SitesBLAST
Comparing WP_040688932.1 NCBI__GCF_000341125.1:WP_040688932.1 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)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
43% identity, 95% coverage: 3:244/254 of query aligns to 4:249/255 of 3q0jC
- active site: A65 (= A67), M70 (= M72), T80 (≠ S84), F84 (≠ Q88), G108 (vs. gap), E111 (vs. gap), P130 (= P125), E131 (= E126), V136 (= V131), P138 (= P133), G139 (= G134), L224 (≠ E219), F234 (= F229)
- binding acetoacetyl-coenzyme a: Q23 (≠ K25), A24 (= A26), L25 (= L27), A27 (= A29), A63 (= A65), G64 (= G66), A65 (= A67), D66 (= D68), I67 (= I69), K68 (= K70), M70 (= M72), F84 (≠ Q88), G107 (vs. gap), G108 (vs. gap), E111 (vs. gap), P130 (= P125), E131 (= E126), P138 (= P133), G139 (= G134), M140 (≠ A135)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
43% identity, 95% coverage: 3:244/254 of query aligns to 4:249/255 of 3q0gC
- active site: A65 (= A67), M70 (= M72), T80 (≠ S84), F84 (≠ Q88), G108 (vs. gap), E111 (vs. gap), P130 (= P125), E131 (= E126), V136 (= V131), P138 (= P133), G139 (= G134), L224 (≠ E219), F234 (= F229)
- binding coenzyme a: L25 (= L27), A63 (= A65), I67 (= I69), K68 (= K70), Y104 (vs. gap), P130 (= P125), E131 (= E126), L134 (= L129)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
43% identity, 95% coverage: 3:244/254 of query aligns to 3:248/256 of 3h81A
- active site: A64 (= A67), M69 (= M72), T79 (≠ S84), F83 (≠ Q88), G107 (vs. gap), E110 (vs. gap), P129 (= P125), E130 (= E126), V135 (= V131), P137 (= P133), G138 (= G134), L223 (≠ E219), F233 (= F229)
- binding calcium ion: F233 (= F229), Q238 (= Q234)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
36% identity, 95% coverage: 3:244/254 of query aligns to 2:251/259 of 5zaiC
- active site: A65 (= A67), F70 (≠ M72), S82 (= S84), R86 (≠ Q88), G110 (vs. gap), E113 (vs. gap), P132 (= P125), E133 (= E126), I138 (≠ V131), P140 (= P133), G141 (= G134), A226 (≠ E219), F236 (= F229)
- binding coenzyme a: K24 (≠ A26), L25 (= L27), A63 (= A65), G64 (= G66), A65 (= A67), D66 (= D68), I67 (= I69), P132 (= P125), R166 (≠ H159), F248 (= F241), K251 (≠ Q244)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
37% identity, 95% coverage: 3:244/254 of query aligns to 2:250/258 of 1ey3A
- active site: A66 (= A67), M71 (= M72), S81 (= S84), L85 (≠ Q88), G109 (vs. gap), E112 (vs. gap), P131 (= P125), E132 (= E126), T137 (≠ V131), P139 (= P133), G140 (= G134), K225 (≠ E219), F235 (= F229)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (= K25), L26 (= L27), A28 (= A29), A64 (= A65), G65 (= G66), A66 (= A67), D67 (= D68), I68 (= I69), L85 (≠ Q88), W88 (≠ L91), G109 (vs. gap), P131 (= P125), L135 (= L129), G140 (= G134)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
37% identity, 95% coverage: 3:244/254 of query aligns to 4:252/260 of 1dubA
- active site: A68 (= A67), M73 (= M72), S83 (= S84), L87 (≠ Q88), G111 (vs. gap), E114 (vs. gap), P133 (= P125), E134 (= E126), T139 (≠ V131), P141 (= P133), G142 (= G134), K227 (≠ E219), F237 (= F229)
- binding acetoacetyl-coenzyme a: K26 (= K25), A27 (= A26), L28 (= L27), A30 (= A29), A66 (= A65), A68 (= A67), D69 (= D68), I70 (= I69), Y107 (vs. gap), G110 (vs. gap), G111 (vs. gap), E114 (vs. gap), P133 (= P125), E134 (= E126), L137 (= L129), G142 (= G134), F233 (= F225), F249 (= F241)
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)
37% identity, 95% coverage: 3:244/254 of query aligns to 34:282/290 of P14604
- E144 (vs. gap) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E126) 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)
38% identity, 95% coverage: 3:244/254 of query aligns to 4:250/258 of 1mj3A
- active site: A68 (= A67), M73 (= M72), S83 (= S84), L85 (= L87), G109 (vs. gap), E112 (vs. gap), P131 (= P125), E132 (= E126), T137 (≠ V131), P139 (= P133), G140 (= G134), K225 (≠ E219), F235 (= F229)
- binding hexanoyl-coenzyme a: K26 (= K25), A27 (= A26), L28 (= L27), A30 (= A29), A66 (= A65), G67 (= G66), A68 (= A67), D69 (= D68), I70 (= I69), G109 (vs. gap), P131 (= P125), E132 (= E126), L135 (= L129), G140 (= G134)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
41% identity, 95% coverage: 3:244/254 of query aligns to 3:244/250 of 3q0gD
- active site: A64 (= A67), M69 (= M72), T75 (= T92), F79 (vs. gap), G103 (vs. gap), E106 (vs. gap), P125 (= P125), E126 (= E126), V131 (= V131), P133 (= P133), G134 (= G134), L219 (≠ E219), F229 (= F229)
- binding Butyryl Coenzyme A: F225 (= F225), F241 (= F241)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
37% identity, 95% coverage: 3:244/254 of query aligns to 3:246/254 of 2dubA
- active site: A67 (= A67), M72 (= M72), S82 (= S84), G105 (vs. gap), E108 (vs. gap), P127 (= P125), E128 (= E126), T133 (≠ V131), P135 (= P133), G136 (= G134), K221 (≠ E219), F231 (= F229)
- binding octanoyl-coenzyme a: K25 (= K25), A26 (= A26), L27 (= L27), A29 (= A29), A65 (= A65), A67 (= A67), D68 (= D68), I69 (= I69), K70 (= K70), G105 (vs. gap), E108 (vs. gap), P127 (= P125), E128 (= E126), G136 (= G134), A137 (= A135)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
36% identity, 95% coverage: 3:244/254 of query aligns to 4:252/260 of 2hw5C
- active site: A68 (= A67), M73 (= M72), S83 (= S84), L87 (≠ Q88), G111 (vs. gap), E114 (vs. gap), P133 (= P125), E134 (= E126), T139 (≠ V131), P141 (= P133), G142 (= G134), K227 (≠ E219), F237 (= F229)
- binding crotonyl coenzyme a: K26 (= K25), A27 (= A26), L28 (= L27), A30 (= A29), K62 (≠ R61), I70 (= I69), F109 (vs. gap)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
35% identity, 96% coverage: 1:244/254 of query aligns to 4:253/261 of 5jbxB
- active site: A67 (= A67), R72 (≠ M72), L84 (≠ S84), R88 (≠ Q88), G112 (vs. gap), E115 (vs. gap), T134 (≠ P125), E135 (= E126), I140 (≠ V131), P142 (= P133), G143 (= G134), A228 (≠ E219), L238 (≠ F229)
- binding coenzyme a: S24 (≠ K25), R25 (≠ A26), R26 (≠ L27), A28 (= A29), A65 (= A65), D68 (= D68), L69 (≠ I69), K70 (= K70), L110 (vs. gap), G111 (vs. gap), T134 (≠ P125), E135 (= E126), L138 (= L129), R168 (≠ H159)
Q13825 Methylglutaconyl-CoA hydratase, mitochondrial; 3-MG-CoA hydratase; AU-specific RNA-binding enoyl-CoA hydratase; AU-binding protein/enoyl-CoA hydratase; Itaconyl-CoA hydratase; EC 4.2.1.18; EC 4.2.1.56 from Homo sapiens (Human) (see 4 papers)
34% identity, 93% coverage: 10:246/254 of query aligns to 83:333/339 of Q13825
- K105 (≠ A32) mutation to N: Abolishes RNA-binding; when associated with E-109 and Q-113.
- 105:119 (vs. 32:46, 7% identical) RNA-binding
- K109 (≠ R36) mutation to E: Abolishes RNA-binding; when associated with N-105 and Q-113.
- K113 (≠ E40) mutation to Q: Abolishes RNA-binding; when associated with N-105 and E-109.
- A240 (≠ G157) to V: in MGCA1; decreased methylglutaconyl-CoA hydratase activity; dbSNP:rs769894315
Sites not aligning to the query:
- 1:67 modified: transit peptide, Mitochondrion
Q08426 Peroxisomal bifunctional enzyme; PBE; PBFE; L-bifunctional protein; LBP; Multifunctional enzyme 1; MFE1; EC 4.2.1.17; EC 5.3.3.8; EC 1.1.1.35 from Homo sapiens (Human) (see 5 papers)
38% identity, 71% coverage: 1:180/254 of query aligns to 1:178/723 of Q08426
- E3 (= E3) to K: in FRTS3; the mutant is mistargeted to mitochondria; results in impaired mitochondrial oxidative phosphorylation and defects in the transport of fluids across the epithelium of renal proximal tubular cells; dbSNP:rs398124646
- V40 (≠ S46) to G: in dbSNP:rs1062551
- I41 (≠ T47) to R: in dbSNP:rs1062552
- T75 (≠ G86) to I: in dbSNP:rs1062553
- K165 (≠ E167) modified: N6-acetyllysine; alternate; mutation to Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-171; Q-346 and Q-584.
- K171 (≠ E173) modified: N6-acetyllysine; mutation to Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-346 and Q-584.
Sites not aligning to the query:
- 274 A → T: in dbSNP:rs2302819
- 325 A → G: in dbSNP:rs1062555
- 346 modified: N6-acetyllysine; K→Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-171 and Q-584.
- 584 modified: N6-acetyllysine; alternate; K→Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-171 and Q-346.
- 598 K → T: in dbSNP:rs1042437
- 606 T → P: in dbSNP:rs1042438
6z5oAAA Peroxisomal bifunctional enzyme (see paper)
36% identity, 71% coverage: 1:180/254 of query aligns to 7:183/716 of 6z5oAAA
- active site: A67 (= A67), F72 (≠ M72), G82 (≠ Q88), G106 (vs. gap), E109 (vs. gap), P128 (= P125), E129 (= E126), G137 (= G134)
- binding coenzyme a: P26 (≠ A26), V27 (≠ L27), A65 (= A65), D68 (= D68), I69 (= I69), P128 (= P125), Y162 (≠ H159)
- binding nicotinamide: A67 (= A67), E109 (vs. gap), E129 (= E126), P136 (= P133)
Sites not aligning to the query:
- active site: 255, 409, 430, 442, 480
- binding coenzyme a: 277, 281
- binding nicotinamide-adenine-dinucleotide: 309, 311, 312, 313, 332, 333, 337, 379, 380, 381, 382, 387, 407, 409, 430
- binding nicotinamide: 261
6zibAAA structure of rat peroxisomal multifunctional enzyme type-1 (rpmfe1) complexed with acetoacetyl-coa and nadh' (see paper)
36% identity, 71% coverage: 1:180/254 of query aligns to 6:182/723 of 6zibAAA
- active site: A66 (= A67), F71 (≠ M72), G81 (≠ Q88), G105 (vs. gap), E108 (vs. gap), P127 (= P125), E128 (= E126), G136 (= G134)
- binding acetoacetyl-coenzyme a: P25 (≠ A26), V26 (≠ L27), A64 (= A65), G65 (= G66), A66 (= A67), D67 (= D68), I68 (= I69), G104 (vs. gap), G105 (vs. gap), E128 (= E126), Y161 (≠ H159)
Sites not aligning to the query:
- active site: 254, 413, 434, 446, 484
- binding 1,4-dihydronicotinamide adenine dinucleotide: 310, 311, 312, 331, 332, 336, 383, 384, 385, 386, 411, 434
5omoA Crystal structure of rat peroxisomal multifunctional enzyme type-1 (rpmfe1) complexed with with 3s-hydroxy-decanoyl-coa and 3-keto- decanoyl-coa
36% identity, 71% coverage: 1:180/254 of query aligns to 6:182/725 of 5omoA
- active site: A66 (= A67), F71 (≠ M72), G81 (≠ Q88), G105 (vs. gap), E108 (vs. gap), P127 (= P125), E128 (= E126), P135 (= P133), G136 (= G134)
- binding (s)-3-hydroxydecanoyl-coa: P25 (≠ A26), V26 (≠ L27), A28 (= A29), P31 (≠ A32), A64 (= A65), A66 (= A67), D67 (= D68), I68 (= I69), L103 (vs. gap), G105 (vs. gap), E108 (vs. gap), P127 (= P125), E128 (= E126), Y161 (≠ H159)
Sites not aligning to the query:
- active site: 254, 415, 436, 448, 486
- binding (s)-3-hydroxydecanoyl-coa: 260, 280
- binding 3-keto-decanoyl-coa: 415, 486, 519, 520, 525, 658
5mgbA Crystal structure of rat peroxisomal multifunctional enzyme type-1 (rpmfe1) complexed with acetoacetyl-coa and NAD (see paper)
36% identity, 71% coverage: 1:180/254 of query aligns to 6:182/725 of 5mgbA
- active site: A66 (= A67), F71 (≠ M72), G81 (≠ Q88), G105 (vs. gap), E108 (vs. gap), P127 (= P125), E128 (= E126), P135 (= P133), G136 (= G134)
- binding acetoacetyl-coenzyme a: P25 (≠ A26), V26 (≠ L27), A64 (= A65), G65 (= G66), A66 (= A67), D67 (= D68), I68 (= I69), G105 (vs. gap), E128 (= E126), Y161 (≠ H159)
Sites not aligning to the query:
- active site: 254, 415, 436, 448, 486
- binding nicotinamide-adenine-dinucleotide: 307, 308, 310, 311, 312, 331, 332, 336, 386, 387, 388, 413, 415, 436
3zwcA Crystal structure of rat peroxisomal multifunctional enzyme type 1 (rpmfe1) complexed with 3s-hydroxy-decanoyl-coa (see paper)
36% identity, 71% coverage: 1:180/254 of query aligns to 6:182/725 of 3zwcA
- active site: A66 (= A67), F71 (≠ M72), G81 (≠ Q88), G105 (vs. gap), E108 (vs. gap), P127 (= P125), E128 (= E126), P135 (= P133), G136 (= G134)
- binding (s)-3-hydroxydecanoyl-coa: V26 (≠ L27), A64 (= A65), G65 (= G66), A66 (= A67), D67 (= D68), I68 (= I69), G77 (≠ A78), L78 (≠ Q79), L80 (= L87), V101 (vs. gap), G104 (vs. gap), G105 (vs. gap), E108 (vs. gap), E128 (= E126)
Sites not aligning to the query:
- active site: 254, 415, 436, 448, 486
- binding (s)-3-hydroxydecanoyl-coa: 260
- binding nicotinamide-adenine-dinucleotide: 308, 310, 311, 312, 331, 336, 385, 386, 387, 388, 393, 413, 415, 436
2x58A The crystal structure of mfe1 liganded with coa (see paper)
36% identity, 71% coverage: 1:180/254 of query aligns to 6:182/725 of 2x58A
- active site: A66 (= A67), F71 (≠ M72), G81 (≠ Q88), G105 (vs. gap), E108 (vs. gap), P127 (= P125), E128 (= E126), P135 (= P133), G136 (= G134)
- binding coenzyme a: V26 (≠ L27), A28 (= A29), A64 (= A65), A66 (= A67), D67 (= D68), I68 (= I69), E128 (= E126)
Sites not aligning to the query:
- active site: 254, 415, 436, 448, 486
- binding adenosine-5'-diphosphate: 310, 311, 312, 331, 332, 336, 386, 392
Query Sequence
>WP_040688932.1 NCBI__GCF_000341125.1:WP_040688932.1
MGEFVRVETDKEHPAVAVIRVDRPKALNALNAQVTREIAEAAAEVSTDAAVRSVVLYGGE
RAFVAGADIKEMAHLTHAQMLEYSRGLQNALTAVARIPKPVVAAVXXALAADFRVAGAKA
KLGLPEITLGVIPGAGGTQRLPRLIGPAKAKDLIFTGRHVPAGEALEIGLVDEVVADEEV
YSAAVAKVARFGEGPAVALAAAKETVDRGLETDLDSGLEIERLHFAGLFATEDQKTGMRS
FIEQGPGKAEFSGR
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