SitesBLAST
Comparing GFF3051 Psest_3109 Enoyl-CoA hydratase/carnithine racemase 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, 93% coverage: 19:272/272 of query aligns to 6:259/259 of 5zaiC
- active site: A65 (= A78), F70 (= F83), S82 (≠ A95), R86 (≠ G99), G110 (= G123), E113 (= E126), P132 (= P145), E133 (= E146), I138 (≠ L151), P140 (= P153), G141 (≠ C154), A226 (= A239), F236 (= F249)
- binding coenzyme a: K24 (≠ A37), L25 (vs. gap), A63 (= A76), G64 (= G77), A65 (= A78), D66 (= D79), I67 (≠ L80), P132 (= P145), R166 (= R179), F248 (= F261), K251 (= K264)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
39% identity, 94% coverage: 18:272/272 of query aligns to 6:261/261 of 5jbxB
- active site: A67 (= A78), R72 (≠ F83), L84 (≠ A95), R88 (≠ G99), G112 (= G123), E115 (= E126), T134 (≠ P145), E135 (= E146), I140 (≠ L151), P142 (= P153), G143 (≠ C154), A228 (= A239), L238 (≠ F249)
- binding coenzyme a: S24 (≠ P35), R25 (≠ P36), R26 (≠ A37), A28 (≠ T39), A65 (= A76), D68 (= D79), L69 (= L80), K70 (= K81), L110 (= L121), G111 (= G122), T134 (≠ P145), E135 (= E146), L138 (≠ V149), R168 (= R179)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
34% identity, 92% coverage: 23:271/272 of query aligns to 13:259/260 of 1dubA
- active site: A68 (= A78), M73 (≠ F83), S83 (≠ A95), L87 (≠ G99), G111 (= G123), E114 (= E126), P133 (= P145), E134 (= E146), T139 (≠ L151), P141 (= P153), G142 (≠ C154), K227 (≠ A239), F237 (= F249)
- binding acetoacetyl-coenzyme a: K26 (≠ P36), A27 (= A37), L28 (≠ N38), A30 (≠ W40), A66 (= A76), A68 (= A78), D69 (= D79), I70 (≠ L80), Y107 (≠ F119), G110 (= G122), G111 (= G123), E114 (= E126), P133 (= P145), E134 (= E146), L137 (≠ V149), G142 (≠ C154), F233 (= F245), F249 (= F261)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
34% identity, 92% coverage: 23:271/272 of query aligns to 13:257/258 of 1mj3A
- active site: A68 (= A78), M73 (≠ F83), S83 (≠ E103), L85 (= L105), G109 (= G123), E112 (= E126), P131 (= P145), E132 (= E146), T137 (≠ L151), P139 (= P153), G140 (≠ C154), K225 (≠ A239), F235 (= F249)
- binding hexanoyl-coenzyme a: K26 (≠ P36), A27 (= A37), L28 (≠ N38), A30 (≠ W40), A66 (= A76), G67 (= G77), A68 (= A78), D69 (= D79), I70 (≠ L80), G109 (= G123), P131 (= P145), E132 (= E146), L135 (≠ V149), G140 (≠ C154)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
34% identity, 92% coverage: 23:271/272 of query aligns to 11:257/258 of 1ey3A
- active site: A66 (= A78), M71 (≠ F83), S81 (≠ A95), L85 (≠ G99), G109 (= G123), E112 (= E126), P131 (= P145), E132 (= E146), T137 (≠ L151), P139 (= P153), G140 (≠ C154), K225 (≠ A239), F235 (= F249)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ P36), L26 (≠ N38), A28 (≠ W40), A64 (= A76), G65 (= G77), A66 (= A78), D67 (= D79), I68 (≠ L80), L85 (≠ G99), W88 (≠ F102), G109 (= G123), P131 (= P145), L135 (≠ V149), G140 (≠ C154)
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)
34% identity, 92% coverage: 23:271/272 of query aligns to 43:289/290 of P14604
- E144 (= E126) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E146) 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)
34% identity, 92% coverage: 23:271/272 of query aligns to 12:253/254 of 2dubA
- active site: A67 (= A78), M72 (≠ F83), S82 (vs. gap), G105 (= G123), E108 (= E126), P127 (= P145), E128 (= E146), T133 (≠ L151), P135 (= P153), G136 (≠ C154), K221 (≠ A239), F231 (= F249)
- binding octanoyl-coenzyme a: K25 (≠ P36), A26 (= A37), L27 (≠ N38), A29 (≠ W40), A65 (= A76), A67 (= A78), D68 (= D79), I69 (≠ L80), K70 (= K81), G105 (= G123), E108 (= E126), P127 (= P145), E128 (= E146), G136 (≠ C154), A137 (= A155)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
34% identity, 94% coverage: 17:272/272 of query aligns to 3:256/256 of 3h81A
- active site: A64 (= A78), M69 (≠ F83), T79 (≠ E103), F83 (vs. gap), G107 (= G123), E110 (= E126), P129 (= P145), E130 (= E146), V135 (≠ L151), P137 (= P153), G138 (≠ C154), L223 (≠ A239), F233 (= F249)
- binding calcium ion: F233 (= F249), Q238 (≠ T254)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
34% identity, 93% coverage: 17:269/272 of query aligns to 4:254/255 of 3q0jC
- active site: A65 (= A78), M70 (≠ F83), T80 (≠ E103), F84 (vs. gap), G108 (= G123), E111 (= E126), P130 (= P145), E131 (= E146), V136 (≠ L151), P138 (= P153), G139 (≠ C154), L224 (≠ A239), F234 (= F249)
- binding acetoacetyl-coenzyme a: Q23 (≠ P36), A24 (= A37), L25 (vs. gap), A27 (≠ T39), A63 (= A76), G64 (= G77), A65 (= A78), D66 (= D79), I67 (≠ L80), K68 (= K81), M70 (≠ F83), F84 (vs. gap), G107 (= G122), G108 (= G123), E111 (= E126), P130 (= P145), E131 (= E146), P138 (= P153), G139 (≠ C154), M140 (≠ A155)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
34% identity, 93% coverage: 17:269/272 of query aligns to 4:254/255 of 3q0gC
- active site: A65 (= A78), M70 (≠ F83), T80 (≠ E103), F84 (vs. gap), G108 (= G123), E111 (= E126), P130 (= P145), E131 (= E146), V136 (≠ L151), P138 (= P153), G139 (≠ C154), L224 (≠ A239), F234 (= F249)
- binding coenzyme a: L25 (vs. gap), A63 (= A76), I67 (≠ L80), K68 (= K81), Y104 (≠ F119), P130 (= P145), E131 (= E146), L134 (≠ V149)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
32% identity, 92% coverage: 23:272/272 of query aligns to 13:260/260 of 2hw5C
- active site: A68 (= A78), M73 (≠ F83), S83 (≠ A95), L87 (≠ G99), G111 (= G123), E114 (= E126), P133 (= P145), E134 (= E146), T139 (≠ L151), P141 (= P153), G142 (≠ C154), K227 (≠ A239), F237 (= F249)
- binding crotonyl coenzyme a: K26 (≠ P36), A27 (= A37), L28 (≠ N38), A30 (≠ W40), K62 (= K72), I70 (≠ L80), F109 (≠ L121)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
35% identity, 93% coverage: 17:269/272 of query aligns to 3:249/250 of 3q0gD
- active site: A64 (= A78), M69 (≠ L82), T75 (≠ A95), F79 (≠ G99), G103 (= G123), E106 (= E126), P125 (= P145), E126 (= E146), V131 (≠ L151), P133 (= P153), G134 (≠ C154), L219 (≠ A239), F229 (= F249)
- binding Butyryl Coenzyme A: F225 (= F245), F241 (= F261)
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
34% identity, 93% coverage: 21:272/272 of query aligns to 12:266/266 of O53561
- K135 (≠ Q141) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 141:148, 38% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (≠ S148) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
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, 78% coverage: 24:235/272 of query aligns to 8:208/723 of Q08426
- V40 (≠ N56) to G: in dbSNP:rs1062551
- I41 (≠ H57) to R: in dbSNP:rs1062552
- T75 (≠ R97) to I: in dbSNP:rs1062553
- K165 (≠ R187) 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 (≠ Q193) 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
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)
32% identity, 99% coverage: 1:270/272 of query aligns to 1:266/270 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)
35% identity, 68% coverage: 13:196/272 of query aligns to 854:1045/1804 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
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
34% identity, 92% coverage: 22:272/272 of query aligns to 8:257/257 of 6slbAAA
- active site: Q64 (≠ A78), F69 (= F83), L80 (≠ A95), N84 (≠ G99), A108 (≠ G123), S111 (≠ E126), A130 (≠ P145), F131 (≠ E146), L136 (= L151), P138 (= P153), D139 (≠ C154), A224 (= A239), G234 (≠ F249)
- 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 (≠ K72), A62 (= A76), Q64 (≠ A78), D65 (= D79), L66 (= L80), Y76 (≠ R92), A108 (≠ G123), F131 (≠ E146), D139 (≠ C154)
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, 86% coverage: 38:270/272 of query aligns to 101:337/339 of Q13825
- K105 (≠ R42) mutation to N: Abolishes RNA-binding; when associated with E-109 and Q-113.
- 105:119 (vs. 42:56, 20% identical) RNA-binding
- K109 (≠ I46) mutation to E: Abolishes RNA-binding; when associated with N-105 and Q-113.
- K113 (≠ Q50) 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
6iunB Crystal structure of enoyl-coa hydratase (ech) from ralstonia eutropha h16 in complex with NAD
35% identity, 63% coverage: 27:196/272 of query aligns to 10:174/692 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
35% identity, 68% coverage: 26:211/272 of query aligns to 12:196/707 of 6yswA
- active site: A66 (= A78), I71 (≠ F83), A84 (≠ R96), Q88 (≠ E100), G112 (= G123), E115 (= E126), P136 (= P145), E137 (= E146), G145 (≠ C154)
- binding coenzyme a: E23 (vs. gap), M25 (≠ A37), A66 (= A78), D67 (= D79), I68 (≠ L80), P136 (= P145), E137 (= E146), L140 (≠ V149)
Sites not aligning to the query:
Query Sequence
>GFF3051 Psest_3109 Enoyl-CoA hydratase/carnithine racemase
MSTAVEPYQSGVFDLTHKLTVEKHGHTALITINHPPANTWDRESLIGLKQVVEHLNHDDD
IYALVISGQGEKFFSAGADLKLFADGDRNRAREMARRFGEAFEALRDFRGVSIAAINGFA
LGGGLECALACDLRIAEQQAQMGLPEASVGLLPCAGGTQALAWLVGEGWAKRMILCGERI
TAETALRIGLIEQVVEPGQARGHALLLAARIARQSPVAVRAIKPLIDGARQRLPHTFGAA
EREAFVELFEAEDTLEGVNAFLEKRDPRWRNR
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