SitesBLAST
Comparing WP_083442176.1 NCBI__GCF_000969705.1:WP_083442176.1 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)
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
56% identity, 97% coverage: 8:268/268 of query aligns to 11:266/266 of O53561
- K135 (≠ I137) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 137:144, 38% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (≠ Q144) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
37% identity, 99% coverage: 5:268/268 of query aligns to 4:259/259 of 5zaiC
- active site: A65 (= A66), F70 (≠ M71), S82 (≠ T84), R86 (= R88), G110 (= G119), E113 (= E122), P132 (≠ T141), E133 (= E142), I138 (≠ L147), P140 (= P149), G141 (≠ L150), A226 (≠ Q235), F236 (= F245)
- binding coenzyme a: K24 (≠ V25), L25 (≠ R26), A63 (= A64), G64 (= G65), A65 (= A66), D66 (= D67), I67 (≠ L68), P132 (≠ T141), R166 (≠ H175), F248 (= F257), K251 (= K260)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
41% identity, 100% coverage: 2:268/268 of query aligns to 2:261/261 of 5jbxB
- active site: A67 (= A66), R72 (= R75), L84 (≠ T84), R88 (= R88), G112 (= G119), E115 (= E122), T134 (= T141), E135 (= E142), I140 (≠ L147), P142 (= P149), G143 (≠ L150), A228 (≠ Q235), L238 (≠ F245)
- binding coenzyme a: S24 (≠ E24), R25 (≠ V25), R26 (= R26), A28 (= A28), A65 (= A64), D68 (= D67), L69 (= L68), K70 (= K69), L110 (= L117), G111 (≠ A118), T134 (= T141), E135 (= E142), L138 (≠ R145), R168 (≠ H175)
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)
38% identity, 94% coverage: 14:266/268 of query aligns to 20:266/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
35% identity, 97% coverage: 6:266/268 of query aligns to 5:258/260 of 1dubA
- active site: A68 (= A66), M73 (= M71), S83 (≠ R88), L87 (≠ T92), G111 (= G119), E114 (= E122), P133 (≠ T141), E134 (= E142), T139 (≠ L147), P141 (= P149), G142 (≠ L150), K227 (≠ Q235), F237 (= F245)
- binding acetoacetyl-coenzyme a: K26 (≠ E24), A27 (≠ V25), L28 (≠ R26), A30 (= A28), A66 (= A64), A68 (= A66), D69 (= D67), I70 (≠ L68), Y107 (= Y115), G110 (≠ A118), G111 (= G119), E114 (= E122), P133 (≠ T141), E134 (= E142), L137 (≠ R145), G142 (≠ L150), F233 (≠ G241), F249 (= F257)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
35% identity, 97% coverage: 6:266/268 of query aligns to 3:256/258 of 1ey3A
- active site: A66 (= A66), M71 (= M71), S81 (≠ R88), L85 (≠ T92), G109 (= G119), E112 (= E122), P131 (≠ T141), E132 (= E142), T137 (≠ L147), P139 (= P149), G140 (≠ L150), K225 (≠ Q235), F235 (= F245)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ E24), L26 (≠ R26), A28 (= A28), A64 (= A64), G65 (= G65), A66 (= A66), D67 (= D67), I68 (≠ L68), L85 (≠ T92), W88 (≠ F95), G109 (= G119), P131 (≠ T141), L135 (≠ R145), G140 (≠ L150)
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, 97% coverage: 6:266/268 of query aligns to 35:288/290 of P14604
- E144 (= E122) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E142) 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
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
36% identity, 97% coverage: 6:266/268 of query aligns to 5:256/258 of 1mj3A
- active site: A68 (= A66), M73 (= M71), S83 (≠ T84), L85 (= L87), G109 (= G119), E112 (= E122), P131 (≠ T141), E132 (= E142), T137 (≠ L147), P139 (= P149), G140 (≠ L150), K225 (≠ Q235), F235 (= F245)
- binding hexanoyl-coenzyme a: K26 (≠ E24), A27 (≠ V25), L28 (≠ R26), A30 (= A28), A66 (= A64), G67 (= G65), A68 (= A66), D69 (= D67), I70 (≠ L68), G109 (= G119), P131 (≠ T141), E132 (= E142), L135 (≠ R145), G140 (≠ L150)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
35% identity, 97% coverage: 6:266/268 of query aligns to 4:252/254 of 2dubA
- active site: A67 (= A66), M72 (= M71), S82 (≠ T84), G105 (= G119), E108 (= E122), P127 (≠ T141), E128 (= E142), T133 (≠ L147), P135 (= P149), G136 (≠ L150), K221 (≠ Q235), F231 (= F245)
- binding octanoyl-coenzyme a: K25 (≠ E24), A26 (≠ V25), L27 (≠ R26), A29 (= A28), A65 (= A64), A67 (= A66), D68 (= D67), I69 (≠ L68), K70 (= K69), G105 (= G119), E108 (= E122), P127 (≠ T141), E128 (= E142), G136 (≠ L150), A137 (≠ G151)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
34% identity, 93% coverage: 18:266/268 of query aligns to 20:258/260 of 2hw5C
- active site: A68 (= A66), M73 (= M71), S83 (≠ R88), L87 (≠ T92), G111 (= G119), E114 (= E122), P133 (≠ T141), E134 (= E142), T139 (≠ L147), P141 (= P149), G142 (≠ L150), K227 (≠ Q235), F237 (= F245)
- binding crotonyl coenzyme a: K26 (≠ E24), A27 (≠ V25), L28 (≠ R26), A30 (= A28), K62 (≠ G60), I70 (≠ L68), F109 (≠ L117)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
34% identity, 97% coverage: 5:265/268 of query aligns to 3:249/250 of 3q0gD
- active site: A64 (= A66), M69 (= M71), T75 (= T84), F79 (= F95), G103 (= G119), E106 (= E122), P125 (≠ T141), E126 (= E142), V131 (≠ L147), P133 (= P149), G134 (≠ L150), L219 (≠ Q235), F229 (= F245)
- binding Butyryl Coenzyme A: F225 (≠ G241), F241 (= F257)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
34% identity, 98% coverage: 7:268/268 of query aligns to 5:256/256 of 3h81A
- active site: A64 (= A66), M69 (= M71), T79 (= T91), F83 (= F95), G107 (= G119), E110 (= E122), P129 (≠ T141), E130 (= E142), V135 (≠ L147), P137 (= P149), G138 (≠ L150), L223 (≠ Q235), F233 (= F245)
- binding calcium ion: F233 (= F245), Q238 (≠ A250)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
34% identity, 97% coverage: 5:265/268 of query aligns to 4:254/255 of 3q0jC
- active site: A65 (= A66), M70 (= M71), T80 (= T91), F84 (= F95), G108 (= G119), E111 (= E122), P130 (≠ T141), E131 (= E142), V136 (≠ L147), P138 (= P149), G139 (≠ L150), L224 (≠ Q235), F234 (= F245)
- binding acetoacetyl-coenzyme a: Q23 (≠ E24), A24 (≠ V25), L25 (≠ R26), A27 (= A28), A63 (= A64), G64 (= G65), A65 (= A66), D66 (= D67), I67 (≠ L68), K68 (= K69), M70 (= M71), F84 (= F95), G107 (≠ A118), G108 (= G119), E111 (= E122), P130 (≠ T141), E131 (= E142), P138 (= P149), G139 (≠ L150), M140 (≠ G151)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
34% identity, 97% coverage: 5:265/268 of query aligns to 4:254/255 of 3q0gC
- active site: A65 (= A66), M70 (= M71), T80 (= T91), F84 (= F95), G108 (= G119), E111 (= E122), P130 (≠ T141), E131 (= E142), V136 (≠ L147), P138 (= P149), G139 (≠ L150), L224 (≠ Q235), F234 (= F245)
- binding coenzyme a: L25 (≠ R26), A63 (= A64), I67 (≠ L68), K68 (= K69), Y104 (= Y115), P130 (≠ T141), E131 (= E142), L134 (≠ R145)
Q5HH38 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Staphylococcus aureus (strain COL) (see paper)
35% identity, 92% coverage: 18:263/268 of query aligns to 26:264/273 of Q5HH38
- R34 (= R26) binding in other chain
- SGGDQ 73:77 (≠ AGADL 64:68) binding in other chain
- S149 (≠ L147) binding in other chain
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
35% identity, 98% coverage: 7:268/268 of query aligns to 5:257/257 of 6slbAAA
- active site: Q64 (≠ A66), F69 (≠ G78), L80 (= L99), N84 (= N103), A108 (≠ G119), S111 (≠ E122), A130 (≠ T141), F131 (≠ E142), L136 (= L147), P138 (= P149), D139 (≠ L150), A224 (≠ Q235), G234 (≠ F245)
- 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 (≠ G60), A62 (= A64), Q64 (≠ A66), D65 (= D67), L66 (= L68), Y76 (≠ F95), A108 (≠ G119), F131 (≠ E142), D139 (≠ L150)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
34% identity, 98% coverage: 7:268/268 of query aligns to 2:245/245 of 6slaAAA
- active site: Q61 (≠ A66), L68 (≠ A73), N72 (≠ S77), A96 (≠ G119), S99 (≠ E122), A118 (≠ T141), F119 (≠ E142), L124 (= L147), P126 (= P149), N127 (≠ L150), A212 (≠ Q235), G222 (≠ F245)
- 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 (≠ R26), A59 (= A64), Q61 (≠ A66), D62 (= D67), L63 (= L68), L68 (≠ A73), Y71 (≠ T76), A94 (≠ L117), G95 (≠ A118), A96 (≠ G119), F119 (≠ E142), I122 (≠ R145), L124 (= L147), N127 (≠ L150), F234 (= F257), K237 (= K260)
2uzfA Crystal structure of staphylococcus aureus 1,4-dihydroxy-2-naphthoyl coa synthase (menb) in complex with acetoacetyl coa (see paper)
34% identity, 92% coverage: 18:263/268 of query aligns to 21:251/260 of 2uzfA
- active site: G70 (≠ A66), R80 (≠ T89), L84 (≠ T93), G108 (= G119), V111 (≠ E122), T130 (= T141), G131 (≠ E142), S136 (≠ L147), D138 (≠ P149), A139 (≠ L150), A225 (≠ L238), Y233 (≠ F245)
- binding acetoacetyl-coenzyme a: V28 (= V25), R29 (= R26), S68 (≠ A64), G69 (= G65), G70 (≠ A66), D71 (= D67), Y104 (= Y115), G108 (= G119)
Q5LLW6 Methylthioacryloyl-CoA hydratase; EC 4.2.1.155 from Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi) (see paper)
34% identity, 93% coverage: 12:260/268 of query aligns to 18:258/267 of Q5LLW6
- K31 (≠ V25) binding 3-(methylsulfanyl)acryloyl-CoA
- R32 (= R26) binding 3-(methylsulfanyl)acryloyl-CoA
- A69 (= A64) binding 3-(methylsulfanyl)acryloyl-CoA
- L71 (≠ A66) binding 3-(methylsulfanyl)acryloyl-CoA
- L73 (= L68) binding 3-(methylsulfanyl)acryloyl-CoA
- G118 (= G119) binding 3-(methylsulfanyl)acryloyl-CoA
- E121 (= E122) active site, Nucleophile; mutation to A: Abolishes catalytic activity.
- E141 (= E142) active site, Proton acceptor; mutation to A: Abolishes catalytic activity.
- R144 (= R145) binding 3-(methylsulfanyl)acryloyl-CoA
- G149 (≠ L150) binding 3-(methylsulfanyl)acryloyl-CoA
4izcB Crystal structure of dmdd e121a in complex with mta-coa (see paper)
33% identity, 93% coverage: 12:260/268 of query aligns to 17:257/266 of 4izcB
- active site: L70 (≠ A66), H75 (≠ A70), C89 (≠ G86), H93 (≠ R90), G117 (= G119), A120 (≠ E122), E140 (= E142), G148 (≠ L150), Y232 (≠ Q235)
- binding methylthioacryloyl-CoA: D29 (≠ E24), K30 (≠ V25), R31 (= R26), A33 (= A28), A68 (= A64), L70 (≠ A66), D71 (= D67), L72 (= L68), W92 (≠ T89), G117 (= G119), P139 (≠ T141), E140 (= E142), R143 (= R145), G148 (≠ L150)
Query Sequence
>WP_083442176.1 NCBI__GCF_000969705.1:WP_083442176.1
MPATDHVLTDLDGHVFTVTMNRPEVRNAWSAEMLTGLAEAWERIDEDEDIRVAILTGAGG
TFCAGADLKAMSASRTSGGDDGFTEGLRTRTTTPFEGMLRSRNVTKPLIAAVEGYALAGG
TEILQATDIRVASEAAIFGLTEVQRSLFPLGGSTVRLQRQVSYTRAMEILLLGEHLSAQE
ALEIGLVGRLVPEGTALDEARRLADRIARNGPLAVQAIKRSVRETADMTEADGLQRELEI
GMQVFGSEDAKEGARAFAEKRDPVYRGR
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