SitesBLAST
Comparing WP_011383725.1 NCBI__GCF_000009985.1:WP_011383725.1 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)
34% identity, 99% coverage: 3:259/259 of query aligns to 4:259/259 of 5zaiC
- active site: A65 (= A65), F70 (= F70), S82 (≠ D84), R86 (= R88), G110 (= G112), E113 (= E115), P132 (= P134), E133 (≠ I135), I138 (≠ V140), P140 (≠ M142), G141 (≠ A143), A226 (≠ E228), F236 (≠ L236)
- binding coenzyme a: K24 (≠ R23), L25 (≠ M24), A63 (≠ P63), G64 (= G64), A65 (= A65), D66 (= D66), I67 (= I67), P132 (= P134), R166 (≠ I168), F248 (= F248), K251 (= K251)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
36% identity, 98% coverage: 3:257/259 of query aligns to 4:255/255 of 3q0jC
- active site: A65 (= A65), M70 (≠ F70), T80 (≠ D84), F84 (≠ R88), G108 (= G112), E111 (= E115), P130 (= P134), E131 (≠ I135), V136 (= V140), P138 (≠ M142), G139 (≠ A143), L224 (= L229), F234 (≠ L236)
- binding acetoacetyl-coenzyme a: Q23 (≠ D22), A24 (≠ R23), L25 (≠ M24), A27 (= A26), A63 (≠ P63), G64 (= G64), A65 (= A65), D66 (= D66), I67 (= I67), K68 (≠ E68), M70 (≠ F70), F84 (≠ R88), G107 (= G111), G108 (= G112), E111 (= E115), P130 (= P134), E131 (≠ I135), P138 (≠ M142), G139 (≠ A143), M140 (≠ Y144)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
36% identity, 98% coverage: 3:257/259 of query aligns to 4:255/255 of 3q0gC
- active site: A65 (= A65), M70 (≠ F70), T80 (≠ D84), F84 (≠ R88), G108 (= G112), E111 (= E115), P130 (= P134), E131 (≠ I135), V136 (= V140), P138 (≠ M142), G139 (≠ A143), L224 (= L229), F234 (≠ L236)
- binding coenzyme a: L25 (≠ M24), A63 (≠ P63), I67 (= I67), K68 (≠ E68), Y104 (≠ P108), P130 (= P134), E131 (≠ I135), L134 (≠ I138)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
36% identity, 98% coverage: 3:257/259 of query aligns to 3:254/256 of 3h81A
- active site: A64 (= A65), M69 (≠ F70), T79 (≠ D84), F83 (≠ R88), G107 (= G112), E110 (= E115), P129 (= P134), E130 (≠ I135), V135 (= V140), P137 (≠ M142), G138 (≠ A143), L223 (= L229), F233 (≠ L236)
- binding calcium ion: F233 (≠ L236), Q238 (≠ Y241)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
36% identity, 98% coverage: 3:257/259 of query aligns to 3:250/250 of 3q0gD
- active site: A64 (= A65), M69 (≠ F70), T75 (≠ D84), F79 (≠ R88), G103 (= G112), E106 (= E115), P125 (= P134), E126 (≠ I135), V131 (= V140), P133 (≠ M142), G134 (≠ A143), L219 (= L229), F229 (≠ L236)
- binding Butyryl Coenzyme A: F225 (= F235), F241 (= F248)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
31% identity, 95% coverage: 11:256/259 of query aligns to 13:258/261 of 5jbxB
- active site: A67 (= A65), R72 (≠ F70), L84 (≠ D84), R88 (= R88), G112 (= G112), E115 (= E115), T134 (≠ P134), E135 (≠ I135), I140 (≠ V140), P142 (≠ M142), G143 (≠ A143), A228 (≠ P223), L238 (= L236)
- binding coenzyme a: S24 (≠ D22), R25 (= R23), R26 (≠ M24), A28 (= A26), A65 (≠ P63), D68 (= D66), L69 (≠ I67), K70 (≠ E68), L110 (≠ V110), G111 (= G111), T134 (≠ P134), E135 (≠ I135), L138 (≠ I138), R168 (≠ I168)
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)
32% identity, 95% coverage: 12:257/259 of query aligns to 86:331/337 of Q8GYN9
Sites not aligning to the query:
- 20 H→V: Loss of peroxisomal targeting.
Q62651 Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial; EC 5.3.3.- from Rattus norvegicus (Rat) (see paper)
34% identity, 76% coverage: 10:207/259 of query aligns to 63:270/327 of Q62651
- D176 (≠ E115) mutation D->A,D: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- E196 (≠ I135) mutation E->D,Q: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- D204 (≠ A143) mutation D->A,N: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
29% identity, 96% coverage: 9:256/259 of query aligns to 11:255/258 of 1ey3A
- active site: A66 (= A65), M71 (≠ F70), S81 (≠ D84), L85 (≠ R88), G109 (= G112), E112 (= E115), P131 (= P134), E132 (≠ I135), T137 (≠ V140), P139 (≠ M142), G140 (≠ A143), K225 (≠ E228), F235 (≠ L236)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ D22), L26 (≠ M24), A28 (= A26), A64 (≠ P63), G65 (= G64), A66 (= A65), D67 (= D66), I68 (= I67), L85 (≠ R88), W88 (≠ L91), G109 (= G112), P131 (= P134), L135 (≠ I138), G140 (≠ A143)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
29% identity, 96% coverage: 9:256/259 of query aligns to 13:257/260 of 1dubA
- active site: A68 (= A65), M73 (≠ F70), S83 (≠ D84), L87 (≠ R88), G111 (= G112), E114 (= E115), P133 (= P134), E134 (≠ I135), T139 (≠ V140), P141 (≠ M142), G142 (≠ A143), K227 (≠ E228), F237 (≠ L236)
- binding acetoacetyl-coenzyme a: K26 (≠ D22), A27 (≠ R23), L28 (≠ M24), A30 (= A26), A66 (≠ P63), A68 (= A65), D69 (= D66), I70 (= I67), Y107 (≠ P108), G110 (= G111), G111 (= G112), E114 (= E115), P133 (= P134), E134 (≠ I135), L137 (≠ I138), G142 (≠ A143), F233 (≠ C232), F249 (= F248)
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)
29% identity, 96% coverage: 9:256/259 of query aligns to 43:287/290 of P14604
- E144 (= E115) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (≠ I135) 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
3t88A Crystal structure of escherichia coli menb in complex with substrate analogue, osb-ncoa (see paper)
30% identity, 95% coverage: 12:257/259 of query aligns to 29:275/281 of 3t88A
- active site: G82 (≠ A65), R87 (≠ F70), Y93 (≠ N76), H101 (≠ D84), L105 (≠ R88), G129 (= G112), V132 (≠ E115), G152 (≠ I135), S157 (≠ V140), D159 (≠ M142), G160 (≠ A143), A246 (≠ E228), Y254 (≠ L236)
- binding o-succinylbenzoyl-N-coenzyme A: Q39 (≠ D22), V40 (≠ R23), R41 (≠ M24), A43 (= A26), S80 (≠ P63), G81 (= G64), G82 (≠ A65), D83 (= D66), Q84 (≠ I67), K85 (≠ E68), Y93 (≠ N76), V104 (≠ M87), L105 (≠ R88), Y125 (≠ P108), G129 (= G112), T151 (≠ P134), V155 (≠ I138), F158 (≠ V141), D159 (≠ M142), T250 (≠ C232), Y254 (≠ L236), F266 (= F248), K269 (= K251)
4i42A E.Coli. 1,4-dihydroxy-2-naphthoyl coenzyme a synthase (ecmenb) in complex with 1-hydroxy-2-naphthoyl-coa (see paper)
30% identity, 95% coverage: 12:257/259 of query aligns to 33:279/285 of 4i42A
- active site: G86 (≠ A65), R91 (≠ F70), Y97 (≠ N76), H105 (≠ D84), L109 (≠ R88), G133 (= G112), V136 (≠ E115), G156 (≠ I135), S161 (≠ V140), D163 (≠ M142), G164 (≠ A143), A250 (≠ E228), Y258 (≠ L236)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (≠ R23), R45 (≠ M24), S84 (≠ P63), G85 (= G64), G86 (≠ A65), D87 (= D66), Q88 (≠ I67), K89 (≠ E68), Y97 (≠ N76), V108 (≠ M87), Y129 (≠ P108), G133 (= G112), T155 (≠ P134), S161 (≠ V140), T254 (≠ C232), F270 (= F248), K273 (= K251)
P0ABU0 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Escherichia coli (strain K12) (see 4 papers)
30% identity, 95% coverage: 12:257/259 of query aligns to 33:279/285 of P0ABU0
- R45 (≠ M24) binding in other chain
- SGGDQK 84:89 (≠ PGADIE 63:68) binding in other chain
- K89 (≠ E68) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- R91 (≠ F70) mutation to A: Loss of DHNA-CoA synthase activity.
- Y97 (≠ N76) binding in other chain; mutation to F: Loss of DHNA-CoA synthase activity.
- YSIGG 129:133 (≠ PCVGG 108:112) binding in other chain
- Q154 (≠ V133) 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 (≠ VPI 133:135) binding
- T155 (≠ P134) binding in other chain
- G156 (≠ I135) mutation to D: Loss of DHNA-CoA synthase activity.
- S161 (≠ V140) binding in other chain
- W184 (≠ L163) mutation to F: Reduces the specific DHNA-CoA synthase activity by 530-fold, whereas its affinity for hydrogencarbonate is reduced by 20-fold.
- Y258 (≠ L236) binding
- R267 (≠ L245) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- F270 (= F248) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- K273 (= K251) binding ; mutation to A: Impairs protein folding.
3t3wF Crystal structure of probable enoyl-coa hydratase from mycobacterium thermoresistibile (see paper)
36% identity, 76% coverage: 13:209/259 of query aligns to 14:206/248 of 3t3wF
- active site: H65 (≠ A65), D71 (= D71), S83 (≠ Y83), L87 (≠ M87), G111 (= G112), L114 (≠ E115), V134 (≠ I135), I139 (≠ V140), G140 (vs. gap), E143 (≠ M142)
- binding zinc ion: E82 (≠ A82), E143 (≠ M142)
Sites not aligning to the query:
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
29% identity, 96% coverage: 9:256/259 of query aligns to 12:251/254 of 2dubA
- active site: A67 (= A65), M72 (≠ F70), S82 (≠ K81), G105 (= G112), E108 (= E115), P127 (= P134), E128 (≠ I135), T133 (≠ V140), P135 (≠ M142), G136 (≠ A143), K221 (≠ E228), F231 (≠ L236)
- binding octanoyl-coenzyme a: K25 (≠ D22), A26 (≠ R23), L27 (≠ M24), A29 (= A26), A65 (≠ P63), A67 (= A65), D68 (= D66), I69 (= I67), K70 (≠ E68), G105 (= G112), E108 (= E115), P127 (= P134), E128 (≠ I135), G136 (≠ A143), A137 (≠ Y144)
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)
29% identity, 94% coverage: 13:256/259 of query aligns to 21:265/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
29% identity, 96% coverage: 9:256/259 of query aligns to 13:257/260 of 2hw5C
- active site: A68 (= A65), M73 (≠ F70), S83 (≠ D84), L87 (≠ R88), G111 (= G112), E114 (= E115), P133 (= P134), E134 (≠ I135), T139 (≠ V140), P141 (≠ M142), G142 (≠ A143), K227 (≠ E228), F237 (≠ L236)
- binding crotonyl coenzyme a: K26 (≠ D22), A27 (≠ R23), L28 (≠ M24), A30 (= A26), K62 (= K59), I70 (= I67), F109 (≠ V110)
Q7CQ56 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
29% identity, 95% coverage: 12:257/259 of query aligns to 33:279/285 of Q7CQ56
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
29% identity, 96% coverage: 9:256/259 of query aligns to 13:255/258 of 1mj3A
- active site: A68 (= A65), M73 (≠ F70), S83 (≠ E78), L85 (≠ A80), G109 (= G112), E112 (= E115), P131 (= P134), E132 (≠ I135), T137 (≠ V140), P139 (≠ M142), G140 (≠ A143), K225 (≠ E228), F235 (≠ L236)
- binding hexanoyl-coenzyme a: K26 (≠ D22), A27 (≠ R23), L28 (≠ M24), A30 (= A26), A66 (≠ P63), G67 (= G64), A68 (= A65), D69 (= D66), I70 (= I67), G109 (= G112), P131 (= P134), E132 (≠ I135), L135 (≠ I138), G140 (≠ A143)
Query Sequence
>WP_011383725.1 NCBI__GCF_000009985.1:WP_011383725.1
MSDVIQLVREGAIATVTLNRPDRMNALNLPMWRGLAEAFETISADRSIHVVILRGAGTKA
FAPGADIEEFDTLRANAEQAKAYDLVMRKALDTVRACPQPVIAAIWGPCVGGGLELACCC
DIRLSAKSGKFGVPINKISVVMAYPELAQIRRVAGPAAALEILLEGRIMDADEAAAKRLV
NRVVEDDAMDAEVAATAKRIAAGAPLANRWHKAFIARLDDPTPVSEAELDECYRFLDTKD
YAEGLAAFRAKRKPVFTAE
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