SitesBLAST
Comparing AO353_19310 FitnessBrowser__pseudo3_N2E3:AO353_19310 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)
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)
34% identity, 94% coverage: 18:265/265 of query aligns to 21:267/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
34% identity, 96% coverage: 10:263/265 of query aligns to 5:254/257 of 6slbAAA
- active site: Q64 (≠ G69), F69 (≠ M74), L80 (≠ Y85), N84 (= N89), A108 (≠ G117), S111 (≠ G120), A130 (≠ P139), F131 (≠ E140), L136 (= L145), P138 (= P147), D139 (≠ A148), A224 (≠ D233), G234 (≠ V243)
- 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 (≠ G63), A62 (= A67), Q64 (≠ G69), D65 (= D70), L66 (= L71), Y76 (≠ G81), A108 (≠ G117), F131 (≠ E140), D139 (≠ A148)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
34% identity, 96% coverage: 10:263/265 of query aligns to 2:242/245 of 6slaAAA
- active site: Q61 (≠ G69), L68 (≠ Y85), N72 (= N89), A96 (≠ G117), S99 (≠ G120), A118 (≠ P139), F119 (≠ E140), L124 (= L145), P126 (= P147), N127 (≠ A148), A212 (≠ D233), G222 (≠ V243)
- 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 (≠ R29), A59 (= A67), Q61 (≠ G69), D62 (= D70), L63 (= L71), L68 (≠ Y85), Y71 (≠ L88), A94 (≠ L115), G95 (= G116), A96 (≠ G117), F119 (≠ E140), I122 (≠ L143), L124 (= L145), N127 (≠ A148), F234 (= F255), K237 (= K258)
Q62651 Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial; EC 5.3.3.- from Rattus norvegicus (Rat) (see paper)
29% identity, 91% coverage: 18:259/265 of query aligns to 66:317/327 of Q62651
- D176 (≠ G120) mutation D->A,D: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- E196 (= E140) mutation E->D,Q: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- D204 (vs. gap) mutation D->A,N: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
6l3pA Crystal strcuture of feruloyl-coa hydratase lyase(fchl) complexed with coa
33% identity, 71% coverage: 9:196/265 of query aligns to 9:190/244 of 6l3pA
- active site: M69 (≠ G69), Y74 (≠ M74), R86 (= R86), Q90 (≠ R90), G114 (= G117), S117 (≠ G120), S136 (≠ P139), E137 (= E140), I142 (≠ L145), P144 (= P147), G145 (≠ A148)
- binding coenzyme a: K28 (≠ C28), R29 (= R29), A31 (= A31), A67 (= A67), M69 (≠ G69), D70 (= D70), L71 (= L71), G113 (= G116)
Sites not aligning to the query:
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
32% identity, 97% coverage: 8:263/265 of query aligns to 4:254/255 of 3q0jC
- active site: A65 (≠ G69), M70 (= M74), T80 (≠ Q83), F84 (≠ N89), G108 (= G117), E111 (≠ G120), P130 (= P139), E131 (= E140), V136 (≠ L145), P138 (= P147), G139 (≠ A148), L224 (= L231), F234 (≠ V243)
- binding acetoacetyl-coenzyme a: Q23 (≠ D27), A24 (≠ C28), L25 (≠ R29), A27 (= A31), A63 (= A67), G64 (= G68), A65 (≠ G69), D66 (= D70), I67 (≠ L71), K68 (= K72), M70 (= M74), F84 (≠ N89), G107 (= G116), G108 (= G117), E111 (≠ G120), P130 (= P139), E131 (= E140), P138 (= P147), G139 (≠ A148), M140 (≠ Q149)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
32% identity, 97% coverage: 8:263/265 of query aligns to 4:254/255 of 3q0gC
- active site: A65 (≠ G69), M70 (= M74), T80 (≠ Q83), F84 (≠ N89), G108 (= G117), E111 (≠ G120), P130 (= P139), E131 (= E140), V136 (≠ L145), P138 (= P147), G139 (≠ A148), L224 (= L231), F234 (≠ V243)
- binding coenzyme a: L25 (≠ R29), A63 (= A67), I67 (≠ L71), K68 (= K72), Y104 (≠ A113), P130 (= P139), E131 (= E140), L134 (= L143)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
32% identity, 97% coverage: 8:263/265 of query aligns to 3:253/256 of 3h81A
- active site: A64 (≠ G69), M69 (= M74), T79 (≠ Q83), F83 (≠ N89), G107 (= G117), E110 (≠ G120), P129 (= P139), E130 (= E140), V135 (≠ L145), P137 (= P147), G138 (≠ A148), L223 (= L231), F233 (≠ V243)
- binding calcium ion: F233 (≠ V243), Q238 (≠ G248)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
26% identity, 96% coverage: 8:261/265 of query aligns to 4:254/259 of 5zaiC
- active site: A65 (≠ G69), F70 (≠ M74), S82 (≠ R86), R86 (= R90), G110 (= G117), E113 (≠ G120), P132 (= P139), E133 (= E140), I138 (≠ L145), P140 (= P147), G141 (≠ A148), A226 (vs. gap), F236 (≠ V243)
- binding coenzyme a: K24 (≠ C28), L25 (≠ R29), A63 (= A67), G64 (= G68), A65 (≠ G69), D66 (= D70), I67 (≠ L71), P132 (= P139), R166 (= R172), F248 (= F255), K251 (= K258)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
32% identity, 97% coverage: 8:263/265 of query aligns to 3:249/250 of 3q0gD
- active site: A64 (≠ G69), M69 (= M74), T75 (≠ A79), F79 (≠ N89), G103 (= G117), E106 (≠ G120), P125 (= P139), E126 (= E140), V131 (≠ L145), P133 (= P147), G134 (≠ A148), L219 (= L231), F229 (≠ V243)
- binding Butyryl Coenzyme A: F225 (= F239), F241 (= F255)
Q5HH38 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Staphylococcus aureus (strain COL) (see paper)
29% identity, 98% coverage: 3:263/265 of query aligns to 8:266/273 of Q5HH38
- R34 (= R29) binding in other chain
- SGGDQ 73:77 (≠ AGGDL 67:71) binding in other chain
- S149 (≠ L145) binding in other chain
6p5uE Structure of an enoyl-coa hydratase/aldolase isolated from a lignin- degrading consortium (see paper)
32% identity, 67% coverage: 9:185/265 of query aligns to 7:186/246 of 6p5uE
- active site: M67 (≠ G69), Y72 (≠ M74), D77 (≠ A79), R89 (= R90), A93 (= A94), G117 (= G117), T120 (≠ G120), E140 (= E140), I145 (≠ L145), P147 (= P147), A148 (= A148)
- binding coenzyme a: D25 (= D27), K26 (≠ C28), R27 (= R29), A29 (= A31), A65 (= A67), M67 (≠ G69), D68 (= D70), L69 (= L71), W113 (≠ A113), F115 (≠ L115), S139 (≠ P139), W143 (≠ L143)
Sites not aligning to the query:
Q9LKJ1 3-hydroxyisobutyryl-CoA hydrolase 1; CoA-thioester hydrolase CHY1; EC 3.1.2.-; EC 3.1.2.4 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
32% identity, 67% coverage: 10:187/265 of query aligns to 11:190/378 of Q9LKJ1
- G70 (= G69) mutation to S: Loss of activity.
- E142 (= E140) mutation to A: Loss of activity.
- D150 (≠ A148) mutation to G: Reduced activity.
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
31% identity, 91% coverage: 22:263/265 of query aligns to 19:258/261 of 5jbxB
- active site: A67 (≠ G69), R72 (≠ M74), L84 (≠ R86), R88 (≠ N89), G112 (= G117), E115 (≠ G120), T134 (≠ P139), E135 (= E140), I140 (≠ L145), P142 (= P147), G143 (≠ A148), A228 (≠ D233), L238 (≠ V243)
- binding coenzyme a: S24 (≠ D27), R25 (≠ C28), R26 (= R29), A28 (= A31), A65 (= A67), D68 (= D70), L69 (= L71), K70 (= K72), L110 (= L115), G111 (= G116), T134 (≠ P139), E135 (= E140), L138 (= L143), R168 (= R172)
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
33% identity, 77% coverage: 1:204/265 of query aligns to 1:208/266 of O53561
- K135 (≠ Q135) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 135:142, 38% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (≠ S142) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
2uzfA Crystal structure of staphylococcus aureus 1,4-dihydroxy-2-naphthoyl coa synthase (menb) in complex with acetoacetyl coa (see paper)
29% identity, 98% coverage: 3:263/265 of query aligns to 3:253/260 of 2uzfA
- active site: G70 (= G69), R80 (≠ E87), L84 (≠ A91), G108 (= G117), V111 (≠ G120), T130 (≠ P139), G131 (≠ E140), S136 (≠ L145), D138 (≠ P147), A139 (= A148), A225 (= A235), Y233 (≠ V243)
- binding acetoacetyl-coenzyme a: V28 (≠ C28), R29 (= R29), S68 (≠ A67), G69 (= G68), G70 (= G69), D71 (= D70), Y104 (≠ A113), G108 (= G117)
3bptA Crystal structure of human beta-hydroxyisobutyryl-coa hydrolase in complex with quercetin
30% identity, 67% coverage: 21:197/265 of query aligns to 18:196/362 of 3bptA
- active site: G67 (= G69), P84 (vs. gap), R88 (= R86), G115 (= G117), G118 (= G120), E138 (= E140), D146 (≠ A148)
- binding (2r)-3-hydroxy-2-methylpropanoic acid: G66 (= G68), G67 (= G69), I69 (≠ L71), E90 (vs. gap), G114 (= G116), G115 (= G117), E138 (= E140), D146 (≠ A148), V147 (≠ Q149)
- binding 3,5,7,3',4'-pentahydroxyflavone: F25 (≠ C28), L26 (≠ R29), A28 (= A31), G66 (= G68), G67 (= G69), I69 (≠ L71), P137 (= P139), I141 (≠ L143)
Sites not aligning to the query:
2vssD Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
30% identity, 67% coverage: 8:185/265 of query aligns to 7:187/246 of 2vssD
- active site: M68 (≠ G69), Y73 (≠ M74), D78 (≠ A79), R90 (≠ A91), Q94 (= Q100), G118 (= G117), S121 (≠ G120), S140 (≠ P139), E141 (= E140), I146 (≠ L145), P148 (= P147), G149 (≠ A148)
- binding acetyl coenzyme *a: E26 (≠ D27), K27 (≠ C28), R28 (= R29), A30 (= A31), A66 (= A67), M68 (≠ G69), D69 (= D70), L70 (= L71), F74 (≠ A75), W114 (≠ A113), F116 (≠ L115), S140 (≠ P139)
- binding 4-hydroxy-3-methoxybenzaldehyde: M68 (≠ G69), Y73 (≠ M74), F74 (≠ A75), Q96 (≠ A102), E141 (= E140), G149 (≠ A148), N150 (≠ Q149)
Sites not aligning to the query:
2vssB Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
30% identity, 67% coverage: 8:185/265 of query aligns to 6:186/247 of 2vssB
- active site: M67 (≠ G69), Y72 (≠ M74), D77 (≠ A79), R89 (≠ A91), Q93 (= Q100), G117 (= G117), S120 (≠ G120), S139 (≠ P139), E140 (= E140), I145 (≠ L145), P147 (= P147), G148 (≠ A148)
- binding acetyl coenzyme *a: E25 (≠ D27), K26 (≠ C28), R27 (= R29), A29 (= A31), A65 (= A67), M67 (≠ G69), D68 (= D70), W113 (≠ A113), F115 (≠ L115), G117 (= G117), S139 (≠ P139), E140 (= E140)
Sites not aligning to the query:
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, 67% coverage: 8:185/265 of query aligns to 9:189/276 of O69762
- K29 (≠ C28) binding
- A68 (= A67) binding
- M70 (≠ G69) binding
- L72 (= L71) binding
- Y75 (≠ M74) binding
- G120 (= G117) binding
- S123 (≠ G120) mutation to A: Reduced kcat compared to wild-type but not markerdly.
- S142 (≠ P139) binding
- E143 (= E140) mutation to A: Abolishes catalytic activity.
- W146 (≠ L143) binding
- G151 (≠ A148) 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.
Query Sequence
>AO353_19310 FitnessBrowser__pseudo3_N2E3:AO353_19310
MTTLPVCQTLLLELHNGVLHLTLNRPDCRNAMSLQMVAELRAVLAAVRDDRDIRAIVLGG
AGGHFSAGGDLKDMANARAQGQQAYRELNRAFGALLEEAQHAPQVLITVLQGAVLGGGFG
LVCVSDIALTDHNAQFGLPETSLGLLPAQIAPFVVQRIGLTQARRLALTAARFDGHEARR
LGLVHFVEHDAQALAERLDAVLAHVLCCAPGANAATKVLLLASTEQSMGPLLDQAADWFS
EAVTGAEGVEGTMAFVQKRKPGWAP
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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