SitesBLAST
Comparing 354228 FitnessBrowser__Btheta:354228 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)
66% identity, 99% coverage: 3:274/274 of query aligns to 2:273/273 of Q5HH38
- R34 (= R35) binding in other chain
- SGGDQ 73:77 (= SGGDQ 74:78) binding in other chain
- S149 (= S150) 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)
65% identity, 98% coverage: 7:274/274 of query aligns to 1:260/260 of 2uzfA
- active site: G70 (= G76), R80 (= R94), L84 (= L98), G108 (= G122), V111 (= V125), T130 (= T144), G131 (= G145), S136 (= S150), D138 (= D152), A139 (= A153), A225 (= A239), Y233 (= Y247)
- binding acetoacetyl-coenzyme a: V28 (≠ Y34), R29 (= R35), S68 (= S74), G69 (= G75), G70 (= G76), D71 (= D77), Y104 (≠ F118), G108 (= G122)
4i52A Scmenb im complex with 1-hydroxy-2-naphthoyl-coa (see paper)
62% identity, 98% coverage: 6:274/274 of query aligns to 2:275/275 of 4i52A
- active site: G77 (= G76), R82 (≠ K81), Y87 (= Y86), R95 (= R94), L99 (= L98), G123 (= G122), V126 (= V125), G146 (= G145), S151 (= S150), D153 (= D152), G154 (≠ A153), A240 (= A239), Y248 (= Y247)
- binding 1-hydroxy-2-naphthoyl-CoA: H29 (≠ R33), K30 (≠ Y34), R31 (= R35), A33 (= A37), S75 (= S74), G76 (= G75), G77 (= G76), D78 (= D77), Q79 (= Q78), L96 (= L95), V98 (= V97), Y119 (≠ F118), I121 (= I120), G123 (= G122), T145 (= T144), V149 (= V148), S151 (= S150), F152 (= F151)
4i4zA Synechocystis sp. Pcc 6803 1,4-dihydroxy-2-naphthoyl-coenzyme a synthase (menb) in complex with salicylyl-coa (see paper)
62% identity, 98% coverage: 6:274/274 of query aligns to 2:275/275 of 4i4zA
- active site: G77 (= G76), R82 (≠ K81), Y87 (= Y86), R95 (= R94), L99 (= L98), G123 (= G122), V126 (= V125), G146 (= G145), S151 (= S150), D153 (= D152), G154 (≠ A153), A240 (= A239), Y248 (= Y247)
- binding Salicylyl CoA: H29 (≠ R33), K30 (≠ Y34), R31 (= R35), S75 (= S74), G76 (= G75), G77 (= G76), D78 (= D77), Q79 (= Q78), Y87 (= Y86), V98 (= V97), G123 (= G122), T145 (= T144), V149 (= V148), S151 (= S150), F260 (= F259), K263 (= K262)
- binding bicarbonate ion: G122 (= G121), Q144 (= Q143), T145 (= T144), G146 (= G145), W174 (= W173)
3t88A Crystal structure of escherichia coli menb in complex with substrate analogue, osb-ncoa (see paper)
63% identity, 98% coverage: 6:274/274 of query aligns to 10:281/281 of 3t88A
- active site: G82 (= G76), R87 (≠ K81), Y93 (= Y86), H101 (≠ R94), L105 (= L98), G129 (= G122), V132 (= V125), G152 (= G145), S157 (= S150), D159 (= D152), G160 (≠ A153), A246 (= A239), Y254 (= Y247)
- binding o-succinylbenzoyl-N-coenzyme A: Q39 (≠ R33), V40 (≠ Y34), R41 (= R35), A43 (= A37), S80 (= S74), G81 (= G75), G82 (= G76), D83 (= D77), Q84 (= Q78), K85 (≠ N79), Y93 (= Y86), V104 (= V97), L105 (= L98), Y125 (≠ F118), G129 (= G122), T151 (= T144), V155 (= V148), F158 (= F151), D159 (= D152), T250 (= T243), Y254 (= Y247), F266 (= F259), K269 (= K262)
4i42A E.Coli. 1,4-dihydroxy-2-naphthoyl coenzyme a synthase (ecmenb) in complex with 1-hydroxy-2-naphthoyl-coa (see paper)
63% identity, 98% coverage: 6:274/274 of query aligns to 14:285/285 of 4i42A
- active site: G86 (= G76), R91 (≠ K81), Y97 (= Y86), H105 (≠ R94), L109 (= L98), G133 (= G122), V136 (= V125), G156 (= G145), S161 (= S150), D163 (= D152), G164 (≠ A153), A250 (= A239), Y258 (= Y247)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (≠ Y34), R45 (= R35), S84 (= S74), G85 (= G75), G86 (= G76), D87 (= D77), Q88 (= Q78), K89 (≠ N79), Y97 (= Y86), V108 (= V97), Y129 (≠ F118), G133 (= G122), T155 (= T144), S161 (= S150), T254 (= T243), F270 (= F259), K273 (= K262)
P0ABU0 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Escherichia coli (strain K12) (see 4 papers)
63% identity, 98% coverage: 6:274/274 of query aligns to 14:285/285 of P0ABU0
- R45 (= R35) binding in other chain
- SGGDQK 84:89 (≠ SGGDQN 74:79) binding in other chain
- K89 (≠ N79) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- R91 (≠ K81) mutation to A: Loss of DHNA-CoA synthase activity.
- Y97 (= Y86) binding in other chain; mutation to F: Loss of DHNA-CoA synthase activity.
- YSIGG 129:133 (≠ FAIGG 118:122) binding in other chain
- Q154 (= Q143) 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 143:145) binding
- T155 (= T144) binding in other chain
- G156 (= G145) mutation to D: Loss of DHNA-CoA synthase activity.
- S161 (= S150) binding in other chain
- W184 (= W173) mutation to F: Reduces the specific DHNA-CoA synthase activity by 530-fold, whereas its affinity for hydrogencarbonate is reduced by 20-fold.
- Y258 (= Y247) binding
- R267 (≠ K256) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- F270 (= F259) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- K273 (= K262) 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)
63% identity, 98% coverage: 6:274/274 of query aligns to 14:285/285 of Q7CQ56
4elwA Structure of e. Coli. 1,4-dihydroxy-2- naphthoyl coenzyme a synthases (menb) in complex with nitrate (see paper)
61% identity, 98% coverage: 6:274/274 of query aligns to 11:267/267 of 4elwA
- active site: G83 (= G76), L91 (= L98), G115 (= G122), V118 (= V125), G138 (= G145), S143 (= S150), D145 (= D152), G146 (≠ A153), A232 (= A239), Y240 (= Y247)
- binding nitrate ion: G114 (= G121), T137 (= T144), G138 (= G145), F144 (= F151), W166 (= W173)
4elxA Structure of apo e.Coli. 1,4-dihydroxy-2- naphthoyl coa synthases with cl (see paper)
61% identity, 98% coverage: 6:274/274 of query aligns to 11:268/268 of 4elxA
- active site: G83 (= G76), H88 (≠ R94), L92 (= L98), G116 (= G122), V119 (= V125), G139 (= G145), S144 (= S150), D146 (= D152), G147 (≠ A153), A233 (= A239), Y241 (= Y247)
- binding chloride ion: G115 (= G121), G139 (= G145), W167 (= W173)
3h02A 2.15 angstrom resolution crystal structure of naphthoate synthase from salmonella typhimurium.
60% identity, 98% coverage: 6:274/274 of query aligns to 10:266/266 of 3h02A
- active site: G82 (= G76), H86 (≠ R94), L90 (= L98), G114 (= G122), V117 (= V125), G137 (= G145), S142 (= S150), D144 (= D152), G145 (≠ A153), A231 (= A239), Y239 (= Y247)
- binding bicarbonate ion: G113 (= G121), Q135 (= Q143), G137 (= G145), W165 (= W173)
4emlA Synechocystis sp. Pcc 6803 1,4-dihydroxy-2-naphthoyl-coenzyme a synthase (menb) in complex with bicarbonate (see paper)
59% identity, 98% coverage: 6:274/274 of query aligns to 2:261/261 of 4emlA
- active site: G77 (= G76), R81 (= R94), L85 (= L98), G109 (= G122), V112 (= V125), G132 (= G145), S137 (= S150), D139 (= D152), G140 (≠ A153), A226 (= A239), Y234 (= Y247)
- binding bicarbonate ion: G108 (= G121), Q130 (= Q143), G132 (= G145), W160 (= W173)
- binding chloride ion: D184 (≠ E197), R185 (≠ Q198), E187 (= E200), E188 (≠ D201)
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)
56% identity, 96% coverage: 11:274/274 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)
45% identity, 98% coverage: 5:273/274 of query aligns to 23:313/314 of P9WNP5
- R58 (= R35) binding in other chain
- K95 (vs. gap) binding in other chain
- SGGDQ 103:107 (= SGGDQ 74:78) binding in other chain
- R133 (= R94) mutation to A: Loss of DHNA-CoA synthase activity.
- WAAGG 157:161 (≠ FAIGG 118:122) binding in other chain
- T184 (= T144) binding in other chain
- D185 (≠ G145) mutation to E: Nearly abolishes DHNA-CoA synthase activity.; mutation D->G,N: Loss of DHNA-CoA synthase activity.
- S190 (= S150) mutation to A: Reduces affinity for substrate. Nearly abolishes DHNA-CoA synthase activity.
- D192 (= D152) mutation to N: Loss of DHNA-CoA synthase activity.
- Y287 (= Y247) 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)
45% identity, 98% coverage: 5:273/274 of query aligns to 10:300/301 of 4qijA
- active site: G92 (= G76), R97 (≠ K81), Y102 (= Y86), R117 (vs. gap), H122 (≠ S96), G148 (= G122), S151 (≠ V125), D172 (≠ G145), S177 (= S150), D179 (= D152), G180 (≠ A153), A266 (= A239), Y274 (= Y247)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (≠ Y34), R45 (= R35), A47 (= A37), F48 (= F38), K82 (vs. gap), S90 (= S74), G91 (= G75), G92 (= G76), D93 (= D77), Q94 (= Q78), Y102 (= Y86), L121 (= L95), I123 (≠ V97), W144 (≠ F118), G148 (= G122), T171 (= T144), D172 (≠ G145), S177 (= S150), F286 (= F259), K289 (= K262)
4qiiB Crystal structure of type ii menb from mycobacteria tuberculosis (see paper)
45% identity, 98% coverage: 5:273/274 of query aligns to 10:300/301 of 4qiiB
- active site: G92 (= G76), R97 (≠ K81), Y102 (= Y86), R117 (vs. gap), H122 (≠ S96), G148 (= G122), S151 (≠ V125), D172 (≠ G145), S177 (= S150), D179 (= D152), G180 (≠ A153), A266 (= A239), Y274 (= Y247)
- binding Salicylyl CoA: V44 (≠ Y34), R45 (= R35), A47 (= A37), K82 (vs. gap), S90 (= S74), G92 (= G76), D93 (= D77), Q94 (= Q78), Y102 (= Y86), W144 (≠ F118), G147 (= G121), G148 (= G122), T171 (= T144), D172 (≠ G145), V175 (= V148), S177 (= S150), Y274 (= Y247), F286 (= F259), K289 (= K262)
1q51B Crystal structure of mycobacterium tuberculosis menb in complex with acetoacetyl-coenzyme a, a key enzyme in vitamin k2 biosynthesis (see paper)
46% identity, 98% coverage: 5:273/274 of query aligns to 6:279/280 of 1q51B
- active site: G88 (= G76), H101 (≠ S96), G127 (= G122), S130 (≠ V125), D151 (≠ G145), S156 (= S150), D158 (= D152), G159 (≠ A153), A245 (= A239), Y253 (= Y247)
- binding acetoacetyl-coenzyme a: V40 (≠ Y34), R41 (= R35), A43 (= A37), S86 (= S74), G88 (= G76), D89 (= D77), Q90 (= Q78), W123 (≠ F118), G126 (= G121), G127 (= G122), T150 (= T144)
1q51A Crystal structure of mycobacterium tuberculosis menb in complex with acetoacetyl-coenzyme a, a key enzyme in vitamin k2 biosynthesis (see paper)
44% identity, 98% coverage: 5:273/274 of query aligns to 6:270/271 of 1q51A
- active site: G88 (= G76), H92 (≠ S96), G118 (= G122), S121 (≠ V125), D142 (≠ G145), S147 (= S150), D149 (= D152), G150 (≠ A153), A236 (= A239), Y244 (= Y247)
- binding acetoacetyl-coenzyme a: V40 (≠ Y34), R41 (= R35), K78 (vs. gap), S86 (= S74), G88 (= G76), D89 (= D77), Q90 (= Q78), W114 (≠ F118), G117 (= G121), G118 (= G122), T141 (= T144)
1rjnB The crystal structure of menb (rv0548c) from mycobacterium tuberculosis in complex with the coa portion of naphthoyl coa (see paper)
44% identity, 98% coverage: 5:273/274 of query aligns to 10:274/275 of 1rjnB
- active site: G92 (= G76), H96 (≠ S96), G122 (= G122), S125 (≠ V125), D146 (≠ G145), S151 (= S150), D153 (= D152), G154 (≠ A153), A240 (= A239)
- binding coenzyme a: V44 (≠ Y34), R45 (= R35), K82 (vs. gap), S90 (= S74), G92 (= G76), D93 (= D77), Q94 (= Q78), W118 (≠ F118)
- binding 3-[4-(2-hydroxyethyl)piperazin-1-yl]propane-1-sulfonic acid: R163 (= R162), Q164 (≠ V163), V165 (= V164), M188 (= M187)
3t8aB Crystal structure of mycobacterium tuberculosis menb in complex with substrate analogue, osb-ncoa (see paper)
44% identity, 98% coverage: 5:273/274 of query aligns to 9:273/274 of 3t8aB
- active site: G91 (= G76), H97 (≠ S96), G123 (= G122), S126 (≠ V125), D147 (≠ G145), S152 (= S150), D154 (= D152), G155 (≠ A153), A241 (= A239), Y249 (= Y247)
- binding o-succinylbenzoyl-N-coenzyme A: V43 (≠ Y34), R44 (= R35), K81 (vs. gap), S89 (= S74), G91 (= G76), D92 (= D77), Q93 (= Q78), W119 (≠ F118)
Query Sequence
>354228 FitnessBrowser__Btheta:354228
MSTQREWTTIREYEDILFDYYNGIARITINRERYRNAFTPTTTAEMSDALRICREEADID
VIVITGAGDKAFCSGGDQNVKGRGGYIGKDGVPRLSVLDVQKQIRSIPKPVIAAVNGFAI
GGGHVLHVVCDLSIASENAIFGQTGPRVGSFDAGFGASYLARVVGQKKAREIWFLCRKYN
AQEALDMGLVNKVVPLEQLEDEYVQWAEEMMLLSPLALRMIKAGLNAELDGQAGIQELAG
DATLLYYLTDEAQEGKNAFLEKRKPNFKKYPKFP
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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