SitesBLAST
Comparing WP_004299879.1 NCBI__GCF_000310185.1:WP_004299879.1 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)
33% identity, 99% coverage: 1:259/261 of query aligns to 1:256/259 of 5zaiC
- active site: A65 (= A65), F70 (≠ M70), S82 (= S85), R86 (≠ A89), G110 (= G113), E113 (≠ G116), P132 (≠ S135), E133 (= E136), I138 (= I141), P140 (= P143), G141 (≠ A144), A226 (= A228), F236 (≠ R239)
- binding coenzyme a: K24 (≠ V24), L25 (≠ F25), A63 (= A63), G64 (= G64), A65 (= A65), D66 (= D66), I67 (≠ L67), P132 (≠ S135), R166 (= R168), F248 (= F251), K251 (= K254)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
35% identity, 99% coverage: 1:259/261 of query aligns to 1:254/255 of 3q0jC
- active site: A65 (= A65), M70 (= M70), T80 (≠ S85), F84 (≠ A89), G108 (= G113), E111 (≠ G116), P130 (≠ S135), E131 (= E136), V136 (≠ I141), P138 (= P143), G139 (≠ A144), L224 (≠ I235), F234 (vs. gap)
- binding acetoacetyl-coenzyme a: Q23 (≠ A23), A24 (≠ V24), L25 (≠ F25), A27 (= A27), A63 (= A63), G64 (= G64), A65 (= A65), D66 (= D66), I67 (≠ L67), K68 (≠ N68), M70 (= M70), F84 (≠ A89), G107 (= G112), G108 (= G113), E111 (≠ G116), P130 (≠ S135), E131 (= E136), P138 (= P143), G139 (≠ A144), M140 (≠ V145)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
35% identity, 99% coverage: 1:259/261 of query aligns to 1:254/255 of 3q0gC
- active site: A65 (= A65), M70 (= M70), T80 (≠ S85), F84 (≠ A89), G108 (= G113), E111 (≠ G116), P130 (≠ S135), E131 (= E136), V136 (≠ I141), P138 (= P143), G139 (≠ A144), L224 (≠ I235), F234 (vs. gap)
- binding coenzyme a: L25 (≠ F25), A63 (= A63), I67 (≠ L67), K68 (≠ N68), Y104 (≠ A109), P130 (≠ S135), E131 (= E136), L134 (≠ F139)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
35% identity, 100% coverage: 2:261/261 of query aligns to 1:255/256 of 3h81A
- active site: A64 (= A65), M69 (= M70), T79 (≠ S85), F83 (≠ A89), G107 (= G113), E110 (≠ G116), P129 (≠ S135), E130 (= E136), V135 (≠ I141), P137 (= P143), G138 (≠ A144), L223 (≠ I235), F233 (vs. gap)
- binding calcium ion: F233 (vs. gap), Q238 (≠ A244)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
35% identity, 99% coverage: 2:259/261 of query aligns to 1:249/250 of 3q0gD
- active site: A64 (= A65), M69 (= M70), T75 (≠ E78), F79 (≠ L82), G103 (= G113), E106 (≠ G116), P125 (≠ S135), E126 (= E136), V131 (≠ I141), P133 (= P143), G134 (≠ A144), L219 (≠ I235), F229 (vs. gap)
- binding Butyryl Coenzyme A: F225 (vs. gap), F241 (= F251)
6p5uE Structure of an enoyl-coa hydratase/aldolase isolated from a lignin- degrading consortium (see paper)
36% identity, 90% coverage: 5:240/261 of query aligns to 7:243/246 of 6p5uE
- active site: M67 (≠ A65), Y72 (≠ M70), D77 (= D75), R89 (≠ K87), A93 (vs. gap), G117 (= G113), T120 (≠ G116), E140 (= E136), I145 (= I141), P147 (= P143), A148 (= A144), A236 (≠ G233)
- binding coenzyme a: D25 (≠ A23), K26 (≠ V24), R27 (≠ F25), A29 (= A27), A65 (= A63), M67 (≠ A65), D68 (= D66), L69 (= L67), W113 (≠ A109), F115 (≠ L111), S139 (= S135), W143 (≠ F139)
Sites not aligning to the query:
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
32% identity, 98% coverage: 2:256/261 of query aligns to 2:254/260 of 2hw5C
- active site: A68 (= A65), M73 (= M70), S83 (= S85), L87 (≠ A89), G111 (= G113), E114 (≠ G116), P133 (≠ S135), E134 (= E136), T139 (≠ I141), P141 (= P143), G142 (vs. gap), K227 (≠ I235), F237 (vs. gap)
- binding crotonyl coenzyme a: K26 (≠ A23), A27 (≠ V24), L28 (≠ F25), A30 (= A27), K62 (= K59), I70 (≠ L67), F109 (≠ L111)
2vssB Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
34% identity, 81% coverage: 3:213/261 of query aligns to 5:218/247 of 2vssB
- active site: M67 (≠ A65), Y72 (≠ M70), D77 (= D75), R89 (≠ K87), Q93 (≠ M91), G117 (= G113), S120 (≠ G116), S139 (= S135), E140 (= E136), I145 (= I141), P147 (= P143), G148 (≠ A144)
- binding acetyl coenzyme *a: E25 (≠ A23), K26 (≠ V24), R27 (≠ F25), A29 (= A27), A65 (= A63), M67 (≠ A65), D68 (= D66), W113 (≠ A109), F115 (≠ L111), G117 (= G113), S139 (= S135), E140 (= E136)
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)
34% identity, 81% coverage: 3:213/261 of query aligns to 8:221/276 of O69762
- K29 (≠ V24) binding acetyl-CoA
- A68 (= A63) binding acetyl-CoA
- M70 (≠ A65) binding acetyl-CoA
- L72 (= L67) binding acetyl-CoA
- Y75 (≠ M70) binding vanillin
- G120 (= G113) binding acetyl-CoA
- S123 (≠ G116) mutation to A: Reduced kcat compared to wild-type but not markerdly.
- S142 (= S135) binding acetyl-CoA
- E143 (= E136) mutation to A: Abolishes catalytic activity.
- W146 (≠ F139) binding acetyl-CoA
- G151 (≠ A144) binding vanillin
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 239 binding vanillin; 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)
34% identity, 81% coverage: 3:213/261 of query aligns to 6:219/246 of 2vssD
- active site: M68 (≠ A65), Y73 (≠ M70), D78 (= D75), R90 (≠ K87), Q94 (≠ M91), G118 (= G113), S121 (≠ G116), S140 (= S135), E141 (= E136), I146 (= I141), P148 (= P143), G149 (≠ A144)
- binding acetyl coenzyme *a: E26 (≠ A23), K27 (≠ V24), R28 (≠ F25), A30 (= A27), A66 (= A63), M68 (≠ A65), D69 (= D66), L70 (= L67), F74 (≠ R71), W114 (≠ A109), F116 (≠ L111), S140 (= S135)
- binding 4-hydroxy-3-methoxybenzaldehyde: M68 (≠ A65), Y73 (≠ M70), F74 (≠ R71), Q96 (vs. gap), E141 (= E136), G149 (≠ A144), N150 (vs. gap)
Sites not aligning to the query:
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
31% identity, 98% coverage: 2:256/261 of query aligns to 2:254/260 of 1dubA
- active site: A68 (= A65), M73 (= M70), S83 (= S85), L87 (≠ A89), G111 (= G113), E114 (≠ G116), P133 (≠ S135), E134 (= E136), T139 (≠ I141), P141 (= P143), G142 (vs. gap), K227 (≠ I235), F237 (vs. gap)
- binding acetoacetyl-coenzyme a: K26 (≠ A23), A27 (≠ V24), L28 (≠ F25), A30 (= A27), A66 (= A63), A68 (= A65), D69 (= D66), I70 (≠ L67), Y107 (≠ A109), G110 (= G112), G111 (= G113), E114 (≠ G116), P133 (≠ S135), E134 (= E136), L137 (≠ F139), G142 (vs. gap), F233 (vs. gap), F249 (= F251)
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)
31% identity, 98% coverage: 2:256/261 of query aligns to 32:284/290 of P14604
- E144 (≠ G116) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E136) 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
2uzfA Crystal structure of staphylococcus aureus 1,4-dihydroxy-2-naphthoyl coa synthase (menb) in complex with acetoacetyl coa (see paper)
32% identity, 99% coverage: 3:261/261 of query aligns to 7:255/260 of 2uzfA
- active site: G70 (≠ A65), R80 (≠ A79), L84 (≠ A83), G108 (= G113), V111 (≠ G116), T130 (≠ S135), G131 (≠ E136), S136 (≠ I141), D138 (≠ P143), A139 (= A144), A225 (= A232), Y233 (≠ R239)
- binding acetoacetyl-coenzyme a: V28 (= V24), R29 (≠ F25), S68 (≠ A63), G69 (= G64), G70 (≠ A65), D71 (= D66), Y104 (≠ A109), G108 (= G113)
6l3pA Crystal strcuture of feruloyl-coa hydratase lyase(fchl) complexed with coa
33% identity, 81% coverage: 3:213/261 of query aligns to 7:215/244 of 6l3pA
- active site: M69 (≠ A65), Y74 (≠ M70), R86 (≠ L82), Q90 (≠ R86), G114 (= G113), S117 (≠ G116), S136 (= S135), E137 (= E136), I142 (= I141), P144 (= P143), G145 (≠ A144)
- binding coenzyme a: K28 (≠ V24), R29 (≠ F25), A31 (= A27), A67 (= A63), M69 (≠ A65), D70 (= D66), L71 (= L67), G113 (= G112)
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)
32% identity, 99% coverage: 3:261/261 of query aligns to 12:268/273 of Q5HH38
- R34 (≠ F25) binding in other chain
- SGGDQ 73:77 (≠ AGADL 63:67) binding in other chain
- S149 (≠ I141) binding in other chain
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
31% identity, 97% coverage: 3:256/261 of query aligns to 1:252/258 of 1ey3A
- active site: A66 (= A65), M71 (= M70), S81 (= S85), L85 (≠ A89), G109 (= G113), E112 (≠ G116), P131 (≠ S135), E132 (= E136), T137 (≠ I141), P139 (= P143), G140 (vs. gap), K225 (≠ I235), F235 (vs. gap)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ A23), L26 (≠ F25), A28 (= A27), A64 (= A63), G65 (= G64), A66 (= A65), D67 (= D66), I68 (≠ L67), L85 (≠ A89), W88 (≠ L92), G109 (= G113), P131 (≠ S135), L135 (≠ F139), G140 (vs. gap)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
30% identity, 98% coverage: 2:256/261 of query aligns to 2:252/258 of 1mj3A
- active site: A68 (= A65), M73 (= M70), S83 (≠ K87), L85 (≠ A89), G109 (= G113), E112 (≠ G116), P131 (≠ S135), E132 (= E136), T137 (≠ I141), P139 (= P143), G140 (vs. gap), K225 (≠ I235), F235 (vs. gap)
- binding hexanoyl-coenzyme a: K26 (≠ A23), A27 (≠ V24), L28 (≠ F25), A30 (= A27), A66 (= A63), G67 (= G64), A68 (= A65), D69 (= D66), I70 (≠ L67), G109 (= G113), P131 (≠ S135), E132 (= E136), L135 (≠ F139), G140 (vs. gap)
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
32% identity, 97% coverage: 8:261/261 of query aligns to 12:265/266 of O53561
- K135 (≠ S131) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 131:138, 50% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (= K138) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
30% identity, 98% coverage: 2:256/261 of query aligns to 1:248/254 of 2dubA
- active site: A67 (= A65), M72 (= M70), S82 (≠ A90), G105 (= G113), E108 (≠ G116), P127 (≠ S135), E128 (= E136), T133 (≠ I141), P135 (= P143), G136 (vs. gap), K221 (≠ I235), F231 (vs. gap)
- binding octanoyl-coenzyme a: K25 (≠ A23), A26 (≠ V24), L27 (≠ F25), A29 (= A27), A65 (= A63), A67 (= A65), D68 (= D66), I69 (≠ L67), K70 (≠ N68), G105 (= G113), E108 (≠ G116), P127 (≠ S135), E128 (= E136), G136 (vs. gap), A137 (= A144)
4emlA Synechocystis sp. Pcc 6803 1,4-dihydroxy-2-naphthoyl-coenzyme a synthase (menb) in complex with bicarbonate (see paper)
31% identity, 100% coverage: 2:261/261 of query aligns to 8:256/261 of 4emlA
- active site: G77 (≠ A65), R81 (≠ W69), L85 (≠ A83), G109 (= G113), V112 (≠ G116), G132 (≠ E136), S137 (≠ I141), D139 (≠ P143), G140 (≠ A144), A226 (= A232), Y234 (≠ R239)
- binding bicarbonate ion: G108 (= G112), Q130 (≠ T134), G132 (≠ E136), W160 (≠ F163)
- binding chloride ion: D184 (= D187), R185 (≠ E188), E187 (≠ D190), E188 (≠ A191)
Query Sequence
>WP_004299879.1 NCBI__GCF_000310185.1:WP_004299879.1
MNYETLAIERRGAVATIWMDRPAVFNAFNEQLIAELAAACAELDADAGVRVVVLAGRGKH
FSAGADLNWMRRASDSTEAENLADSRKFAAMLRTLSGMSKPTIARVQGAALGGGTGLTAA
CDMAIAADDASFATSEVKFGIIPAVISPYVLRAIGPRHALRYFQSAERFGAAEAKAMGLV
GEVVTLDELDAAVDRLVQALLACGPQAQLAAKQLIAALAGRPIDDAVAEETAGRIARQRA
TAEAREGFTAFFEKRSPAWMQ
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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