SitesBLAST
Comparing WP_057509133.1 NCBI__GCF_001431535.1:WP_057509133.1 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)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
29% identity, 97% coverage: 3:256/262 of query aligns to 4:254/259 of 5zaiC
- active site: A65 (= A64), F70 (≠ M69), S82 (≠ R81), R86 (≠ A88), G110 (= G112), E113 (≠ G115), P132 (≠ T134), E133 (= E135), I138 (≠ L140), P140 (= P142), G141 (≠ A143), A226 (≠ R238), F236 (vs. gap)
- binding coenzyme a: K24 (≠ L23), L25 (≠ H24), A63 (= A62), G64 (= G63), A65 (= A64), D66 (= D65), I67 (≠ L66), P132 (≠ T134), R166 (≠ Q167), F248 (= F250), K251 (= K253)
Q5HH38 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Staphylococcus aureus (strain COL) (see paper)
32% identity, 98% coverage: 3:258/262 of query aligns to 13:266/273 of Q5HH38
- R34 (≠ H24) binding in other chain
- SGGD-Q 73:77 (≠ AGADLQ 62:67) binding in other chain
- S149 (≠ L140) 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)
31% identity, 98% coverage: 3:258/262 of query aligns to 8:253/260 of 2uzfA
- active site: G70 (≠ A64), R80 (= R81), L84 (= L85), G108 (= G112), V111 (≠ G115), T130 (= T134), G131 (≠ E135), S136 (≠ L140), D138 (≠ P142), A139 (= A143), A225 (≠ N230), Y233 (≠ R238)
- binding acetoacetyl-coenzyme a: V28 (≠ L23), R29 (≠ H24), S68 (≠ A62), G69 (= G63), G70 (≠ A64), D71 (= D65), Y104 (≠ S108), G108 (= G112)
Q7CQ56 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
30% identity, 97% coverage: 2:256/262 of query aligns to 23:276/285 of Q7CQ56
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
32% identity, 98% coverage: 3:258/262 of query aligns to 3:249/250 of 3q0gD
- active site: A64 (= A64), M69 (= M69), T75 (≠ A75), F79 (≠ E79), G103 (= G112), E106 (≠ G115), P125 (≠ T134), E126 (= E135), V131 (≠ L140), P133 (= P142), G134 (≠ A143), L219 (≠ Q228), F229 (≠ R238)
- binding Butyryl Coenzyme A: F225 (≠ I234), F241 (= F250)
4i52A Scmenb im complex with 1-hydroxy-2-naphthoyl-coa (see paper)
31% identity, 97% coverage: 3:256/262 of query aligns to 10:266/275 of 4i52A
- active site: G77 (≠ A64), R82 (= R70), Y87 (≠ A75), R95 (= R81), L99 (= L85), G123 (= G112), V126 (≠ G115), G146 (≠ E135), S151 (≠ L140), D153 (≠ P142), G154 (≠ A143), A240 (vs. gap), Y248 (≠ R236)
- binding 1-hydroxy-2-naphthoyl-CoA: H29 (≠ A22), K30 (≠ L23), R31 (≠ H24), A33 (= A26), S75 (≠ A62), G76 (= G63), G77 (≠ A64), D78 (= D65), Q79 (= Q67), L96 (≠ Q82), V98 (≠ A84), Y119 (≠ S108), I121 (≠ F110), G123 (= G112), T145 (= T134), V149 (≠ L138), S151 (≠ L140), F152 (≠ L141)
4i4zA Synechocystis sp. Pcc 6803 1,4-dihydroxy-2-naphthoyl-coenzyme a synthase (menb) in complex with salicylyl-coa (see paper)
31% identity, 97% coverage: 3:256/262 of query aligns to 10:266/275 of 4i4zA
- active site: G77 (≠ A64), R82 (= R70), Y87 (≠ A75), R95 (= R81), L99 (= L85), G123 (= G112), V126 (≠ G115), G146 (≠ E135), S151 (≠ L140), D153 (≠ P142), G154 (≠ A143), A240 (vs. gap), Y248 (≠ R236)
- binding Salicylyl CoA: H29 (≠ A22), K30 (≠ L23), R31 (≠ H24), S75 (≠ A62), G76 (= G63), G77 (≠ A64), D78 (= D65), Q79 (= Q67), Y87 (≠ A75), V98 (≠ A84), G123 (= G112), T145 (= T134), V149 (≠ L138), S151 (≠ L140), F260 (= F250), K263 (= K253)
- binding bicarbonate ion: G122 (= G111), Q144 (≠ L133), T145 (= T134), G146 (≠ E135), W174 (≠ F162)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
33% identity, 98% coverage: 3:258/262 of query aligns to 4:254/255 of 3q0jC
- active site: A65 (= A64), M70 (= M69), T80 (≠ A86), F84 (≠ M91), G108 (= G112), E111 (≠ G115), P130 (≠ T134), E131 (= E135), V136 (≠ L140), P138 (= P142), G139 (≠ A143), L224 (≠ Q228), F234 (≠ R238)
- binding acetoacetyl-coenzyme a: Q23 (≠ A22), A24 (≠ L23), L25 (≠ H24), A27 (= A26), A63 (= A62), G64 (= G63), A65 (= A64), D66 (= D65), I67 (≠ L66), K68 (≠ Q67), M70 (= M69), F84 (≠ M91), G107 (= G111), G108 (= G112), E111 (≠ G115), P130 (≠ T134), E131 (= E135), P138 (= P142), G139 (≠ A143), M140 (≠ V144)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
33% identity, 98% coverage: 3:258/262 of query aligns to 4:254/255 of 3q0gC
- active site: A65 (= A64), M70 (= M69), T80 (≠ A86), F84 (≠ M91), G108 (= G112), E111 (≠ G115), P130 (≠ T134), E131 (= E135), V136 (≠ L140), P138 (= P142), G139 (≠ A143), L224 (≠ Q228), F234 (≠ R238)
- binding coenzyme a: L25 (≠ H24), A63 (= A62), I67 (≠ L66), K68 (≠ Q67), Y104 (≠ S108), P130 (≠ T134), E131 (= E135), L134 (= L138)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
33% identity, 98% coverage: 3:258/262 of query aligns to 3:253/256 of 3h81A
- active site: A64 (= A64), M69 (= M69), T79 (≠ A86), F83 (≠ M91), G107 (= G112), E110 (≠ G115), P129 (≠ T134), E130 (= E135), V135 (≠ L140), P137 (= P142), G138 (≠ A143), L223 (≠ Q228), F233 (≠ R238)
- binding calcium ion: F233 (≠ R238), Q238 (≠ G243)
4emlA Synechocystis sp. Pcc 6803 1,4-dihydroxy-2-naphthoyl-coenzyme a synthase (menb) in complex with bicarbonate (see paper)
31% identity, 97% coverage: 3:256/262 of query aligns to 10:252/261 of 4emlA
- active site: G77 (≠ A64), R81 (= R81), L85 (= L85), G109 (= G112), V112 (≠ G115), G132 (≠ E135), S137 (≠ L140), D139 (≠ P142), G140 (≠ A143), A226 (vs. gap), Y234 (≠ R236)
- binding bicarbonate ion: G108 (= G111), Q130 (≠ L133), G132 (≠ E135), W160 (≠ F162)
- binding chloride ion: D184 (= D186), R185 (≠ Q187), E187 (≠ D189), E188 (≠ A190)
4i42A E.Coli. 1,4-dihydroxy-2-naphthoyl coenzyme a synthase (ecmenb) in complex with 1-hydroxy-2-naphthoyl-coa (see paper)
30% identity, 92% coverage: 16:256/262 of query aligns to 37:276/285 of 4i42A
- active site: G86 (≠ A64), R91 (= R70), Y97 (≠ S76), H105 (≠ A84), L109 (≠ A88), G133 (= G112), V136 (≠ G115), G156 (≠ E135), S161 (≠ L140), D163 (≠ P142), G164 (≠ A143), A250 (= A235), Y258 (≠ R238)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (≠ L23), R45 (≠ H24), S84 (≠ A62), G85 (= G63), G86 (≠ A64), D87 (= D65), Q88 (= Q67), K89 (≠ W68), Y97 (≠ S76), V108 (≠ L87), Y129 (≠ S108), G133 (= G112), T155 (= T134), S161 (≠ L140), T254 (vs. gap), F270 (= F250), K273 (= K253)
P0ABU0 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Escherichia coli (strain K12) (see 4 papers)
30% identity, 92% coverage: 16:256/262 of query aligns to 37:276/285 of P0ABU0
- R45 (≠ H24) binding in other chain
- SGGD-QK 84:89 (≠ AGADLQW 62:68) binding in other chain
- K89 (≠ W68) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- R91 (= R70) mutation to A: Loss of DHNA-CoA synthase activity.
- Y97 (≠ S76) binding in other chain; mutation to F: Loss of DHNA-CoA synthase activity.
- YSIGG 129:133 (≠ SAFGG 108:112) binding in other chain
- Q154 (≠ L133) 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 (≠ LTE 133:135) binding
- T155 (= T134) binding in other chain
- G156 (≠ E135) mutation to D: Loss of DHNA-CoA synthase activity.
- S161 (≠ L140) binding in other chain
- W184 (≠ F162) mutation to F: Reduces the specific DHNA-CoA synthase activity by 530-fold, whereas its affinity for hydrogencarbonate is reduced by 20-fold.
- Y258 (≠ R238) binding
- R267 (≠ L247) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- F270 (= F250) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- K273 (= K253) binding ; mutation to A: Impairs protein folding.
3t88A Crystal structure of escherichia coli menb in complex with substrate analogue, osb-ncoa (see paper)
30% identity, 92% coverage: 16:256/262 of query aligns to 33:272/281 of 3t88A
- active site: G82 (≠ A64), R87 (= R70), Y93 (≠ S76), H101 (≠ A84), L105 (≠ A88), G129 (= G112), V132 (≠ G115), G152 (≠ E135), S157 (≠ L140), D159 (≠ P142), G160 (≠ A143), A246 (= A235), Y254 (≠ R238)
- binding o-succinylbenzoyl-N-coenzyme A: Q39 (≠ A22), V40 (≠ L23), R41 (≠ H24), A43 (= A26), S80 (≠ A62), G81 (= G63), G82 (≠ A64), D83 (= D65), Q84 (= Q67), K85 (≠ W68), Y93 (≠ S76), V104 (≠ L87), L105 (≠ A88), Y125 (≠ S108), G129 (= G112), T151 (= T134), V155 (≠ L138), F158 (≠ L141), D159 (≠ P142), T250 (vs. gap), Y254 (≠ R238), F266 (= F250), K269 (= K253)
O69762 Hydroxycinnamoyl-CoA hydratase-lyase; HCHL; P-hydroxycinnamoyl CoA hydratase/lyase; Trans-feruloyl-CoA hydratase/vanillin synthase; EC 4.1.2.61 from Pseudomonas fluorescens (see 2 papers)
30% identity, 92% coverage: 18:257/262 of query aligns to 24:270/276 of O69762
- K29 (≠ L23) binding
- A68 (= A62) binding
- M70 (≠ A64) binding
- L72 (= L66) binding
- Y75 (≠ W68) binding
- G120 (= G112) binding
- S123 (≠ G115) mutation to A: Reduced kcat compared to wild-type but not markerdly.
- S142 (≠ T134) binding
- E143 (= E135) mutation to A: Abolishes catalytic activity.
- W146 (≠ L138) binding
- G151 (≠ A143) binding
- Y239 (≠ N230) binding ; mutation to F: Increased KM for feruloyl-CoA but retains a significant amount of catalytic activity with a kcat 10 times less than that of the wild-type.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
31% identity, 97% coverage: 6:258/262 of query aligns to 11:263/266 of O53561
- K135 (≠ R130) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 130:137, 38% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (≠ R137) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
3h02A 2.15 angstrom resolution crystal structure of naphthoate synthase from salmonella typhimurium.
30% identity, 97% coverage: 2:256/262 of query aligns to 19:257/266 of 3h02A
- active site: G82 (≠ A64), H86 (≠ R81), L90 (= L85), G114 (= G112), V117 (≠ G115), G137 (≠ E135), S142 (≠ L140), D144 (≠ P142), G145 (≠ A143), A231 (= A235), Y239 (≠ R238)
- binding bicarbonate ion: G113 (= G111), Q135 (≠ L133), G137 (≠ E135), W165 (≠ F162)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
29% identity, 98% coverage: 3:260/262 of query aligns to 4:259/260 of 2hw5C
- active site: A68 (= A64), M73 (= M69), S83 (≠ A86), L87 (≠ M91), G111 (= G112), E114 (≠ G115), P133 (≠ T134), E134 (= E135), T139 (≠ L140), P141 (= P142), G142 (vs. gap), K227 (≠ Q228), F237 (≠ R238)
- binding crotonyl coenzyme a: K26 (≠ A22), A27 (≠ L23), L28 (≠ H24), A30 (= A26), K62 (≠ A58), I70 (≠ L66), F109 (= F110)
6l3pA Crystal strcuture of feruloyl-coa hydratase lyase(fchl) complexed with coa
31% identity, 79% coverage: 4:211/262 of query aligns to 9:214/244 of 6l3pA
- active site: M69 (≠ A64), Y74 (≠ M69), R86 (= R81), Q90 (≠ L85), G114 (= G112), S117 (≠ G115), S136 (≠ T134), E137 (= E135), I142 (≠ L140), P144 (= P142), G145 (≠ A143)
- binding coenzyme a: K28 (≠ L23), R29 (≠ H24), A31 (= A26), A67 (= A62), M69 (≠ A64), D70 (= D65), L71 (= L66), G113 (= G111)
Sites not aligning to the query:
2vssB Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
33% identity, 74% coverage: 18:211/262 of query aligns to 21:217/247 of 2vssB
- active site: M67 (≠ A64), Y72 (≠ W68), D77 (≠ A73), R89 (= R81), Q93 (≠ L85), G117 (= G112), S120 (≠ G115), S139 (≠ T134), E140 (= E135), I145 (≠ L140), P147 (= P142), G148 (≠ A143)
- binding acetyl coenzyme *a: E25 (≠ A22), K26 (≠ L23), R27 (≠ H24), A29 (= A26), A65 (= A62), M67 (≠ A64), D68 (= D65), W113 (≠ S108), F115 (= F110), G117 (= G112), S139 (≠ T134), E140 (= E135)
Sites not aligning to the query:
Query Sequence
>WP_057509133.1 NCBI__GCF_001431535.1:WP_057509133.1
MTDSLLVERSGALLTLRLHRPALHNAFDDGLIAELTHALDQAGRDPSVRAVVLAGEGASF
SAGADLQWMRGMAAASESENRQDALALARLMRTLDELPKPTLARVHGSAFGGGVGLVACC
DIAIAADSARFGLTESRLGLLPAVISPYVIAAIGTRQARRWFATGEQFDAATALRIGLVH
AVVADDQLDAAVEQQLALLMAAGPVAAASAKALVRQVVVSHDPDARDQANAELIARLRVS
AEGQEGLGAFLGKRRPGWIDAG
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