SitesBLAST
Comparing AZOBR_RS22290 FitnessBrowser__azobra:AZOBR_RS22290 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)
30% identity, 94% coverage: 15:263/264 of query aligns to 12:257/259 of 5zaiC
- active site: A65 (= A68), F70 (≠ M73), S82 (≠ A88), R86 (≠ A92), G110 (= G116), E113 (≠ G119), P132 (≠ T138), E133 (= E139), I138 (≠ L144), P140 (= P146), G141 (≠ A147), A226 (≠ V231), F236 (≠ R242)
- binding coenzyme a: K24 (≠ V27), L25 (≠ H28), A63 (= A66), G64 (= G67), A65 (= A68), D66 (= D69), I67 (≠ L70), P132 (≠ T138), R166 (= R171), F248 (= F254), K251 (= K257)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
33% identity, 93% coverage: 17:262/264 of query aligns to 13:249/250 of 3q0gD
- active site: A64 (= A68), M69 (= M76), T75 (≠ G82), F79 (≠ E86), G103 (= G116), E106 (≠ G119), P125 (≠ T138), E126 (= E139), V131 (≠ L144), P133 (= P146), G134 (≠ A147), L219 (≠ V231), F229 (vs. gap)
- binding Butyryl Coenzyme A: F225 (≠ A239), F241 (= F254)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
33% identity, 93% coverage: 17:262/264 of query aligns to 14:254/255 of 3q0jC
- active site: A65 (= A68), M70 (= M76), T80 (≠ E86), F84 (≠ L91), G108 (= G116), E111 (≠ G119), P130 (≠ T138), E131 (= E139), V136 (≠ L144), P138 (= P146), G139 (≠ A147), L224 (≠ V231), F234 (vs. gap)
- binding acetoacetyl-coenzyme a: Q23 (≠ E26), A24 (≠ V27), L25 (≠ H28), A27 (= A30), A63 (= A66), G64 (= G67), A65 (= A68), D66 (= D69), I67 (≠ L70), K68 (= K74), M70 (= M76), F84 (≠ L91), G107 (= G115), G108 (= G116), E111 (≠ G119), P130 (≠ T138), E131 (= E139), P138 (= P146), G139 (≠ A147), M140 (≠ V148)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
33% identity, 93% coverage: 17:262/264 of query aligns to 14:254/255 of 3q0gC
- active site: A65 (= A68), M70 (= M76), T80 (≠ E86), F84 (≠ L91), G108 (= G116), E111 (≠ G119), P130 (≠ T138), E131 (= E139), V136 (≠ L144), P138 (= P146), G139 (≠ A147), L224 (≠ V231), F234 (vs. gap)
- binding coenzyme a: L25 (≠ H28), A63 (= A66), I67 (≠ L70), K68 (= K74), Y104 (≠ P112), P130 (≠ T138), E131 (= E139), L134 (= L142)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
33% identity, 93% coverage: 17:262/264 of query aligns to 13:253/256 of 3h81A
- active site: A64 (= A68), M69 (= M76), T79 (≠ E86), F83 (≠ L91), G107 (= G116), E110 (≠ G119), P129 (≠ T138), E130 (= E139), V135 (≠ L144), P137 (= P146), G138 (≠ A147), L223 (≠ V231), F233 (vs. gap)
- binding calcium ion: F233 (vs. gap), Q238 (≠ G247)
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, 98% coverage: 2:260/264 of query aligns to 19:276/285 of Q7CQ56
6l3pA Crystal strcuture of feruloyl-coa hydratase lyase(fchl) complexed with coa
33% identity, 76% coverage: 16:215/264 of query aligns to 17:214/244 of 6l3pA
- active site: M69 (≠ A68), Y74 (= Y79), R86 (vs. gap), Q90 (≠ A92), G114 (= G116), S117 (≠ G119), S136 (≠ T138), E137 (= E139), I142 (≠ L144), P144 (= P146), G145 (≠ A147)
- binding coenzyme a: K28 (≠ V27), R29 (≠ H28), A31 (= A30), A67 (= A66), M69 (≠ A68), D70 (= D69), L71 (= L70), G113 (= G115)
Sites not aligning to the query:
4i42A E.Coli. 1,4-dihydroxy-2-naphthoyl coenzyme a synthase (ecmenb) in complex with 1-hydroxy-2-naphthoyl-coa (see paper)
29% identity, 96% coverage: 7:260/264 of query aligns to 24:276/285 of 4i42A
- active site: G86 (≠ A68), R91 (≠ M73), Y97 (= Y79), H105 (≠ A88), L109 (≠ A92), G133 (= G116), V136 (≠ G119), G156 (≠ E139), S161 (≠ L144), D163 (≠ P146), G164 (≠ A147), A250 (vs. gap), Y258 (vs. gap)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (= V27), R45 (≠ H28), S84 (≠ A66), G85 (= G67), G86 (≠ A68), D87 (= D69), Q88 (≠ L70), K89 (≠ G71), Y97 (= Y79), V108 (≠ L91), Y129 (≠ P112), G133 (= G116), T155 (= T138), S161 (≠ L144), T254 (vs. gap), F270 (= F254), K273 (= K257)
P0ABU0 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Escherichia coli (strain K12) (see 4 papers)
29% identity, 96% coverage: 7:260/264 of query aligns to 24:276/285 of P0ABU0
- R45 (≠ H28) binding in other chain
- SGGDQK 84:89 (≠ AGADLG 66:71) binding in other chain
- K89 (≠ G71) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- R91 (≠ M73) mutation to A: Loss of DHNA-CoA synthase activity.
- Y97 (= Y79) binding in other chain; mutation to F: Loss of DHNA-CoA synthase activity.
- YSIGG 129:133 (≠ PAFGG 112:116) binding in other chain
- Q154 (≠ L137) 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 137:139) binding
- T155 (= T138) binding in other chain
- G156 (≠ E139) mutation to D: Loss of DHNA-CoA synthase activity.
- S161 (≠ L144) binding in other chain
- W184 (≠ F166) mutation to F: Reduces the specific DHNA-CoA synthase activity by 530-fold, whereas its affinity for hydrogencarbonate is reduced by 20-fold.
- Y258 (vs. gap) binding
- R267 (≠ V251) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- F270 (= F254) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- K273 (= K257) binding ; mutation to A: Impairs protein folding.
3t88A Crystal structure of escherichia coli menb in complex with substrate analogue, osb-ncoa (see paper)
29% identity, 96% coverage: 7:260/264 of query aligns to 20:272/281 of 3t88A
- active site: G82 (≠ A68), R87 (≠ M73), Y93 (= Y79), H101 (≠ A88), L105 (≠ A92), G129 (= G116), V132 (≠ G119), G152 (≠ E139), S157 (≠ L144), D159 (≠ P146), G160 (≠ A147), A246 (vs. gap), Y254 (vs. gap)
- binding o-succinylbenzoyl-N-coenzyme A: Q39 (≠ E26), V40 (= V27), R41 (≠ H28), A43 (= A30), S80 (≠ A66), G81 (= G67), G82 (≠ A68), D83 (= D69), Q84 (≠ L70), K85 (≠ G71), Y93 (= Y79), V104 (≠ L91), L105 (≠ A92), Y125 (≠ P112), G129 (= G116), T151 (= T138), V155 (≠ L142), F158 (≠ I145), D159 (≠ P146), T250 (vs. gap), Y254 (vs. gap), F266 (= F254), K269 (= K257)
3h02A 2.15 angstrom resolution crystal structure of naphthoate synthase from salmonella typhimurium.
30% identity, 98% coverage: 2:260/264 of query aligns to 15:257/266 of 3h02A
- active site: G82 (≠ A68), H86 (≠ G82), L90 (≠ E86), G114 (= G116), V117 (≠ G119), G137 (≠ E139), S142 (≠ L144), D144 (≠ P146), G145 (≠ A147), A231 (vs. gap), Y239 (vs. gap)
- binding bicarbonate ion: G113 (= G115), Q135 (≠ L137), G137 (≠ E139), W165 (≠ F166)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
31% identity, 95% coverage: 12:263/264 of query aligns to 12:258/260 of 2hw5C
- active site: A68 (= A68), M73 (= M73), S83 (≠ G90), L87 (= L95), G111 (= G116), E114 (≠ G119), P133 (≠ T138), E134 (= E139), T139 (≠ L144), P141 (= P146), G142 (vs. gap), K227 (≠ A239), F237 (vs. gap)
- binding crotonyl coenzyme a: K26 (≠ E26), A27 (≠ V27), L28 (≠ H28), A30 (= A30), K62 (= K62), I70 (≠ L70), F109 (= F114)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
32% identity, 95% coverage: 12:263/264 of query aligns to 11:252/254 of 2dubA
- active site: A67 (= A68), M72 (= M73), S82 (= S80), G105 (= G116), E108 (≠ G119), P127 (≠ T138), E128 (= E139), T133 (≠ L144), P135 (= P146), G136 (vs. gap), K221 (≠ A239), F231 (vs. gap)
- binding octanoyl-coenzyme a: K25 (≠ E26), A26 (≠ V27), L27 (≠ H28), A29 (= A30), A65 (= A66), A67 (= A68), D68 (= D69), I69 (≠ L70), K70 (≠ G71), G105 (= G116), E108 (≠ G119), P127 (≠ T138), E128 (= E139), G136 (vs. gap), A137 (= A147)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
31% identity, 95% coverage: 12:263/264 of query aligns to 12:256/258 of 1mj3A
- active site: A68 (= A68), M73 (= M73), S83 (≠ A77), L85 (≠ Y79), G109 (= G116), E112 (≠ G119), P131 (≠ T138), E132 (= E139), T137 (≠ L144), P139 (= P146), G140 (vs. gap), K225 (≠ A239), F235 (vs. gap)
- binding hexanoyl-coenzyme a: K26 (≠ E26), A27 (≠ V27), L28 (≠ H28), A30 (= A30), A66 (= A66), G67 (= G67), A68 (= A68), D69 (= D69), I70 (≠ L70), G109 (= G116), P131 (≠ T138), E132 (= E139), L135 (= L142), G140 (vs. gap)
4elxA Structure of apo e.Coli. 1,4-dihydroxy-2- naphthoyl coa synthases with cl (see paper)
30% identity, 96% coverage: 7:260/264 of query aligns to 21:259/268 of 4elxA
- active site: G83 (≠ A68), H88 (≠ G82), L92 (≠ E86), G116 (= G116), V119 (≠ G119), G139 (≠ E139), S144 (≠ L144), D146 (≠ P146), G147 (≠ A147), A233 (vs. gap), Y241 (vs. gap)
- binding chloride ion: G115 (= G115), G139 (≠ E139), W167 (≠ F166)
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)
32% identity, 76% coverage: 16:215/264 of query aligns to 18:220/276 of O69762
- K29 (≠ V27) binding
- A68 (= A66) binding
- M70 (≠ A68) binding
- L72 (= L70) binding
- Y75 (≠ K75) binding
- G120 (= G116) binding
- S123 (≠ G119) mutation to A: Reduced kcat compared to wild-type but not markerdly.
- S142 (≠ T138) binding
- E143 (= E139) mutation to A: Abolishes catalytic activity.
- W146 (≠ L142) binding
- G151 (≠ A147) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 239 binding ; Y→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.
2vssB Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
32% identity, 76% coverage: 16:215/264 of query aligns to 15:217/247 of 2vssB
- active site: M67 (≠ A68), Y72 (≠ K75), D77 (≠ S80), R89 (vs. gap), Q93 (≠ M89), G117 (= G116), S120 (≠ G119), S139 (≠ T138), E140 (= E139), I145 (≠ L144), P147 (= P146), G148 (≠ A147)
- binding acetyl coenzyme *a: E25 (= E26), K26 (≠ V27), R27 (≠ H28), A29 (= A30), A65 (= A66), M67 (≠ A68), D68 (= D69), W113 (≠ P112), F115 (= F114), G117 (= G116), S139 (≠ T138), E140 (= E139)
Sites not aligning to the query:
2vssD Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
32% identity, 76% coverage: 16:216/264 of query aligns to 16:219/246 of 2vssD
- active site: M68 (≠ A68), Y73 (≠ K75), D78 (≠ S80), R90 (vs. gap), Q94 (≠ M89), G118 (= G116), S121 (≠ G119), S140 (≠ T138), E141 (= E139), I146 (≠ L144), P148 (= P146), G149 (≠ A147)
- binding acetyl coenzyme *a: E26 (= E26), K27 (≠ V27), R28 (≠ H28), A30 (= A30), A66 (= A66), M68 (≠ A68), D69 (= D69), L70 (= L70), F74 (≠ M76), W114 (≠ P112), F116 (= F114), S140 (≠ T138)
- binding 4-hydroxy-3-methoxybenzaldehyde: M68 (≠ A68), Y73 (≠ K75), F74 (≠ M76), Q96 (≠ L91), E141 (= E139), G149 (≠ A147), N150 (vs. gap)
Sites not aligning to the query:
Q5HH38 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Staphylococcus aureus (strain COL) (see paper)
31% identity, 93% coverage: 16:260/264 of query aligns to 22:264/273 of Q5HH38
- R34 (≠ H28) binding in other chain
- SGGDQ 73:77 (≠ AGADL 66:70) binding in other chain
- S149 (≠ L144) binding in other chain
4elwA Structure of e. Coli. 1,4-dihydroxy-2- naphthoyl coenzyme a synthases (menb) in complex with nitrate (see paper)
28% identity, 96% coverage: 7:260/264 of query aligns to 21:258/267 of 4elwA
- active site: G83 (≠ A68), L91 (≠ A92), G115 (= G116), V118 (≠ G119), G138 (≠ E139), S143 (≠ L144), D145 (≠ P146), G146 (≠ A147), A232 (vs. gap), Y240 (vs. gap)
- binding nitrate ion: G114 (= G115), T137 (= T138), G138 (≠ E139), F144 (≠ I145), W166 (≠ F166)
Query Sequence
>AZOBR_RS22290 FitnessBrowser__azobra:AZOBR_RS22290
MSDILIDIAANGSMGGVATVTMNRAEVHNAFNERVIADLTDAVLSLGSNPDVRAILLRGA
GKSFSAGADLGWMKKMAGYSHGENVEDAMGLATMLRTLDECPKPTIAVVQGPAFGGGVGL
VAACDIAIAAEAASFALTEVRLGLIPAVISPYVVAAMGERACRRYFLTAERFSAAEALRL
GLLHQTVPAAELDAAVEVMVRNLLQCGPASQTAAKELIRAVARRPLNDALVRDTAERIAR
QRASDEGREGVGAFLEKREPAWRS
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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