SitesBLAST
Comparing Synpcc7942_0597 Synpcc7942_0597 naphthoate synthase 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)
80% identity, 99% coverage: 4:279/279 of query aligns to 1:275/275 of 4i52A
- active site: G77 (= G81), R82 (= R86), Y87 (= Y91), R95 (= R99), L99 (= L103), G123 (= G127), V126 (= V130), G146 (= G150), S151 (= S155), D153 (= D157), G154 (= G158), A240 (= A244), Y248 (= Y252)
- binding 1-hydroxy-2-naphthoyl-CoA: H29 (= H33), K30 (= K34), R31 (= R35), A33 (= A37), S75 (≠ A79), G76 (= G80), G77 (= G81), D78 (= D82), Q79 (= Q83), L96 (= L100), V98 (= V102), Y119 (= Y123), I121 (= I125), G123 (= G127), T145 (= T149), V149 (= V153), S151 (= S155), F152 (= F156)
4i4zA Synechocystis sp. Pcc 6803 1,4-dihydroxy-2-naphthoyl-coenzyme a synthase (menb) in complex with salicylyl-coa (see paper)
80% identity, 99% coverage: 4:279/279 of query aligns to 1:275/275 of 4i4zA
- active site: G77 (= G81), R82 (= R86), Y87 (= Y91), R95 (= R99), L99 (= L103), G123 (= G127), V126 (= V130), G146 (= G150), S151 (= S155), D153 (= D157), G154 (= G158), A240 (= A244), Y248 (= Y252)
- binding Salicylyl CoA: H29 (= H33), K30 (= K34), R31 (= R35), S75 (≠ A79), G76 (= G80), G77 (= G81), D78 (= D82), Q79 (= Q83), Y87 (= Y91), V98 (= V102), G123 (= G127), T145 (= T149), V149 (= V153), S151 (= S155), F260 (= F264), K263 (= K267)
- binding bicarbonate ion: G122 (= G126), Q144 (= Q148), T145 (= T149), G146 (= G150), W174 (= W178)
4emlA Synechocystis sp. Pcc 6803 1,4-dihydroxy-2-naphthoyl-coenzyme a synthase (menb) in complex with bicarbonate (see paper)
76% identity, 99% coverage: 4:279/279 of query aligns to 1:261/261 of 4emlA
- active site: G77 (= G81), R81 (= R99), L85 (= L103), G109 (= G127), V112 (= V130), G132 (= G150), S137 (= S155), D139 (= D157), G140 (= G158), A226 (= A244), Y234 (= Y252)
- binding bicarbonate ion: G108 (= G126), Q130 (= Q148), G132 (= G150), W160 (= W178)
- binding chloride ion: D184 (≠ E202), R185 (≠ E203), E187 (= E205), E188 (≠ A206)
3t88A Crystal structure of escherichia coli menb in complex with substrate analogue, osb-ncoa (see paper)
68% identity, 100% coverage: 2:279/279 of query aligns to 7:281/281 of 3t88A
- active site: G82 (= G81), R87 (= R86), Y93 (= Y91), H101 (≠ R99), L105 (= L103), G129 (= G127), V132 (= V130), G152 (= G150), S157 (= S155), D159 (= D157), G160 (= G158), A246 (= A244), Y254 (= Y252)
- binding o-succinylbenzoyl-N-coenzyme A: Q39 (≠ H33), V40 (≠ K34), R41 (= R35), A43 (= A37), S80 (≠ A79), G81 (= G80), G82 (= G81), D83 (= D82), Q84 (= Q83), K85 (≠ S84), Y93 (= Y91), V104 (= V102), L105 (= L103), Y125 (= Y123), G129 (= G127), T151 (= T149), V155 (= V153), F158 (= F156), D159 (= D157), T250 (= T248), Y254 (= Y252), F266 (= F264), K269 (= K267)
4i42A E.Coli. 1,4-dihydroxy-2-naphthoyl coenzyme a synthase (ecmenb) in complex with 1-hydroxy-2-naphthoyl-coa (see paper)
68% identity, 100% coverage: 2:279/279 of query aligns to 11:285/285 of 4i42A
- active site: G86 (= G81), R91 (= R86), Y97 (= Y91), H105 (≠ R99), L109 (= L103), G133 (= G127), V136 (= V130), G156 (= G150), S161 (= S155), D163 (= D157), G164 (= G158), A250 (= A244), Y258 (= Y252)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (≠ K34), R45 (= R35), S84 (≠ A79), G85 (= G80), G86 (= G81), D87 (= D82), Q88 (= Q83), K89 (≠ S84), Y97 (= Y91), V108 (= V102), Y129 (= Y123), G133 (= G127), T155 (= T149), S161 (= S155), T254 (= T248), F270 (= F264), K273 (= K267)
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, 100% coverage: 2:279/279 of query aligns to 11:285/285 of P0ABU0
- R45 (= R35) binding in other chain
- SGGDQK 84:89 (≠ AGGDQS 79:84) binding in other chain
- K89 (≠ S84) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- R91 (= R86) mutation to A: Loss of DHNA-CoA synthase activity.
- Y97 (= Y91) binding in other chain; mutation to F: Loss of DHNA-CoA synthase activity.
- YSIGG 129:133 (≠ YAIGG 123:127) binding in other chain
- Q154 (= Q148) 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 148:150) binding
- T155 (= T149) binding in other chain
- G156 (= G150) mutation to D: Loss of DHNA-CoA synthase activity.
- S161 (= S155) binding in other chain
- W184 (= W178) mutation to F: Reduces the specific DHNA-CoA synthase activity by 530-fold, whereas its affinity for hydrogencarbonate is reduced by 20-fold.
- Y258 (= Y252) binding
- R267 (≠ K261) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- F270 (= F264) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- K273 (= K267) 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)
66% identity, 100% coverage: 2:279/279 of query aligns to 11:285/285 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: 5:279/279 of query aligns to 5:273/273 of Q5HH38
- R34 (= R35) binding in other chain
- SGGDQ 73:77 (≠ AGGDQ 79:83) binding in other chain
- S149 (= S155) 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, 100% coverage: 2:279/279 of query aligns to 8:267/267 of 4elwA
- active site: G83 (= G81), L91 (= L103), G115 (= G127), V118 (= V130), G138 (= G150), S143 (= S155), D145 (= D157), G146 (= G158), A232 (= A244), Y240 (= Y252)
- binding nitrate ion: G114 (= G126), T137 (= T149), G138 (= G150), F144 (= F156), W166 (= W178)
4elxA Structure of apo e.Coli. 1,4-dihydroxy-2- naphthoyl coa synthases with cl (see paper)
65% identity, 100% coverage: 2:279/279 of query aligns to 8:268/268 of 4elxA
- active site: G83 (= G81), H88 (≠ R99), L92 (= L103), G116 (= G127), V119 (= V130), G139 (= G150), S144 (= S155), D146 (= D157), G147 (= G158), A233 (= A244), Y241 (= Y252)
- binding chloride ion: G115 (= G126), G139 (= G150), W167 (= W178)
3h02A 2.15 angstrom resolution crystal structure of naphthoate synthase from salmonella typhimurium.
64% identity, 100% coverage: 2:279/279 of query aligns to 7:266/266 of 3h02A
- active site: G82 (= G81), H86 (≠ R99), L90 (= L103), G114 (= G127), V117 (= V130), G137 (= G150), S142 (= S155), D144 (= D157), G145 (= G158), A231 (= A244), Y239 (= Y252)
- binding bicarbonate ion: G113 (= G126), Q135 (= Q148), G137 (= G150), W165 (= W178)
2uzfA Crystal structure of staphylococcus aureus 1,4-dihydroxy-2-naphthoyl coa synthase (menb) in complex with acetoacetyl coa (see paper)
63% identity, 98% coverage: 6:279/279 of query aligns to 1:260/260 of 2uzfA
- active site: G70 (= G81), R80 (= R99), L84 (= L103), G108 (= G127), V111 (= V130), T130 (= T149), G131 (= G150), S136 (= S155), D138 (= D157), A139 (≠ G158), A225 (= A244), Y233 (= Y252)
- binding acetoacetyl-coenzyme a: V28 (≠ K34), R29 (= R35), S68 (≠ A79), G69 (= G80), G70 (= G81), D71 (= D82), Y104 (= Y123), G108 (= G127)
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: 10:279/279 of query aligns to 72:337/337 of Q8GYN9
Sites not aligning to the query:
- 20 H→V: Loss of peroxisomal targeting.
4qijA Crystal structure of menb from mycobacteria tuberculosis in complex with 1-hna-coa (see paper)
50% identity, 97% coverage: 6:276/279 of query aligns to 12:298/301 of 4qijA
- active site: G92 (= G81), R97 (= R86), Y102 (= Y91), R117 (≠ G96), H122 (≠ N101), G148 (= G127), S151 (≠ V130), D172 (≠ G150), S177 (= S155), D179 (= D157), G180 (= G158), A266 (= A244), Y274 (= Y252)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (≠ K34), R45 (= R35), A47 (= A37), F48 (= F38), K82 (≠ T71), S90 (≠ A79), G91 (= G80), G92 (= G81), D93 (= D82), Q94 (= Q83), Y102 (= Y91), L121 (= L100), I123 (≠ V102), W144 (≠ Y123), G148 (= G127), T171 (= T149), D172 (≠ G150), S177 (= S155), F286 (= F264), K289 (= K267)
4qiiB Crystal structure of type ii menb from mycobacteria tuberculosis (see paper)
50% identity, 97% coverage: 6:276/279 of query aligns to 12:298/301 of 4qiiB
- active site: G92 (= G81), R97 (= R86), Y102 (= Y91), R117 (≠ G96), H122 (≠ N101), G148 (= G127), S151 (≠ V130), D172 (≠ G150), S177 (= S155), D179 (= D157), G180 (= G158), A266 (= A244), Y274 (= Y252)
- binding Salicylyl CoA: V44 (≠ K34), R45 (= R35), A47 (= A37), K82 (≠ T71), S90 (≠ A79), G92 (= G81), D93 (= D82), Q94 (= Q83), Y102 (= Y91), W144 (≠ Y123), G147 (= G126), G148 (= G127), T171 (= T149), D172 (≠ G150), V175 (= V153), S177 (= S155), Y274 (= Y252), F286 (= F264), K289 (= K267)
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, 97% coverage: 6:276/279 of query aligns to 25:311/314 of P9WNP5
- R58 (= R35) binding in other chain
- K95 (≠ T71) binding in other chain
- SGGDQ 103:107 (≠ AGGDQ 79:83) binding in other chain
- R133 (= R99) mutation to A: Loss of DHNA-CoA synthase activity.
- WAAGG 157:161 (≠ YAIGG 123:127) binding in other chain
- T184 (= T149) binding in other chain
- D185 (≠ G150) mutation to E: Nearly abolishes DHNA-CoA synthase activity.; mutation D->G,N: Loss of DHNA-CoA synthase activity.
- S190 (= S155) mutation to A: Reduces affinity for substrate. Nearly abolishes DHNA-CoA synthase activity.
- D192 (= D157) mutation to N: Loss of DHNA-CoA synthase activity.
- Y287 (= Y252) mutation to F: Loss of DHNA-CoA synthase activity.
1q51B Crystal structure of mycobacterium tuberculosis menb in complex with acetoacetyl-coenzyme a, a key enzyme in vitamin k2 biosynthesis (see paper)
51% identity, 97% coverage: 6:276/279 of query aligns to 8:277/280 of 1q51B
- active site: G88 (= G81), H101 (≠ N101), G127 (= G127), S130 (≠ V130), D151 (≠ G150), S156 (= S155), D158 (= D157), G159 (= G158), A245 (= A244), Y253 (= Y252)
- binding acetoacetyl-coenzyme a: V40 (≠ K34), R41 (= R35), A43 (= A37), S86 (≠ A79), G88 (= G81), D89 (= D82), Q90 (= Q83), W123 (≠ Y123), G126 (= G126), G127 (= G127), T150 (= T149)
1q51A Crystal structure of mycobacterium tuberculosis menb in complex with acetoacetyl-coenzyme a, a key enzyme in vitamin k2 biosynthesis (see paper)
50% identity, 97% coverage: 6:276/279 of query aligns to 8:268/271 of 1q51A
- active site: G88 (= G81), H92 (≠ N101), G118 (= G127), S121 (≠ V130), D142 (≠ G150), S147 (= S155), D149 (= D157), G150 (= G158), A236 (= A244), Y244 (= Y252)
- binding acetoacetyl-coenzyme a: V40 (≠ K34), R41 (= R35), K78 (≠ T71), S86 (≠ A79), G88 (= G81), D89 (= D82), Q90 (= Q83), W114 (≠ Y123), G117 (= G126), G118 (= G127), T141 (= T149)
1rjnB The crystal structure of menb (rv0548c) from mycobacterium tuberculosis in complex with the coa portion of naphthoyl coa (see paper)
49% identity, 97% coverage: 6:276/279 of query aligns to 12:272/275 of 1rjnB
- active site: G92 (= G81), H96 (≠ N101), G122 (= G127), S125 (≠ V130), D146 (≠ G150), S151 (= S155), D153 (= D157), G154 (= G158), A240 (= A244)
- binding coenzyme a: V44 (≠ K34), R45 (= R35), K82 (≠ T71), S90 (≠ A79), G92 (= G81), D93 (= D82), Q94 (= Q83), W118 (≠ Y123)
- binding 3-[4-(2-hydroxyethyl)piperazin-1-yl]propane-1-sulfonic acid: R163 (= R167), Q164 (≠ L168), V165 (= V169), M188 (= M192)
3t8aB Crystal structure of mycobacterium tuberculosis menb in complex with substrate analogue, osb-ncoa (see paper)
50% identity, 97% coverage: 6:276/279 of query aligns to 11:271/274 of 3t8aB
- active site: G91 (= G81), H97 (≠ N101), G123 (= G127), S126 (≠ V130), D147 (≠ G150), S152 (= S155), D154 (= D157), G155 (= G158), A241 (= A244), Y249 (= Y252)
- binding o-succinylbenzoyl-N-coenzyme A: V43 (≠ K34), R44 (= R35), K81 (≠ T71), S89 (≠ A79), G91 (= G81), D92 (= D82), Q93 (= Q83), W119 (≠ Y123)
Query Sequence
>Synpcc7942_0597 Synpcc7942_0597 naphthoate synthase
VAQVQWQSVREYEDIRYEKCAEGIAKITINRPHKRNAFRPKTVVELYDAFCDAREDIAIG
VILLTGAGPHTDGRYAFCAGGDQSVRGAGGYIDEEGLPRLNVLDLQRLIRTIPKVVIALV
AGYAIGGGHVLHILCDLTIAADNAVFGQTGPKVGSFDGGFGASYLARLVGQKKAREIWFL
CRQYGAKEALQMGLVNTVVPVEELEAEGIRWALEILEKSPIAIRCLKAAFNAELDGMAGI
QELAGHATHLYYLTEEGSEGKQAFLEKRSPDFRQYPWLP
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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