SitesBLAST
Comparing Ga0059261_2160 FitnessBrowser__Korea:Ga0059261_2160 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)
P09110 3-ketoacyl-CoA thiolase, peroxisomal; Acetyl-CoA C-myristoyltransferase; Acetyl-CoA acyltransferase; Beta-ketothiolase; Peroxisomal 3-oxoacyl-CoA thiolase; EC 2.3.1.16; EC 2.3.1.155; EC 2.3.1.9 from Homo sapiens (Human) (see 3 papers)
43% identity, 99% coverage: 3:398/398 of query aligns to 37:422/424 of P09110
- V387 (≠ I364) to A: in dbSNP:rs2229528
Sites not aligning to the query:
- 1:26 PTS2-type peroxisomal targeting signal
- 5 mutation Q->D,K,L: Does not affect localization to peroxisomes.
- 6 V→D: Abolished localization to peroxisomes.; V→K: Does not affect localization to peroxisomes.
- 7 mutation V->D,K: Abolished localization to peroxisomes.
- 8 mutation L->D,K: Does not affect localization to peroxisomes.
- 9 mutation G->D,R,L: Does not affect localization to peroxisomes.
- 10 H→E: In S3E mutant; Abolished localization to peroxisomes.
P14611 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337) (Ralstonia eutropha) (see paper)
40% identity, 98% coverage: 1:392/398 of query aligns to 1:387/393 of P14611
- C88 (= C90) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (≠ P146) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ G218) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (= R220) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S253) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H354) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C384) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
39% identity, 98% coverage: 6:396/398 of query aligns to 7:390/392 of P07097
- Q64 (≠ G65) mutation to A: Slightly lower activity.
- C89 (= C90) mutation to A: Loss of activity.
- C378 (= C384) mutation to G: Loss of activity.
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
39% identity, 98% coverage: 6:396/398 of query aligns to 7:390/392 of 1ou6A
- active site: C89 (= C90), H348 (= H354), C378 (= C384), G380 (≠ A386)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (= L137), H156 (≠ M145), M157 (= M147), F235 (≠ W235), A243 (= A249), S247 (= S253), A318 (= A324), F319 (= F325), H348 (= H354)
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
39% identity, 98% coverage: 6:396/398 of query aligns to 4:387/389 of 2vu2A
- active site: C86 (= C90), H345 (= H354), C375 (= C384), G377 (≠ A386)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (≠ M145), M154 (= M147), F232 (≠ W235), S244 (= S253), G245 (≠ Q254), F316 (= F325), H345 (= H354)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
39% identity, 98% coverage: 6:396/398 of query aligns to 4:387/389 of 1dm3A
- active site: C86 (= C90), H345 (= H354), C375 (= C384), G377 (≠ A386)
- binding acetyl coenzyme *a: C86 (= C90), L145 (= L137), H153 (≠ M145), M154 (= M147), R217 (= R220), S224 (≠ A227), M225 (≠ L228), A240 (= A249), S244 (= S253), M285 (= M294), A315 (= A324), F316 (= F325), H345 (= H354), C375 (= C384)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
39% identity, 98% coverage: 6:396/398 of query aligns to 4:387/389 of 1dlvA
- active site: C86 (= C90), H345 (= H354), C375 (= C384), G377 (≠ A386)
- binding coenzyme a: C86 (= C90), L145 (= L137), H153 (≠ M145), M154 (= M147), R217 (= R220), L228 (= L231), A240 (= A249), S244 (= S253), H345 (= H354)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
39% identity, 98% coverage: 6:396/398 of query aligns to 6:389/391 of 2vu1A
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
39% identity, 98% coverage: 1:392/398 of query aligns to 1:387/393 of 4o9cC
- active site: S88 (≠ C90), H349 (= H354), C379 (= C384), G381 (≠ A386)
- binding coenzyme a: S88 (≠ C90), L148 (vs. gap), R221 (= R220), F236 (≠ W235), A244 (= A249), S248 (= S253), L250 (= L255), A319 (= A324), F320 (= F325), H349 (= H354)
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
39% identity, 98% coverage: 6:396/398 of query aligns to 4:387/389 of 2wkuA
- active site: C86 (= C90), H345 (= H354), C375 (= C384), G377 (≠ A386)
- binding D-mannose: S6 (= S8), A7 (≠ T9), R38 (= R41), K182 (≠ R175), D194 (≠ E187), V280 (≠ C289), D281 (≠ A290), T287 (≠ I296), P331 (= P340), S332 (≠ E341), V334 (≠ Y343), V336 (= V345), F360 (≠ I369)
2d3tC Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form v (see paper)
37% identity, 99% coverage: 2:396/398 of query aligns to 5:388/390 of 2d3tC
- active site: C94 (= C90), H346 (= H354), C376 (= C384), G378 (≠ A386)
- binding acetyl coenzyme *a: C94 (= C90), R214 (= R220), L222 (= L228), L225 (= L231), A238 (= A249), G239 (= G250), S242 (= S253), I244 (≠ L255), A313 (= A324), F314 (= F325), H346 (= H354), C376 (= C384)
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
39% identity, 98% coverage: 6:396/398 of query aligns to 5:388/390 of 1m1oA
- active site: A87 (≠ C90), H346 (= H354), C376 (= C384), G378 (≠ A386)
- binding acetoacetyl-coenzyme a: L86 (≠ K89), A87 (≠ C90), L146 (= L137), H154 (≠ M145), M155 (= M147), R218 (= R220), S225 (≠ A227), M226 (≠ L228), A241 (= A249), G242 (= G250), S245 (= S253), A316 (= A324), F317 (= F325), H346 (= H354), I377 (≠ T385), G378 (≠ A386)
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
40% identity, 99% coverage: 1:396/398 of query aligns to 1:389/391 of 5f38B
- active site: C88 (= C90), H347 (= H354), C377 (= C384), G379 (≠ A386)
- binding coenzyme a: C88 (= C90), L149 (= L137), K219 (≠ R220), F234 (≠ W235), A242 (= A249), S246 (= S253), A317 (= A324), F318 (= F325), H347 (= H354)
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
39% identity, 99% coverage: 1:396/398 of query aligns to 3:393/394 of 5f38D
- active site: C90 (= C90), A348 (= A351), A378 (≠ V381), L380 (≠ M383)
- binding [(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(2-sulfanylethylamino)propyl]amino]butyl] phosphono hydrogen phosphate: C90 (= C90), L151 (= L137), A246 (= A249), S250 (= S253), I252 (≠ L255), A321 (= A324), F322 (= F325), H351 (= H354)
A0R1Y7 Probable acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; EC 2.3.1.9 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
38% identity, 97% coverage: 6:392/398 of query aligns to 2:383/388 of A0R1Y7
- K187 (≠ A181) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
6pccA Crystal structure of beta-ketoadipyl-coa thiolase mutant (h356a) in complex hexanoyl coenzyme a (see paper)
39% identity, 98% coverage: 1:392/398 of query aligns to 4:397/403 of 6pccA
- active site: C93 (= C90), A359 (≠ H354), C389 (= C384), G391 (≠ A386)
- binding coenzyme a: C93 (= C90), I148 (≠ D127), R229 (= R220), T232 (= T223), A252 (= A249), S256 (= S253), N325 (= N322), F328 (= F325)
- binding hexanal: N61 (= N58), T146 (= T125), I148 (≠ D127), G149 (≠ A128), R151 (= R130), L361 (≠ F356)
6pcbA Crystal structure of beta-ketoadipyl-coa thiolase mutant (h356a) in complex with coa (see paper)
39% identity, 98% coverage: 1:392/398 of query aligns to 4:397/403 of 6pcbA
- active site: C93 (= C90), A359 (≠ H354), C389 (= C384), G391 (≠ A386)
- binding coenzyme a: C93 (= C90), I148 (≠ D127), R229 (= R220), A252 (= A249), S256 (= S253), G257 (≠ Q254), N325 (= N322), F328 (= F325)
P42765 3-ketoacyl-CoA thiolase, mitochondrial; Acetyl-CoA acetyltransferase; Acetyl-CoA acyltransferase; Acyl-CoA hydrolase, mitochondrial; Beta-ketothiolase; Mitochondrial 3-oxoacyl-CoA thiolase; T1; EC 2.3.1.16; EC 2.3.1.9; EC 3.1.2.-; EC 3.1.2.1; EC 3.1.2.2 from Homo sapiens (Human) (see paper)
35% identity, 99% coverage: 1:396/398 of query aligns to 4:394/397 of P42765
- C92 (= C90) mutation to A: Decreased acyl-CoA hydrolase activity.; mutation to S: Decreased acyl-CoA hydrolase activity; when associated with A-382.
- R224 (= R220) binding
- T227 (= T223) binding
- S251 (= S253) binding
- C382 (= C384) mutation to S: Decreased acyl-CoA hydrolase activity; when associated with S-92.
4c2jD Crystal structure of human mitochondrial 3-ketoacyl-coa thiolase in complex with coa (see paper)
35% identity, 99% coverage: 1:396/398 of query aligns to 7:393/395 of 4c2jD
6pcdA Crystal structure of beta-ketoadipyl-coa thiolase mutant (c90s-h356a) in complex octanoyl coenzyme a (see paper)
38% identity, 98% coverage: 1:392/398 of query aligns to 5:395/401 of 6pcdA
- active site: S94 (≠ C90), A357 (≠ H354), C387 (= C384), G389 (≠ A386)
- binding coenzyme a: I149 (≠ D127), M167 (= M147), R227 (= R220), T230 (= T223), A250 (= A249), S254 (= S253), G255 (≠ Q254), A325 (= A324), A357 (≠ H354)
- binding octanal: N62 (= N58), T147 (= T125), T148 (≠ K126), I149 (≠ D127), G150 (≠ A128), R152 (= R130), L359 (≠ F356)
Query Sequence
>Ga0059261_2160 FitnessBrowser__Korea:Ga0059261_2160
MREAAIVSTARTGIGKAYRGAFNTTEAPVLAGHVMNAAVERAGVDPARIDDIFWGVGNQW
GTQGGNAGRMAVFAAGLPQSVPAFTLDRKCGSGLTALALAARSIIAGDIDIALSGGMESI
SLTVTKDAPRYANQSVLANEPHAYMPMIETAEIVAERYGISRARQDEYGAMSQQRAEAGL
ASGAFAEEIAPITVEKAIFDKEGNRTGSERVTVTQDEGIRAGTTAEALAGLKTVWKDGQV
VKEGRHITAGNASQLSDGAAAQIVMDRAIAEAEGKEILGIYRGFQAAGCAPDEMGIGPVF
AIPKLLGRAGLEVADIGLWELNEAFASQCLYCRDTLGIDPEKYNVNGGAIAIGHPFGMTG
ARLIGHALIEGRKRGVRWVVVSMCTAGGMGAAGLFEIP
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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