SitesBLAST
Comparing PfGW456L13_2285 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_2285 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)
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)
33% identity, 93% coverage: 18:263/265 of query aligns to 21:265/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
27% identity, 96% coverage: 8:261/265 of query aligns to 4:254/259 of 5zaiC
- active site: A65 (≠ G69), F70 (≠ M74), S82 (≠ N89), R86 (≠ G93), G110 (= G117), E113 (≠ G120), P132 (= P139), E133 (= E140), I138 (≠ L145), P140 (= P147), G141 (≠ A148), A226 (≠ D233), F236 (≠ V243)
- binding coenzyme a: K24 (≠ S28), L25 (≠ R29), A63 (= A67), G64 (= G68), A65 (≠ G69), D66 (= D70), I67 (= I71), P132 (= P139), R166 (= R172), F248 (= F255), K251 (= K258)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
33% identity, 97% coverage: 8:263/265 of query aligns to 3:253/256 of 3h81A
- active site: A64 (≠ G69), M69 (= M74), T79 (= T83), F83 (≠ N89), G107 (= G117), E110 (≠ G120), P129 (= P139), E130 (= E140), V135 (≠ L145), P137 (= P147), G138 (≠ A148), L223 (= L232), F233 (≠ V243)
- binding calcium ion: F233 (≠ V243), Q238 (≠ G248)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
33% identity, 97% coverage: 8:263/265 of query aligns to 4:254/255 of 3q0jC
- active site: A65 (≠ G69), M70 (= M74), T80 (= T83), F84 (≠ N89), G108 (= G117), E111 (≠ G120), P130 (= P139), E131 (= E140), V136 (≠ L145), P138 (= P147), G139 (≠ A148), L224 (= L232), F234 (≠ V243)
- binding acetoacetyl-coenzyme a: Q23 (≠ E27), A24 (≠ S28), L25 (≠ R29), A27 (= A31), A63 (= A67), G64 (= G68), A65 (≠ G69), D66 (= D70), I67 (= I71), K68 (= K72), M70 (= M74), F84 (≠ N89), G107 (= G116), G108 (= G117), E111 (≠ G120), P130 (= P139), E131 (= E140), P138 (= P147), G139 (≠ A148), M140 (≠ Q149)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
33% identity, 97% coverage: 8:263/265 of query aligns to 4:254/255 of 3q0gC
- active site: A65 (≠ G69), M70 (= M74), T80 (= T83), F84 (≠ N89), G108 (= G117), E111 (≠ G120), P130 (= P139), E131 (= E140), V136 (≠ L145), P138 (= P147), G139 (≠ A148), L224 (= L232), F234 (≠ V243)
- binding coenzyme a: L25 (≠ R29), A63 (= A67), I67 (= I71), K68 (= K72), Y104 (≠ A113), P130 (= P139), E131 (= E140), L134 (= L143)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
32% identity, 97% coverage: 8:263/265 of query aligns to 3:249/250 of 3q0gD
- active site: A64 (≠ G69), M69 (= M74), T75 (= T83), F79 (≠ N89), G103 (= G117), E106 (≠ G120), P125 (= P139), E126 (= E140), V131 (≠ L145), P133 (= P147), G134 (≠ A148), L219 (= L232), F229 (≠ V243)
- binding Butyryl Coenzyme A: F225 (= F239), F241 (= F255)
Q62651 Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial; EC 5.3.3.- from Rattus norvegicus (Rat) (see paper)
28% identity, 91% coverage: 18:259/265 of query aligns to 66:317/327 of Q62651
- D176 (≠ G120) mutation D->A,D: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- E196 (= E140) mutation E->D,Q: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- D204 (≠ A148) mutation D->A,N: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
29% identity, 92% coverage: 21:263/265 of query aligns to 19:251/254 of 2dubA
- active site: A67 (≠ G69), M72 (= M74), S82 (≠ A84), G105 (= G117), E108 (≠ G120), P127 (= P139), E128 (= E140), T133 (≠ L145), P135 (= P147), G136 (vs. gap), K221 (vs. gap), F231 (≠ V243)
- binding octanoyl-coenzyme a: K25 (≠ E27), A26 (≠ S28), L27 (≠ R29), A29 (= A31), A65 (= A67), A67 (≠ G69), D68 (= D70), I69 (= I71), K70 (= K72), G105 (= G117), E108 (≠ G120), P127 (= P139), E128 (= E140), G136 (vs. gap), A137 (= A148)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
30% identity, 96% coverage: 10:263/265 of query aligns to 5:254/257 of 6slbAAA
- active site: Q64 (≠ G69), F69 (≠ M74), L80 (≠ H85), N84 (= N89), A108 (≠ G117), S111 (≠ G120), A130 (≠ P139), F131 (≠ E140), L136 (= L145), P138 (= P147), D139 (≠ A148), A224 (≠ D233), G234 (≠ V243)
- 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 (≠ G63), A62 (= A67), Q64 (≠ G69), D65 (= D70), L66 (≠ I71), Y76 (≠ G81), A108 (≠ G117), F131 (≠ E140), D139 (≠ A148)
Q9LKJ1 3-hydroxyisobutyryl-CoA hydrolase 1; CoA-thioester hydrolase CHY1; EC 3.1.2.-; EC 3.1.2.4 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
30% identity, 67% coverage: 10:187/265 of query aligns to 11:190/378 of Q9LKJ1
- G70 (= G69) mutation to S: Loss of activity.
- E142 (= E140) mutation to A: Loss of activity.
- D150 (≠ A148) mutation to G: Reduced activity.
6l3pA Crystal strcuture of feruloyl-coa hydratase lyase(fchl) complexed with coa
31% identity, 67% coverage: 9:185/265 of query aligns to 9:183/244 of 6l3pA
- active site: M69 (≠ G69), Y74 (≠ M74), R86 (= R86), Q90 (≠ R90), G114 (= G117), S117 (≠ G120), S136 (≠ P139), E137 (= E140), I142 (≠ L145), P144 (= P147), G145 (≠ A148)
- binding coenzyme a: K28 (≠ S28), R29 (= R29), A31 (= A31), A67 (= A67), M69 (≠ G69), D70 (= D70), L71 (≠ I71), G113 (= G116)
Sites not aligning to the query:
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
29% identity, 92% coverage: 21:263/265 of query aligns to 18:255/258 of 1ey3A
- active site: A66 (≠ G69), M71 (= M74), S81 (≠ A84), L85 (= L96), G109 (= G117), E112 (≠ G120), P131 (= P139), E132 (= E140), T137 (≠ L145), P139 (= P147), G140 (vs. gap), K225 (vs. gap), F235 (≠ V243)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ E27), L26 (≠ R29), A28 (= A31), A64 (= A67), G65 (= G68), A66 (≠ G69), D67 (= D70), I68 (= I71), L85 (= L96), W88 (≠ V99), G109 (= G117), P131 (= P139), L135 (= L143), G140 (vs. gap)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
29% identity, 92% coverage: 21:263/265 of query aligns to 20:257/260 of 1dubA
- active site: A68 (≠ G69), M73 (= M74), S83 (≠ A84), L87 (= L96), G111 (= G117), E114 (≠ G120), P133 (= P139), E134 (= E140), T139 (≠ L145), P141 (= P147), G142 (vs. gap), K227 (vs. gap), F237 (≠ V243)
- binding acetoacetyl-coenzyme a: K26 (≠ E27), A27 (≠ S28), L28 (≠ R29), A30 (= A31), A66 (= A67), A68 (≠ G69), D69 (= D70), I70 (= I71), Y107 (≠ A113), G110 (= G116), G111 (= G117), E114 (≠ G120), P133 (= P139), E134 (= E140), L137 (= L143), G142 (vs. gap), F233 (= F239), F249 (= F255)
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)
29% identity, 92% coverage: 21:263/265 of query aligns to 50:287/290 of P14604
- E144 (≠ G120) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E140) 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
2vssB Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
30% identity, 67% coverage: 8:185/265 of query aligns to 6:186/247 of 2vssB
- active site: M67 (≠ G69), Y72 (≠ M74), D77 (≠ A79), R89 (≠ V91), Q93 (≠ L95), G117 (= G117), S120 (≠ G120), S139 (≠ P139), E140 (= E140), I145 (≠ L145), P147 (= P147), G148 (≠ A148)
- binding acetyl coenzyme *a: E25 (= E27), K26 (≠ S28), R27 (= R29), A29 (= A31), A65 (= A67), M67 (≠ G69), D68 (= D70), W113 (≠ A113), F115 (≠ L115), G117 (= G117), S139 (≠ P139), E140 (= E140)
Sites not aligning to the query:
2vssD Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
30% identity, 67% coverage: 8:185/265 of query aligns to 7:187/246 of 2vssD
- active site: M68 (≠ G69), Y73 (≠ M74), D78 (≠ A79), R90 (≠ V91), Q94 (≠ L95), G118 (= G117), S121 (≠ G120), S140 (≠ P139), E141 (= E140), I146 (≠ L145), P148 (= P147), G149 (≠ A148)
- binding acetyl coenzyme *a: E26 (= E27), K27 (≠ S28), R28 (= R29), A30 (= A31), A66 (= A67), M68 (≠ G69), D69 (= D70), L70 (≠ I71), F74 (≠ A75), W114 (≠ A113), F116 (≠ L115), S140 (≠ P139)
- binding 4-hydroxy-3-methoxybenzaldehyde: M68 (≠ G69), Y73 (≠ M74), F74 (≠ A75), Q96 (= Q97), E141 (= E140), G149 (≠ A148), N150 (≠ Q149)
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)
30% identity, 67% coverage: 8:185/265 of query aligns to 9:189/276 of O69762
- K29 (≠ S28) binding
- A68 (= A67) binding
- M70 (≠ G69) binding
- L72 (≠ I71) binding
- Y75 (≠ M74) binding
- G120 (= G117) binding
- S123 (≠ G120) mutation to A: Reduced kcat compared to wild-type but not markerdly.
- S142 (≠ P139) binding
- E143 (= E140) mutation to A: Abolishes catalytic activity.
- W146 (≠ L143) binding
- G151 (≠ A148) 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.
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
28% identity, 94% coverage: 15:263/265 of query aligns to 14:257/260 of 2hw5C
- active site: A68 (≠ G69), M73 (= M74), S83 (≠ A84), L87 (= L96), G111 (= G117), E114 (≠ G120), P133 (= P139), E134 (= E140), T139 (≠ L145), P141 (= P147), G142 (vs. gap), K227 (vs. gap), F237 (≠ V243)
- binding crotonyl coenzyme a: K26 (≠ E27), A27 (≠ S28), L28 (≠ R29), A30 (= A31), K62 (≠ G63), I70 (= I71), F109 (≠ L115)
4izdA Crystal structure of dmdd e121a in complex with mmpa-coa (see paper)
33% identity, 65% coverage: 16:187/265 of query aligns to 18:188/253 of 4izdA
- active site: L70 (≠ G69), H75 (≠ M74), C89 (≠ D87), H93 (≠ G93), G117 (= G117), A120 (≠ G120), E140 (= E140), G148 (≠ A148)
- binding 3-methylmercaptopropionate-CoA (MMPA-CoA): D29 (≠ E27), K30 (≠ S28), R31 (= R29), A33 (= A31), A68 (= A67), L70 (≠ G69), D71 (= D70), L72 (≠ I71)
Sites not aligning to the query:
4izcB Crystal structure of dmdd e121a in complex with mta-coa (see paper)
33% identity, 65% coverage: 16:187/265 of query aligns to 18:188/266 of 4izcB
- active site: L70 (≠ G69), H75 (≠ M74), C89 (≠ D87), H93 (≠ G93), G117 (= G117), A120 (≠ G120), E140 (= E140), G148 (≠ A148)
- binding methylthioacryloyl-CoA: D29 (≠ E27), K30 (≠ S28), R31 (= R29), A33 (= A31), A68 (= A67), L70 (≠ G69), D71 (= D70), L72 (≠ I71), W92 (≠ F92), G117 (= G117), P139 (= P139), E140 (= E140), R143 (≠ L143), G148 (≠ A148)
Sites not aligning to the query:
Query Sequence
>PfGW456L13_2285 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_2285
MNSLPVCQTLLLELHNGVLHITLNRPESRNAMSLQMVAELRSVLAAVRDKPGVRALVIGG
VGGHFCAGGDIKDMANARAQGPTAHRDLNRVFGTLLQEVQHAPQVVITVLQGAVLGGGLG
LACVSDIALSDHQAQFGLPETSLGLLPAQIVPFVVQRIGLTQTRRLALTAARFDGHQARR
MGLVHFVEHDPQALAERLDEVLAHVLCCAPGANAATKKLLLASAGQPSDALLDQAAEWFS
EAVTGAEGIEGTMAFVQKRKPGWAS
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