SitesBLAST
Comparing WP_011384970.1 NCBI__GCF_000009985.1:WP_011384970.1 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)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
35% identity, 94% coverage: 17:272/272 of query aligns to 9:257/257 of 6slbAAA
- active site: Q64 (≠ G73), F69 (≠ I78), L80 (≠ T94), N84 (≠ G98), A108 (= A122), S111 (≠ M125), A130 (≠ L144), F131 (= F145), L136 (= L150), P138 (≠ A153), D139 (= D154), A224 (≠ E239), G234 (≠ M249)
- 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 (≠ G67), A62 (≠ S71), Q64 (≠ G73), D65 (= D74), L66 (≠ V75), Y76 (≠ L90), A108 (= A122), F131 (= F145), D139 (= D154)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
35% identity, 94% coverage: 17:272/272 of query aligns to 6:245/245 of 6slaAAA
- active site: Q61 (≠ G73), L68 (= L90), N72 (≠ T94), A96 (= A122), S99 (≠ M125), A118 (≠ L144), F119 (= F145), L124 (= L150), P126 (≠ A153), N127 (≠ D154), A212 (≠ E239), G222 (≠ M249)
- 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 (≠ K33), A59 (≠ S71), Q61 (≠ G73), D62 (= D74), L63 (≠ V75), L68 (= L90), Y71 (≠ F93), A94 (= A120), G95 (= G121), A96 (= A122), F119 (= F145), I122 (≠ V148), L124 (= L150), N127 (≠ D154), F234 (= F261), K237 (= K264)
1jxzB Structure of the h90q mutant of 4-chlorobenzoyl-coenzyme a dehalogenase complexed with 4-hydroxybenzoyl-coenzyme a (product) (see paper)
31% identity, 83% coverage: 17:243/272 of query aligns to 8:234/269 of 1jxzB
- active site: C61 (= C70), F64 (≠ G73), I69 (= I78), A86 (vs. gap), Q90 (≠ T94), G113 (= G121), G114 (≠ A122), G117 (≠ M125), A136 (≠ L144), W137 (≠ F145), I142 (≠ L150), N144 (≠ A153), D145 (= D154), E230 (= E239)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ D31), H23 (≠ R32), R24 (≠ K33), A62 (≠ S71), F64 (≠ G73), Y65 (≠ D74), L66 (≠ V75), R67 (≠ H76), W89 (≠ F93), G113 (= G121), A136 (≠ L144), W137 (≠ F145), I142 (≠ L150), D145 (= D154), T146 (≠ M155)
- binding calcium ion: G49 (≠ K58), L202 (= L211), A203 (= A212), A205 (≠ G214), T207 (= T216), Q210 (≠ H219)
Sites not aligning to the query:
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
26% identity, 95% coverage: 14:272/272 of query aligns to 6:259/259 of 5zaiC
- active site: A65 (≠ G73), F70 (≠ L82), S82 (≠ T94), R86 (≠ G98), G110 (≠ A122), E113 (≠ M125), P132 (≠ L144), E133 (≠ F145), I138 (≠ L150), P140 (≠ A153), G141 (≠ D154), A226 (≠ E239), F236 (≠ M249)
- binding coenzyme a: K24 (≠ R32), L25 (≠ K33), A63 (≠ S71), G64 (= G72), A65 (≠ G73), D66 (= D74), I67 (≠ V75), P132 (≠ L144), R166 (≠ A179), F248 (= F261), K251 (= K264)
1nzyB 4-chlorobenzoyl coenzyme a dehalogenase from pseudomonas sp. Strain cbs-3 (see paper)
31% identity, 83% coverage: 17:243/272 of query aligns to 8:234/269 of 1nzyB
- active site: C61 (= C70), F64 (≠ G73), I69 (= I78), A86 (vs. gap), H90 (≠ T94), G114 (≠ A122), G117 (≠ M125), A136 (≠ L144), W137 (≠ F145), I142 (≠ L150), N144 (≠ A153), D145 (= D154), E230 (= E239)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ D31), H23 (≠ R32), R24 (≠ K33), A62 (≠ S71), F64 (≠ G73), Y65 (≠ D74), L66 (≠ V75), R67 (≠ H76), W89 (≠ F93), G113 (= G121), G114 (≠ A122), A136 (≠ L144), W137 (≠ F145), D145 (= D154), T146 (≠ M155)
- binding calcium ion: G49 (≠ K58), L202 (= L211), A203 (= A212), A205 (≠ G214), T207 (= T216), Q210 (≠ H219)
- binding phosphate ion: E57 (≠ G66), N108 (≠ D116), K188 (≠ P197), R192 (≠ L201)
Sites not aligning to the query:
A5JTM5 4-chlorobenzoyl coenzyme A dehalogenase; 4-CBA-CoA dehalogenase; 4-CBCoA dehalogenase; 4-chlorobenzoyl-CoA dehalogenase; EC 3.8.1.7 from Pseudomonas sp. (strain CBS-3) (see 7 papers)
30% identity, 83% coverage: 17:243/272 of query aligns to 8:234/269 of A5JTM5
- R24 (≠ K33) binding in other chain; mutation R->K,L: Does not strongly affect catalytic activity, but reduces substrate CoA binding.
- E34 (= E43) mutation to T: Forms inclusion bodies.
- E43 (≠ V52) mutation to A: No effect on catalytic activity.
- D45 (≠ A54) mutation to A: No effect on catalytic activity.
- D46 (= D55) mutation to A: No effect on catalytic activity.
- G63 (= G72) mutation G->A,I,P: Yields insoluble protein.
- F64 (≠ G73) mutation to A: 30-fold reduction in catalytic activity, substrate benzoyl group binding is unaffected.; mutation to L: Retains catalytic activity, but substrate benzoyl group binding is decreased.; mutation to P: Severely reduces catalytic activity. Arylated intermediate does not accumulate.
- Y65 (≠ D74) mutation to D: Catalytic activity is almost as efficient as wild type.
- R67 (≠ H76) mutation to K: Reduces substrate CoA binding.; mutation to L: Forms inclusion bodies.
- E68 (= E77) mutation to T: No effect on catalytic activity.
- H81 (≠ M87) mutation to Q: Loss of catalytic activity, substrate benzoyl group binding is not affected.
- F82 (≠ P88) mutation to L: Retains catalytic activity, but substrate benzoyl group binding is decreased.
- W89 (≠ F93) mutation to F: Retains catalytic activity, but substrate benzoyl group binding is decreased.; mutation to Y: Reduced activity and substrate benzoyl group binding.
- H90 (≠ T94) active site, Proton acceptor; mutation to Q: Complete loss of catalytic activity (PubMed:8718880, PubMed:9063883). Significantly reduced activity (PubMed:11695894). Substrate binding is not significantly affected. Reduced arylated intermediate formation.
- H94 (≠ G98) mutation to Q: No effect on catalytic activity.
- A112 (= A120) mutation to G: Yields insoluble protein.; mutation to S: Protein precipitates upon purification.; mutation to V: Catalytic activity is almost as efficient as wild type.
- G113 (= G121) mutation to A: Strongly reduced catalytic activity and substrate benzoyl group binding. Arylated intermediate does not accumulate.; mutation G->N,S: Strongly reduced catalytic activity. Arylated intermediate does not accumulate.; mutation to V: Protein precipitates upon purification.
- G114 (≠ A122) mutation to A: Strongly reduced catalytic activity and substrate benzoyl group binding.; mutation to P: Unstable.
- G115 (= G123) mutation G->L,N,S,V: Yields insoluble protein.
- D123 (= D131) mutation to T: No effect on catalytic activity.
- D129 (≠ A137) mutation to T: No effect on catalytic activity.
- W137 (≠ F145) mutation to F: Low catalytic activity, but KM unaffected (PubMed:8718880). Retains catalytic activity, but substrate benzoyl group binding is decreased (PubMed:9063883).
- D145 (= D154) active site, Nucleophile; mutation to A: Complete loss of catalytic activity, but not substrate binding.
- E163 (= E172) mutation to T: No effect on catalytic activity.
- E175 (= E184) mutation to D: No effect on catalytic activity.
- W179 (≠ V188) mutation to F: No effect on catalytic activity.
- H208 (≠ F217) mutation to Q: No effect on catalytic activity.
- R216 (≠ M225) mutation R->E,K,L: Yields insoluble protein.
- E232 (= E241) mutation E->A,N,Q,R: Yields insoluble protein.; mutation to D: Reduced catalytic activity, increased substrate binding.
Sites not aligning to the query:
- 257 R→K: Retains catalytic activity and substrate CoA binding.; R→L: Significantly reduces catalytic activity and substrate CoA binding.
Q9P4U9 Enoyl-CoA hydratase AKT3-1; AF-toxin biosynthesis protein 3-1; EC 4.2.1.17 from Alternaria alternata (Alternaria rot fungus) (Torula alternata) (see paper)
30% identity, 94% coverage: 15:270/272 of query aligns to 14:269/296 of Q9P4U9
Sites not aligning to the query:
- 294:296 Peroxisomal targeting signal type 1
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
30% identity, 95% coverage: 15:272/272 of query aligns to 6:261/261 of 5jbxB
- active site: A67 (≠ G73), R72 (≠ I78), L84 (= L91), R88 (= R95), G112 (≠ A122), E115 (≠ M125), T134 (≠ L144), E135 (≠ F145), I140 (≠ L150), P142 (≠ G152), G143 (≠ A153), A228 (≠ E239), L238 (≠ M249)
- binding coenzyme a: S24 (≠ D31), R25 (= R32), R26 (≠ K33), A28 (≠ P35), A65 (≠ S71), D68 (= D74), L69 (≠ V75), K70 (≠ H76), L110 (≠ A120), G111 (= G121), T134 (≠ L144), E135 (≠ F145), L138 (≠ V148), R168 (≠ A179)
3omeC Crystal structure of a probable enoyl-coa hydratase from mycobacterium smegmatis (see paper)
29% identity, 80% coverage: 12:228/272 of query aligns to 4:213/247 of 3omeC
- active site: H65 (≠ G73), E70 (≠ T83), A82 (≠ T94), L86 (≠ G98), G110 (≠ A122), L113 (≠ M125), V133 (≠ F145), I138 (≠ L150), G139 (≠ A151), E142 (≠ D154)
- binding zinc ion: E81 (vs. gap), E142 (≠ D154)
Sites not aligning to the query:
Q62651 Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial; EC 5.3.3.- from Rattus norvegicus (Rat) (see paper)
28% identity, 90% coverage: 22:265/272 of query aligns to 66:317/327 of Q62651
- D176 (≠ M125) mutation D->A,D: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- E196 (≠ F145) mutation E->D,Q: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- D204 (= D154) mutation D->A,N: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
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)
27% identity, 90% coverage: 25:269/272 of query aligns to 24:265/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
27% identity, 92% coverage: 19:269/272 of query aligns to 10:249/250 of 3q0gD
- active site: A64 (≠ G73), M69 (≠ I78), T75 (≠ K84), F79 (≠ R95), G103 (≠ A122), E106 (≠ M125), P125 (≠ L144), E126 (≠ F145), V131 (≠ L150), P133 (≠ G152), G134 (≠ A153), L219 (≠ E239), F229 (≠ M249)
- binding Butyryl Coenzyme A: F225 (≠ Q245), F241 (= F261)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
29% identity, 92% coverage: 19:269/272 of query aligns to 10:253/256 of 3h81A
- active site: A64 (≠ G73), M69 (≠ I78), T79 (≠ E89), F83 (= F93), G107 (≠ A122), E110 (≠ M125), P129 (≠ L144), E130 (≠ F145), V135 (≠ L150), P137 (≠ G152), G138 (≠ A153), L223 (≠ E239), F233 (≠ M249)
- binding calcium ion: F233 (≠ M249), Q238 (≠ F254)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
29% identity, 92% coverage: 19:269/272 of query aligns to 11:254/255 of 3q0jC
- active site: A65 (≠ G73), M70 (≠ I78), T80 (≠ E89), F84 (= F93), G108 (≠ A122), E111 (≠ M125), P130 (≠ L144), E131 (≠ F145), V136 (≠ L150), P138 (≠ G152), G139 (≠ A153), L224 (≠ E239), F234 (≠ M249)
- binding acetoacetyl-coenzyme a: Q23 (≠ D31), A24 (≠ R32), L25 (≠ K33), A27 (≠ P35), A63 (≠ S71), G64 (= G72), A65 (≠ G73), D66 (= D74), I67 (≠ V75), K68 (≠ H76), M70 (≠ I78), F84 (= F93), G107 (= G121), G108 (≠ A122), E111 (≠ M125), P130 (≠ L144), E131 (≠ F145), P138 (≠ G152), G139 (≠ A153), M140 (= M155)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
29% identity, 92% coverage: 19:269/272 of query aligns to 11:254/255 of 3q0gC
- active site: A65 (≠ G73), M70 (≠ I78), T80 (≠ E89), F84 (= F93), G108 (≠ A122), E111 (≠ M125), P130 (≠ L144), E131 (≠ F145), V136 (≠ L150), P138 (≠ G152), G139 (≠ A153), L224 (≠ E239), F234 (≠ M249)
- binding coenzyme a: L25 (≠ K33), A63 (≠ S71), I67 (≠ V75), K68 (≠ H76), Y104 (≠ I118), P130 (≠ L144), E131 (≠ F145), L134 (≠ V148)
3t3wF Crystal structure of probable enoyl-coa hydratase from mycobacterium thermoresistibile (see paper)
29% identity, 80% coverage: 12:228/272 of query aligns to 4:214/248 of 3t3wF
- active site: H65 (= H76), D71 (vs. gap), S83 (≠ F93), L87 (≠ T97), G111 (≠ A122), L114 (≠ M125), V134 (≠ F145), I139 (≠ L150), G140 (≠ A151), E143 (≠ D154)
- binding zinc ion: E82 (= E92), E143 (≠ D154)
Sites not aligning to the query:
P40939 Trifunctional enzyme subunit alpha, mitochondrial; 78 kDa gastrin-binding protein; Monolysocardiolipin acyltransferase; TP-alpha; EC 2.3.1.-; EC 4.2.1.17; EC 1.1.1.211 from Homo sapiens (Human) (see 5 papers)
24% identity, 85% coverage: 13:242/272 of query aligns to 40:272/763 of P40939
Sites not aligning to the query:
- 282 V → D: in MTPD1; mild phenotype with slowly progressive myopathy and sensorimotor polyneuropathy; dbSNP:rs137852773
- 305 I → N: in MTPD1; mild phenotype with slowly progressive myopathy and sensorimotor polyneuropathy; dbSNP:rs137852774
- 342 L → P: in LCHAD deficiency; dbSNP:rs137852772
- 510 active site, For hydroxyacyl-coenzyme A dehydrogenase activity; E → Q: in AFLP and LCHAD deficiency; loss of long-chain-3-hydroxyacyl-CoA dehydrogenase activity; dbSNP:rs137852769
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)
28% identity, 97% coverage: 8:272/272 of query aligns to 76:339/339 of Q13825
- K105 (≠ F38) mutation to N: Abolishes RNA-binding; when associated with E-109 and Q-113.
- 105:119 (vs. 38:52, 7% identical) RNA-binding
- K109 (≠ G42) mutation to E: Abolishes RNA-binding; when associated with N-105 and Q-113.
- K113 (≠ D46) mutation to Q: Abolishes RNA-binding; when associated with N-105 and E-109.
- A240 (≠ G177) to V: in MGCA1; decreased methylglutaconyl-CoA hydratase activity; dbSNP:rs769894315
Sites not aligning to the query:
- 1:67 modified: transit peptide, Mitochondrion
7borA Structure of pseudomonas aeruginosa coa-bound odaa (see paper)
31% identity, 59% coverage: 24:184/272 of query aligns to 14:166/247 of 7borA
- active site: N63 (≠ G73), F68 (≠ I78), D77 (= D86), G81 (= G98), I105 (≠ A122), T108 (≠ M125), F128 (= F145), L133 (= L150), P135 (≠ A153), E136 (≠ D154)
- binding coenzyme a: D21 (= D31), K22 (≠ R32), A25 (≠ P35), S61 (= S71), I65 (≠ V75), V103 (≠ A120), F128 (= F145), L131 (≠ V148)
Sites not aligning to the query:
3rrvB Crystal structure of an enoyl-coa hydratase/isomerase from mycobacterium paratuberculosis (see paper)
27% identity, 93% coverage: 13:265/272 of query aligns to 7:254/254 of 3rrvB
Query Sequence
>WP_011384970.1 NCBI__GCF_000009985.1:WP_011384970.1
MRKFKAAEYKAVHFDWKVDGKVATLTLNRPDRKNPLTFDSYGELRDLFENMVYADDVKAV
IVTGSGGNFCSGGDVHEIIGPLTKMDMPELLEFTRMTGDAVRAMRNAPQPIIAAIDGICA
GAGTMLGCASDIRLGTARSKVAFLFVRVGLAGADMGACTLLPRLIGLSRAAELLYTGRAM
GGEEAERVGYYNSLHAPEELLDAANKLAQSLANGPTFGHAMTKKMLWQEWNHGLGECIEA
EAQAQAICMQTKDFERAYVAFANKQAPVFEGN
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