SitesBLAST
Comparing WP_013257936.1 NCBI__GCF_000143965.1:WP_013257936.1 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)
40% identity, 99% coverage: 4:260/260 of query aligns to 2:259/259 of 5zaiC
- active site: A65 (= A67), F70 (= F72), S82 (≠ N84), R86 (≠ N86), G110 (= G110), E113 (= E113), P132 (= P132), E133 (= E133), I138 (≠ F138), P140 (= P140), G141 (= G141), A226 (≠ K226), F236 (≠ L237)
- binding coenzyme a: K24 (≠ A26), L25 (vs. gap), A63 (= A65), G64 (= G66), A65 (= A67), D66 (= D68), I67 (= I69), P132 (= P132), R166 (≠ F166), F248 (= F249), K251 (= K252)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
39% identity, 96% coverage: 9:257/260 of query aligns to 10:255/258 of 1mj3A
- active site: A68 (= A67), M73 (≠ L75), S83 (≠ N84), L85 (≠ N86), G109 (= G110), E112 (= E113), P131 (= P132), E132 (= E133), T137 (≠ F138), P139 (= P140), G140 (= G141), K225 (= K226), F235 (≠ L237)
- binding hexanoyl-coenzyme a: K26 (≠ P25), A27 (= A26), L28 (vs. gap), A30 (= A28), A66 (= A65), G67 (= G66), A68 (= A67), D69 (= D68), I70 (= I69), G109 (= G110), P131 (= P132), E132 (= E133), L135 (= L136), G140 (= G141)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
39% identity, 97% coverage: 5:257/260 of query aligns to 3:257/260 of 2hw5C
- active site: A68 (= A67), M73 (≠ F72), S83 (≠ K82), L87 (≠ N86), G111 (= G110), E114 (= E113), P133 (= P132), E134 (= E133), T139 (≠ F138), P141 (= P140), G142 (= G141), K227 (= K226), F237 (≠ L237)
- binding crotonyl coenzyme a: K26 (≠ P25), A27 (= A26), L28 (vs. gap), A30 (= A28), K62 (= K61), I70 (= I69), F109 (= F108)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
38% identity, 96% coverage: 9:257/260 of query aligns to 8:255/258 of 1ey3A
- active site: A66 (= A67), M71 (≠ F72), S81 (≠ V80), L85 (≠ N84), G109 (= G110), E112 (= E113), P131 (= P132), E132 (= E133), T137 (≠ F138), P139 (= P140), G140 (= G141), K225 (= K226), F235 (≠ L237)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ P25), L26 (vs. gap), A28 (= A28), A64 (= A65), G65 (= G66), A66 (= A67), D67 (= D68), I68 (= I69), L85 (≠ N84), W88 (≠ F89), G109 (= G110), P131 (= P132), L135 (= L136), G140 (= G141)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
38% identity, 96% coverage: 9:257/260 of query aligns to 10:257/260 of 1dubA
- active site: A68 (= A67), M73 (≠ F72), S83 (≠ V80), L87 (≠ N84), G111 (= G110), E114 (= E113), P133 (= P132), E134 (= E133), T139 (≠ F138), P141 (= P140), G142 (= G141), K227 (= K226), F237 (≠ L237)
- binding acetoacetyl-coenzyme a: K26 (≠ P25), A27 (= A26), L28 (vs. gap), A30 (= A28), A66 (= A65), A68 (= A67), D69 (= D68), I70 (= I69), Y107 (≠ A106), G110 (= G109), G111 (= G110), E114 (= E113), P133 (= P132), E134 (= E133), L137 (= L136), G142 (= G141), F233 (≠ V233), F249 (= F249)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
39% identity, 96% coverage: 9:257/260 of query aligns to 9:251/254 of 2dubA
- active site: A67 (= A67), M72 (≠ L75), S82 (≠ N84), G105 (= G110), E108 (= E113), P127 (= P132), E128 (= E133), T133 (≠ F138), P135 (= P140), G136 (= G141), K221 (= K226), F231 (≠ L237)
- binding octanoyl-coenzyme a: K25 (≠ P25), A26 (= A26), L27 (vs. gap), A29 (= A28), A65 (= A65), A67 (= A67), D68 (= D68), I69 (= I69), K70 (≠ S70), G105 (= G110), E108 (= E113), P127 (= P132), E128 (= E133), G136 (= G141), A137 (≠ W142)
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)
38% identity, 96% coverage: 9:257/260 of query aligns to 40:287/290 of P14604
- E144 (= E113) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E133) 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
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
39% identity, 98% coverage: 7:260/260 of query aligns to 6:261/261 of 5jbxB
- active site: A67 (= A67), R72 (≠ F72), L84 (vs. gap), R88 (≠ N86), G112 (= G110), E115 (= E113), T134 (≠ P132), E135 (= E133), I140 (≠ F138), P142 (= P140), G143 (= G141), A228 (≠ K226), L238 (= L237)
- binding coenzyme a: S24 (≠ P24), R25 (≠ P25), R26 (≠ A26), A28 (= A28), A65 (= A65), D68 (= D68), L69 (≠ I69), K70 (≠ S70), L110 (≠ F108), G111 (= G109), T134 (≠ P132), E135 (= E133), L138 (= L136), R168 (≠ F166)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
33% identity, 98% coverage: 5:260/260 of query aligns to 2:256/256 of 3h81A
- active site: A64 (= A67), M69 (≠ F72), T79 (≠ K82), F83 (≠ N86), G107 (= G110), E110 (= E113), P129 (= P132), E130 (= E133), V135 (≠ F138), P137 (= P140), G138 (= G141), L223 (≠ K226), F233 (≠ L237)
- binding calcium ion: F233 (≠ L237), Q238 (≠ F242)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
33% identity, 98% coverage: 5:258/260 of query aligns to 3:255/255 of 3q0jC
- active site: A65 (= A67), M70 (≠ F72), T80 (≠ K82), F84 (≠ N86), G108 (= G110), E111 (= E113), P130 (= P132), E131 (= E133), V136 (≠ F138), P138 (= P140), G139 (= G141), L224 (≠ K226), F234 (≠ L237)
- binding acetoacetyl-coenzyme a: Q23 (≠ P25), A24 (= A26), L25 (vs. gap), A27 (= A28), A63 (= A65), G64 (= G66), A65 (= A67), D66 (= D68), I67 (= I69), K68 (≠ S70), M70 (≠ F72), F84 (≠ N86), G107 (= G109), G108 (= G110), E111 (= E113), P130 (= P132), E131 (= E133), P138 (= P140), G139 (= G141), M140 (≠ W142)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
33% identity, 98% coverage: 5:258/260 of query aligns to 3:255/255 of 3q0gC
- active site: A65 (= A67), M70 (≠ F72), T80 (≠ K82), F84 (≠ N86), G108 (= G110), E111 (= E113), P130 (= P132), E131 (= E133), V136 (≠ F138), P138 (= P140), G139 (= G141), L224 (≠ K226), F234 (≠ L237)
- binding coenzyme a: L25 (vs. gap), A63 (= A65), I67 (= I69), K68 (≠ S70), Y104 (≠ A106), P130 (= P132), E131 (= E133), L134 (= L136)
6yswA E. Coli anaerobic trifunctional enzyme subunit-alpha in complex with coenzyme a
42% identity, 76% coverage: 16:212/260 of query aligns to 13:217/707 of 6yswA
- active site: A66 (= A67), I71 (≠ F72), A84 (≠ K82), Q88 (≠ N86), G112 (= G110), E115 (= E113), P136 (= P132), E137 (= E133), G145 (= G141)
- binding coenzyme a: E23 (vs. gap), M25 (≠ A26), A66 (= A67), D67 (= D68), I68 (= I69), P136 (= P132), E137 (= E133), L140 (= L136)
Sites not aligning to the query:
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)
40% identity, 75% coverage: 14:209/260 of query aligns to 9:198/723 of Q08426
- V40 (≠ Q45) to G: in dbSNP:rs1062551
- I41 (≠ A46) to R: in dbSNP:rs1062552
- T75 (vs. gap) to I: in dbSNP:rs1062553
- K165 (≠ A174) 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 (≠ A180) 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
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
32% identity, 98% coverage: 5:258/260 of query aligns to 2:250/250 of 3q0gD
- active site: A64 (= A67), M69 (≠ F72), T75 (≠ N84), F79 (vs. gap), G103 (= G110), E106 (= E113), P125 (= P132), E126 (= E133), V131 (≠ F138), P133 (= P140), G134 (= G141), L219 (≠ K226), F229 (≠ L237)
- binding Butyryl Coenzyme A: F225 (≠ V233), F241 (= F249)
6eqoA Tri-functional propionyl-coa synthase of erythrobacter sp. Nap1 with bound NADP+ and phosphomethylphosphonic acid adenylate ester (see paper)
39% identity, 70% coverage: 16:198/260 of query aligns to 867:1061/1804 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
6iunB Crystal structure of enoyl-coa hydratase (ech) from ralstonia eutropha h16 in complex with NAD
40% identity, 78% coverage: 12:214/260 of query aligns to 7:205/692 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
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
35% identity, 97% coverage: 8:260/260 of query aligns to 6:257/257 of 6slbAAA
- active site: Q64 (≠ A67), F69 (= F72), L80 (vs. gap), N84 (= N86), A108 (≠ G110), S111 (≠ E113), A130 (≠ P132), F131 (≠ E133), L136 (≠ F138), P138 (= P140), D139 (≠ G141), A224 (= A231), G234 (vs. gap)
- 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 (= Y83), A108 (≠ G110), F131 (≠ E133), D139 (≠ G141)
3zwaA Crystal structure of rat peroxisomal multifunctional enzyme type 1 (rpmfe1) complexed with 3s-hydroxy-hexanoyl-coa (see paper)
41% identity, 73% coverage: 23:211/260 of query aligns to 24:205/727 of 3zwaA
- active site: A67 (= A67), F72 (= F72), G82 (≠ N86), G106 (= G110), E109 (= E113), P128 (= P132), E129 (= E133), P136 (= P140), G137 (= G141)
- binding (S)-3-Hydroxyhexanoyl-CoA: V27 (≠ A26), A65 (= A65), G66 (= G66), A67 (= A67), D68 (= D68), I69 (= I69), L104 (≠ F108), E109 (= E113), R124 (≠ I128), E129 (= E133), L132 (= L136), G137 (= G141), Y162 (≠ F166)
Sites not aligning to the query:
6zicAAA structure of rat peroxisomal multifunctional enzyme type-1 (rpmfe1) complexed with 3s-hydroxybutanoyl-coa and nadh'
41% identity, 73% coverage: 23:211/260 of query aligns to 23:204/723 of 6zicAAA
- active site: A66 (= A67), F71 (= F72), G81 (≠ N86), G105 (= G110), E108 (= E113), P127 (= P132), E128 (= E133), G136 (= G141)
- binding 3-hydroxybutanoyl-coenzyme a: P25 (= P25), V26 (≠ A26), A28 (= A28), A66 (= A67), D67 (= D68), I68 (= I69), G104 (= G109), G105 (= G110), E108 (= E113), E128 (= E133), Y161 (≠ F166)
Sites not aligning to the query:
- active site: 254, 413, 434, 446, 484
- binding 1,4-dihydronicotinamide adenine dinucleotide: 308, 310, 311, 312, 331, 332, 336, 383, 384, 385, 386, 390, 391, 411, 413, 434
6z5oAAA Peroxisomal bifunctional enzyme (see paper)
41% identity, 73% coverage: 23:211/260 of query aligns to 24:205/716 of 6z5oAAA
- active site: A67 (= A67), F72 (= F72), G82 (≠ N86), G106 (= G110), E109 (= E113), P128 (= P132), E129 (= E133), G137 (= G141)
- binding coenzyme a: P26 (= P25), V27 (≠ A26), A65 (= A65), D68 (= D68), I69 (= I69), P128 (= P132), Y162 (≠ F166)
- binding nicotinamide: A67 (= A67), E109 (= E113), E129 (= E133), P136 (= P140)
Sites not aligning to the query:
- active site: 255, 409, 430, 442, 480
- binding coenzyme a: 277, 281
- binding nicotinamide-adenine-dinucleotide: 309, 311, 312, 313, 332, 333, 337, 379, 380, 381, 382, 387, 407, 409, 430
- binding nicotinamide: 261
Query Sequence
>WP_013257936.1 NCBI__GCF_000143965.1:WP_013257936.1
MAYEFEKIKATQDGAVLVATIDSPPANALGQGVLRDLSALLDQAQADEAVRVIVLCGQGP
KLFSAGADISEFAGLQAGVVPKYNGNEIFSRIETFPKVVIAAMQGAAFGGGLELCLCCHL
RVMSEKAICGLPEVKLGFMPGWGGTQRLPRLIGKTKAMELILTGDFISANQALALGLVCA
LAPAEETVAHAVKLAQKLAAGAPLAQREIIKAIHNGLQTTVADGVKNVEGAGVATLLGSQ
DFKEGAKAFLEKRKAQFVGR
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