SitesBLAST
Comparing GFF929 FitnessBrowser__Marino:GFF929 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)
38% identity, 99% coverage: 3:259/259 of query aligns to 4:259/259 of 5zaiC
- active site: A65 (= A64), F70 (= F69), S82 (≠ G81), R86 (≠ G85), G110 (= G109), E113 (= E112), P132 (= P131), E133 (= E132), I138 (≠ L137), P140 (= P139), G141 (≠ C140), A226 (≠ R226), F236 (= F236)
- binding coenzyme a: K24 (≠ P22), L25 (≠ A23), A63 (= A62), G64 (= G63), A65 (= A64), D66 (= D65), I67 (≠ L66), P132 (= P131), R166 (= R165), F248 (= F248), K251 (= K251)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
38% identity, 98% coverage: 5:259/259 of query aligns to 7:261/261 of 5jbxB
- active site: A67 (= A64), R72 (vs. gap), L84 (≠ E79), R88 (≠ G85), G112 (= G109), E115 (= E112), T134 (≠ P131), E135 (= E132), I140 (≠ L137), P142 (= P139), G143 (≠ C140), A228 (≠ R226), L238 (≠ F236)
- binding coenzyme a: S24 (≠ P22), R25 (≠ A23), R26 (vs. gap), A28 (≠ T25), A65 (= A62), D68 (= D65), L69 (= L66), K70 (= K67), L110 (≠ M107), G111 (= G108), T134 (≠ P131), E135 (= E132), L138 (≠ V135), R168 (= R165)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
38% identity, 98% coverage: 5:259/259 of query aligns to 5:256/256 of 3h81A
- active site: A64 (= A64), M69 (≠ F69), T79 (≠ G81), F83 (≠ G85), G107 (= G109), E110 (= E112), P129 (= P131), E130 (= E132), V135 (≠ L137), P137 (= P139), G138 (≠ C140), L223 (≠ R226), F233 (= F236)
- binding calcium ion: F233 (= F236), Q238 (= Q241)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
38% identity, 99% coverage: 3:259/259 of query aligns to 4:260/260 of 2hw5C
- active site: A68 (= A64), M73 (vs. gap), S83 (≠ K74), L87 (≠ G85), G111 (= G109), E114 (= E112), P133 (= P131), E134 (= E132), T139 (≠ L137), P141 (= P139), G142 (≠ C140), K227 (≠ R226), F237 (= F236)
- binding crotonyl coenzyme a: K26 (≠ P22), A27 (= A23), L28 (≠ N24), A30 (≠ W26), K62 (= K58), I70 (≠ L66), F109 (≠ M107)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
38% identity, 97% coverage: 5:256/259 of query aligns to 6:254/255 of 3q0jC
- active site: A65 (= A64), M70 (≠ F69), T80 (≠ G81), F84 (≠ G85), G108 (= G109), E111 (= E112), P130 (= P131), E131 (= E132), V136 (≠ L137), P138 (= P139), G139 (≠ C140), L224 (≠ R226), F234 (= F236)
- binding acetoacetyl-coenzyme a: Q23 (≠ P22), A24 (= A23), L25 (vs. gap), A27 (≠ T25), A63 (= A62), G64 (= G63), A65 (= A64), D66 (= D65), I67 (≠ L66), K68 (= K67), M70 (≠ F69), F84 (≠ G85), G107 (= G108), G108 (= G109), E111 (= E112), P130 (= P131), E131 (= E132), P138 (= P139), G139 (≠ C140), M140 (≠ A141)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
38% identity, 97% coverage: 5:256/259 of query aligns to 6:254/255 of 3q0gC
- active site: A65 (= A64), M70 (≠ F69), T80 (≠ G81), F84 (≠ G85), G108 (= G109), E111 (= E112), P130 (= P131), E131 (= E132), V136 (≠ L137), P138 (= P139), G139 (≠ C140), L224 (≠ R226), F234 (= F236)
- binding coenzyme a: L25 (vs. gap), A63 (= A62), I67 (≠ L66), K68 (= K67), Y104 (= Y105), P130 (= P131), E131 (= E132), L134 (≠ V135)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
39% identity, 97% coverage: 5:256/259 of query aligns to 5:249/250 of 3q0gD
- active site: A64 (= A64), M69 (≠ T68), T75 (≠ K74), F79 (≠ G85), G103 (= G109), E106 (= E112), P125 (= P131), E126 (= E132), V131 (≠ L137), P133 (= P139), G134 (≠ C140), L219 (≠ R226), F229 (= F236)
- binding Butyryl Coenzyme A: F225 (= F232), F241 (= F248)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
37% identity, 98% coverage: 5:259/259 of query aligns to 4:258/258 of 1ey3A
- active site: A66 (= A64), M71 (vs. gap), S81 (≠ K74), L85 (≠ G85), G109 (= G109), E112 (= E112), P131 (= P131), E132 (= E132), T137 (≠ L137), P139 (= P139), G140 (≠ C140), K225 (≠ R226), F235 (= F236)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ P22), L26 (≠ N24), A28 (≠ W26), A64 (= A62), G65 (= G63), A66 (= A64), D67 (= D65), I68 (≠ L66), L85 (≠ G85), W88 (≠ F88), G109 (= G109), P131 (= P131), L135 (≠ V135), G140 (≠ C140)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
37% identity, 98% coverage: 5:259/259 of query aligns to 6:260/260 of 1dubA
- active site: A68 (= A64), M73 (vs. gap), S83 (≠ K74), L87 (≠ G85), G111 (= G109), E114 (= E112), P133 (= P131), E134 (= E132), T139 (≠ L137), P141 (= P139), G142 (≠ C140), K227 (≠ R226), F237 (= F236)
- binding acetoacetyl-coenzyme a: K26 (≠ P22), A27 (= A23), L28 (≠ N24), A30 (≠ W26), A66 (= A62), A68 (= A64), D69 (= D65), I70 (≠ L66), Y107 (= Y105), G110 (= G108), G111 (= G109), E114 (= E112), P133 (= P131), E134 (= E132), L137 (≠ V135), G142 (≠ C140), F233 (= F232), F249 (= F248)
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)
37% identity, 98% coverage: 5:259/259 of query aligns to 36:290/290 of P14604
- E144 (= E112) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E132) 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)
36% identity, 98% coverage: 5:259/259 of query aligns to 5:254/254 of 2dubA
- active site: A67 (= A64), M72 (≠ F69), S82 (= S89), G105 (= G109), E108 (= E112), P127 (= P131), E128 (= E132), T133 (≠ L137), P135 (= P139), G136 (≠ C140), K221 (≠ R226), F231 (= F236)
- binding octanoyl-coenzyme a: K25 (≠ P22), A26 (= A23), L27 (≠ N24), A29 (≠ W26), A65 (= A62), A67 (= A64), D68 (= D65), I69 (≠ L66), K70 (= K67), G105 (= G109), E108 (= E112), P127 (= P131), E128 (= E132), G136 (≠ C140), A137 (= A141)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
36% identity, 98% coverage: 5:259/259 of query aligns to 6:258/258 of 1mj3A
- active site: A68 (= A64), M73 (≠ F69), S83 (= S89), L85 (= L91), G109 (= G109), E112 (= E112), P131 (= P131), E132 (= E132), T137 (≠ L137), P139 (= P139), G140 (≠ C140), K225 (≠ R226), F235 (= F236)
- binding hexanoyl-coenzyme a: K26 (≠ P22), A27 (= A23), L28 (≠ N24), A30 (≠ W26), A66 (= A62), G67 (= G63), A68 (= A64), D69 (= D65), I70 (≠ L66), G109 (= G109), P131 (= P131), E132 (= E132), L135 (≠ V135), G140 (≠ C140)
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
31% identity, 98% coverage: 7:259/259 of query aligns to 12:266/266 of O53561
- K135 (≠ Q127) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 127:134, 25% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (≠ G134) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
34% identity, 99% coverage: 4:259/259 of query aligns to 4:257/257 of 6slbAAA
- active site: Q64 (≠ A64), F69 (= F69), L80 (≠ M80), N84 (≠ G85), A108 (≠ G109), S111 (≠ E112), A130 (≠ P131), F131 (≠ E132), L136 (= L137), P138 (= P139), D139 (≠ C140), A224 (≠ R226), G234 (≠ F236)
- 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 (≠ E57), A62 (= A62), Q64 (≠ A64), D65 (= D65), L66 (= L66), Y76 (≠ R76), A108 (≠ G109), F131 (≠ E132), D139 (≠ C140)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
35% identity, 99% coverage: 4:259/259 of query aligns to 1:245/245 of 6slaAAA
- active site: Q61 (≠ A64), L68 (≠ K74), N72 (= N78), A96 (≠ G109), S99 (≠ E112), A118 (≠ P131), F119 (≠ E132), L124 (= L137), P126 (= P139), N127 (≠ C140), A212 (≠ R226), G222 (≠ F236)
- 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 (≠ A23), A59 (= A62), Q61 (≠ A64), D62 (= D65), L63 (= L66), L68 (≠ K74), Y71 (≠ A77), A94 (≠ M107), G95 (= G108), A96 (≠ G109), F119 (≠ E132), I122 (≠ V135), L124 (= L137), N127 (≠ C140), F234 (= F248), K237 (= K251)
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)
36% identity, 78% coverage: 13:214/259 of query aligns to 11:205/723 of Q08426
- V40 (≠ N42) to G: in dbSNP:rs1062551
- I41 (≠ E43) to R: in dbSNP:rs1062552
- T75 (≠ L83) to I: in dbSNP:rs1062553
- K165 (≠ R173) 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 (≠ E179) 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)
33% identity, 95% coverage: 12:257/259 of query aligns to 20:266/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
6yswA E. Coli anaerobic trifunctional enzyme subunit-alpha in complex with coenzyme a
35% identity, 75% coverage: 12:204/259 of query aligns to 12:206/707 of 6yswA
- active site: A66 (= A64), I71 (≠ F69), A84 (≠ G81), Q88 (≠ G85), G112 (= G109), E115 (= E112), P136 (= P131), E137 (= E132), G145 (≠ C140)
- binding coenzyme a: E23 (vs. gap), M25 (≠ A23), A66 (= A64), D67 (= D65), I68 (≠ L66), P136 (= P131), E137 (= E132), L140 (≠ V135)
Sites not aligning to the query:
6iunB Crystal structure of enoyl-coa hydratase (ech) from ralstonia eutropha h16 in complex with NAD
30% identity, 95% coverage: 6:252/259 of query aligns to 3:274/692 of 6iunB
Sites not aligning to the query:
- active site: 407, 428, 440, 478
- binding nicotinamide-adenine-dinucleotide: 300, 301, 302, 321, 322, 365, 377, 378, 380, 384, 388, 405, 407
6eqoA Tri-functional propionyl-coa synthase of erythrobacter sp. Nap1 with bound NADP+ and phosphomethylphosphonic acid adenylate ester (see paper)
35% identity, 76% coverage: 3:200/259 of query aligns to 859:1060/1804 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
>GFF929 FitnessBrowser__Marino:GFF929
MSDLIQLEKRGHIAVLTINNPPANTWTKDSLIALTNIVKELNEDRDIFALVMTGQGEKFY
SAGADLKTFADGDKARANEMGQLFGEAFSTLQRFRGVSIAAVNGYAMGGGLECAMACDIR
IAEEHAQMALPEAGVGLLPCAGGTQNLPWLVGEGWAKRMILCGERVKADTALRIGLVEEV
VPSGQGLDKALELAEMACQQSPSSTARCKTLVMSARDGRSHDDGWRMERELFVELFSTED
QKEGVNAFLEKRKPEWKNR
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