SitesBLAST
Comparing WP_072904870.1 NCBI__GCF_900142125.1:WP_072904870.1 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)
46% identity, 100% coverage: 1:260/260 of query aligns to 1:259/259 of 5zaiC
- active site: A65 (≠ G66), F70 (≠ M71), S82 (≠ A83), R86 (≠ Q87), G110 (= G111), E113 (= E114), P132 (= P133), E133 (= E134), I138 (= I139), P140 (= P141), G141 (= G142), A226 (≠ S227), F236 (= F237)
- binding coenzyme a: K24 (≠ A24), L25 (= L25), A63 (= A64), G64 (= G65), A65 (≠ G66), D66 (= D67), I67 (= I68), P132 (= P133), R166 (≠ M167), F248 (= F249), K251 (= K252)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
45% identity, 99% coverage: 3:260/260 of query aligns to 2:256/256 of 3h81A
- active site: A64 (≠ G66), M69 (= M71), T79 (≠ K81), F83 (≠ K85), G107 (= G111), E110 (= E114), P129 (= P133), E130 (= E134), V135 (≠ I139), P137 (= P141), G138 (= G142), L223 (≠ S227), F233 (= F237)
- binding calcium ion: F233 (= F237), Q238 (= Q242)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
45% identity, 99% coverage: 1:257/260 of query aligns to 1:254/255 of 3q0jC
- active site: A65 (≠ G66), M70 (= M71), T80 (≠ K81), F84 (≠ K85), G108 (= G111), E111 (= E114), P130 (= P133), E131 (= E134), V136 (≠ I139), P138 (= P141), G139 (= G142), L224 (≠ S227), F234 (= F237)
- binding acetoacetyl-coenzyme a: Q23 (≠ K23), A24 (= A24), L25 (= L25), A27 (≠ S27), A63 (= A64), G64 (= G65), A65 (≠ G66), D66 (= D67), I67 (= I68), K68 (≠ S69), M70 (= M71), F84 (≠ K85), 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
45% identity, 99% coverage: 1:257/260 of query aligns to 1:254/255 of 3q0gC
- active site: A65 (≠ G66), M70 (= M71), T80 (≠ K81), F84 (≠ K85), G108 (= G111), E111 (= E114), P130 (= P133), E131 (= E134), V136 (≠ I139), P138 (= P141), G139 (= G142), L224 (≠ S227), F234 (= F237)
- binding coenzyme a: L25 (= L25), A63 (= A64), I67 (= I68), K68 (≠ S69), Y104 (= Y107), P130 (= P133), E131 (= E134), L134 (= L137)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
46% identity, 96% coverage: 12:260/260 of query aligns to 15:260/260 of 2hw5C
- active site: A68 (≠ G66), M73 (= M71), S83 (≠ A83), L87 (≠ Q87), G111 (= G111), E114 (= E114), P133 (= P133), E134 (= E134), T139 (≠ I139), P141 (= P141), G142 (= G142), K227 (≠ S227), F237 (= F237)
- binding crotonyl coenzyme a: K26 (= K23), A27 (= A24), L28 (= L25), A30 (≠ S27), K62 (= K60), I70 (= I68), F109 (≠ L109)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
46% identity, 96% coverage: 12:260/260 of query aligns to 14:254/254 of 2dubA
- active site: A67 (≠ G66), M72 (= M71), S82 (≠ Q88), G105 (= G111), E108 (= E114), P127 (= P133), E128 (= E134), T133 (≠ I139), P135 (= P141), G136 (= G142), K221 (≠ S227), F231 (= F237)
- binding octanoyl-coenzyme a: K25 (= K23), A26 (= A24), L27 (= L25), A29 (≠ S27), A65 (= A64), A67 (≠ G66), D68 (= D67), I69 (= I68), K70 (≠ S69), G105 (= G111), E108 (= E114), P127 (= P133), E128 (= E134), G136 (= G142), A137 (≠ W143)
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)
47% identity, 96% coverage: 12:260/260 of query aligns to 45:290/290 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
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
47% identity, 96% coverage: 12:260/260 of query aligns to 13:258/258 of 1ey3A
- active site: A66 (≠ G66), M71 (= M71), S81 (≠ A83), L85 (≠ Q87), G109 (= G111), E112 (= E114), P131 (= P133), E132 (= E134), T137 (≠ I139), P139 (= P141), G140 (= G142), K225 (≠ S227), F235 (= F237)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (= K23), L26 (= L25), A28 (≠ S27), A64 (= A64), G65 (= G65), A66 (≠ G66), D67 (= D67), I68 (= I68), L85 (≠ Q87), W88 (≠ F90), G109 (= G111), P131 (= P133), L135 (= L137), G140 (= G142)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
47% identity, 96% coverage: 12:260/260 of query aligns to 15:260/260 of 1dubA
- active site: A68 (≠ G66), M73 (= M71), S83 (≠ A83), L87 (≠ Q87), G111 (= G111), E114 (= E114), P133 (= P133), E134 (= E134), T139 (≠ I139), P141 (= P141), G142 (= G142), K227 (≠ S227), F237 (= F237)
- binding acetoacetyl-coenzyme a: K26 (= K23), A27 (= A24), L28 (= L25), A30 (≠ S27), A66 (= A64), A68 (≠ G66), D69 (= D67), I70 (= I68), Y107 (= Y107), G110 (= G110), G111 (= G111), E114 (= E114), P133 (= P133), E134 (= E134), L137 (= L137), G142 (= G142), F233 (= F233), F249 (= F249)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
44% identity, 98% coverage: 3:257/260 of query aligns to 2:249/250 of 3q0gD
- active site: A64 (≠ G66), M69 (= M77), T75 (≠ A83), F79 (≠ Q87), G103 (= G111), E106 (= E114), P125 (= P133), E126 (= E134), V131 (≠ I139), P133 (= P141), G134 (= G142), L219 (≠ S227), F229 (= F237)
- binding Butyryl Coenzyme A: F225 (= F233), F241 (= F249)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
46% identity, 96% coverage: 12:260/260 of query aligns to 15:258/258 of 1mj3A
- active site: A68 (≠ G66), M73 (= M71), S83 (≠ K85), L85 (≠ Q87), G109 (= G111), E112 (= E114), P131 (= P133), E132 (= E134), T137 (≠ I139), P139 (= P141), G140 (= G142), K225 (≠ S227), F235 (= F237)
- binding hexanoyl-coenzyme a: K26 (= K23), A27 (= A24), L28 (= L25), A30 (≠ S27), A66 (= A64), G67 (= G65), A68 (≠ G66), D69 (= D67), I70 (= I68), G109 (= G111), P131 (= P133), E132 (= E134), L135 (= L137), G140 (= G142)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
38% identity, 98% coverage: 6:260/260 of query aligns to 7:261/261 of 5jbxB
- active site: A67 (≠ G66), R72 (≠ M71), L84 (≠ A83), R88 (≠ Q87), G112 (= G111), E115 (= E114), T134 (≠ P133), E135 (= E134), I140 (= I139), P142 (= P141), G143 (= G142), A228 (≠ S227), L238 (≠ F237)
- binding coenzyme a: S24 (≠ K23), R25 (≠ A24), R26 (≠ L25), A28 (≠ S27), A65 (= A64), D68 (= D67), L69 (≠ I68), K70 (≠ S69), L110 (= L109), G111 (= G110), T134 (≠ P133), E135 (= E134), L138 (= L137), R168 (≠ M167)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
33% identity, 97% coverage: 9:260/260 of query aligns to 8:257/257 of 6slbAAA
- active site: Q64 (≠ G66), F69 (≠ M71), L80 (≠ A83), N84 (≠ Q87), A108 (≠ G111), S111 (≠ E114), A130 (≠ P133), F131 (≠ E134), L136 (≠ I139), P138 (= P141), D139 (≠ G142), A224 (≠ S227), G234 (≠ F237)
- 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 (≠ K60), A62 (= A64), Q64 (≠ G66), D65 (= D67), L66 (≠ I68), Y76 (≠ A79), A108 (≠ G111), F131 (≠ E134), D139 (≠ G142)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
32% identity, 97% coverage: 9:260/260 of query aligns to 5:245/245 of 6slaAAA
- active site: Q61 (≠ G66), L68 (≠ A83), N72 (≠ Q87), A96 (≠ G111), S99 (≠ E114), A118 (≠ P133), F119 (≠ E134), L124 (≠ I139), P126 (= P141), N127 (≠ G142), A212 (≠ S227), G222 (≠ F237)
- 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 (= A64), Q61 (≠ G66), D62 (= D67), L63 (≠ I68), L68 (≠ A83), Y71 (≠ A86), A94 (≠ L109), G95 (= G110), A96 (≠ G111), F119 (≠ E134), I122 (≠ L137), L124 (≠ I139), N127 (≠ G142), F234 (= F249), K237 (= K252)
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)
33% identity, 95% coverage: 13:258/260 of query aligns to 20:266/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
4elwA Structure of e. Coli. 1,4-dihydroxy-2- naphthoyl coenzyme a synthases (menb) in complex with nitrate (see paper)
33% identity, 98% coverage: 3:257/260 of query aligns to 19:260/267 of 4elwA
- active site: G83 (= G66), L91 (≠ M77), G115 (= G111), V118 (≠ E114), G138 (≠ E134), S143 (≠ I139), D145 (≠ P141), G146 (= G142), A232 (≠ F233), Y240 (≠ F237)
- binding nitrate ion: G114 (= G110), T137 (≠ P133), G138 (≠ E134), F144 (≠ I140), W166 (≠ M162)
4elxA Structure of apo e.Coli. 1,4-dihydroxy-2- naphthoyl coa synthases with cl (see paper)
33% identity, 98% coverage: 3:257/260 of query aligns to 19:261/268 of 4elxA
- active site: G83 (= G66), H88 (≠ P73), L92 (≠ M77), G116 (= G111), V119 (≠ E114), G139 (≠ E134), S144 (≠ I139), D146 (≠ P141), G147 (= G142), A233 (≠ F233), Y241 (≠ F237)
- binding chloride ion: G115 (= G110), G139 (≠ E134), W167 (≠ M162)
3t88A Crystal structure of escherichia coli menb in complex with substrate analogue, osb-ncoa (see paper)
33% identity, 98% coverage: 3:257/260 of query aligns to 18:274/281 of 3t88A
- active site: G82 (= G66), R87 (≠ M71), Y93 (≠ M77), H101 (≠ A83), L105 (≠ Q87), G129 (= G111), V132 (≠ E114), G152 (≠ E134), S157 (≠ I139), D159 (≠ P141), G160 (= G142), A246 (≠ F233), Y254 (≠ F237)
- binding o-succinylbenzoyl-N-coenzyme A: Q39 (≠ K23), V40 (≠ A24), R41 (≠ L25), A43 (≠ S27), S80 (≠ A64), G81 (= G65), G82 (= G66), D83 (= D67), Q84 (≠ I68), K85 (≠ S69), Y93 (≠ M77), V104 (≠ A86), L105 (≠ Q87), Y125 (= Y107), G129 (= G111), T151 (≠ P133), V155 (≠ L137), F158 (≠ I140), D159 (≠ P141), T250 (vs. gap), Y254 (≠ F237), F266 (= F249), K269 (= K252)
4i42A E.Coli. 1,4-dihydroxy-2-naphthoyl coenzyme a synthase (ecmenb) in complex with 1-hydroxy-2-naphthoyl-coa (see paper)
33% identity, 98% coverage: 3:257/260 of query aligns to 22:278/285 of 4i42A
- active site: G86 (= G66), R91 (≠ M71), Y97 (≠ M77), H105 (≠ A83), L109 (≠ Q87), G133 (= G111), V136 (≠ E114), G156 (≠ E134), S161 (≠ I139), D163 (≠ P141), G164 (= G142), A250 (≠ F233), Y258 (≠ F237)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (≠ A24), R45 (≠ L25), S84 (≠ A64), G85 (= G65), G86 (= G66), D87 (= D67), Q88 (≠ I68), K89 (≠ S69), Y97 (≠ M77), V108 (≠ A86), Y129 (= Y107), G133 (= G111), T155 (≠ P133), S161 (≠ I139), T254 (vs. gap), F270 (= F249), K273 (= K252)
P0ABU0 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Escherichia coli (strain K12) (see 4 papers)
33% identity, 98% coverage: 3:257/260 of query aligns to 22:278/285 of P0ABU0
- R45 (≠ L25) binding in other chain
- SGGDQK 84:89 (≠ AGGDIS 64:69) binding in other chain
- K89 (≠ S69) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- R91 (≠ M71) mutation to A: Loss of DHNA-CoA synthase activity.
- Y97 (≠ M77) binding in other chain; mutation to F: Loss of DHNA-CoA synthase activity.
- YSIGG 129:133 (≠ YALGG 107:111) binding in other chain
- Q154 (= Q132) 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 132:134) binding hydrogencarbonate
- T155 (≠ P133) binding in other chain
- G156 (≠ E134) mutation to D: Loss of DHNA-CoA synthase activity.
- S161 (≠ I139) binding in other chain
- W184 (≠ M162) mutation to F: Reduces the specific DHNA-CoA synthase activity by 530-fold, whereas its affinity for hydrogencarbonate is reduced by 20-fold.
- Y258 (≠ F237) binding substrate
- R267 (≠ M246) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- F270 (= F249) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- K273 (= K252) binding substrate; mutation to A: Impairs protein folding.
Query Sequence
>WP_072904870.1 NCBI__GCF_900142125.1:WP_072904870.1
MAYENLRIEIENNITLITIDRPKALNSLNMVTMDALSQAIADLQANTEVKVIILTGAGEK
AFVAGGDISAMQPLGPMDARKVAQKAQQLFNDIEYGKKVVIGAINGYALGGGCELAMACD
IRIASDNAKFGQPEIKLGIIPGWAGTQRLPRLIGKGKAKELMFTGDMISAEEAVQLGLAN
QVVAQSALIATAKQMAEKIAAMPQVAISLIKEAVNNGIEMESQKAFSYEAELFGLCFATE
DQKEGMGAFLEKRTPEWKDR
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