILYDVNDGVATITINRPERYNAFRGQTCMELLDAFNCAGWDKSVGVIVLA
GAGDKAFCTGGDQSAHEGQYDGRGIIGLPVEELQTLIRQVPKPVIARVQGFAIGGGHVLA
LVCDLTIASENAVFGQVGPKVGSVDPGFGTAYMARVIGEKRAREIWYLCRKYSAAQALEW
GLCNAVVPADKLDEEVRQWCDEILEKSPTALSIAKRSFNADSENIAGIGAMGMQALSLYY
DTEESKEGVAAFKEKRKPDFRKF
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