SitesBLAST
Comparing WP_086511946.1 NCBI__GCF_002151265.1:WP_086511946.1 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)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
62% identity, 100% coverage: 2:257/257 of query aligns to 2:256/256 of 3h81A
- active site: A64 (= A64), M69 (≠ I69), T79 (≠ L79), F83 (≠ I83), G107 (= G108), E110 (= E111), P129 (= P130), E130 (= E131), V135 (≠ T136), P137 (= P138), G138 (= G139), L223 (≠ R224), F233 (= F234)
- binding calcium ion: F233 (= F234), Q238 (= Q239)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
62% identity, 98% coverage: 2:254/257 of query aligns to 3:254/255 of 3q0jC
- active site: A65 (= A64), M70 (≠ I69), T80 (≠ L79), F84 (≠ I83), G108 (= G108), E111 (= E111), P130 (= P130), E131 (= E131), V136 (≠ T136), P138 (= P138), G139 (= G139), L224 (≠ R224), F234 (= F234)
- binding acetoacetyl-coenzyme a: Q23 (≠ D22), A24 (= A23), L25 (≠ H24), A27 (= A26), A63 (= A62), G64 (= G63), A65 (= A64), D66 (= D65), I67 (= I66), K68 (= K67), M70 (≠ I69), F84 (≠ I83), G107 (= G107), G108 (= G108), E111 (= E111), P130 (= P130), E131 (= E131), P138 (= P138), G139 (= G139), M140 (≠ A140)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
62% identity, 98% coverage: 2:254/257 of query aligns to 3:254/255 of 3q0gC
- active site: A65 (= A64), M70 (≠ I69), T80 (≠ L79), F84 (≠ I83), G108 (= G108), E111 (= E111), P130 (= P130), E131 (= E131), V136 (≠ T136), P138 (= P138), G139 (= G139), L224 (≠ R224), F234 (= F234)
- binding coenzyme a: L25 (≠ H24), A63 (= A62), I67 (= I66), K68 (= K67), Y104 (≠ M104), P130 (= P130), E131 (= E131), L134 (≠ V134)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
61% identity, 98% coverage: 2:254/257 of query aligns to 2:249/250 of 3q0gD
- active site: A64 (= A64), M69 (≠ I69), T75 (≠ L79), F79 (≠ I83), G103 (= G108), E106 (= E111), P125 (= P130), E126 (= E131), V131 (≠ T136), P133 (= P138), G134 (= G139), L219 (≠ R224), F229 (= F234)
- binding Butyryl Coenzyme A: F225 (≠ L230), F241 (= F246)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
54% identity, 96% coverage: 9:255/257 of query aligns to 13:258/260 of 1dubA
- active site: A68 (= A64), M73 (≠ I69), S83 (= S80), L87 (≠ T84), G111 (= G108), E114 (= E111), P133 (= P130), E134 (= E131), T139 (= T136), P141 (= P138), G142 (= G139), K227 (≠ R224), F237 (= F234)
- binding acetoacetyl-coenzyme a: K26 (≠ D22), A27 (= A23), L28 (≠ H24), A30 (= A26), A66 (= A62), A68 (= A64), D69 (= D65), I70 (= I66), Y107 (≠ M104), G110 (= G107), G111 (= G108), E114 (= E111), P133 (= P130), E134 (= E131), L137 (≠ V134), G142 (= G139), F233 (≠ L230), F249 (= F246)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
54% identity, 96% coverage: 9:255/257 of query aligns to 11:256/258 of 1ey3A
- active site: A66 (= A64), M71 (≠ I69), S81 (= S80), L85 (≠ T84), G109 (= G108), E112 (= E111), P131 (= P130), E132 (= E131), T137 (= T136), P139 (= P138), G140 (= G139), K225 (≠ R224), F235 (= F234)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ D22), L26 (≠ H24), A28 (= A26), A64 (= A62), G65 (= G63), A66 (= A64), D67 (= D65), I68 (= I66), L85 (≠ T84), W88 (= W87), G109 (= G108), P131 (= P130), L135 (≠ V134), G140 (= G139)
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)
54% identity, 96% coverage: 9:255/257 of query aligns to 43:288/290 of P14604
- E144 (= E111) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E131) 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
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
53% identity, 96% coverage: 9:255/257 of query aligns to 12:252/254 of 2dubA
- active site: A67 (= A64), M72 (≠ I69), S82 (= S85), G105 (= G108), E108 (= E111), P127 (= P130), E128 (= E131), T133 (= T136), P135 (= P138), G136 (= G139), K221 (≠ R224), F231 (= F234)
- binding octanoyl-coenzyme a: K25 (≠ D22), A26 (= A23), L27 (≠ H24), A29 (= A26), A65 (= A62), A67 (= A64), D68 (= D65), I69 (= I66), K70 (= K67), G105 (= G108), E108 (= E111), P127 (= P130), E128 (= E131), G136 (= G139), A137 (= A140)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
54% identity, 96% coverage: 9:255/257 of query aligns to 13:256/258 of 1mj3A
- active site: A68 (= A64), M73 (≠ I69), S83 (= S80), L85 (= L82), G109 (= G108), E112 (= E111), P131 (= P130), E132 (= E131), T137 (= T136), P139 (= P138), G140 (= G139), K225 (≠ R224), F235 (= F234)
- binding hexanoyl-coenzyme a: K26 (≠ D22), A27 (= A23), L28 (≠ H24), A30 (= A26), A66 (= A62), G67 (= G63), A68 (= A64), D69 (= D65), I70 (= I66), G109 (= G108), P131 (= P130), E132 (= E131), L135 (≠ V134), G140 (= G139)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
52% identity, 97% coverage: 9:257/257 of query aligns to 13:260/260 of 2hw5C
- active site: A68 (= A64), M73 (≠ I69), S83 (≠ L79), L87 (≠ I83), G111 (= G108), E114 (= E111), P133 (= P130), E134 (= E131), T139 (= T136), P141 (= P138), G142 (= G139), K227 (≠ R224), F237 (= F234)
- binding crotonyl coenzyme a: K26 (≠ D22), A27 (= A23), L28 (≠ H24), A30 (= A26), K62 (≠ R58), I70 (= I66), F109 (≠ L106)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
42% identity, 100% coverage: 2:257/257 of query aligns to 3:259/259 of 5zaiC
- active site: A65 (= A64), F70 (≠ I69), S82 (= S80), R86 (≠ T84), G110 (= G108), E113 (= E111), P132 (= P130), E133 (= E131), I138 (≠ T136), P140 (= P138), G141 (= G139), A226 (≠ R224), F236 (= F234)
- binding coenzyme a: K24 (≠ A23), L25 (≠ H24), A63 (= A62), G64 (= G63), A65 (= A64), D66 (= D65), I67 (= I66), P132 (= P130), R166 (≠ L164), F248 (= F246), K251 (= K249)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
37% identity, 98% coverage: 5:257/257 of query aligns to 7:261/261 of 5jbxB
- active site: A67 (= A64), R72 (≠ I69), L84 (≠ S80), R88 (≠ T84), G112 (= G108), E115 (= E111), T134 (≠ P130), E135 (= E131), I140 (≠ T136), P142 (= P138), G143 (= G139), A228 (≠ R224), L238 (≠ F234)
- binding coenzyme a: S24 (≠ D22), R25 (≠ A23), R26 (≠ H24), A28 (= A26), A65 (= A62), D68 (= D65), L69 (≠ I66), K70 (= K67), L110 (= L106), G111 (= G107), T134 (≠ P130), E135 (= E131), L138 (≠ V134), R168 (≠ L164)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
36% identity, 97% coverage: 8:257/257 of query aligns to 5:245/245 of 6slaAAA
- active site: Q61 (≠ A64), L68 (≠ S71), N72 (≠ S75), A96 (≠ G108), S99 (≠ E111), A118 (≠ P130), F119 (≠ E131), L124 (≠ T136), P126 (= P138), N127 (≠ G139), A212 (≠ R224), G222 (≠ F234)
- 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 (≠ H24), A59 (= A62), Q61 (≠ A64), D62 (= D65), L63 (≠ I66), L68 (≠ S71), Y71 (≠ F74), A94 (≠ L106), G95 (= G107), A96 (≠ G108), F119 (≠ E131), I122 (≠ V134), L124 (≠ T136), N127 (≠ G139), F234 (= F246), K237 (= K249)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
37% identity, 97% coverage: 8:257/257 of query aligns to 8:257/257 of 6slbAAA
- active site: Q64 (≠ A64), F69 (≠ I69), L80 (= L82), N84 (≠ D86), A108 (≠ G108), S111 (≠ E111), A130 (≠ P130), F131 (≠ E131), L136 (≠ T136), P138 (= P138), D139 (≠ G139), A224 (≠ R224), G234 (≠ F234)
- 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 (= R58), A62 (= A62), Q64 (≠ A64), D65 (= D65), L66 (≠ I66), Y76 (= Y78), A108 (≠ G108), F131 (≠ E131), D139 (≠ G139)
4i52A Scmenb im complex with 1-hydroxy-2-naphthoyl-coa (see paper)
36% identity, 98% coverage: 2:252/257 of query aligns to 9:266/275 of 4i52A
- active site: G77 (≠ A64), R82 (≠ T73), Y87 (= Y78), R95 (vs. gap), L99 (≠ S85), G123 (= G108), V126 (≠ E111), G146 (≠ E131), S151 (≠ T136), D153 (≠ P138), G154 (= G139), A240 (= A220), Y248 (≠ F234)
- binding 1-hydroxy-2-naphthoyl-CoA: H29 (≠ D22), K30 (≠ A23), R31 (≠ H24), A33 (= A26), S75 (≠ A62), G76 (= G63), G77 (≠ A64), D78 (= D65), Q79 (= Q70), L96 (= L82), V98 (≠ T84), Y119 (≠ M104), I121 (≠ L106), G123 (= G108), T145 (≠ P130), V149 (= V134), S151 (≠ T136), F152 (≠ L137)
4i4zA Synechocystis sp. Pcc 6803 1,4-dihydroxy-2-naphthoyl-coenzyme a synthase (menb) in complex with salicylyl-coa (see paper)
36% identity, 98% coverage: 2:252/257 of query aligns to 9:266/275 of 4i4zA
- active site: G77 (≠ A64), R82 (≠ T73), Y87 (= Y78), R95 (vs. gap), L99 (≠ S85), G123 (= G108), V126 (≠ E111), G146 (≠ E131), S151 (≠ T136), D153 (≠ P138), G154 (= G139), A240 (= A220), Y248 (≠ F234)
- binding Salicylyl CoA: H29 (≠ D22), K30 (≠ A23), R31 (≠ H24), S75 (≠ A62), G76 (= G63), G77 (≠ A64), D78 (= D65), Q79 (= Q70), Y87 (= Y78), V98 (≠ T84), G123 (= G108), T145 (≠ P130), V149 (= V134), S151 (≠ T136), F260 (= F246), K263 (= K249)
- binding bicarbonate ion: G122 (= G107), Q144 (= Q129), T145 (≠ P130), G146 (≠ E131), W174 (≠ C159)
4emlA Synechocystis sp. Pcc 6803 1,4-dihydroxy-2-naphthoyl-coenzyme a synthase (menb) in complex with bicarbonate (see paper)
36% identity, 98% coverage: 2:252/257 of query aligns to 9:252/261 of 4emlA
- active site: G77 (≠ A64), R81 (≠ E68), L85 (= L72), G109 (= G108), V112 (≠ E111), G132 (≠ E131), S137 (≠ T136), D139 (≠ P138), G140 (= G139), A226 (= A220), Y234 (≠ F234)
- binding bicarbonate ion: G108 (= G107), Q130 (= Q129), G132 (≠ E131), W160 (≠ C159)
- binding chloride ion: D184 (≠ E183), R185 (= R184), E187 (≠ L186), E188 (≠ D187)
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)
34% identity, 96% coverage: 10:255/257 of query aligns to 18:266/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
Q8GYN9 1,4-dihydroxy-2-naphthoyl-CoA synthase, peroxisomal; DHNS; Enoyl-CoA hydratase/isomerase D; ECHID; Naphthoate synthase; EC 4.1.3.36 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
34% identity, 94% coverage: 12:252/257 of query aligns to 86:328/337 of Q8GYN9
Sites not aligning to the query:
- 20 H→V: Loss of peroxisomal targeting.
4elwA Structure of e. Coli. 1,4-dihydroxy-2- naphthoyl coenzyme a synthases (menb) in complex with nitrate (see paper)
34% identity, 98% coverage: 2:252/257 of query aligns to 19:258/267 of 4elwA
- active site: G83 (≠ A64), L91 (= L72), G115 (= G108), V118 (≠ E111), G138 (≠ E131), S143 (≠ T136), D145 (≠ P138), G146 (= G139), A232 (= A220), Y240 (≠ F234)
- binding nitrate ion: G114 (= G107), T137 (≠ P130), G138 (≠ E131), F144 (≠ L137), W166 (≠ C159)
Query Sequence
>WP_086511946.1 NCBI__GCF_002151265.1:WP_086511946.1
MYENLQVERTGAVGVITLYRPDAHNALNGALMRELGCALRAFEQDDAIGAMVITGGERVF
AAGADIKEIQSLTFSETYLSDLITSDWEEVTRCRKPVIAAVAGMALGGGCELAMMCDLII
AADTARFGQPEIKVGTLPGAGGTQRLTRAIGKAKAMDLCLTGRLMAADEAERSGLVSRVV
PAERLLDEAMTAAAQVASMSAVAVRLNKEAVERAQETTLAEGVRFERRLLHASFATEDQK
EGMQAFIEKRPPVWRHR
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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