SitesBLAST
Comparing AZOBR_RS09775 FitnessBrowser__azobra:AZOBR_RS09775 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)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
39% identity, 93% coverage: 20:263/263 of query aligns to 12:251/259 of 5zaiC
- active site: A65 (= A74), F70 (= F79), S82 (≠ F94), R86 (≠ Q98), G110 (= G122), E113 (= E125), P132 (≠ A144), E133 (= E145), I138 (≠ M150), P140 (= P152), G141 (≠ T153), A226 (= A238), F236 (≠ A248)
- binding coenzyme a: K24 (= K32), L25 (= L33), A63 (= A72), G64 (= G73), A65 (= A74), D66 (= D75), I67 (= I76), P132 (≠ A144), R166 (≠ T178), F248 (≠ W260), K251 (≠ R263)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
36% identity, 92% coverage: 22:263/263 of query aligns to 16:246/254 of 2dubA
- active site: A67 (= A74), M72 (≠ F79), S82 (≠ T99), G105 (= G122), E108 (= E125), P127 (≠ A144), E128 (= E145), T133 (≠ M150), P135 (= P152), G136 (≠ T153), K221 (≠ A238), F231 (≠ A248)
- binding octanoyl-coenzyme a: K25 (≠ A31), A26 (≠ K32), L27 (= L33), A29 (= A35), A65 (= A72), A67 (= A74), D68 (= D75), I69 (= I76), K70 (≠ A77), G105 (= G122), E108 (= E125), P127 (≠ A144), E128 (= E145), G136 (≠ T153), A137 (≠ F154)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
36% identity, 92% coverage: 22:263/263 of query aligns to 17:250/258 of 1mj3A
- active site: A68 (= A74), M73 (≠ F79), S83 (≠ P96), L85 (≠ Q98), G109 (= G122), E112 (= E125), P131 (≠ A144), E132 (= E145), T137 (≠ M150), P139 (= P152), G140 (≠ T153), K225 (≠ A238), F235 (≠ A248)
- binding hexanoyl-coenzyme a: K26 (≠ A31), A27 (≠ K32), L28 (= L33), A30 (= A35), A66 (= A72), G67 (= G73), A68 (= A74), D69 (= D75), I70 (= I76), G109 (= G122), P131 (≠ A144), E132 (= E145), L135 (= L148), G140 (≠ T153)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
37% identity, 92% coverage: 22:263/263 of query aligns to 17:252/260 of 1dubA
- active site: A68 (= A74), M73 (≠ F79), S83 (≠ V91), L87 (≠ R95), G111 (= G122), E114 (= E125), P133 (≠ A144), E134 (= E145), T139 (≠ M150), P141 (= P152), G142 (≠ T153), K227 (≠ A238), F237 (≠ A248)
- binding acetoacetyl-coenzyme a: K26 (≠ A31), A27 (≠ K32), L28 (= L33), A30 (= A35), A66 (= A72), A68 (= A74), D69 (= D75), I70 (= I76), Y107 (≠ I118), G110 (= G121), G111 (= G122), E114 (= E125), P133 (≠ A144), E134 (= E145), L137 (= L148), G142 (≠ T153), F233 (= F244), F249 (≠ W260)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
37% identity, 92% coverage: 22:263/263 of query aligns to 15:250/258 of 1ey3A
- active site: A66 (= A74), M71 (≠ F79), S81 (≠ V91), L85 (≠ R95), G109 (= G122), E112 (= E125), P131 (≠ A144), E132 (= E145), T137 (≠ M150), P139 (= P152), G140 (≠ T153), K225 (≠ A238), F235 (≠ A248)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ A31), L26 (= L33), A28 (= A35), A64 (= A72), G65 (= G73), A66 (= A74), D67 (= D75), I68 (= I76), L85 (≠ R95), W88 (≠ Q98), G109 (= G122), P131 (≠ A144), L135 (= L148), G140 (≠ T153)
P14604 Enoyl-CoA hydratase, mitochondrial; mECH; mECH1; Enoyl-CoA hydratase 1; ECHS1; Short-chain enoyl-CoA hydratase; SCEH; EC 4.2.1.17; EC 5.3.3.8 from Rattus norvegicus (Rat) (see 3 papers)
37% identity, 92% coverage: 22:263/263 of query aligns to 47:282/290 of P14604
- E144 (= E125) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E145) mutation to D: Reduces activity 1250-fold.; mutation to Q: Reduces activity 330000-fold.
Sites not aligning to the query:
- 1:29 modified: transit peptide, Mitochondrion
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
34% identity, 92% coverage: 22:263/263 of query aligns to 17:252/260 of 2hw5C
- active site: A68 (= A74), M73 (≠ F79), S83 (≠ A89), L87 (≠ F94), G111 (= G122), E114 (= E125), P133 (≠ A144), E134 (= E145), T139 (≠ M150), P141 (= P152), G142 (≠ T153), K227 (≠ A238), F237 (≠ A248)
- binding crotonyl coenzyme a: K26 (≠ A31), A27 (≠ K32), L28 (= L33), A30 (= A35), K62 (≠ R68), I70 (= I76), F109 (≠ Y120)
Q4WF54 Mevalonyl-coenzyme A hydratase sidH; Siderophore biosynthesis protein H; EC 4.2.1.- from Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata) (see paper)
37% identity, 92% coverage: 22:263/263 of query aligns to 21:260/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
36% identity, 95% coverage: 10:260/263 of query aligns to 2:250/261 of 5jbxB
- active site: A67 (= A74), R72 (≠ F79), L84 (≠ R95), R88 (≠ T99), G112 (= G122), E115 (= E125), T134 (≠ A144), E135 (= E145), I140 (≠ M150), P142 (= P152), G143 (≠ T153), A228 (= A238), L238 (≠ A248)
- binding coenzyme a: S24 (≠ A31), R25 (≠ K32), R26 (≠ L33), A28 (= A35), A65 (= A72), D68 (= D75), L69 (≠ I76), K70 (≠ A77), L110 (≠ Y120), G111 (= G121), T134 (≠ A144), E135 (= E145), L138 (= L148), R168 (≠ T178)
2vssB Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
37% identity, 75% coverage: 21:218/263 of query aligns to 15:213/247 of 2vssB
- active site: M67 (≠ A74), Y72 (≠ F79), D77 (≠ R84), R89 (vs. gap), Q93 (= Q98), G117 (= G122), S120 (≠ E125), S139 (≠ A144), E140 (= E145), I145 (≠ M150), P147 (= P152), G148 (≠ T153)
- binding acetyl coenzyme *a: E25 (≠ A31), K26 (= K32), R27 (≠ L33), A29 (= A35), A65 (= A72), M67 (≠ A74), D68 (= D75), W113 (≠ I118), F115 (≠ Y120), G117 (= G122), S139 (≠ A144), E140 (= E145)
Sites not aligning to the query:
2vssD Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
37% identity, 75% coverage: 21:218/263 of query aligns to 16:214/246 of 2vssD
- active site: M68 (≠ A74), Y73 (≠ F79), D78 (≠ R84), R90 (vs. gap), Q94 (= Q98), G118 (= G122), S121 (≠ E125), S140 (≠ A144), E141 (= E145), I146 (≠ M150), P148 (= P152), G149 (≠ T153)
- binding acetyl coenzyme *a: E26 (≠ A31), K27 (= K32), R28 (≠ L33), A30 (= A35), A66 (= A72), M68 (≠ A74), D69 (= D75), L70 (≠ I76), F74 (≠ T80), W114 (≠ I118), F116 (≠ Y120), S140 (≠ A144)
- binding 4-hydroxy-3-methoxybenzaldehyde: M68 (≠ A74), Y73 (≠ F79), F74 (≠ T80), Q96 (≠ L100), E141 (= E145), G149 (≠ T153), N150 (≠ F154)
Sites not aligning to the query:
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)
37% identity, 75% coverage: 21:218/263 of query aligns to 18:216/276 of O69762
- K29 (= K32) binding
- A68 (= A72) binding
- M70 (≠ A74) binding
- L72 (≠ I76) binding
- Y75 (≠ F79) binding
- G120 (= G122) binding
- S123 (≠ E125) mutation to A: Reduced kcat compared to wild-type but not markerdly.
- S142 (≠ A144) binding
- E143 (= E145) mutation to A: Abolishes catalytic activity.
- W146 (≠ L148) binding
- G151 (≠ T153) 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.
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
35% identity, 92% coverage: 22:263/263 of query aligns to 13:244/250 of 3q0gD
- active site: A64 (= A74), M69 (vs. gap), T75 (≠ R84), F79 (vs. gap), G103 (= G122), E106 (= E125), P125 (≠ A144), E126 (= E145), V131 (≠ M150), P133 (= P152), G134 (≠ T153), L219 (≠ A238), F229 (≠ A248)
- binding Butyryl Coenzyme A: F225 (= F244), F241 (≠ W260)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
35% identity, 92% coverage: 22:263/263 of query aligns to 13:248/256 of 3h81A
- active site: A64 (= A74), M69 (≠ F79), T79 (≠ A89), F83 (≠ A93), G107 (= G122), E110 (= E125), P129 (≠ A144), E130 (= E145), V135 (≠ M150), P137 (= P152), G138 (≠ T153), L223 (≠ A238), F233 (≠ A248)
- binding calcium ion: F233 (≠ A248), Q238 (≠ L253)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
35% identity, 92% coverage: 22:263/263 of query aligns to 14:249/255 of 3q0jC
- active site: A65 (= A74), M70 (≠ F79), T80 (≠ A89), F84 (≠ A93), G108 (= G122), E111 (= E125), P130 (≠ A144), E131 (= E145), V136 (≠ M150), P138 (= P152), G139 (≠ T153), L224 (≠ A238), F234 (≠ A248)
- binding acetoacetyl-coenzyme a: Q23 (≠ A31), A24 (≠ K32), L25 (= L33), A27 (= A35), A63 (= A72), G64 (= G73), A65 (= A74), D66 (= D75), I67 (= I76), K68 (≠ A77), M70 (≠ F79), F84 (≠ A93), G107 (= G121), G108 (= G122), E111 (= E125), P130 (≠ A144), E131 (= E145), P138 (= P152), G139 (≠ T153), M140 (≠ F154)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
35% identity, 92% coverage: 22:263/263 of query aligns to 14:249/255 of 3q0gC
- active site: A65 (= A74), M70 (≠ F79), T80 (≠ A89), F84 (≠ A93), G108 (= G122), E111 (= E125), P130 (≠ A144), E131 (= E145), V136 (≠ M150), P138 (= P152), G139 (≠ T153), L224 (≠ A238), F234 (≠ A248)
- binding coenzyme a: L25 (= L33), A63 (= A72), I67 (= I76), K68 (≠ A77), Y104 (≠ I118), P130 (≠ A144), E131 (= E145), L134 (= L148)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
34% identity, 94% coverage: 14:260/263 of query aligns to 5:246/257 of 6slbAAA
- active site: Q64 (≠ A74), F69 (= F79), L80 (≠ A93), N84 (≠ G97), A108 (≠ G122), S111 (≠ E125), A130 (= A144), F131 (≠ E145), L136 (≠ M150), P138 (= P152), D139 (≠ T153), A224 (= A238), G234 (≠ A248)
- binding (~{E})-6-[2-[3-[[(2~{R})-4-[[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-4-oxidanyl-3-phosphonooxy-oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxy-3,3-dimethyl-2-oxidanyl-butanoyl]amino]propanoylamino]ethylsulfanyl]-6-oxidanylidene-hex-3-enoic acid: R58 (= R68), A62 (= A72), Q64 (≠ A74), D65 (= D75), L66 (≠ I76), Y76 (≠ A89), A108 (≠ G122), F131 (≠ E145), D139 (≠ T153)
6p5uE Structure of an enoyl-coa hydratase/aldolase isolated from a lignin- degrading consortium (see paper)
35% identity, 79% coverage: 21:227/263 of query aligns to 15:222/246 of 6p5uE
- active site: M67 (≠ A74), Y72 (≠ F79), D77 (≠ R84), R89 (vs. gap), A93 (≠ Q98), G117 (= G122), T120 (≠ E125), E140 (= E145), I145 (≠ M150), P147 (= P152), A148 (≠ T153)
- binding coenzyme a: D25 (≠ A31), K26 (= K32), R27 (≠ L33), A29 (= A35), A65 (= A72), M67 (≠ A74), D68 (= D75), L69 (≠ I76), W113 (≠ I118), F115 (≠ Y120), S139 (≠ A144), W143 (≠ L148)
Sites not aligning to the query:
6yswA E. Coli anaerobic trifunctional enzyme subunit-alpha in complex with coenzyme a
38% identity, 74% coverage: 15:209/263 of query aligns to 6:201/707 of 6yswA
- active site: A66 (= A74), I71 (≠ T80), A84 (= A93), Q88 (= Q98), G112 (= G122), E115 (= E125), P136 (≠ A144), E137 (= E145), G145 (≠ T153)
- binding coenzyme a: E23 (vs. gap), M25 (≠ L33), A66 (= A74), D67 (= D75), I68 (= I76), P136 (≠ A144), E137 (= E145), L140 (= L148)
Sites not aligning to the query:
3p85A Crystal structure enoyl-coa hydratase from mycobacterium avium (see paper)
36% identity, 86% coverage: 14:240/263 of query aligns to 3:210/224 of 3p85A
- active site: L62 (≠ A74), L67 (≠ F79), P68 (≠ T80), G92 (= G122), E95 (= E125), T114 (≠ A144), H115 (≠ E145), L120 (≠ M150), P122 (= P152), T123 (= T153), W208 (≠ A238)
- binding calcium ion: D43 (= D54), D45 (≠ A56)
Sites not aligning to the query:
Query Sequence
>AZOBR_RS09775 FitnessBrowser__azobra:AZOBR_RS09775
MPLTTKHADPANPVLCVTAGGIATLTLNRPAKLNAISTALAAAMLDTLDALEVDAAVRAI
IVTGAGERAFSAGADIAEFTPAVRRGPEAAVRAFRPGQTLCARIESFPKPIIAAVNGICY
GGGCEILEASHLAVASERASFSKAEIRLGMMPTFGGTQRLPRNAGRKRALEWLLTGDTFP
PAMALAVGLVNQVVPHDALLPAAFELAGRIVRHSPAAVSGILGAVTRGLNMTIGEGLAVE
TERFARLAPGADLRDGLEAWLAR
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