SitesBLAST
Comparing GFF4202 FitnessBrowser__Marino:GFF4202 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)
54% identity, 99% coverage: 3:260/260 of query aligns to 12:271/273 of Q5HH38
- R34 (≠ Y25) binding in other chain
- SGGDQ 73:77 (≠ TGGDQ 64:68) binding in other chain
- S149 (= S138) binding in other chain
4i52A Scmenb im complex with 1-hydroxy-2-naphthoyl-coa (see paper)
57% identity, 98% coverage: 3:258/260 of query aligns to 9:271/275 of 4i52A
- active site: G77 (= G66), R82 (≠ H71), Y87 (= Y75), R95 (≠ G82), L99 (≠ E86), G123 (= G110), V126 (= V113), G146 (= G133), S151 (= S138), D153 (= D140), G154 (≠ P141), A240 (≠ G227), Y248 (= Y235)
- binding 1-hydroxy-2-naphthoyl-CoA: H29 (≠ D23), K30 (≠ R24), R31 (≠ Y25), A33 (= A27), S75 (≠ T64), G76 (= G65), G77 (= G66), D78 (= D67), Q79 (= Q68), L96 (= L83), V98 (= V85), Y119 (≠ F106), I121 (= I108), G123 (= G110), T145 (≠ V132), V149 (= V136), S151 (= S138), F152 (≠ V139)
4i4zA Synechocystis sp. Pcc 6803 1,4-dihydroxy-2-naphthoyl-coenzyme a synthase (menb) in complex with salicylyl-coa (see paper)
57% identity, 98% coverage: 3:258/260 of query aligns to 9:271/275 of 4i4zA
- active site: G77 (= G66), R82 (≠ H71), Y87 (= Y75), R95 (≠ G82), L99 (≠ E86), G123 (= G110), V126 (= V113), G146 (= G133), S151 (= S138), D153 (= D140), G154 (≠ P141), A240 (≠ G227), Y248 (= Y235)
- binding Salicylyl CoA: H29 (≠ D23), K30 (≠ R24), R31 (≠ Y25), S75 (≠ T64), G76 (= G65), G77 (= G66), D78 (= D67), Q79 (= Q68), Y87 (= Y75), V98 (= V85), G123 (= G110), T145 (≠ V132), V149 (= V136), S151 (= S138), F260 (= F247), K263 (= K250)
- binding bicarbonate ion: G122 (= G109), Q144 (= Q131), T145 (≠ V132), G146 (= G133), W174 (= W161)
2uzfA Crystal structure of staphylococcus aureus 1,4-dihydroxy-2-naphthoyl coa synthase (menb) in complex with acetoacetyl coa (see paper)
53% identity, 99% coverage: 3:260/260 of query aligns to 7:258/260 of 2uzfA
- active site: G70 (= G66), R80 (≠ G82), L84 (≠ E86), G108 (= G110), V111 (= V113), T130 (≠ V132), G131 (= G133), S136 (= S138), D138 (= D140), A139 (≠ P141), A225 (≠ G227), Y233 (= Y235)
- binding acetoacetyl-coenzyme a: V28 (≠ R24), R29 (≠ Y25), S68 (≠ T64), G69 (= G65), G70 (= G66), D71 (= D67), Y104 (≠ F106), G108 (= G110)
3t88A Crystal structure of escherichia coli menb in complex with substrate analogue, osb-ncoa (see paper)
53% identity, 99% coverage: 3:260/260 of query aligns to 18:279/281 of 3t88A
- active site: G82 (= G66), R87 (vs. gap), Y93 (≠ Q74), H101 (≠ G82), L105 (≠ E86), G129 (= G110), V132 (= V113), G152 (= G133), S157 (= S138), D159 (= D140), G160 (≠ P141), A246 (≠ G227), Y254 (= Y235)
- binding o-succinylbenzoyl-N-coenzyme A: Q39 (≠ D23), V40 (≠ R24), R41 (≠ Y25), A43 (= A27), S80 (≠ T64), G81 (= G65), G82 (= G66), D83 (= D67), Q84 (= Q68), K85 (vs. gap), Y93 (≠ Q74), V104 (= V85), L105 (≠ E86), Y125 (≠ F106), G129 (= G110), T151 (≠ V132), V155 (= V136), F158 (≠ V139), D159 (= D140), T250 (≠ L231), Y254 (= Y235), F266 (= F247), K269 (= K250)
4i42A E.Coli. 1,4-dihydroxy-2-naphthoyl coenzyme a synthase (ecmenb) in complex with 1-hydroxy-2-naphthoyl-coa (see paper)
53% identity, 99% coverage: 3:260/260 of query aligns to 22:283/285 of 4i42A
- active site: G86 (= G66), R91 (vs. gap), Y97 (≠ Q74), H105 (≠ G82), L109 (≠ E86), G133 (= G110), V136 (= V113), G156 (= G133), S161 (= S138), D163 (= D140), G164 (≠ P141), A250 (≠ G227), Y258 (= Y235)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (≠ R24), R45 (≠ Y25), S84 (≠ T64), G85 (= G65), G86 (= G66), D87 (= D67), Q88 (= Q68), K89 (vs. gap), Y97 (≠ Q74), V108 (= V85), Y129 (≠ F106), G133 (= G110), T155 (≠ V132), S161 (= S138), T254 (≠ L231), F270 (= F247), K273 (= K250)
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, 99% coverage: 3:260/260 of query aligns to 22:283/285 of P0ABU0
- R45 (≠ Y25) binding in other chain
- SGGDQK 84:89 (≠ TGGDQ- 64:68) binding in other chain
- K89 (vs. gap) 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 (≠ Q74) binding in other chain; mutation to F: Loss of DHNA-CoA synthase activity.
- YSIGG 129:133 (≠ FAIGG 106:110) binding in other chain
- Q154 (= Q131) 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 131:133) binding
- T155 (≠ V132) binding in other chain
- G156 (= G133) mutation to D: Loss of DHNA-CoA synthase activity.
- S161 (= S138) binding in other chain
- W184 (= W161) mutation to F: Reduces the specific DHNA-CoA synthase activity by 530-fold, whereas its affinity for hydrogencarbonate is reduced by 20-fold.
- Y258 (= Y235) binding
- R267 (≠ V244) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- F270 (= F247) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- K273 (= K250) 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, 99% coverage: 3:260/260 of query aligns to 22:283/285 of Q7CQ56
4emlA Synechocystis sp. Pcc 6803 1,4-dihydroxy-2-naphthoyl-coenzyme a synthase (menb) in complex with bicarbonate (see paper)
56% identity, 98% coverage: 3:258/260 of query aligns to 9:257/261 of 4emlA
- active site: G77 (= G66), R81 (≠ A70), L85 (≠ E86), G109 (= G110), V112 (= V113), G132 (= G133), S137 (= S138), D139 (= D140), G140 (≠ P141), A226 (≠ G227), Y234 (= Y235)
- binding bicarbonate ion: G108 (= G109), Q130 (= Q131), G132 (= G133), W160 (= W161)
- binding chloride ion: D184 (≠ E185), R185 (≠ Q186), E187 (≠ D188), E188 (= E189)
4elxA Structure of apo e.Coli. 1,4-dihydroxy-2- naphthoyl coa synthases with cl (see paper)
52% identity, 99% coverage: 3:260/260 of query aligns to 19:266/268 of 4elxA
- active site: G83 (= G66), H88 (= H71), L92 (≠ E86), G116 (= G110), V119 (= V113), G139 (= G133), S144 (= S138), D146 (= D140), G147 (≠ P141), A233 (≠ G227), Y241 (= Y235)
- binding chloride ion: G115 (= G109), G139 (= G133), W167 (= W161)
4elwA Structure of e. Coli. 1,4-dihydroxy-2- naphthoyl coenzyme a synthases (menb) in complex with nitrate (see paper)
52% identity, 99% coverage: 3:260/260 of query aligns to 19:265/267 of 4elwA
- active site: G83 (= G66), L91 (≠ E86), G115 (= G110), V118 (= V113), G138 (= G133), S143 (= S138), D145 (= D140), G146 (≠ P141), A232 (≠ G227), Y240 (= Y235)
- binding nitrate ion: G114 (= G109), T137 (≠ V132), G138 (= G133), F144 (≠ V139), W166 (= W161)
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)
50% identity, 99% coverage: 3:260/260 of query aligns to 74:335/337 of Q8GYN9
Sites not aligning to the query:
- 20 H→V: Loss of peroxisomal targeting.
3h02A 2.15 angstrom resolution crystal structure of naphthoate synthase from salmonella typhimurium.
52% identity, 99% coverage: 3:260/260 of query aligns to 18:264/266 of 3h02A
- active site: G82 (= G66), H86 (≠ E72), L90 (≠ E86), G114 (= G110), V117 (= V113), G137 (= G133), S142 (= S138), D144 (= D140), G145 (≠ P141), A231 (≠ G227), Y239 (= Y235)
- binding bicarbonate ion: G113 (= G109), Q135 (= Q131), G137 (= G133), W165 (= W161)
1q51B 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: 5:259/260 of query aligns to 19:280/280 of 1q51B
- active site: G88 (= G66), H101 (≠ P84), G127 (= G110), S130 (≠ V113), D151 (≠ G133), S156 (= S138), D158 (= D140), G159 (≠ P141), A245 (≠ G227), Y253 (= Y235)
- binding acetoacetyl-coenzyme a: V40 (≠ R24), R41 (≠ Y25), A43 (= A27), S86 (≠ T64), G88 (= G66), D89 (= D67), Q90 (= Q68), W123 (≠ F106), G126 (= G109), G127 (= G110), T150 (≠ V132)
1q51A Crystal structure of mycobacterium tuberculosis menb in complex with acetoacetyl-coenzyme a, a key enzyme in vitamin k2 biosynthesis (see paper)
43% identity, 98% coverage: 5:259/260 of query aligns to 19:271/271 of 1q51A
- active site: G88 (= G66), H92 (≠ P84), G118 (= G110), S121 (≠ V113), D142 (≠ G133), S147 (= S138), D149 (= D140), G150 (≠ P141), A236 (≠ G227), Y244 (= Y235)
- binding acetoacetyl-coenzyme a: V40 (≠ R24), R41 (≠ Y25), K78 (vs. gap), S86 (≠ T64), G88 (= G66), D89 (= D67), Q90 (= Q68), W114 (≠ F106), G117 (= G109), G118 (= G110), T141 (≠ V132)
1rjnB The crystal structure of menb (rv0548c) from mycobacterium tuberculosis in complex with the coa portion of naphthoyl coa (see paper)
43% identity, 98% coverage: 5:259/260 of query aligns to 23:275/275 of 1rjnB
- active site: G92 (= G66), H96 (≠ G79), G122 (= G110), S125 (≠ V113), D146 (≠ G133), S151 (= S138), D153 (= D140), G154 (≠ P141), A240 (≠ G227)
- binding coenzyme a: V44 (≠ R24), R45 (≠ Y25), K82 (vs. gap), S90 (≠ T64), G92 (= G66), D93 (= D67), Q94 (= Q68), W118 (≠ F106)
- binding 3-[4-(2-hydroxyethyl)piperazin-1-yl]propane-1-sulfonic acid: R163 (= R150), Q164 (≠ V151), V165 (= V152), M188 (≠ W175)
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)
43% identity, 98% coverage: 5:259/260 of query aligns to 36:314/314 of P9WNP5
- R58 (≠ Y25) binding in other chain
- K95 (vs. gap) binding in other chain
- SGGDQ 103:107 (≠ TGGDQ 64:68) binding in other chain
- R133 (vs. gap) mutation to A: Loss of DHNA-CoA synthase activity.
- WAAGG 157:161 (≠ FAIGG 106:110) binding in other chain
- T184 (≠ V132) binding in other chain
- D185 (≠ G133) mutation to E: Nearly abolishes DHNA-CoA synthase activity.; mutation D->G,N: Loss of DHNA-CoA synthase activity.
- S190 (= S138) mutation to A: Reduces affinity for substrate. Nearly abolishes DHNA-CoA synthase activity.
- D192 (= D140) mutation to N: Loss of DHNA-CoA synthase activity.
- Y287 (= Y235) 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)
43% identity, 98% coverage: 5:259/260 of query aligns to 23:301/301 of 4qijA
- active site: G92 (= G66), R97 (vs. gap), Y102 (≠ G73), R117 (vs. gap), H122 (≠ P84), G148 (= G110), S151 (≠ V113), D172 (≠ G133), S177 (= S138), D179 (= D140), G180 (≠ P141), A266 (≠ G227), Y274 (= Y235)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (≠ R24), R45 (≠ Y25), A47 (= A27), F48 (= F28), K82 (vs. gap), S90 (≠ T64), G91 (= G65), G92 (= G66), D93 (= D67), Q94 (= Q68), Y102 (≠ G73), L121 (= L83), I123 (≠ V85), W144 (≠ F106), G148 (= G110), T171 (≠ V132), D172 (≠ G133), S177 (= S138), F286 (= F247), K289 (= K250)
4qiiB Crystal structure of type ii menb from mycobacteria tuberculosis (see paper)
43% identity, 98% coverage: 5:259/260 of query aligns to 23:301/301 of 4qiiB
- active site: G92 (= G66), R97 (vs. gap), Y102 (≠ G73), R117 (vs. gap), H122 (≠ P84), G148 (= G110), S151 (≠ V113), D172 (≠ G133), S177 (= S138), D179 (= D140), G180 (≠ P141), A266 (≠ G227), Y274 (= Y235)
- binding Salicylyl CoA: V44 (≠ R24), R45 (≠ Y25), A47 (= A27), K82 (vs. gap), S90 (≠ T64), G92 (= G66), D93 (= D67), Q94 (= Q68), Y102 (≠ G73), W144 (≠ F106), G147 (= G109), G148 (= G110), T171 (≠ V132), D172 (≠ G133), V175 (= V136), S177 (= S138), Y274 (= Y235), F286 (= F247), K289 (= K250)
3t8aB Crystal structure of mycobacterium tuberculosis menb in complex with substrate analogue, osb-ncoa (see paper)
43% identity, 98% coverage: 5:259/260 of query aligns to 22:274/274 of 3t8aB
- active site: G91 (= G66), H97 (≠ P84), G123 (= G110), S126 (≠ V113), D147 (≠ G133), S152 (= S138), D154 (= D140), G155 (≠ P141), A241 (≠ G227), Y249 (= Y235)
- binding o-succinylbenzoyl-N-coenzyme A: V43 (≠ R24), R44 (≠ Y25), K81 (vs. gap), S89 (≠ T64), G91 (= G66), D92 (= D67), Q93 (= Q68), W119 (≠ F106)
Query Sequence
>GFF4202 FitnessBrowser__Marino:GFF4202
MTYEDILYDENNGVATITINRPDRYNAFRGQTCMELLDAFNRAGWNKDIGVIVFTGAGEK
AFCTGGDQGAHEGQYDGRGLIGLPVEELQRTIREVPKPVIARVNGFAIGGGHVLHVICDL
SIASETAIFGQVGPKVGSVDPGFGTAYLARVVGEKRAREIWYLCRKYSAQQALEWGLVNA
VVPPEQLDEEVQKWCEEILEKSPTAISIAKRSFNADSDNIAGIGALGMQALSLYYDTDES
KEGVNAFLEKRKPEFRKYYK
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