SitesBLAST
Comparing WP_027456806.1 NCBI__GCF_000519045.1:WP_027456806.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
59% identity, 99% coverage: 4:257/257 of query aligns to 4:256/256 of 3h81A
- active site: A64 (= A64), M69 (= M69), T79 (≠ K79), F83 (≠ I83), G107 (= G108), E110 (= E111), P129 (= P130), E130 (= E131), V135 (≠ T136), P137 (= P138), G138 (= G139), L223 (= L224), F233 (= F234)
- binding calcium ion: F233 (= F234), Q238 (= Q239)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
59% identity, 98% coverage: 4:254/257 of query aligns to 5:254/255 of 3q0jC
- active site: A65 (= A64), M70 (= M69), T80 (≠ K79), F84 (≠ I83), G108 (= G108), E111 (= E111), P130 (= P130), E131 (= E131), V136 (≠ T136), P138 (= P138), G139 (= G139), L224 (= L224), F234 (= F234)
- binding acetoacetyl-coenzyme a: Q23 (≠ E22), A24 (= A23), L25 (≠ M24), A27 (= A26), A63 (= A62), G64 (= G63), A65 (= A64), D66 (= D65), I67 (= I66), K68 (≠ G67), M70 (= M69), 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
59% identity, 98% coverage: 4:254/257 of query aligns to 5:254/255 of 3q0gC
- active site: A65 (= A64), M70 (= M69), T80 (≠ K79), F84 (≠ I83), G108 (= G108), E111 (= E111), P130 (= P130), E131 (= E131), V136 (≠ T136), P138 (= P138), G139 (= G139), L224 (= L224), F234 (= F234)
- binding coenzyme a: L25 (≠ M24), A63 (= A62), I67 (= I66), K68 (≠ G67), Y104 (≠ F104), P130 (= P130), E131 (= E131), L134 (= L134)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
59% identity, 98% coverage: 4:254/257 of query aligns to 4:249/250 of 3q0gD
- active site: A64 (= A64), M69 (= M69), T75 (≠ K79), F79 (≠ I83), G103 (= G108), E106 (= E111), P125 (= P130), E126 (= E131), V131 (≠ T136), P133 (= P138), G134 (= G139), L219 (= L224), F229 (= F234)
- binding Butyryl Coenzyme A: F225 (= F230), F241 (= F246)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
52% identity, 98% coverage: 5:255/257 of query aligns to 6:258/260 of 1dubA
- active site: A68 (= A64), M73 (= M69), S83 (≠ K79), L87 (≠ I83), G111 (= G108), E114 (= E111), P133 (= P130), E134 (= E131), T139 (= T136), P141 (= P138), G142 (= G139), K227 (≠ L224), F237 (= F234)
- binding acetoacetyl-coenzyme a: K26 (≠ E22), A27 (= A23), L28 (≠ M24), A30 (= A26), A66 (= A62), A68 (= A64), D69 (= D65), I70 (= I66), Y107 (≠ F104), G110 (= G107), G111 (= G108), E114 (= E111), P133 (= P130), E134 (= E131), L137 (= L134), G142 (= G139), F233 (= F230), F249 (= F246)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
52% identity, 98% coverage: 5:255/257 of query aligns to 4:256/258 of 1ey3A
- active site: A66 (= A64), M71 (= M69), S81 (≠ K79), L85 (≠ I83), G109 (= G108), E112 (= E111), P131 (= P130), E132 (= E131), T137 (= T136), P139 (= P138), G140 (= G139), K225 (≠ L224), F235 (= F234)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ E22), L26 (≠ M24), A28 (= A26), A64 (= A62), G65 (= G63), A66 (= A64), D67 (= D65), I68 (= I66), L85 (≠ I83), W88 (= W87), G109 (= G108), P131 (= P130), L135 (= L134), 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)
52% identity, 98% coverage: 5:255/257 of query aligns to 36:288/290 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)
52% identity, 98% coverage: 5:255/257 of query aligns to 5:252/254 of 2dubA
- active site: A67 (= A64), M72 (= M69), S82 (≠ K79), G105 (= G108), E108 (= E111), P127 (= P130), E128 (= E131), T133 (= T136), P135 (= P138), G136 (= G139), K221 (≠ L224), F231 (= F234)
- binding octanoyl-coenzyme a: K25 (≠ E22), A26 (= A23), L27 (≠ M24), A29 (= A26), A65 (= A62), A67 (= A64), D68 (= D65), I69 (= I66), K70 (≠ G67), 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)
52% identity, 98% coverage: 5:255/257 of query aligns to 6:256/258 of 1mj3A
- active site: A68 (= A64), M73 (= M69), S83 (≠ K79), L85 (≠ T84), G109 (= G108), E112 (= E111), P131 (= P130), E132 (= E131), T137 (= T136), P139 (= P138), G140 (= G139), K225 (≠ L224), F235 (= F234)
- binding hexanoyl-coenzyme a: K26 (≠ E22), A27 (= A23), L28 (≠ M24), A30 (= A26), A66 (= A62), G67 (= G63), A68 (= A64), D69 (= D65), I70 (= I66), G109 (= G108), P131 (= P130), E132 (= E131), L135 (= L134), G140 (= G139)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
50% identity, 98% coverage: 5:257/257 of query aligns to 6:260/260 of 2hw5C
- active site: A68 (= A64), M73 (= M69), S83 (≠ K79), L87 (≠ I83), G111 (= G108), E114 (= E111), P133 (= P130), E134 (= E131), T139 (= T136), P141 (= P138), G142 (= G139), K227 (≠ L224), F237 (= F234)
- binding crotonyl coenzyme a: K26 (≠ E22), A27 (= A23), L28 (≠ M24), A30 (= A26), K62 (= K58), I70 (= I66), F109 (≠ L106)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
42% identity, 98% coverage: 7:257/257 of query aligns to 8:259/259 of 5zaiC
- active site: A65 (= A64), F70 (≠ M69), S82 (≠ D81), R86 (= R85), G110 (= G108), E113 (= E111), P132 (= P130), E133 (= E131), I138 (≠ T136), P140 (= P138), G141 (= G139), A226 (≠ L224), F236 (= F234)
- binding coenzyme a: K24 (≠ A23), L25 (≠ M24), A63 (= A62), G64 (= G63), A65 (= A64), D66 (= D65), I67 (= I66), P132 (= P130), R166 (≠ M164), F248 (= F246), K251 (= K249)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
35% identity, 91% coverage: 25:257/257 of query aligns to 27:261/261 of 5jbxB
- active site: A67 (= A64), R72 (≠ M69), L84 (≠ T80), R88 (≠ T84), G112 (= G108), E115 (= E111), T134 (≠ P130), E135 (= E131), I140 (≠ T136), P142 (= P138), G143 (= G139), A228 (≠ L224), L238 (≠ F234)
- binding coenzyme a: A28 (= A26), A65 (= A62), D68 (= D65), L69 (≠ I66), K70 (≠ G67), L110 (= L106), G111 (= G107), T134 (≠ P130), E135 (= E131), L138 (= L134), R168 (≠ M164)
Sites not aligning to the query:
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
33% identity, 99% coverage: 4:257/257 of query aligns to 4:257/257 of 6slbAAA
- active site: Q64 (≠ A64), F69 (≠ M69), L80 (≠ T80), N84 (≠ T84), A108 (≠ G108), S111 (≠ E111), A130 (≠ P130), F131 (≠ E131), L136 (≠ T136), P138 (= P138), D139 (≠ G139), A224 (≠ L224), 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 (≠ K58), A62 (= A62), Q64 (≠ A64), D65 (= D65), L66 (≠ I66), Y76 (≠ H76), A108 (≠ G108), F131 (≠ E131), D139 (≠ G139)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
33% identity, 99% coverage: 4:257/257 of query aligns to 1:245/245 of 6slaAAA
- active site: Q61 (≠ A64), L68 (≠ T84), N72 (≠ E88), A96 (≠ G108), S99 (≠ E111), A118 (≠ P130), F119 (≠ E131), L124 (≠ T136), P126 (= P138), N127 (≠ G139), A212 (≠ L224), 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 (≠ M24), A59 (= A62), Q61 (≠ A64), D62 (= D65), L63 (≠ I66), L68 (≠ T84), Y71 (≠ W87), A94 (≠ L106), G95 (= G107), A96 (≠ G108), F119 (≠ E131), I122 (≠ L134), L124 (≠ T136), N127 (≠ G139), F234 (= F246), K237 (= K249)
3p85A Crystal structure enoyl-coa hydratase from mycobacterium avium (see paper)
33% identity, 87% coverage: 4:226/257 of query aligns to 2:210/224 of 3p85A
- active site: L62 (≠ A64), L67 (≠ M69), P68 (≠ K70), G92 (= G108), E95 (= E111), T114 (≠ P130), H115 (≠ E131), L120 (≠ T136), P122 (= P138), T123 (≠ G139), W208 (≠ L224)
- binding calcium ion: D43 (= D45), D45 (≠ N47)
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)
34% identity, 94% coverage: 15:255/257 of query aligns to 23:266/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
3t88A Crystal structure of escherichia coli menb in complex with substrate analogue, osb-ncoa (see paper)
32% identity, 93% coverage: 16:254/257 of query aligns to 33:274/281 of 3t88A
- active site: G82 (≠ A64), R87 (vs. gap), Y93 (≠ F68), H101 (= H76), L105 (≠ T80), G129 (= G108), V132 (≠ E111), G152 (≠ E131), S157 (≠ T136), D159 (≠ P138), G160 (= G139), A246 (vs. gap), Y254 (≠ F234)
- binding o-succinylbenzoyl-N-coenzyme A: Q39 (≠ E22), V40 (≠ A23), R41 (≠ M24), A43 (= A26), S80 (≠ A62), G81 (= G63), G82 (≠ A64), D83 (= D65), Q84 (≠ I66), K85 (vs. gap), Y93 (≠ F68), V104 (≠ K79), L105 (≠ T80), Y125 (≠ F104), G129 (= G108), T151 (≠ P130), V155 (≠ L134), F158 (≠ L137), D159 (≠ P138), T250 (≠ G222), Y254 (≠ F234), F266 (= F246), K269 (= K249)
4i42A E.Coli. 1,4-dihydroxy-2-naphthoyl coenzyme a synthase (ecmenb) in complex with 1-hydroxy-2-naphthoyl-coa (see paper)
32% identity, 93% coverage: 16:254/257 of query aligns to 37:278/285 of 4i42A
- active site: G86 (≠ A64), R91 (vs. gap), Y97 (≠ F68), H105 (= H76), L109 (≠ T80), G133 (= G108), V136 (≠ E111), G156 (≠ E131), S161 (≠ T136), D163 (≠ P138), G164 (= G139), A250 (vs. gap), Y258 (≠ F234)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (≠ A23), R45 (≠ M24), S84 (≠ A62), G85 (= G63), G86 (≠ A64), D87 (= D65), Q88 (≠ I66), K89 (vs. gap), Y97 (≠ F68), V108 (≠ K79), Y129 (≠ F104), G133 (= G108), T155 (≠ P130), S161 (≠ T136), T254 (≠ G222), F270 (= F246), K273 (= K249)
P0ABU0 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Escherichia coli (strain K12) (see 4 papers)
32% identity, 93% coverage: 16:254/257 of query aligns to 37:278/285 of P0ABU0
- R45 (≠ M24) binding in other chain
- SGGDQK 84:89 (≠ AGADI- 62:66) binding in other chain
- K89 (vs. gap) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- R91 (vs. gap) mutation to A: Loss of DHNA-CoA synthase activity.
- Y97 (≠ F68) binding in other chain; mutation to F: Loss of DHNA-CoA synthase activity.
- YSIGG 129:133 (≠ FALGG 104:108) binding in other chain
- Q154 (= Q129) mutation to A: Reduces the specific DHNA-CoA synthase activity by 15-fold, whereas its affinity for hydrogencarbonate is reduced by 36-fold.
- QTG 154:156 (≠ QPE 129:131) binding hydrogencarbonate
- T155 (≠ P130) binding in other chain
- G156 (≠ E131) mutation to D: Loss of DHNA-CoA synthase activity.
- S161 (≠ T136) binding in other chain
- W184 (≠ C159) mutation to F: Reduces the specific DHNA-CoA synthase activity by 530-fold, whereas its affinity for hydrogencarbonate is reduced by 20-fold.
- Y258 (≠ F234) binding substrate
- R267 (≠ M243) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- F270 (= F246) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- K273 (= K249) binding substrate; mutation to A: Impairs protein folding.
Q7CQ56 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
32% identity, 93% coverage: 16:254/257 of query aligns to 37:278/285 of Q7CQ56
Query Sequence
>WP_027456806.1 NCBI__GCF_000519045.1:WP_027456806.1
MSTVVLTEIHGRVGLIRINRPEAMNALNNEVVDGIGAAIDAFEADENIGCIVITGNEKAF
AAGADIGFMKDFDYLHAYKTDFITRNWERIKTARKPVIAAVSGFALGGGCEMAMMCDMIF
AADTAKFGQPEIRLGTLPGAGGTQRLPRAVGKAKAMDMCLSARMMDAPEAEKAGLVARIY
PADQLLDETLKAAQTIAGFSLPVVMMIKESVNRAFESSLNEGLLFERRVFHAAFAVEDQK
EGMAAFVEKRKPAFKHR
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