SitesBLAST
Comparing WP_106712562.1 NCBI__GCF_003010955.1:WP_106712562.1 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)
42% identity, 98% coverage: 6:258/259 of query aligns to 6:259/259 of 5zaiC
- active site: A65 (≠ G65), F70 (≠ W70), S82 (≠ V83), R86 (≠ H87), G110 (= G111), E113 (= E114), P132 (= P133), E133 (= E134), I138 (≠ M139), P140 (= P141), G141 (= G142), A226 (= A225), F236 (≠ A235)
- binding coenzyme a: K24 (= K24), L25 (= L25), A63 (= A63), G64 (= G64), A65 (≠ G65), D66 (= D66), I67 (= I67), P132 (= P133), R166 (≠ I167), F248 (= F247), K251 (= K250)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
38% identity, 98% coverage: 4:257/259 of query aligns to 5:260/261 of 5jbxB
- active site: A67 (≠ G65), R72 (≠ W70), L84 (≠ V83), R88 (≠ H87), G112 (= G111), E115 (= E114), T134 (≠ P133), E135 (= E134), I140 (≠ M139), P142 (= P141), G143 (= G142), A228 (= A225), L238 (≠ A235)
- binding coenzyme a: S24 (≠ E23), R25 (≠ K24), R26 (≠ L25), A28 (= A27), A65 (= A63), D68 (= D66), L69 (≠ I67), K70 (≠ N68), L110 (= L109), G111 (= G110), T134 (≠ P133), E135 (= E134), L138 (= L137), R168 (≠ I167)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
36% identity, 94% coverage: 14:256/259 of query aligns to 17:256/258 of 1mj3A
- active site: A68 (≠ G65), M73 (= M73), S83 (≠ V83), L85 (≠ F85), G109 (= G111), E112 (= E114), P131 (= P133), E132 (= E134), T137 (≠ M139), P139 (= P141), G140 (= G142), K225 (≠ A225), F235 (≠ A235)
- binding hexanoyl-coenzyme a: K26 (≠ E23), A27 (≠ K24), L28 (= L25), A30 (= A27), A66 (= A63), G67 (= G64), A68 (≠ G65), D69 (= D66), I70 (= I67), G109 (= G111), P131 (= P133), E132 (= E134), L135 (= L137), G140 (= G142)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
36% identity, 94% coverage: 14:256/259 of query aligns to 16:252/254 of 2dubA
- active site: A67 (≠ G65), M72 (= M73), S82 (≠ V83), G105 (= G111), E108 (= E114), P127 (= P133), E128 (= E134), T133 (≠ M139), P135 (= P141), G136 (= G142), K221 (≠ A225), F231 (≠ A235)
- binding octanoyl-coenzyme a: K25 (≠ E23), A26 (≠ K24), L27 (= L25), A29 (= A27), A65 (= A63), A67 (≠ G65), D68 (= D66), I69 (= I67), K70 (≠ N68), G105 (= G111), E108 (= E114), P127 (= P133), E128 (= E134), G136 (= G142), A137 (≠ W143)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
34% identity, 93% coverage: 14:255/259 of query aligns to 13:253/256 of 3h81A
- active site: A64 (≠ G65), M69 (≠ W70), T79 (≠ V83), F83 (≠ H87), G107 (= G111), E110 (= E114), P129 (= P133), E130 (= E134), V135 (≠ M139), P137 (= P141), G138 (= G142), L223 (≠ A225), F233 (≠ A235)
- binding calcium ion: F233 (≠ A235), Q238 (≠ L240)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
34% identity, 93% coverage: 14:255/259 of query aligns to 14:254/255 of 3q0jC
- active site: A65 (≠ G65), M70 (≠ W70), T80 (≠ V83), F84 (≠ H87), G108 (= G111), E111 (= E114), P130 (= P133), E131 (= E134), V136 (≠ M139), P138 (= P141), G139 (= G142), L224 (≠ A225), F234 (≠ A235)
- binding acetoacetyl-coenzyme a: Q23 (≠ E23), A24 (≠ K24), L25 (= L25), A27 (= A27), A63 (= A63), G64 (= G64), A65 (≠ G65), D66 (= D66), I67 (= I67), K68 (≠ N68), M70 (≠ W70), F84 (≠ H87), G107 (= G110), G108 (= G111), E111 (= E114), P130 (= P133), E131 (= E134), P138 (= P141), G139 (= G142), M140 (≠ W143)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
34% identity, 93% coverage: 14:255/259 of query aligns to 14:254/255 of 3q0gC
- active site: A65 (≠ G65), M70 (≠ W70), T80 (≠ V83), F84 (≠ H87), G108 (= G111), E111 (= E114), P130 (= P133), E131 (= E134), V136 (≠ M139), P138 (= P141), G139 (= G142), L224 (≠ A225), F234 (≠ A235)
- binding coenzyme a: L25 (= L25), A63 (= A63), I67 (= I67), K68 (≠ N68), Y104 (≠ H107), P130 (= P133), E131 (= E134), L134 (= L137)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
35% identity, 94% coverage: 14:256/259 of query aligns to 17:258/260 of 1dubA
- active site: A68 (≠ G65), M73 (= M73), S83 (≠ V83), L87 (≠ H87), G111 (= G111), E114 (= E114), P133 (= P133), E134 (= E134), T139 (≠ M139), P141 (= P141), G142 (= G142), K227 (≠ A225), F237 (≠ A235)
- binding acetoacetyl-coenzyme a: K26 (≠ E23), A27 (≠ K24), L28 (= L25), A30 (= A27), A66 (= A63), A68 (≠ G65), D69 (= D66), I70 (= I67), Y107 (≠ H107), G110 (= G110), G111 (= G111), E114 (= E114), P133 (= P133), E134 (= E134), L137 (= L137), G142 (= G142), F233 (≠ S231), F249 (= F247)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
35% identity, 94% coverage: 14:256/259 of query aligns to 15:256/258 of 1ey3A
- active site: A66 (≠ G65), M71 (= M73), S81 (≠ V83), L85 (≠ H87), G109 (= G111), E112 (= E114), P131 (= P133), E132 (= E134), T137 (≠ M139), P139 (= P141), G140 (= G142), K225 (≠ A225), F235 (≠ A235)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ E23), L26 (= L25), A28 (= A27), A64 (= A63), G65 (= G64), A66 (≠ G65), D67 (= D66), I68 (= I67), L85 (≠ H87), W88 (≠ F90), G109 (= G111), P131 (= P133), L135 (= L137), G140 (= G142)
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)
35% identity, 94% coverage: 14:256/259 of query aligns to 47:288/290 of P14604
- E144 (= E114) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E134) 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
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
34% identity, 93% coverage: 14:255/259 of query aligns to 13:249/250 of 3q0gD
- active site: A64 (≠ G65), M69 (≠ W70), T75 (≠ V83), F79 (≠ H87), G103 (= G111), E106 (= E114), P125 (= P133), E126 (= E134), V131 (≠ M139), P133 (= P141), G134 (= G142), L219 (≠ A225), F229 (≠ A235)
- binding Butyryl Coenzyme A: F225 (≠ S231), F241 (= F247)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
33% identity, 95% coverage: 14:258/259 of query aligns to 17:260/260 of 2hw5C
- active site: A68 (≠ G65), M73 (≠ W70), S83 (≠ V83), L87 (≠ H87), G111 (= G111), E114 (= E114), P133 (= P133), E134 (= E134), T139 (≠ M139), P141 (= P141), G142 (= G142), K227 (≠ A225), F237 (≠ A235)
- binding crotonyl coenzyme a: K26 (≠ E23), A27 (≠ K24), L28 (= L25), A30 (= A27), K62 (= K59), I70 (= I67), F109 (≠ L109)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
36% identity, 94% coverage: 14:257/259 of query aligns to 13:256/257 of 6slbAAA
- active site: Q64 (≠ G65), F69 (≠ W70), L80 (≠ V83), N84 (≠ H87), A108 (≠ G111), S111 (≠ E114), A130 (≠ P133), F131 (≠ E134), L136 (≠ M139), P138 (= P141), D139 (≠ G142), A224 (= A225), G234 (≠ A235)
- 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 (≠ K59), A62 (= A63), Q64 (≠ G65), D65 (= D66), L66 (≠ I67), Y76 (≠ E77), A108 (≠ G111), F131 (≠ E134), D139 (≠ G142)
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
33% identity, 93% coverage: 17:256/259 of query aligns to 21:264/266 of O53561
- K135 (≠ R129) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 129:136, 25% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (≠ G136) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
Q13825 Methylglutaconyl-CoA hydratase, mitochondrial; 3-MG-CoA hydratase; AU-specific RNA-binding enoyl-CoA hydratase; AU-binding protein/enoyl-CoA hydratase; Itaconyl-CoA hydratase; EC 4.2.1.18; EC 4.2.1.56 from Homo sapiens (Human) (see 4 papers)
36% identity, 95% coverage: 14:258/259 of query aligns to 89:339/339 of Q13825
- K105 (≠ I30) mutation to N: Abolishes RNA-binding; when associated with E-109 and Q-113.
- 105:119 (vs. 30:44, 33% identical) RNA-binding
- K109 (= K34) mutation to E: Abolishes RNA-binding; when associated with N-105 and Q-113.
- K113 (≠ A38) mutation to Q: Abolishes RNA-binding; when associated with N-105 and E-109.
- A240 (≠ G165) to V: in MGCA1; decreased methylglutaconyl-CoA hydratase activity; dbSNP:rs769894315
Sites not aligning to the query:
- 1:67 modified: transit peptide, Mitochondrion
6tnmA E. Coli aerobic trifunctional enzyme subunit-alpha (see paper)
35% identity, 69% coverage: 14:193/259 of query aligns to 17:198/719 of 6tnmA
Sites not aligning to the query:
P21177 Fatty acid oxidation complex subunit alpha; EC 4.2.1.17; EC 5.1.2.3; EC 5.3.3.8; EC 1.1.1.35 from Escherichia coli (strain K12) (see 2 papers)
35% identity, 69% coverage: 14:193/259 of query aligns to 17:198/729 of P21177
- G116 (= G111) mutation to F: Absence of both enoyl-CoA hydratase and 3-hydroxyacyl-CoA epimerase activities. Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase is only slightly affected.
Sites not aligning to the query:
- 322 G→A: 10-fold increase in KM for NADH.
- 450 active site, For 3-hydroxyacyl-CoA dehydrogenase activity; mutation H->A,Q: Almost complete loss of 3-hydroxyacyl-CoA dehydrogenase activity.
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
35% identity, 94% coverage: 14:257/259 of query aligns to 10:244/245 of 6slaAAA
- active site: Q61 (≠ G65), L68 (≠ V83), N72 (≠ H87), A96 (≠ G111), S99 (≠ E114), A118 (≠ P133), F119 (≠ E134), L124 (≠ M139), P126 (= P141), N127 (≠ G142), A212 (= A225), G222 (≠ A235)
- 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 (= L25), A59 (= A63), Q61 (≠ G65), D62 (= D66), L63 (≠ I67), L68 (≠ V83), Y71 (≠ G86), A94 (≠ L109), G95 (= G110), A96 (≠ G111), F119 (≠ E134), I122 (≠ L137), L124 (≠ M139), N127 (≠ G142), F234 (= F247), K237 (= K250)
Q5LLW6 Methylthioacryloyl-CoA hydratase; EC 4.2.1.155 from Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi) (see paper)
33% identity, 92% coverage: 14:250/259 of query aligns to 21:258/267 of Q5LLW6
- K31 (= K24) binding 3-(methylsulfanyl)acryloyl-CoA
- R32 (≠ L25) binding 3-(methylsulfanyl)acryloyl-CoA
- A69 (= A63) binding 3-(methylsulfanyl)acryloyl-CoA
- L71 (≠ G65) binding 3-(methylsulfanyl)acryloyl-CoA
- L73 (vs. gap) binding 3-(methylsulfanyl)acryloyl-CoA
- G118 (= G111) binding 3-(methylsulfanyl)acryloyl-CoA
- E121 (= E114) active site, Nucleophile; mutation to A: Abolishes catalytic activity.
- E141 (= E134) active site, Proton acceptor; mutation to A: Abolishes catalytic activity.
- R144 (≠ L137) binding 3-(methylsulfanyl)acryloyl-CoA
- G149 (= G142) binding 3-(methylsulfanyl)acryloyl-CoA
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)
31% identity, 98% coverage: 2:256/259 of query aligns to 5:266/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
Query Sequence
>WP_106712562.1 NCBI__GCF_003010955.1:WP_106712562.1
MAEPRIEVTFAGPVATITVSRPEKLNAFDIDMLKDLSAACDTVEANLDVRVTILTGAGKA
FSAGGDINAWAAMTPNEFGHAWVRFGHRVFERLATLRMPLIAALNGHALGGGLELAAAAD
IRIAETQIRLGLPETGLGMVPGWSGTQRLVRRFGAQVVRRMALGGEIFSATEGLGLGLID
HVVETGAAVNAAQTHAERIAKRGPAAVEVAKLMIAVANGEDNGTAVEALGSILVAKTADL
KEGVSAFAEKREPVFKGEW
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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