SitesBLAST
Comparing Echvi_4069 Echvi_4069 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)
44% identity, 99% coverage: 3:261/261 of query aligns to 2:259/259 of 5zaiC
- active site: A65 (= A67), F70 (≠ I72), S82 (= S84), R86 (≠ Q88), G110 (= G112), E113 (= E115), P132 (= P134), E133 (= E135), I138 (= I140), P140 (= P142), G141 (= G143), A226 (≠ L228), F236 (≠ V238)
- binding coenzyme a: K24 (= K25), L25 (= L26), A63 (= A65), G64 (= G66), A65 (= A67), D66 (= D68), I67 (= I69), P132 (= P134), R166 (≠ M168), F248 (= F250), K251 (= K253)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
40% identity, 97% coverage: 6:258/261 of query aligns to 4:253/256 of 3h81A
- active site: A64 (= A67), M69 (≠ I72), T79 (≠ S84), F83 (≠ Q88), G107 (= G112), E110 (= E115), P129 (= P134), E130 (= E135), V135 (≠ I140), P137 (= P142), G138 (= G143), L223 (= L228), F233 (≠ V238)
- binding calcium ion: F233 (≠ V238), Q238 (≠ Y243)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
40% identity, 97% coverage: 6:258/261 of query aligns to 5:254/255 of 3q0jC
- active site: A65 (= A67), M70 (≠ I72), T80 (≠ S84), F84 (≠ Q88), G108 (= G112), E111 (= E115), P130 (= P134), E131 (= E135), V136 (≠ I140), P138 (= P142), G139 (= G143), L224 (= L228), F234 (≠ V238)
- binding acetoacetyl-coenzyme a: Q23 (≠ S24), A24 (≠ K25), L25 (= L26), A27 (= A28), A63 (= A65), G64 (= G66), A65 (= A67), D66 (= D68), I67 (= I69), K68 (≠ S70), M70 (≠ I72), F84 (≠ Q88), G107 (= G111), G108 (= G112), E111 (= E115), P130 (= P134), E131 (= E135), P138 (= P142), G139 (= G143), M140 (≠ Y144)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
40% identity, 97% coverage: 6:258/261 of query aligns to 5:254/255 of 3q0gC
- active site: A65 (= A67), M70 (≠ I72), T80 (≠ S84), F84 (≠ Q88), G108 (= G112), E111 (= E115), P130 (= P134), E131 (= E135), V136 (≠ I140), P138 (= P142), G139 (= G143), L224 (= L228), F234 (≠ V238)
- binding coenzyme a: L25 (= L26), A63 (= A65), I67 (= I69), K68 (≠ S70), Y104 (≠ F108), P130 (= P134), E131 (= E135), L134 (= L138)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
39% identity, 97% coverage: 6:258/261 of query aligns to 4:249/250 of 3q0gD
- active site: A64 (= A67), M69 (≠ L78), T75 (≠ S84), F79 (≠ Q88), G103 (= G112), E106 (= E115), P125 (= P134), E126 (= E135), V131 (≠ I140), P133 (= P142), G134 (= G143), L219 (= L228), F229 (≠ V238)
- binding Butyryl Coenzyme A: F225 (= F234), F241 (= F250)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
41% identity, 97% coverage: 7:259/261 of query aligns to 6:256/258 of 1mj3A
- active site: A68 (= A67), M73 (≠ L78), S83 (≠ N86), L85 (≠ Q88), G109 (= G112), E112 (= E115), P131 (= P134), E132 (= E135), T137 (≠ I140), P139 (= P142), G140 (= G143), K225 (≠ L228), F235 (≠ V238)
- binding hexanoyl-coenzyme a: K26 (≠ S24), A27 (≠ K25), L28 (= L26), A30 (= A28), A66 (= A65), G67 (= G66), A68 (= A67), D69 (= D68), I70 (= I69), G109 (= G112), P131 (= P134), E132 (= E135), L135 (= L138), G140 (= G143)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
38% identity, 94% coverage: 15:260/261 of query aligns to 15:260/261 of 5jbxB
- active site: A67 (= A67), R72 (≠ I72), L84 (≠ S84), R88 (≠ Q88), G112 (= G112), E115 (= E115), T134 (≠ P134), E135 (= E135), I140 (= I140), P142 (= P142), G143 (= G143), A228 (≠ L228), L238 (≠ V238)
- binding coenzyme a: S24 (= S24), R25 (≠ K25), R26 (≠ L26), A28 (= A28), A65 (= A65), D68 (= D68), L69 (≠ I69), K70 (≠ S70), L110 (= L110), G111 (= G111), T134 (≠ P134), E135 (= E135), L138 (= L138), R168 (≠ M168)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
42% identity, 93% coverage: 18:259/261 of query aligns to 19:252/254 of 2dubA
- active site: A67 (= A67), M72 (≠ L78), S82 (≠ E89), G105 (= G112), E108 (= E115), P127 (= P134), E128 (= E135), T133 (≠ I140), P135 (= P142), G136 (= G143), K221 (≠ L228), F231 (≠ V238)
- binding octanoyl-coenzyme a: K25 (≠ S24), A26 (≠ K25), L27 (= L26), A29 (= A28), A65 (= A65), A67 (= A67), D68 (= D68), I69 (= I69), K70 (≠ N76), G105 (= G112), E108 (= E115), P127 (= P134), E128 (= E135), G136 (= G143), A137 (≠ Y144)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
40% identity, 97% coverage: 7:259/261 of query aligns to 4:256/258 of 1ey3A
- active site: A66 (= A67), M71 (≠ I72), S81 (≠ A80), L85 (≠ S84), G109 (= G112), E112 (= E115), P131 (= P134), E132 (= E135), T137 (≠ I140), P139 (= P142), G140 (= G143), K225 (≠ L228), F235 (≠ V238)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ S24), L26 (= L26), A28 (= A28), A64 (= A65), G65 (= G66), A66 (= A67), D67 (= D68), I68 (= I69), L85 (≠ S84), W88 (≠ F91), G109 (= G112), P131 (= P134), L135 (= L138), G140 (= G143)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
40% identity, 97% coverage: 7:259/261 of query aligns to 6:258/260 of 1dubA
- active site: A68 (= A67), M73 (≠ I72), S83 (≠ A80), L87 (≠ S84), G111 (= G112), E114 (= E115), P133 (= P134), E134 (= E135), T139 (≠ I140), P141 (= P142), G142 (= G143), K227 (≠ L228), F237 (≠ V238)
- binding acetoacetyl-coenzyme a: K26 (≠ S24), A27 (≠ K25), L28 (= L26), A30 (= A28), A66 (= A65), A68 (= A67), D69 (= D68), I70 (= I69), Y107 (≠ F108), G110 (= G111), G111 (= G112), E114 (= E115), P133 (= P134), E134 (= E135), L137 (= L138), G142 (= G143), F233 (= F234), F249 (= F250)
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)
40% identity, 97% coverage: 7:259/261 of query aligns to 36:288/290 of P14604
- E144 (= E115) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E135) 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
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
39% identity, 93% coverage: 18:261/261 of query aligns to 20:260/260 of 2hw5C
- active site: A68 (= A67), M73 (≠ I72), S83 (≠ A80), L87 (≠ S84), G111 (= G112), E114 (= E115), P133 (= P134), E134 (= E135), T139 (≠ I140), P141 (= P142), G142 (= G143), K227 (≠ L228), F237 (≠ V238)
- binding crotonyl coenzyme a: K26 (≠ S24), A27 (≠ K25), L28 (= L26), A30 (= A28), K62 (= K61), I70 (= I69), F109 (≠ L110)
6eqoA Tri-functional propionyl-coa synthase of erythrobacter sp. Nap1 with bound NADP+ and phosphomethylphosphonic acid adenylate ester (see paper)
39% identity, 69% coverage: 22:202/261 of query aligns to 873:1062/1804 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)
33% identity, 97% coverage: 7:260/261 of query aligns to 5:256/257 of 6slbAAA
- active site: Q64 (≠ A67), F69 (≠ I72), L80 (≠ A80), N84 (≠ S84), A108 (≠ G112), S111 (≠ E115), A130 (≠ P134), F131 (≠ E135), L136 (≠ I140), P138 (= P142), D139 (≠ G143), A224 (≠ L228), G234 (≠ V238)
- 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 (≠ K61), A62 (= A65), Q64 (≠ A67), D65 (= D68), L66 (≠ I69), Y76 (vs. gap), A108 (≠ G112), F131 (≠ E135), D139 (≠ G143)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
33% identity, 97% coverage: 7:260/261 of query aligns to 2:244/245 of 6slaAAA
- active site: Q61 (≠ A67), L68 (= L75), N72 (= N79), A96 (≠ G112), S99 (≠ E115), A118 (≠ P134), F119 (≠ E135), L124 (≠ I140), P126 (= P142), N127 (≠ G143), A212 (≠ L228), G222 (≠ V238)
- 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 (= L26), A59 (= A65), Q61 (≠ A67), D62 (= D68), L63 (≠ I69), L68 (= L75), Y71 (≠ L78), A94 (≠ L110), G95 (= G111), A96 (≠ G112), F119 (≠ E135), I122 (≠ L138), L124 (≠ I140), N127 (≠ G143), F234 (= F250), K237 (= K253)
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)
33% identity, 94% coverage: 15:259/261 of query aligns to 21:266/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
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, 97% coverage: 8:261/261 of query aligns to 82:339/339 of Q13825
- K105 (≠ F31) mutation to N: Abolishes RNA-binding; when associated with E-109 and Q-113.
- 105:119 (vs. 31:45, 7% identical) RNA-binding
- K109 (≠ E35) mutation to E: Abolishes RNA-binding; when associated with N-105 and Q-113.
- K113 (≠ N39) mutation to Q: Abolishes RNA-binding; when associated with N-105 and E-109.
- A240 (≠ G166) to V: in MGCA1; decreased methylglutaconyl-CoA hydratase activity; dbSNP:rs769894315
Sites not aligning to the query:
- 1:67 modified: transit peptide, Mitochondrion
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)
36% identity, 66% coverage: 24:196/261 of query aligns to 59:234/763 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
6yswA E. Coli anaerobic trifunctional enzyme subunit-alpha in complex with coenzyme a
39% identity, 66% coverage: 13:184/261 of query aligns to 11:186/707 of 6yswA
- active site: A66 (= A67), I71 (= I72), A84 (≠ S84), Q88 (= Q88), G112 (= G112), E115 (= E115), P136 (= P134), E137 (= E135), G145 (= G143)
- binding coenzyme a: E23 (vs. gap), M25 (≠ L26), A66 (= A67), D67 (= D68), I68 (= I69), P136 (= P134), E137 (= E135), L140 (= L138)
Sites not aligning to the query:
4emlA Synechocystis sp. Pcc 6803 1,4-dihydroxy-2-naphthoyl-coenzyme a synthase (menb) in complex with bicarbonate (see paper)
35% identity, 97% coverage: 6:258/261 of query aligns to 11:254/261 of 4emlA
- active site: G77 (≠ A67), R81 (≠ E71), L85 (= L78), G109 (= G112), V112 (≠ E115), G132 (≠ E135), S137 (≠ I140), D139 (≠ P142), G140 (= G143), A226 (≠ E230), Y234 (≠ V238)
- binding bicarbonate ion: G108 (= G111), Q130 (= Q133), G132 (≠ E135), W160 (≠ L163)
- binding chloride ion: D184 (vs. gap), R185 (≠ Q185), E187 (≠ K187), E188 (≠ A188)
Query Sequence
>Echvi_4069 Echvi_4069 Enoyl-CoA hydratase/carnithine racemase
MAESTNILSENKDGILYLTINRESKLNAINFDTLEELKNIFNEVSDNKSIRGVVLTGSGE
KAFVAGADISEIAELNELNARKFSENGQEVFSLIESCHKPVIAVVNGFALGGGCELSMAC
HMRIATSNAKFGQPEVNLGIIPGYGGTQRLTFLIGRTKANELLMTGDMVDAAEAKALGLV
NYVTQTKAEAIQKAEEILQKIMTKAPLSIGMIIDCVNAVYSNDENGYLIEANSFARCVKS
EDYSEGTSAFLEKRKPNFKGE
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