SitesBLAST
Comparing WP_054558757.1 NCBI__GCF_001306415.1:WP_054558757.1 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)
49% identity, 100% coverage: 1:260/260 of query aligns to 1:259/259 of 5zaiC
- active site: A65 (= A66), F70 (= F71), S82 (≠ A83), R86 (≠ Q87), G110 (= G112), E113 (= E115), P132 (= P134), E133 (= E135), I138 (≠ V140), P140 (= P142), G141 (= G143), A226 (= A227), F236 (= F237)
- binding coenzyme a: K24 (= K24), L25 (= L25), A63 (= A64), G64 (= G65), A65 (= A66), D66 (= D67), I67 (= I68), P132 (= P134), R166 (≠ M168), F248 (= F249), K251 (= K252)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
46% identity, 94% coverage: 13:257/260 of query aligns to 16:257/260 of 1dubA
- active site: A68 (= A66), M73 (≠ F71), S83 (≠ G79), L87 (≠ A83), G111 (= G112), E114 (= E115), P133 (= P134), E134 (= E135), T139 (≠ V140), P141 (= P142), G142 (= G143), K227 (≠ A227), F237 (= F237)
- binding acetoacetyl-coenzyme a: K26 (= K23), A27 (≠ K24), L28 (= L25), A30 (= A27), A66 (= A64), A68 (= A66), D69 (= D67), I70 (= I68), Y107 (≠ F108), G110 (= G111), G111 (= G112), E114 (= E115), P133 (= P134), E134 (= E135), L137 (= L138), G142 (= G143), F233 (= F233), F249 (= F249)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
46% identity, 94% coverage: 13:257/260 of query aligns to 14:255/258 of 1ey3A
- active site: A66 (= A66), M71 (≠ F71), S81 (≠ G79), L85 (≠ A83), G109 (= G112), E112 (= E115), P131 (= P134), E132 (= E135), T137 (≠ V140), P139 (= P142), G140 (= G143), K225 (≠ A227), F235 (= F237)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (= K23), L26 (= L25), A28 (= A27), A64 (= A64), G65 (= G65), A66 (= A66), D67 (= D67), I68 (= I68), L85 (≠ A83), W88 (≠ F91), G109 (= G112), P131 (= P134), L135 (= L138), G140 (= G143)
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)
46% identity, 94% coverage: 13:257/260 of query aligns to 46:287/290 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
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
46% identity, 94% coverage: 13:257/260 of query aligns to 16:255/258 of 1mj3A
- active site: A68 (= A66), M73 (≠ F71), S83 (≠ G79), L85 (≠ V81), G109 (= G112), E112 (= E115), P131 (= P134), E132 (= E135), T137 (≠ V140), P139 (= P142), G140 (= G143), K225 (≠ A227), F235 (= F237)
- binding hexanoyl-coenzyme a: K26 (= K23), A27 (≠ K24), L28 (= L25), A30 (= A27), A66 (= A64), G67 (= G65), A68 (= A66), D69 (= D67), I70 (= I68), G109 (= G112), P131 (= P134), E132 (= E135), L135 (= L138), G140 (= G143)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
45% identity, 94% coverage: 13:257/260 of query aligns to 15:251/254 of 2dubA
- active site: A67 (= A66), M72 (≠ F71), S82 (≠ V81), G105 (= G112), E108 (= E115), P127 (= P134), E128 (= E135), T133 (≠ V140), P135 (= P142), G136 (= G143), K221 (≠ A227), F231 (= F237)
- binding octanoyl-coenzyme a: K25 (= K23), A26 (≠ K24), L27 (= L25), A29 (= A27), A65 (= A64), A67 (= A66), D68 (= D67), I69 (= I68), K70 (≠ S69), G105 (= G112), E108 (= E115), P127 (= P134), E128 (= E135), G136 (= G143), A137 (≠ Y144)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
44% identity, 94% coverage: 13:257/260 of query aligns to 16:257/260 of 2hw5C
- active site: A68 (= A66), M73 (≠ F71), S83 (≠ G86), L87 (= L90), G111 (= G112), E114 (= E115), P133 (= P134), E134 (= E135), T139 (≠ V140), P141 (= P142), G142 (= G143), K227 (≠ A227), F237 (= F237)
- binding crotonyl coenzyme a: K26 (= K23), A27 (≠ K24), L28 (= L25), A30 (= A27), K62 (= K60), I70 (= I68), F109 (≠ L110)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
43% identity, 99% coverage: 1:257/260 of query aligns to 1:254/255 of 3q0jC
- active site: A65 (= A66), M70 (≠ F71), T80 (vs. gap), F84 (≠ L82), G108 (= G112), E111 (= E115), P130 (= P134), E131 (= E135), V136 (= V140), P138 (= P142), G139 (= G143), L224 (≠ A227), F234 (= F237)
- binding acetoacetyl-coenzyme a: Q23 (≠ K23), A24 (≠ K24), L25 (= L25), A27 (= A27), A63 (= A64), G64 (= G65), A65 (= A66), D66 (= D67), I67 (= I68), K68 (≠ S69), M70 (≠ F71), F84 (≠ L82), 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
43% identity, 99% coverage: 1:257/260 of query aligns to 1:254/255 of 3q0gC
- active site: A65 (= A66), M70 (≠ F71), T80 (vs. gap), F84 (≠ L82), G108 (= G112), E111 (= E115), P130 (= P134), E131 (= E135), V136 (= V140), P138 (= P142), G139 (= G143), L224 (≠ A227), F234 (= F237)
- binding coenzyme a: L25 (= L25), A63 (= A64), I67 (= I68), K68 (≠ S69), Y104 (≠ F108), P130 (= P134), E131 (= E135), L134 (= L138)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
42% identity, 98% coverage: 3:257/260 of query aligns to 2:253/256 of 3h81A
- active site: A64 (= A66), M69 (≠ F71), T79 (vs. gap), F83 (≠ L82), G107 (= G112), E110 (= E115), P129 (= P134), E130 (= E135), V135 (= V140), P137 (= P142), G138 (= G143), L223 (≠ A227), F233 (= F237)
- binding calcium ion: F233 (= F237), Q238 (≠ F242)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
43% identity, 98% coverage: 3:257/260 of query aligns to 2:249/250 of 3q0gD
- active site: A64 (= A66), M69 (≠ F71), T75 (≠ E78), F79 (≠ L82), G103 (= G112), E106 (= E115), P125 (= P134), E126 (= E135), V131 (= V140), P133 (= P142), G134 (= G143), L219 (≠ A227), F229 (= F237)
- binding Butyryl Coenzyme A: F225 (= F233), F241 (= F249)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
41% identity, 93% coverage: 18:259/260 of query aligns to 19:260/261 of 5jbxB
- active site: A67 (= A66), R72 (≠ F71), L84 (≠ A83), R88 (≠ E88), G112 (= G112), E115 (= E115), T134 (≠ P134), E135 (= E135), I140 (≠ V140), P142 (= P142), G143 (= G143), A228 (= A227), L238 (≠ F237)
- binding coenzyme a: S24 (≠ K23), R25 (≠ K24), R26 (≠ L25), A28 (= A27), A65 (= A64), D68 (= D67), L69 (≠ I68), K70 (≠ S69), L110 (= L110), G111 (= G111), T134 (≠ P134), E135 (= E135), L138 (= L138), R168 (≠ M168)
6yswA E. Coli anaerobic trifunctional enzyme subunit-alpha in complex with coenzyme a
41% identity, 78% coverage: 13:214/260 of query aligns to 12:217/707 of 6yswA
- active site: A66 (= A66), I71 (≠ F71), A84 (= A83), Q88 (= Q87), G112 (= G112), E115 (= E115), P136 (= P134), E137 (= E135), G145 (= G143)
- binding coenzyme a: E23 (≠ K23), M25 (≠ L25), A66 (= A66), D67 (= D67), I68 (= I68), P136 (= P134), E137 (= E135), L140 (= L138)
Sites not aligning to the query:
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)
36% identity, 93% coverage: 17:257/260 of query aligns to 24:265/270 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)
39% identity, 99% coverage: 2:259/260 of query aligns to 76:338/339 of Q13825
- K105 (= K30) mutation to N: Abolishes RNA-binding; when associated with E-109 and Q-113.
- 105:119 (vs. 30:44, 33% identical) RNA-binding
- K109 (≠ E34) mutation to E: Abolishes RNA-binding; when associated with N-105 and Q-113.
- K113 (≠ V38) mutation to Q: Abolishes RNA-binding; when associated with N-105 and E-109.
- A240 (= A166) to V: in MGCA1; decreased methylglutaconyl-CoA hydratase activity; dbSNP:rs769894315
Sites not aligning to the query:
- 1:67 modified: transit peptide, Mitochondrion
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
34% identity, 98% coverage: 6:259/260 of query aligns to 2:244/245 of 6slaAAA
- active site: Q61 (≠ A66), L68 (≠ F74), N72 (≠ E78), A96 (≠ G112), S99 (≠ E115), A118 (≠ P134), F119 (≠ E135), L124 (≠ V140), P126 (= P142), N127 (≠ G143), A212 (= A227), G222 (≠ F237)
- 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 (= L25), A59 (= A64), Q61 (≠ A66), D62 (= D67), L63 (≠ I68), L68 (≠ F74), Y71 (≠ K77), A94 (≠ L110), G95 (= G111), A96 (≠ G112), F119 (≠ E135), I122 (≠ L138), L124 (≠ V140), N127 (≠ G143), F234 (= F249), K237 (= K252)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
33% identity, 98% coverage: 6:259/260 of query aligns to 5:256/257 of 6slbAAA
- active site: Q64 (≠ A66), F69 (= F71), L80 (≠ F74), N84 (≠ E78), A108 (≠ G112), S111 (≠ E115), A130 (≠ P134), F131 (≠ E135), L136 (≠ V140), P138 (= P142), D139 (≠ G143), A224 (= A227), G234 (≠ F237)
- 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 (≠ K60), A62 (= A64), Q64 (≠ A66), D65 (= D67), L66 (≠ I68), Y76 (vs. gap), A108 (≠ G112), F131 (≠ E135), D139 (≠ G143)
6eqoA Tri-functional propionyl-coa synthase of erythrobacter sp. Nap1 with bound NADP+ and phosphomethylphosphonic acid adenylate ester (see paper)
39% identity, 68% coverage: 12:188/260 of query aligns to 865:1048/1804 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
1wdlA Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form ii (native4) (see paper)
41% identity, 63% coverage: 25:189/260 of query aligns to 29:194/715 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, 63% coverage: 25:189/260 of query aligns to 29:194/715 of P28793
Sites not aligning to the query:
- 297 binding substrate
- 325 binding NAD(+)
- 344 binding NAD(+)
- 401:403 binding NAD(+)
- 408 binding NAD(+)
- 430 binding NAD(+)
- 454 binding NAD(+)
- 501 binding substrate
- 660 binding substrate
Query Sequence
>WP_054558757.1 NCBI__GCF_001306415.1:WP_054558757.1
MEYKNIYIEEERNLGTITIDRPKKLNALNKATIEELHVAFKELDADKNIKAIIITGNGEK
AFVAGADISEFAHFSEKEGGVLAAKGQELLFDFIAHLSTPVIAAVNGFALGGGLELAMAC
HFRVASSNAKMGLPEVSLGVIPGYGGTQRLPQLVGKGRAMEMIMTAGMISAEQALDYGLV
NYVVEPEDLMPLCTKLASKISNNSPVAIAHAINAINAGYSFNTNGYAAEIEAFGACFGTN
DFKEGTTAFLEKRKANFPGS
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