SitesBLAST
Comparing WP_011384972.1 NCBI__GCF_000009985.1:WP_011384972.1 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)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
37% identity, 100% coverage: 1:255/255 of query aligns to 1:251/259 of 5zaiC
- active site: A65 (= A64), F70 (≠ M69), S82 (≠ V86), R86 (≠ Q90), G110 (= G114), E113 (= E117), P132 (= P136), E133 (= E137), I138 (≠ L142), P140 (= P144), G141 (= G145), A226 (≠ E229), F236 (≠ L240)
- binding coenzyme a: K24 (≠ P23), L25 (≠ V24), A63 (= A62), G64 (= G63), A65 (= A64), D66 (= D65), I67 (≠ L66), P132 (= P136), R166 (≠ I170), F248 (= F252), K251 (= K255)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
41% identity, 82% coverage: 11:218/255 of query aligns to 12:216/261 of 5jbxB
- active site: A67 (= A64), R72 (= R70), L84 (≠ V86), R88 (≠ Q90), G112 (= G114), E115 (= E117), T134 (≠ P136), E135 (= E137), I140 (≠ L142), P142 (= P144), G143 (= G145)
- binding coenzyme a: S24 (≠ P22), R25 (≠ P23), R26 (≠ V24), A28 (= A26), A65 (= A62), D68 (= D65), L69 (= L66), K70 (≠ A67), L110 (≠ M112), G111 (= G113), T134 (≠ P136), E135 (= E137), L138 (= L140), R168 (≠ I170)
Sites not aligning to the query:
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
34% identity, 87% coverage: 2:222/255 of query aligns to 2:219/260 of 2hw5C
- active site: A68 (= A64), M73 (= M69), S83 (≠ D80), L87 (≠ A84), G111 (= G114), E114 (= E117), P133 (= P136), E134 (= E137), T139 (≠ L142), P141 (= P144), G142 (= G145)
- binding crotonyl coenzyme a: K26 (≠ P23), A27 (vs. gap), L28 (≠ V24), A30 (= A26), K62 (= K58), I70 (≠ L66), F109 (≠ M112)
Sites not aligning to the query:
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
32% identity, 87% coverage: 2:222/255 of query aligns to 1:213/254 of 2dubA
- active site: A67 (= A64), M72 (= M69), S82 (≠ N91), G105 (= G114), E108 (= E117), P127 (= P136), E128 (= E137), T133 (≠ L142), P135 (= P144), G136 (= G145)
- binding octanoyl-coenzyme a: K25 (≠ P23), A26 (vs. gap), L27 (≠ V24), A29 (= A26), A65 (= A62), A67 (= A64), D68 (= D65), I69 (≠ L66), K70 (≠ A67), G105 (= G114), E108 (= E117), P127 (= P136), E128 (= E137), G136 (= G145), A137 (= A146)
Sites not aligning to the query:
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
33% identity, 87% coverage: 2:222/255 of query aligns to 2:219/260 of 1dubA
- active site: A68 (= A64), M73 (= M69), S83 (≠ D80), L87 (≠ A84), G111 (= G114), E114 (= E117), P133 (= P136), E134 (= E137), T139 (≠ L142), P141 (= P144), G142 (= G145)
- binding acetoacetyl-coenzyme a: K26 (≠ P23), A27 (vs. gap), L28 (≠ V24), A30 (= A26), A66 (= A62), A68 (= A64), D69 (= D65), I70 (≠ L66), Y107 (≠ A110), G110 (= G113), G111 (= G114), E114 (= E117), P133 (= P136), E134 (= E137), L137 (= L140), G142 (= G145)
Sites not aligning to the query:
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
33% identity, 86% coverage: 3:222/255 of query aligns to 1:217/258 of 1ey3A
- active site: A66 (= A64), M71 (= M69), S81 (≠ D80), L85 (≠ A84), G109 (= G114), E112 (= E117), P131 (= P136), E132 (= E137), T137 (≠ L142), P139 (= P144), G140 (= G145)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ P23), L26 (≠ V24), A28 (= A26), A64 (= A62), G65 (= G63), A66 (= A64), D67 (= D65), I68 (≠ L66), L85 (≠ A84), W88 (≠ R87), G109 (= G114), P131 (= P136), L135 (= L140), G140 (= G145)
Sites not aligning to the query:
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)
33% identity, 87% coverage: 2:222/255 of query aligns to 32:249/290 of P14604
- E144 (= E117) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E137) 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)
33% identity, 87% coverage: 2:222/255 of query aligns to 2:217/258 of 1mj3A
- active site: A68 (= A64), M73 (= M69), S83 (≠ I83), L85 (≠ F85), G109 (= G114), E112 (= E117), P131 (= P136), E132 (= E137), T137 (≠ L142), P139 (= P144), G140 (= G145)
- binding hexanoyl-coenzyme a: K26 (≠ P23), A27 (vs. gap), L28 (≠ V24), A30 (= A26), A66 (= A62), G67 (= G63), A68 (= A64), D69 (= D65), I70 (≠ L66), G109 (= G114), P131 (= P136), E132 (= E137), L135 (= L140), G140 (= G145)
Sites not aligning to the query:
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
32% identity, 100% coverage: 1:255/255 of query aligns to 1:249/255 of 3q0jC
- active site: A65 (= A64), M70 (= M69), T80 (≠ V86), F84 (≠ Q90), G108 (= G114), E111 (= E117), P130 (= P136), E131 (= E137), V136 (≠ L142), P138 (= P144), G139 (= G145), L224 (≠ T233), F234 (≠ P243)
- binding acetoacetyl-coenzyme a: Q23 (≠ P23), A24 (vs. gap), L25 (≠ V24), A27 (= A26), A63 (= A62), G64 (= G63), A65 (= A64), D66 (= D65), I67 (≠ L66), K68 (≠ A67), M70 (= M69), F84 (≠ Q90), G107 (= G113), G108 (= G114), E111 (= E117), P130 (= P136), E131 (= E137), P138 (= P144), G139 (= G145), M140 (≠ A146)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
32% identity, 100% coverage: 1:255/255 of query aligns to 1:249/255 of 3q0gC
- active site: A65 (= A64), M70 (= M69), T80 (≠ V86), F84 (≠ Q90), G108 (= G114), E111 (= E117), P130 (= P136), E131 (= E137), V136 (≠ L142), P138 (= P144), G139 (= G145), L224 (≠ T233), F234 (≠ P243)
- binding coenzyme a: L25 (≠ V24), A63 (= A62), I67 (≠ L66), K68 (≠ A67), Y104 (≠ A110), P130 (= P136), E131 (= E137), L134 (= L140)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
32% identity, 100% coverage: 2:255/255 of query aligns to 1:248/256 of 3h81A
- active site: A64 (= A64), M69 (= M69), T79 (≠ V86), F83 (≠ Q90), G107 (= G114), E110 (= E117), P129 (= P136), E130 (= E137), V135 (≠ L142), P137 (= P144), G138 (= G145), L223 (≠ T233), F233 (≠ P243)
- binding calcium ion: F233 (≠ P243), Q238 (≠ R248)
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)
44% identity, 73% coverage: 25:211/255 of query aligns to 101:285/339 of Q13825
- K105 (≠ R29) mutation to N: Abolishes RNA-binding; when associated with E-109 and Q-113.
- 105:119 (vs. 29:43, 40% identical) RNA-binding
- K109 (= K33) mutation to E: Abolishes RNA-binding; when associated with N-105 and Q-113.
- K113 (≠ A37) mutation to Q: Abolishes RNA-binding; when associated with N-105 and E-109.
- A240 (= A168) to V: in MGCA1; decreased methylglutaconyl-CoA hydratase activity; dbSNP:rs769894315
Sites not aligning to the query:
- 1:67 modified: transit peptide, Mitochondrion
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
31% identity, 100% coverage: 2:255/255 of query aligns to 1:244/250 of 3q0gD
- active site: A64 (= A64), M69 (= M69), T75 (≠ V86), F79 (≠ Q90), G103 (= G114), E106 (= E117), P125 (= P136), E126 (= E137), V131 (≠ L142), P133 (= P144), G134 (= G145), L219 (≠ T233), F229 (≠ P243)
- binding Butyryl Coenzyme A: F225 (≠ L239), F241 (= F252)
1wdmA Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form i (native3) (see paper)
41% identity, 55% coverage: 19:157/255 of query aligns to 24:160/707 of 1wdmA
Sites not aligning to the query:
- active site: 430, 451, 463, 501
- binding acetyl coenzyme *a: 297, 459, 501, 534, 652, 658
- binding nicotinamide-adenine-dinucleotide: 321, 322, 324, 325, 344, 401, 403, 428, 430, 454
1wdlA Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form ii (native4) (see paper)
41% identity, 55% coverage: 19:157/255 of query aligns to 24:160/715 of 1wdlA
Sites not aligning to the query:
- active site: 430, 451, 463, 501
- binding nicotinamide-adenine-dinucleotide: 322, 324, 325, 344, 345, 400, 401, 403, 428, 429, 430
P28793 Fatty acid oxidation complex subunit alpha; EC 4.2.1.17; EC 5.1.2.3; EC 5.3.3.8; EC 1.1.1.35 from Pseudomonas fragi (see paper)
41% identity, 55% coverage: 19:157/255 of query aligns to 24:160/715 of P28793
Sites not aligning to the query:
- 297 binding
- 325 binding
- 344 binding
- 401:403 binding
- 408 binding
- 430 binding
- 454 binding
- 501 binding
- 660 binding
6iunB Crystal structure of enoyl-coa hydratase (ech) from ralstonia eutropha h16 in complex with NAD
31% identity, 95% coverage: 13:255/255 of query aligns to 9:273/692 of 6iunB
Sites not aligning to the query:
- active site: 407, 428, 440, 478
- binding nicotinamide-adenine-dinucleotide: 300, 301, 302, 321, 322, 365, 377, 378, 380, 384, 388, 405, 407
6eqoA Tri-functional propionyl-coa synthase of erythrobacter sp. Nap1 with bound NADP+ and phosphomethylphosphonic acid adenylate ester (see paper)
36% identity, 71% coverage: 1:182/255 of query aligns to 856:1040/1804 of 6eqoA
Sites not aligning to the query:
- binding phosphomethylphosphonic acid adenylate ester: 456, 458, 535, 536, 537, 538, 558, 559, 560, 561, 562, 688, 714
- binding nadp nicotinamide-adenine-dinucleotide phosphate: 1261, 1265, 1379, 1400, 1403, 1404, 1405, 1424, 1425, 1429, 1444, 1492, 1493, 1497, 1514, 1517, 1713, 1730, 1731, 1774
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)
35% identity, 76% coverage: 13:206/255 of query aligns to 10:192/723 of Q08426
- V40 (≠ E43) to G: in dbSNP:rs1062551
- I41 (≠ A44) to R: in dbSNP:rs1062552
- T75 (≠ D88) to I: in dbSNP:rs1062553
- K165 (≠ A178) 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 (≠ S185) 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:
- 3 E → 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
- 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
6yswA E. Coli anaerobic trifunctional enzyme subunit-alpha in complex with coenzyme a
34% identity, 74% coverage: 13:201/255 of query aligns to 14:201/707 of 6yswA
- active site: A66 (= A64), I71 (≠ L73), A84 (≠ V86), Q88 (= Q90), G112 (= G114), E115 (= E117), P136 (= P136), E137 (= E137), G145 (= G145)
- binding coenzyme a: E23 (≠ P22), M25 (≠ V24), A66 (= A64), D67 (= D65), I68 (≠ L66), P136 (= P136), E137 (= E137), L140 (= L140)
Sites not aligning to the query:
Query Sequence
>WP_011384972.1 NCBI__GCF_000009985.1:WP_011384972.1
MSFSVLNTARRGAVFVVTLASPPVNALSRALIKDLHAAMDMVEADKTIRVLHLRSEQKAF
CAGADLAEMRENLANPDLVDAQIAFVRDLQNVLKRIETLALATVAEVGGAAMGGGLELAL
ACDFRMAANEAKLALPEVNLGLIPGAGGTQRLTRLCGPAIAKRLILGAEILDGQSAEAMG
IVHWSAPRAELADKAATLADRLATLPRAAVAASKSCIEASLDPSRDGYEEELTATRNLLL
HEPETRHRVEAFLSK
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