SitesBLAST
Comparing Pf1N1B4_679 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_679 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)
7borA Structure of pseudomonas aeruginosa coa-bound odaa (see paper)
68% identity, 98% coverage: 5:248/249 of query aligns to 4:247/247 of 7borA
- active site: N63 (= N64), F68 (= F69), D77 (= D78), G81 (≠ Y82), I105 (= I106), T108 (= T109), F128 (= F129), L133 (= L134), P135 (= P136), E136 (= E137), A222 (≠ E223), L232 (= L233)
- binding coenzyme a: D21 (≠ E22), K22 (= K23), A25 (= A26), S61 (≠ A62), I65 (= I66), V103 (= V104), F128 (= F129), L131 (= L132), F244 (= F245), R247 (= R248)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
34% identity, 96% coverage: 8:245/249 of query aligns to 8:246/257 of 6slbAAA
- active site: Q64 (≠ N64), F69 (= F69), L80 (≠ S79), N84 (≠ H83), A108 (≠ I106), S111 (≠ T109), A130 (≠ P128), F131 (= F129), L136 (= L134), P138 (= P136), D139 (≠ E137), A224 (≠ E223), G234 (≠ L233)
- 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 (≠ E58), A62 (= A62), Q64 (≠ N64), D65 (= D65), L66 (≠ I66), Y76 (≠ I76), A108 (≠ I106), F131 (= F129), D139 (≠ E137)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
33% identity, 71% coverage: 3:178/249 of query aligns to 4:182/259 of 5zaiC
- active site: A65 (≠ N64), F70 (= F69), S82 (≠ D78), R86 (≠ Y82), G110 (≠ I106), E113 (≠ T109), P132 (= P128), E133 (≠ F129), I138 (≠ L134), P140 (= P136), G141 (≠ E137)
- binding coenzyme a: K24 (= K23), L25 (≠ K24), A63 (= A62), G64 (= G63), A65 (≠ N64), D66 (= D65), I67 (= I66), P132 (= P128), R166 (≠ G162)
Sites not aligning to the query:
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
29% identity, 99% coverage: 3:249/249 of query aligns to 3:245/250 of 3q0gD
- active site: A64 (≠ N64), M69 (≠ F69), T75 (≠ D78), F79 (≠ Y82), G103 (≠ I106), E106 (≠ T109), P125 (= P128), E126 (≠ F129), V131 (≠ L134), P133 (= P136), G134 (≠ E137), L219 (≠ E223), F229 (≠ L233)
- binding Butyryl Coenzyme A: F225 (= F229), F241 (= F245)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
30% identity, 99% coverage: 3:249/249 of query aligns to 4:250/255 of 3q0jC
- active site: A65 (≠ N64), M70 (≠ F69), T80 (≠ V81), F84 (≠ M85), G108 (≠ I106), E111 (≠ T109), P130 (= P128), E131 (≠ F129), V136 (≠ L134), P138 (= P136), G139 (≠ E137), L224 (≠ E223), F234 (≠ L233)
- binding acetoacetyl-coenzyme a: Q23 (≠ E22), A24 (≠ K23), L25 (≠ K24), A27 (= A26), A63 (= A62), G64 (= G63), A65 (≠ N64), D66 (= D65), I67 (= I66), K68 (≠ F67), M70 (≠ F69), F84 (≠ M85), G107 (= G105), G108 (≠ I106), E111 (≠ T109), P130 (= P128), E131 (≠ F129), P138 (= P136), G139 (≠ E137), M140 (≠ F138)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
30% identity, 99% coverage: 3:249/249 of query aligns to 4:250/255 of 3q0gC
- active site: A65 (≠ N64), M70 (≠ F69), T80 (≠ V81), F84 (≠ M85), G108 (≠ I106), E111 (≠ T109), P130 (= P128), E131 (≠ F129), V136 (≠ L134), P138 (= P136), G139 (≠ E137), L224 (≠ E223), F234 (≠ L233)
- binding coenzyme a: L25 (≠ K24), A63 (= A62), I67 (= I66), K68 (≠ F67), Y104 (≠ A102), P130 (= P128), E131 (≠ F129), L134 (= L132)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
34% identity, 96% coverage: 8:245/249 of query aligns to 5:234/245 of 6slaAAA
- active site: Q61 (≠ N64), L68 (= L70), N72 (≠ P74), A96 (≠ I106), S99 (≠ T109), A118 (≠ P128), F119 (= F129), L124 (= L134), P126 (= P136), N127 (≠ E137), A212 (≠ E223), G222 (≠ L233)
- binding ~{S}-[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]ethyl] 2-(2,5-dihydrooxepin-7-yl)ethanethioate: L21 (≠ K24), A59 (= A62), Q61 (≠ N64), D62 (= D65), L63 (≠ I66), L68 (= L70), Y71 (≠ P73), A94 (≠ V104), G95 (= G105), A96 (≠ I106), F119 (= F129), I122 (≠ L132), L124 (= L134), N127 (≠ E137), F234 (= F245)
Sites not aligning to the query:
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
30% identity, 99% coverage: 3:249/249 of query aligns to 3:249/256 of 3h81A
- active site: A64 (≠ N64), M69 (≠ F69), T79 (≠ V81), F83 (≠ M85), G107 (≠ I106), E110 (≠ T109), P129 (= P128), E130 (≠ F129), V135 (≠ L134), P137 (= P136), G138 (≠ E137), L223 (≠ E223), F233 (≠ L233)
- binding calcium ion: F233 (≠ L233), Q238 (≠ A238)
Q62651 Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial; EC 5.3.3.- from Rattus norvegicus (Rat) (see paper)
28% identity, 80% coverage: 10:207/249 of query aligns to 63:275/327 of Q62651
- D176 (≠ T109) mutation D->A,D: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- E196 (≠ F129) mutation E->D,Q: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- D204 (≠ E137) mutation D->A,N: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
28% identity, 94% coverage: 16:248/249 of query aligns to 20:252/260 of 2hw5C
- active site: A68 (≠ N64), M73 (≠ F69), S83 (≠ V81), L87 (≠ M85), G111 (≠ I106), E114 (≠ T109), P133 (= P128), E134 (≠ F129), T139 (≠ L134), P141 (= P136), G142 (≠ E137), K227 (≠ E223), F237 (≠ L233)
- binding crotonyl coenzyme a: K26 (≠ E22), A27 (≠ K23), L28 (≠ K24), A30 (= A26), K62 (≠ E58), I70 (= I66), F109 (≠ V104)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
27% identity, 94% coverage: 16:248/249 of query aligns to 20:250/258 of 1mj3A
- active site: A68 (≠ N64), M73 (≠ F69), S83 (= S79), L85 (≠ V81), G109 (≠ I106), E112 (≠ T109), P131 (= P128), E132 (≠ F129), T137 (≠ L134), P139 (= P136), G140 (≠ E137), K225 (≠ E223), F235 (≠ L233)
- binding hexanoyl-coenzyme a: K26 (≠ E22), A27 (≠ K23), L28 (≠ K24), A30 (= A26), A66 (= A62), G67 (= G63), A68 (≠ N64), D69 (= D65), I70 (= I66), G109 (≠ I106), P131 (= P128), E132 (≠ F129), L135 (= L132), G140 (≠ E137)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
28% identity, 94% coverage: 16:248/249 of query aligns to 19:246/254 of 2dubA
- active site: A67 (≠ N64), M72 (≠ F69), S82 (≠ H83), G105 (≠ I106), E108 (≠ T109), P127 (= P128), E128 (≠ F129), T133 (≠ L134), P135 (= P136), G136 (≠ E137), K221 (≠ E223), F231 (≠ L233)
- binding octanoyl-coenzyme a: K25 (≠ E22), A26 (≠ K23), L27 (≠ K24), A29 (= A26), A65 (= A62), A67 (≠ N64), D68 (= D65), I69 (= I66), K70 (≠ F67), G105 (≠ I106), E108 (≠ T109), P127 (= P128), E128 (≠ F129), G136 (≠ E137), A137 (≠ F138)
Q9P4U9 Enoyl-CoA hydratase AKT3-1; AF-toxin biosynthesis protein 3-1; EC 4.2.1.17 from Alternaria alternata (Alternaria rot fungus) (Torula alternata) (see paper)
26% identity, 95% coverage: 12:248/249 of query aligns to 24:263/296 of Q9P4U9
Sites not aligning to the query:
- 294:296 Peroxisomal targeting signal type 1
3rrvB Crystal structure of an enoyl-coa hydratase/isomerase from mycobacterium paratuberculosis (see paper)
30% identity, 85% coverage: 1:211/249 of query aligns to 4:216/254 of 3rrvB
Sites not aligning to the query:
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)
32% identity, 79% coverage: 13:208/249 of query aligns to 21:218/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
28% identity, 94% coverage: 16:248/249 of query aligns to 18:250/258 of 1ey3A
- active site: A66 (≠ N64), M71 (≠ F69), S81 (≠ V81), L85 (≠ M85), G109 (≠ I106), E112 (≠ T109), P131 (= P128), E132 (≠ F129), T137 (≠ L134), P139 (= P136), G140 (≠ E137), K225 (≠ E223), F235 (≠ L233)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ E22), L26 (≠ K24), A28 (= A26), A64 (= A62), G65 (= G63), A66 (≠ N64), D67 (= D65), I68 (= I66), L85 (≠ M85), W88 (vs. gap), G109 (≠ I106), P131 (= P128), L135 (= L132), G140 (≠ E137)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
28% identity, 94% coverage: 16:248/249 of query aligns to 20:252/260 of 1dubA
- active site: A68 (≠ N64), M73 (≠ F69), S83 (≠ V81), L87 (≠ M85), G111 (≠ I106), E114 (≠ T109), P133 (= P128), E134 (≠ F129), T139 (≠ L134), P141 (= P136), G142 (≠ E137), K227 (≠ E223), F237 (≠ L233)
- binding acetoacetyl-coenzyme a: K26 (≠ E22), A27 (≠ K23), L28 (≠ K24), A30 (= A26), A66 (= A62), A68 (≠ N64), D69 (= D65), I70 (= I66), Y107 (≠ A102), G110 (= G105), G111 (≠ I106), E114 (≠ T109), P133 (= P128), E134 (≠ F129), L137 (= L132), G142 (≠ E137), F233 (= F229), F249 (= F245)
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)
27% identity, 94% coverage: 16:249/249 of query aligns to 50:283/290 of P14604
- E144 (≠ T109) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (≠ F129) 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
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)
28% identity, 76% coverage: 4:193/249 of query aligns to 10:202/276 of O69762
- K29 (= K23) binding
- A68 (= A62) binding
- M70 (≠ N64) binding
- L72 (≠ I66) binding
- Y75 (≠ F69) binding
- G120 (≠ I106) binding
- S123 (≠ T109) mutation to A: Reduced kcat compared to wild-type but not markerdly.
- S142 (≠ P128) binding
- E143 (≠ F129) mutation to A: Abolishes catalytic activity.
- W146 (≠ L132) binding
- G151 (≠ E137) 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.
2vssD Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
28% identity, 76% coverage: 4:193/249 of query aligns to 8:200/246 of 2vssD
- active site: M68 (≠ N64), Y73 (≠ F69), D78 (vs. gap), R90 (vs. gap), Q94 (≠ H83), G118 (≠ I106), S121 (≠ T109), S140 (≠ P128), E141 (≠ F129), I146 (≠ L134), P148 (= P136), G149 (≠ E137)
- binding acetyl coenzyme *a: E26 (= E22), K27 (= K23), R28 (≠ K24), A30 (= A26), A66 (= A62), M68 (≠ N64), D69 (= D65), L70 (≠ I66), F74 (≠ L70), W114 (≠ A102), F116 (≠ V104), S140 (≠ P128)
- binding 4-hydroxy-3-methoxybenzaldehyde: M68 (≠ N64), Y73 (≠ F69), F74 (≠ L70), Q96 (≠ M85), E141 (≠ F129), G149 (≠ E137), N150 (≠ F138)
Sites not aligning to the query:
Query Sequence
>Pf1N1B4_679 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_679
MPDTIQFERERGLLTLRINRPEKKNALTRAMYSQLAEGLRLADSDPEINAVLITGSAECF
TAGNDIFDFLQQPPSILDSPVYHFMLNLLECRKPVIAAVAGAAVGIGTTLLLHCDLVYVS
TDARLRMPFVNLGLCPEFGSSLILPRMLGHAKAAELLLLGEGFSGEQAAAWGIATEALGS
GEAALAKAREMALRFEALPPEAVRISKQLMKAPGREQLRKVIEEEGALFTQRLRSPEAMA
ALSAFIKRH
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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