SitesBLAST
Comparing WP_057507562.1 NCBI__GCF_001431535.1:WP_057507562.1 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)
36% identity, 95% coverage: 12:263/265 of query aligns to 6:257/259 of 5zaiC
- active site: A65 (= A71), F70 (= F76), S82 (≠ A88), R86 (≠ G92), G110 (= G116), E113 (= E119), P132 (= P138), E133 (= E139), I138 (≠ L144), P140 (= P146), G141 (≠ C147), A226 (≠ V232), F236 (= F242)
- binding coenzyme a: K24 (≠ A30), L25 (vs. gap), A63 (= A69), G64 (= G70), A65 (= A71), D66 (= D72), I67 (≠ L73), P132 (= P138), R166 (= R172), F248 (= F254), K251 (= K257)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
36% identity, 95% coverage: 12:263/265 of query aligns to 7:259/261 of 5jbxB
- active site: A67 (= A71), R72 (≠ F76), L84 (≠ A88), R88 (≠ G92), G112 (= G116), E115 (= E119), T134 (≠ P138), E135 (= E139), I140 (≠ L144), P142 (= P146), G143 (≠ C147), A228 (≠ V232), L238 (≠ F242)
- binding coenzyme a: S24 (≠ P29), R25 (≠ A30), R26 (≠ H31), A28 (≠ W33), A65 (= A69), D68 (= D72), L69 (= L73), K70 (≠ N74), L110 (≠ M114), G111 (= G115), T134 (≠ P138), E135 (= E139), L138 (≠ V142), R168 (= R172)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
33% identity, 94% coverage: 17:264/265 of query aligns to 14:257/258 of 1mj3A
- active site: A68 (= A71), M73 (≠ F76), S83 (≠ E96), L85 (= L98), G109 (= G116), E112 (= E119), P131 (= P138), E132 (= E139), T137 (≠ L144), P139 (= P146), G140 (≠ C147), K225 (≠ V232), F235 (= F242)
- binding hexanoyl-coenzyme a: K26 (≠ P29), A27 (= A30), L28 (≠ H31), A30 (≠ W33), A66 (= A69), G67 (= G70), A68 (= A71), D69 (= D72), I70 (≠ L73), G109 (= G116), P131 (= P138), E132 (= E139), L135 (≠ V142), G140 (≠ C147)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
33% identity, 94% coverage: 17:264/265 of query aligns to 14:259/260 of 1dubA
- active site: A68 (= A71), M73 (≠ F76), S83 (≠ A88), L87 (≠ G92), G111 (= G116), E114 (= E119), P133 (= P138), E134 (= E139), T139 (≠ L144), P141 (= P146), G142 (≠ C147), K227 (≠ V232), F237 (= F242)
- binding acetoacetyl-coenzyme a: K26 (≠ P29), A27 (= A30), L28 (≠ H31), A30 (≠ W33), A66 (= A69), A68 (= A71), D69 (= D72), I70 (≠ L73), Y107 (= Y112), G110 (= G115), G111 (= G116), E114 (= E119), P133 (= P138), E134 (= E139), L137 (≠ V142), G142 (≠ C147), F233 (= F238), F249 (= F254)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
33% identity, 94% coverage: 17:264/265 of query aligns to 12:257/258 of 1ey3A
- active site: A66 (= A71), M71 (≠ F76), S81 (≠ A88), L85 (≠ G92), G109 (= G116), E112 (= E119), P131 (= P138), E132 (= E139), T137 (≠ L144), P139 (= P146), G140 (≠ C147), K225 (≠ V232), F235 (= F242)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ P29), L26 (≠ H31), A28 (≠ W33), A64 (= A69), G65 (= G70), A66 (= A71), D67 (= D72), I68 (≠ L73), L85 (≠ G92), W88 (≠ F95), G109 (= G116), P131 (= P138), L135 (≠ V142), G140 (≠ C147)
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, 94% coverage: 17:264/265 of query aligns to 44:289/290 of P14604
- E144 (= E119) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E139) 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
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
33% identity, 94% coverage: 17:264/265 of query aligns to 13:253/254 of 2dubA
- active site: A67 (= A71), M72 (≠ F76), S82 (vs. gap), G105 (= G116), E108 (= E119), P127 (= P138), E128 (= E139), T133 (≠ L144), P135 (= P146), G136 (≠ C147), K221 (≠ V232), F231 (= F242)
- binding octanoyl-coenzyme a: K25 (≠ P29), A26 (= A30), L27 (≠ H31), A29 (≠ W33), A65 (= A69), A67 (= A71), D68 (= D72), I69 (≠ L73), K70 (≠ N74), G105 (= G116), E108 (= E119), P127 (= P138), E128 (= E139), G136 (≠ C147), A137 (= A148)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
33% identity, 94% coverage: 17:264/265 of query aligns to 14:259/260 of 2hw5C
- active site: A68 (= A71), M73 (≠ F76), S83 (≠ E86), L87 (≠ G92), G111 (= G116), E114 (= E119), P133 (= P138), E134 (= E139), T139 (≠ L144), P141 (= P146), G142 (≠ C147), K227 (≠ V232), F237 (= F242)
- binding crotonyl coenzyme a: K26 (≠ P29), A27 (= A30), L28 (≠ H31), A30 (≠ W33), K62 (= K65), I70 (≠ L73), F109 (≠ M114)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
32% identity, 95% coverage: 14:264/265 of query aligns to 7:255/256 of 3h81A
- active site: A64 (= A71), M69 (≠ F76), T79 (≠ E96), F83 (vs. gap), G107 (= G116), E110 (= E119), P129 (= P138), E130 (= E139), V135 (≠ L144), P137 (= P146), G138 (≠ C147), L223 (≠ V232), F233 (= F242)
- binding calcium ion: F233 (= F242), Q238 (= Q247)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
33% identity, 94% coverage: 14:262/265 of query aligns to 8:254/255 of 3q0jC
- active site: A65 (= A71), M70 (≠ F76), T80 (≠ E96), F84 (vs. gap), G108 (= G116), E111 (= E119), P130 (= P138), E131 (= E139), V136 (≠ L144), P138 (= P146), G139 (≠ C147), L224 (≠ V232), F234 (= F242)
- binding acetoacetyl-coenzyme a: Q23 (≠ P29), A24 (= A30), L25 (vs. gap), A27 (≠ T32), A63 (= A69), G64 (= G70), A65 (= A71), D66 (= D72), I67 (≠ L73), K68 (≠ N74), M70 (≠ F76), F84 (vs. gap), G107 (= G115), G108 (= G116), E111 (= E119), P130 (= P138), E131 (= E139), P138 (= P146), G139 (≠ C147), M140 (≠ A148)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
33% identity, 94% coverage: 14:262/265 of query aligns to 8:254/255 of 3q0gC
- active site: A65 (= A71), M70 (≠ F76), T80 (≠ E96), F84 (vs. gap), G108 (= G116), E111 (= E119), P130 (= P138), E131 (= E139), V136 (≠ L144), P138 (= P146), G139 (≠ C147), L224 (≠ V232), F234 (= F242)
- binding coenzyme a: L25 (vs. gap), A63 (= A69), I67 (≠ L73), K68 (≠ N74), Y104 (= Y112), P130 (= P138), E131 (= E139), L134 (≠ V142)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
32% identity, 94% coverage: 14:262/265 of query aligns to 7:249/250 of 3q0gD
- active site: A64 (= A71), M69 (≠ F76), T75 (≠ E96), F79 (vs. gap), G103 (= G116), E106 (= E119), P125 (= P138), E126 (= E139), V131 (≠ L144), P133 (= P146), G134 (≠ C147), L219 (≠ V232), F229 (= F242)
- binding Butyryl Coenzyme A: F225 (= F238), F241 (= F254)
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)
37% identity, 76% coverage: 20:221/265 of query aligns to 11:205/723 of Q08426
- V40 (≠ N49) to G: in dbSNP:rs1062551
- I41 (≠ A50) to R: in dbSNP:rs1062552
- T75 (≠ R90) to I: in dbSNP:rs1062553
- K165 (≠ R180) 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 (≠ Q186) 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
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
35% identity, 95% coverage: 12:263/265 of query aligns to 6:255/257 of 6slbAAA
- active site: Q64 (≠ A71), F69 (= F76), L80 (≠ A88), N84 (≠ G92), A108 (≠ G116), S111 (≠ E119), A130 (≠ P138), F131 (≠ E139), L136 (= L144), P138 (= P146), D139 (≠ C147), A224 (≠ V232), G234 (≠ F242)
- 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 (≠ K65), A62 (= A69), Q64 (≠ A71), D65 (= D72), L66 (= L73), Y76 (≠ R85), A108 (≠ G116), F131 (≠ E139), D139 (≠ C147)
6iunB Crystal structure of enoyl-coa hydratase (ech) from ralstonia eutropha h16 in complex with NAD
43% identity, 58% coverage: 20:173/265 of query aligns to 10:158/692 of 6iunB
Sites not aligning to the query:
- active site: 248, 407, 428, 440, 478
- binding nicotinamide-adenine-dinucleotide: 300, 301, 302, 321, 322, 365, 377, 378, 380, 384, 388, 405, 407
6yswA E. Coli anaerobic trifunctional enzyme subunit-alpha in complex with coenzyme a
34% identity, 75% coverage: 12:211/265 of query aligns to 6:206/707 of 6yswA
- active site: A66 (= A71), I71 (≠ F76), A84 (≠ R89), Q88 (≠ E93), G112 (= G116), E115 (= E119), P136 (= P138), E137 (= E139), G145 (≠ C147)
- binding coenzyme a: E23 (vs. gap), M25 (≠ A30), A66 (= A71), D67 (= D72), I68 (≠ L73), P136 (= P138), E137 (= E139), L140 (≠ V142)
Sites not aligning to the query:
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: 15:264/265 of query aligns to 21:270/296 of Q9P4U9
Sites not aligning to the query:
- 294:296 Peroxisomal targeting signal type 1
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
33% identity, 95% coverage: 12:263/265 of query aligns to 3:243/245 of 6slaAAA
- active site: Q61 (≠ A71), L68 (≠ A88), N72 (≠ G92), A96 (≠ G116), S99 (≠ E119), A118 (≠ P138), F119 (≠ E139), L124 (= L144), P126 (= P146), N127 (≠ C147), A212 (≠ V232), G222 (≠ F242)
- 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 (≠ H31), A59 (= A69), Q61 (≠ A71), D62 (= D72), L63 (= L73), L68 (≠ A88), Y71 (≠ F91), A94 (≠ M114), G95 (= G115), A96 (≠ G116), F119 (≠ E139), I122 (≠ V142), L124 (= L144), N127 (≠ C147), F234 (= F254), K237 (= K257)
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)
30% identity, 92% coverage: 19:263/265 of query aligns to 20:266/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
6eqoA Tri-functional propionyl-coa synthase of erythrobacter sp. Nap1 with bound NADP+ and phosphomethylphosphonic acid adenylate ester (see paper)
37% identity, 62% coverage: 20:182/265 of query aligns to 867:1038/1804 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
Query Sequence
>WP_057507562.1 NCBI__GCF_001431535.1:WP_057507562.1
MNDWRTHDHVGLKVEADGHVAVITLHNPPAHTWTVHSLAALRDLVAALNADRSIYALVIS
GEGEKFFSAGADLNQFASGDRGAAREAARRFGEAFEALSGFRGVSIAAINGYAMGGGLEC
ALACDLRIIEEHAQVALPEATVGLLPCAGGTQNLPRLVGEGWAKRMILLGERIDADTAVR
IGLAEQKAGKGEAKALALEWAKKAGKQSPTSIAACKTLVQSTRTGTHAAALVAEREAFVD
LFDSADQVEGVSAFLEKRSAQWKNA
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