SitesBLAST
Comparing GFF3367 FitnessBrowser__Phaeo:GFF3367 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)
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
37% identity, 97% coverage: 10:261/261 of query aligns to 14:266/266 of O53561
- K135 (≠ T127) 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 (≠ R134) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
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)
38% identity, 94% coverage: 14:259/261 of query aligns to 21:266/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
35% identity, 98% coverage: 6:261/261 of query aligns to 6:259/259 of 5zaiC
- active site: A65 (≠ W65), F70 (≠ A70), S82 (≠ G81), R86 (≠ F85), G110 (= G109), E113 (= E112), P132 (= P131), E133 (= E132), I138 (≠ T137), P140 (≠ A139), G141 (≠ D140), A226 (≠ Q230), F236 (≠ Y238)
- binding coenzyme a: K24 (= K23), L25 (≠ A24), A63 (≠ P63), G64 (= G64), A65 (≠ W65), D66 (= D66), I67 (≠ L67), P132 (= P131), R166 (≠ W164), F248 (= F250), K251 (= K253)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
35% identity, 99% coverage: 1:258/261 of query aligns to 1:254/255 of 3q0jC
- active site: A65 (≠ W65), M70 (≠ A70), T80 (≠ D77), F84 (= F85), G108 (= G109), E111 (= E112), P130 (= P131), E131 (= E132), V136 (≠ T137), P138 (≠ A139), G139 (≠ D140), L224 (≠ K228), F234 (≠ Y238)
- binding acetoacetyl-coenzyme a: Q23 (≠ K23), A24 (= A24), L25 (vs. gap), A27 (= A26), A63 (≠ P63), G64 (= G64), A65 (≠ W65), D66 (= D66), I67 (≠ L67), K68 (= K68), M70 (≠ A70), F84 (= F85), G107 (= G108), G108 (= G109), E111 (= E112), P130 (= P131), E131 (= E132), P138 (≠ A139), G139 (≠ D140), M140 (vs. gap)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
35% identity, 99% coverage: 1:258/261 of query aligns to 1:254/255 of 3q0gC
- active site: A65 (≠ W65), M70 (≠ A70), T80 (≠ D77), F84 (= F85), G108 (= G109), E111 (= E112), P130 (= P131), E131 (= E132), V136 (≠ T137), P138 (≠ A139), G139 (≠ D140), L224 (≠ K228), F234 (≠ Y238)
- binding coenzyme a: L25 (vs. gap), A63 (≠ P63), I67 (≠ L67), K68 (= K68), Y104 (≠ I105), P130 (= P131), E131 (= E132), L134 (≠ S135)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
36% identity, 94% coverage: 17:261/261 of query aligns to 16:256/256 of 3h81A
- active site: A64 (≠ W65), M69 (≠ A70), T79 (≠ D77), F83 (= F85), G107 (= G109), E110 (= E112), P129 (= P131), E130 (= E132), V135 (≠ T137), P137 (≠ A139), G138 (≠ D140), L223 (≠ K228), F233 (≠ Y238)
- binding calcium ion: F233 (≠ Y238), Q238 (= Q243)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
34% identity, 96% coverage: 10:259/261 of query aligns to 13:256/258 of 1mj3A
- active site: A68 (≠ W65), M73 (≠ A70), S83 (≠ Y80), L85 (≠ V82), G109 (= G109), E112 (= E112), P131 (= P131), E132 (= E132), T137 (= T137), P139 (≠ A139), G140 (≠ D140), K225 (≠ R225), F235 (≠ Y238)
- binding hexanoyl-coenzyme a: K26 (= K23), A27 (= A24), L28 (vs. gap), A30 (= A26), A66 (≠ P63), G67 (= G64), A68 (≠ W65), D69 (= D66), I70 (≠ L67), G109 (= G109), P131 (= P131), E132 (= E132), L135 (≠ S135), G140 (≠ D140)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
35% identity, 96% coverage: 10:259/261 of query aligns to 13:258/260 of 2hw5C
- active site: A68 (≠ W65), M73 (≠ A70), S83 (≠ G81), L87 (≠ F85), G111 (= G109), E114 (= E112), P133 (= P131), E134 (= E132), T139 (= T137), P141 (≠ A139), G142 (≠ D140), K227 (= K228), F237 (≠ Y238)
- binding crotonyl coenzyme a: K26 (= K23), A27 (= A24), L28 (vs. gap), A30 (= A26), K62 (= K59), I70 (≠ L67), F109 (≠ C107)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
33% identity, 96% coverage: 10:259/261 of query aligns to 11:256/258 of 1ey3A
- active site: A66 (≠ W65), M71 (≠ A70), S81 (≠ D77), L85 (≠ F85), G109 (= G109), E112 (= E112), P131 (= P131), E132 (= E132), T137 (= T137), P139 (≠ A139), G140 (≠ D140), K225 (≠ R225), F235 (≠ Y238)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (= K23), L26 (vs. gap), A28 (= A26), A64 (≠ P63), G65 (= G64), A66 (≠ W65), D67 (= D66), I68 (≠ L67), L85 (≠ F85), W88 (≠ L88), G109 (= G109), P131 (= P131), L135 (≠ S135), G140 (≠ D140)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
33% identity, 96% coverage: 10:259/261 of query aligns to 13:258/260 of 1dubA
- active site: A68 (≠ W65), M73 (≠ A70), S83 (≠ D77), L87 (≠ F85), G111 (= G109), E114 (= E112), P133 (= P131), E134 (= E132), T139 (= T137), P141 (≠ A139), G142 (≠ D140), K227 (≠ R225), F237 (≠ Y238)
- binding acetoacetyl-coenzyme a: K26 (= K23), A27 (= A24), L28 (vs. gap), A30 (= A26), A66 (≠ P63), A68 (≠ W65), D69 (= D66), I70 (≠ L67), Y107 (≠ I105), G110 (= G108), G111 (= G109), E114 (= E112), P133 (= P131), E134 (= E132), L137 (≠ S135), G142 (≠ D140), F233 (≠ L231), 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)
33% identity, 96% coverage: 10:259/261 of query aligns to 43:288/290 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)
33% identity, 96% coverage: 10:259/261 of query aligns to 12:252/254 of 2dubA
- active site: A67 (≠ W65), M72 (≠ A70), S82 (≠ G86), G105 (= G109), E108 (= E112), P127 (= P131), E128 (= E132), T133 (= T137), P135 (≠ A139), G136 (≠ D140), K221 (≠ R225), F231 (≠ Y238)
- binding octanoyl-coenzyme a: K25 (= K23), A26 (= A24), L27 (vs. gap), A29 (= A26), A65 (≠ P63), A67 (≠ W65), D68 (= D66), I69 (≠ L67), K70 (= K68), G105 (= G109), E108 (= E112), P127 (= P131), E128 (= E132), G136 (≠ D140), A137 (= A141)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
36% identity, 93% coverage: 17:258/261 of query aligns to 16:249/250 of 3q0gD
- active site: A64 (≠ W65), M69 (≠ A70), T75 (≠ D77), F79 (= F85), G103 (= G109), E106 (= E112), P125 (= P131), E126 (= E132), V131 (≠ T137), P133 (≠ A139), G134 (≠ D140), L219 (≠ K228), F229 (≠ Y238)
- binding Butyryl Coenzyme A: F225 (≠ V234), F241 (= F250)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
35% identity, 98% coverage: 6:261/261 of query aligns to 6:257/257 of 6slbAAA
- active site: Q64 (≠ W65), F69 (≠ A70), L80 (≠ V82), N84 (≠ G86), A108 (≠ G109), S111 (≠ E112), A130 (≠ P131), F131 (≠ E132), L136 (≠ T137), P138 (≠ A139), D139 (= D140), A224 (≠ N224), G234 (≠ Y238)
- 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 (≠ K59), A62 (≠ P63), Q64 (≠ W65), D65 (= D66), L66 (= L67), Y76 (≠ G78), A108 (≠ G109), F131 (≠ E132), D139 (= D140)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
34% identity, 98% coverage: 6:261/261 of query aligns to 3:245/245 of 6slaAAA
- active site: Q61 (≠ W65), L68 (≠ A75), N72 (= N79), A96 (≠ G109), S99 (≠ E112), A118 (≠ P131), F119 (≠ E132), L124 (≠ T137), P126 (≠ A139), N127 (≠ D140), A212 (≠ N224), G222 (≠ Y238)
- 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 (≠ A24), A59 (≠ P63), Q61 (≠ W65), D62 (= D66), L63 (= L67), L68 (≠ A75), Y71 (≠ G78), A94 (≠ C107), G95 (= G108), A96 (≠ G109), F119 (≠ E132), I122 (≠ S135), L124 (≠ T137), N127 (≠ D140), F234 (= F250), K237 (= K253)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
34% identity, 96% coverage: 12:261/261 of query aligns to 13:261/261 of 5jbxB
- active site: A67 (≠ W65), R72 (≠ A70), L84 (≠ V82), R88 (≠ L88), G112 (= G109), E115 (= E112), T134 (≠ P131), E135 (= E132), I140 (≠ T137), P142 (vs. gap), G143 (≠ A139), A228 (≠ K228), L238 (≠ Y238)
- binding coenzyme a: S24 (≠ P22), R25 (≠ K23), R26 (≠ A24), A28 (= A26), A65 (≠ P63), D68 (= D66), L69 (= L67), K70 (= K68), L110 (≠ C107), G111 (= G108), T134 (≠ P131), E135 (= E132), L138 (≠ S135), R168 (≠ W164)
1ef9A The crystal structure of methylmalonyl coa decarboxylase complexed with 2s-carboxypropyl coa (see paper)
31% identity, 83% coverage: 46:261/261 of query aligns to 46:261/261 of 1ef9A
- active site: H66 (≠ W65), L71 (≠ A70), D82 (≠ G81), R86 (≠ F85), G110 (= G109), E113 (= E112), P133 (≠ E132), V138 (≠ T137), Y140 (≠ A139), N141 (≠ D140), E228 (≠ N224), Y238 (= Y238)
- binding 2-carboxypropyl-coenzyme a: A64 (≠ P63), H66 (≠ W65), D67 (= D66), I68 (≠ L67), H69 (≠ K68), W108 (≠ C107), G110 (= G109), T132 (≠ P131), P133 (≠ E132), K253 (= K253)
P52045 Methylmalonyl-CoA decarboxylase; MMCD; Transcarboxylase; EC 4.1.1.- from Escherichia coli (strain K12) (see paper)
31% identity, 83% coverage: 46:261/261 of query aligns to 46:261/261 of P52045
- G110 (= G109) binding
- T132 (≠ P131) binding
- K253 (= K253) binding
6n97A Methylmalonyl-coa decarboxylase in complex with 2-sulfonate-propionyl- amino(dethia)-coa (see paper)
31% identity, 83% coverage: 46:261/261 of query aligns to 45:260/260 of 6n97A
- active site: H65 (≠ W65), L70 (≠ A70), G109 (= G109), E112 (= E112), P132 (≠ E132), V137 (≠ T137), Y139 (≠ A139), E227 (≠ N224), Y237 (= Y238)
- binding (2R)-sulfonatepropionyl-amino(dethia)-CoA: K59 (= K59), A63 (≠ P63), H65 (≠ W65), D66 (= D66), I67 (≠ L67), W107 (≠ C107), G108 (= G108), G109 (= G109), T131 (≠ P131), P132 (≠ E132), L135 (≠ S135), Y139 (≠ A139), F249 (= F250), K252 (= K253)
- binding (2S)-sulfonatepropionyl-amino(dethia)-CoA: K59 (= K59), A63 (≠ P63), H65 (≠ W65), D66 (= D66), I67 (≠ L67), W107 (≠ C107), G108 (= G108), G109 (= G109), T131 (≠ P131), P132 (≠ E132), L135 (≠ S135), Y139 (≠ A139), F249 (= F250), K252 (= K253)
Sites not aligning to the query:
6n96A Methylmalonyl-coa decarboxylase in complex with 2-sulfonate-propionyl- oxa(dethia)-coa (see paper)
31% identity, 83% coverage: 46:261/261 of query aligns to 45:260/260 of 6n96A
- active site: H65 (≠ W65), L70 (≠ A70), G109 (= G109), E112 (= E112), P132 (≠ E132), V137 (≠ T137), Y139 (≠ A139), E227 (≠ N224), Y237 (= Y238)
- binding (2~{S})-1-[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]ethoxy]-1-oxidanylidene-propane-2-sulfonic acid: K59 (= K59), A63 (≠ P63), H65 (≠ W65), D66 (= D66), I67 (≠ L67), H68 (≠ K68), W107 (≠ C107), G108 (= G108), G109 (= G109), T131 (≠ P131), P132 (≠ E132), L135 (≠ S135), V137 (≠ T137), Y139 (≠ A139), F249 (= F250), K252 (= K253)
- binding (2~{R})-1-[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]ethoxy]-1-oxidanylidene-propane-2-sulfonic acid: K59 (= K59), A63 (≠ P63), H65 (≠ W65), D66 (= D66), I67 (≠ L67), H68 (≠ K68), W107 (≠ C107), G108 (= G108), G109 (= G109), T131 (≠ P131), P132 (≠ E132), L135 (≠ S135), V137 (≠ T137), Y139 (≠ A139), F249 (= F250), K252 (= K253)
Query Sequence
>GFF3367 FitnessBrowser__Phaeo:GFF3367
MTDTPIRTRRNGPILEITLDRPKANAIDLKTSVAMGEVFRDFRDDPELRVAILTGGGEKF
FCPGWDLKAAADGDAVDGNYGVGGFGGLQELRDMNKPVIAAVNGIACGGGLELALSADMI
VAADHATFALPEIRSGTVADAASIKLPKRIPYHIAMELLLTGRWFDAEEAHRWGLVNEIV
TADQLLDRAWELARLLASGPPLVYAAIKEIVRDAEDSKFQDAMNRITKRQLRSVDVLYDS
EDQMEGARAFAEKRDPVWKGR
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