SitesBLAST
Comparing Ga0059261_2908 FitnessBrowser__Korea:Ga0059261_2908 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)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
34% identity, 87% coverage: 31:269/275 of query aligns to 25:258/261 of 5jbxB
- active site: A67 (≠ I72), R72 (≠ L77), L84 (≠ M89), R88 (≠ A97), G112 (= G125), E115 (≠ Q128), T134 (≠ M147), E135 (= E148), I140 (= I153), P142 (= P155), G143 (≠ D156), A228 (≠ L239), L238 (= L249)
- binding coenzyme a: R25 (≠ K31), R26 (≠ M32), A28 (= A34), A65 (= A70), D68 (= D73), L69 (= L74), K70 (≠ E75), L110 (≠ F123), G111 (= G124), T134 (≠ M147), E135 (= E148), L138 (≠ W151), R168 (≠ V181)
Sites not aligning to the query:
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
30% identity, 93% coverage: 17:271/275 of query aligns to 14:265/266 of O53561
- K135 (= K143) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 143:150, 38% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (≠ R150) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
30% identity, 94% coverage: 11:269/275 of query aligns to 4:256/259 of 5zaiC
- active site: A65 (≠ I72), F70 (≠ L77), S82 (≠ R92), R86 (≠ L96), G110 (= G125), E113 (≠ Q128), P132 (≠ M147), E133 (= E148), I138 (= I153), P140 (= P155), G141 (≠ D156), A226 (≠ L239), F236 (≠ L249)
- binding coenzyme a: K24 (= K31), L25 (≠ M32), A63 (= A70), G64 (= G71), A65 (≠ I72), D66 (= D73), I67 (≠ L74), P132 (≠ M147), R166 (≠ V181), F248 (≠ H261), K251 (≠ Q264)
Q62651 Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial; EC 5.3.3.- from Rattus norvegicus (Rat) (see paper)
32% identity, 89% coverage: 21:265/275 of query aligns to 66:317/327 of Q62651
- D176 (≠ Q128) mutation D->A,D: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- E196 (= E148) mutation E->D,Q: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- D204 (= D156) mutation D->A,N: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
32% identity, 92% coverage: 17:269/275 of query aligns to 9:254/257 of 6slbAAA
- active site: Q64 (≠ I72), F69 (≠ E84), L80 (≠ A97), N84 (≠ Q101), A108 (≠ G125), S111 (≠ Q128), A130 (≠ M147), F131 (≠ E148), L136 (≠ I153), P138 (= P155), D139 (= D156), A224 (≠ L239), G234 (≠ L249)
- 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 (≠ K66), A62 (= A70), Q64 (≠ I72), D65 (= D73), L66 (= L74), Y76 (≠ S91), A108 (≠ G125), F131 (≠ E148), D139 (= D156)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
29% identity, 96% coverage: 8:270/275 of query aligns to 1:255/255 of 3q0jC
- active site: A65 (≠ I72), M70 (≠ L77), T80 (≠ Q101), F84 (≠ L105), G108 (= G125), E111 (≠ Q128), P130 (≠ M147), E131 (= E148), V136 (≠ I153), P138 (= P155), G139 (≠ D156), L224 (= L239), F234 (≠ L249)
- binding acetoacetyl-coenzyme a: Q23 (≠ F30), A24 (≠ K31), L25 (≠ M32), A27 (= A34), A63 (= A70), G64 (= G71), A65 (≠ I72), D66 (= D73), I67 (≠ L74), K68 (≠ E75), M70 (≠ L77), F84 (≠ L105), G107 (= G124), G108 (= G125), E111 (≠ Q128), P130 (≠ M147), E131 (= E148), P138 (= P155), G139 (≠ D156), M140 (= M157)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
29% identity, 96% coverage: 8:270/275 of query aligns to 1:255/255 of 3q0gC
- active site: A65 (≠ I72), M70 (≠ L77), T80 (≠ Q101), F84 (≠ L105), G108 (= G125), E111 (≠ Q128), P130 (≠ M147), E131 (= E148), V136 (≠ I153), P138 (= P155), G139 (≠ D156), L224 (= L239), F234 (≠ L249)
- binding coenzyme a: L25 (≠ M32), A63 (= A70), I67 (≠ L74), K68 (≠ E75), Y104 (≠ V121), P130 (≠ M147), E131 (= E148), L134 (≠ W151)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
30% identity, 90% coverage: 24:270/275 of query aligns to 16:254/256 of 3h81A
- active site: A64 (≠ I72), M69 (≠ L77), T79 (≠ Q101), F83 (≠ L105), G107 (= G125), E110 (≠ Q128), P129 (≠ M147), E130 (= E148), V135 (≠ I153), P137 (= P155), G138 (≠ D156), L223 (= L239), F233 (≠ L249)
- binding calcium ion: F233 (≠ L249), Q238 (= Q254)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
29% identity, 90% coverage: 24:270/275 of query aligns to 16:250/250 of 3q0gD
- active site: A64 (≠ I72), M69 (≠ L77), T75 (≠ Q101), F79 (≠ L105), G103 (= G125), E106 (≠ Q128), P125 (≠ M147), E126 (= E148), V131 (≠ I153), P133 (= P155), G134 (≠ D156), L219 (= L239), F229 (≠ L249)
- binding Butyryl Coenzyme A: F225 (≠ Q245), F241 (≠ H261)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
31% identity, 92% coverage: 17:269/275 of query aligns to 6:242/245 of 6slaAAA
- active site: Q61 (≠ I72), L68 (≠ A97), N72 (≠ Q101), A96 (≠ G125), S99 (≠ Q128), A118 (≠ M147), F119 (≠ E148), L124 (≠ I153), P126 (= P155), N127 (≠ D156), A212 (≠ L239), G222 (≠ L249)
- 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 (≠ M32), A59 (= A70), Q61 (≠ I72), D62 (= D73), L63 (= L74), L68 (≠ A97), Y71 (= Y100), A94 (≠ F123), G95 (= G124), A96 (≠ G125), F119 (≠ E148), I122 (≠ W151), L124 (≠ I153), N127 (≠ D156), F234 (≠ H261), K237 (≠ Q264)
5du6A Crystal structure of m. Tuberculosis echa6 bound to ligand gsk059a. (see paper)
30% identity, 93% coverage: 13:269/275 of query aligns to 3:239/242 of 5du6A
- active site: A61 (≠ I72), P71 (≠ S82), I75 (vs. gap), A99 (≠ G125), Q102 (= Q128), P121 (≠ M147), T122 (≠ E148), L127 (≠ I153), L129 (≠ P155), D130 (= D156), P209 (≠ L239), W219 (≠ L249)
- binding (5R,7R)-5-(4-ethylphenyl)-N-(4-fluorobenzyl)-7-methyl-4,5,6,7-tetrahydropyrazolo[1,5-a]pyrimidine-3-carboxamide: L74 (vs. gap), D82 (≠ Q90), D130 (= D156), W132 (≠ A158), A207 (= A237), K212 (≠ S242), F215 (≠ Q245)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
28% identity, 93% coverage: 16:271/275 of query aligns to 12:259/260 of 2hw5C
- active site: A68 (≠ I72), M73 (≠ L77), S83 (≠ A97), L87 (≠ Q101), G111 (= G125), E114 (≠ Q128), P133 (≠ M147), E134 (= E148), T139 (≠ I153), P141 (= P155), G142 (≠ D156), K227 (≠ L239), F237 (≠ L249)
- binding crotonyl coenzyme a: K26 (≠ F30), A27 (≠ K31), L28 (≠ M32), A30 (= A34), K62 (= K66), I70 (≠ L74), F109 (= F123)
5ducA Crystal structure of m. Tuberculosis echa6 bound to ligand gsk951a (see paper)
31% identity, 93% coverage: 13:269/275 of query aligns to 3:241/244 of 5ducA
- active site: A61 (≠ I72), D66 (≠ Q78), P73 (≠ A97), I77 (≠ Q101), A101 (≠ G125), Q104 (= Q128), P123 (≠ M147), T124 (≠ E148), L129 (≠ I153), L131 (≠ P155), D132 (= D156), P211 (≠ L239), W221 (≠ L249)
- binding (5R,7S)-N-(1,3-benzodioxol-5-ylmethyl)-5-(4-ethylphenyl)-7-(trifluoromethyl)-4,5,6,7-tetrahydropyrazolo[1,5-a]pyrimidine-3-carboxamide: L76 (≠ Y100), H80 (≠ A104), D84 (≠ R108), Q104 (= Q128), D132 (= D156), W134 (≠ A158), F217 (≠ Q245)
5du4A Crystal structure of m. Tuberculosis echa6 bound to ligand gsk366a (see paper)
31% identity, 93% coverage: 13:269/275 of query aligns to 3:241/244 of 5du4A
- active site: A61 (≠ I72), D66 (≠ Q78), P73 (≠ A97), I77 (≠ Q101), A101 (≠ G125), Q104 (= Q128), P123 (≠ M147), T124 (≠ E148), L129 (≠ I153), L131 (≠ P155), D132 (= D156), P211 (≠ L239), W221 (≠ L249)
- binding (5R,7S)-5-(4-ethylphenyl)-N-(4-methoxybenzyl)-7-(trifluoromethyl)-4,5,6,7-tetrahydropyrazolo[1,5-a]pyrimidine-3-carboxamide: L76 (≠ Y100), I77 (≠ Q101), H80 (≠ A104), D84 (≠ R108), Q104 (= Q128), D132 (= D156), W134 (≠ A158)
5dtwA Crystal structure of m. Tuberculosis echa6 bound to c20-coa (see paper)
31% identity, 93% coverage: 13:269/275 of query aligns to 3:241/244 of 5dtwA
- active site: A61 (≠ I72), D66 (≠ Q78), P73 (≠ A97), I77 (≠ Q101), A101 (≠ G125), Q104 (= Q128), P123 (≠ M147), T124 (≠ E148), L129 (≠ I153), L131 (≠ P155), D132 (= D156), P211 (≠ L239), W221 (≠ L249)
- binding Arachinoyl-CoA: R18 (= R28), E20 (≠ F30), R21 (≠ K31), R21 (≠ K31), R22 (≠ M32), A24 (= A34), A59 (= A70), A61 (≠ I72), D62 (= D73), L63 (= L74), H80 (≠ A104), D84 (≠ R108), G100 (= G124), A101 (≠ G125), Y127 (≠ W151), W134 (≠ A158)
5dufA Crystal structure of m. Tuberculosis echa6 bound to ligand gsk729a (see paper)
31% identity, 93% coverage: 13:269/275 of query aligns to 4:242/245 of 5dufA
- active site: A62 (≠ I72), D67 (≠ Q78), P74 (≠ A97), I78 (≠ Q101), A102 (≠ G125), Q105 (= Q128), P124 (≠ M147), T125 (≠ E148), L130 (≠ I153), L132 (≠ P155), D133 (= D156), P212 (≠ L239), W222 (≠ L249)
- binding (5R,7S)-5-(4-ethylphenyl)-7-(trifluoromethyl)-4,5,6,7-tetrahydropyrazolo[1,5-a]pyrimidine-3-carboxylic acid: L77 (≠ Y100), I78 (≠ Q101), H81 (≠ A104), D85 (≠ R108), Q105 (= Q128), D133 (= D156), W135 (≠ A158)
O69762 Hydroxycinnamoyl-CoA hydratase-lyase; HCHL; P-hydroxycinnamoyl CoA hydratase/lyase; Trans-feruloyl-CoA hydratase/vanillin synthase; EC 4.1.2.61 from Pseudomonas fluorescens (see 2 papers)
30% identity, 78% coverage: 20:233/275 of query aligns to 18:230/276 of O69762
- K29 (= K31) binding
- A68 (= A70) binding
- M70 (≠ I72) binding
- L72 (= L74) binding
- Y75 (≠ L77) binding
- G120 (= G125) binding
- S123 (≠ Q128) mutation to A: Reduced kcat compared to wild-type but not markerdly.
- S142 (≠ M147) binding
- E143 (= E148) mutation to A: Abolishes catalytic activity.
- W146 (= W151) binding
- G151 (= G159) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 239 binding ; Y→F: Increased KM for feruloyl-CoA but retains a significant amount of catalytic activity with a kcat 10 times less than that of the wild-type.
2vssD Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
30% identity, 78% coverage: 20:233/275 of query aligns to 16:228/246 of 2vssD
- active site: M68 (≠ I72), Y73 (≠ L77), D78 (= D83), R90 (≠ G95), Q94 (≠ R99), G118 (= G125), S121 (≠ Q128), S140 (≠ M147), E141 (= E148), I146 (= I153), P148 (= P155), G149 (= G159)
- binding acetyl coenzyme *a: E26 (≠ F30), K27 (= K31), R28 (≠ M32), A30 (= A34), A66 (= A70), M68 (≠ I72), D69 (= D73), L70 (= L74), F74 (≠ Q78), W114 (≠ V121), F116 (= F123), S140 (≠ M147)
- binding 4-hydroxy-3-methoxybenzaldehyde: M68 (≠ I72), Y73 (≠ L77), F74 (≠ Q78), Q96 (= Q101), E141 (= E148), G149 (= G159), N150 (≠ T160)
Sites not aligning to the query:
2vssB Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
30% identity, 78% coverage: 20:233/275 of query aligns to 15:227/247 of 2vssB
- active site: M67 (≠ I72), Y72 (≠ L77), D77 (= D83), R89 (≠ G95), Q93 (≠ R99), G117 (= G125), S120 (≠ Q128), S139 (≠ M147), E140 (= E148), I145 (= I153), P147 (= P155), G148 (= G159)
- binding acetyl coenzyme *a: E25 (≠ F30), K26 (= K31), R27 (≠ M32), A29 (= A34), A65 (= A70), M67 (≠ I72), D68 (= D73), W113 (≠ V121), F115 (= F123), G117 (= G125), S139 (≠ M147), E140 (= E148)
Sites not aligning to the query:
Q5LLW6 Methylthioacryloyl-CoA hydratase; EC 4.2.1.155 from Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi) (see paper)
32% identity, 82% coverage: 17:242/275 of query aligns to 17:236/267 of Q5LLW6
- K31 (= K31) binding
- R32 (≠ M32) binding
- A69 (= A70) binding
- L71 (≠ I72) binding
- L73 (= L74) binding
- G118 (= G125) binding
- E121 (≠ Q128) active site, Nucleophile; mutation to A: Abolishes catalytic activity.
- E141 (= E148) active site, Proton acceptor; mutation to A: Abolishes catalytic activity.
- R144 (≠ W151) binding
- G149 (≠ D156) binding
Query Sequence
>Ga0059261_2908 FitnessBrowser__Korea:Ga0059261_2908
MRQLQERMIGDRVSIGRAGAVADIRLRRPFKMNALDGPMFDALIAAAESVAVDPTIRAVV
LSGEGKAFCAGIDLESLQALMSDEGKQAMQSRSHGLANRYQQAALAWREVPVPVIAALHG
VAFGGGLQIPLGADIRISAPDTKFSLMEVRWGIVPDMAGTVLLRSIVREDVLRELIYTAR
VFTGIEAASMGIVTQLAANPHVAALELASSIAEQGPRAVRAAKQLLNETQSVSPQVALLS
ESEAQVGLLAGPDQIEALNAHAEQRKPYYTDPEVS
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