SitesBLAST
Comparing Ga0059261_2807 Ga0059261_2807 Predicted acyl-CoA transferases/carnitine dehydratase 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)
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
30% identity, 98% coverage: 8:402/403 of query aligns to 2:416/417 of 1q6yA
- active site: Q17 (≠ L23), E140 (≠ D146), D169 (= D175), G248 (vs. gap), G249 (vs. gap)
- binding coenzyme a: V16 (= V22), Q17 (≠ L23), S18 (≠ A24), R38 (≠ H44), L72 (= L78), N73 (≠ D79), T74 (≠ I80), K75 (≠ S81), N96 (= N102), F97 (≠ Y103), H98 (≠ K104), M105 (≠ F111), I124 (= I130), K137 (≠ P143), A138 (≠ G144), Y139 (= Y145), D169 (= D175), M200 (≠ L206)
P69902 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; Formyl-CoA transferase; EC 2.8.3.16 from Escherichia coli (strain K12) (see paper)
30% identity, 98% coverage: 8:402/403 of query aligns to 2:416/416 of P69902
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
30% identity, 98% coverage: 8:402/403 of query aligns to 1:415/415 of 1pt5A
- active site: Q16 (≠ L23), E139 (≠ D146), D168 (= D175), G247 (vs. gap), G248 (vs. gap)
- binding acetyl coenzyme *a: V15 (= V22), S17 (≠ A24), R37 (≠ H44), L71 (= L78), N72 (≠ D79), T73 (≠ I80), K74 (≠ S81), N95 (= N102), F96 (≠ Y103), H97 (≠ K104), K124 (≠ S131), K136 (≠ P143), A137 (≠ G144), Y138 (= Y145), E139 (≠ D146), D168 (= D175), M199 (≠ L206)
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
28% identity, 97% coverage: 8:396/403 of query aligns to 2:422/430 of 3ubmB
- active site: Q17 (≠ L23), E140 (≠ D146), D182 (= D175), G261 (vs. gap), G262 (vs. gap)
- binding coenzyme a: V16 (= V22), R38 (≠ H44), L72 (= L78), N73 (≠ D79), T74 (≠ I80), K75 (≠ S81), N96 (= N102), F97 (≠ Y103), R98 (≠ K104), A101 (≠ G107), R104 (≠ K110), K125 (≠ S131), D182 (= D175), M213 (≠ L206)
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
29% identity, 98% coverage: 8:402/403 of query aligns to 2:409/410 of 1q7eA
- active site: Q17 (≠ L23), E133 (≠ D146), D162 (= D175), G241 (vs. gap), G242 (vs. gap)
- binding methionine: N96 (= N102), F97 (≠ Y103), H98 (≠ K104), P99 (≠ G112), K118 (≠ S131), K130 (≠ P143), A131 (≠ G144), W246 (≠ T237), F299 (≠ D291), A303 (= A295), E306 (≠ M298)
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
29% identity, 98% coverage: 10:402/403 of query aligns to 4:428/428 of O06644
- Q17 (≠ L23) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (≠ H44) binding
- W48 (= W54) mutation to F: Little change in the affinity binding and catalytic efficiency, and it does not display major structural changes.; mutation to P: Little change in the affinity binding and catalytic efficiency. It exhibits substrate inhibition with oxalate. It does not display major structural changes.
- R104 (≠ K110) binding
- D169 (= D175) active site, Nucleophile; mutation to A: Loss of CoA-transferase activity.; mutation to E: Loss of CoA-transferase activity.; mutation to S: Loss of CoA-transferase activity.
- G259 (vs. gap) mutation to A: 2.5-fold decrease of the catalytic effiency.
- G260 (vs. gap) mutation to A: 25-fold decrease of the catalytic effiency. Reduction of the affinity binding for both formyl-CoA and oxalate.
1p5rA Formyl-coa transferase in complex with coenzyme a (see paper)
29% identity, 98% coverage: 10:402/403 of query aligns to 3:427/427 of 1p5rA
- active site: Q16 (≠ L23), E139 (≠ D146), D168 (= D175), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R21), V15 (= V22), Q16 (≠ L23), A17 (= A24), R37 (≠ H44), M73 (≠ I80), K74 (≠ S81), N95 (= N102), F96 (≠ Y103), A100 (≠ G107), R103 (≠ K110), K136 (≠ P143), V137 (≠ G144), D168 (= D175), M199 (≠ L206)
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
29% identity, 98% coverage: 10:402/403 of query aligns to 3:427/427 of 2vjoA
- active site: A16 (≠ L23), E139 (≠ D146), D168 (= D175), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R21), A16 (≠ L23), A17 (= A24), R37 (≠ H44), L71 (= L78), M73 (≠ I80), N95 (= N102), F96 (≠ Y103), G97 (≠ K104), R103 (≠ K110), M104 (≠ F111), K136 (≠ P143), V137 (≠ G144), Y138 (= Y145), D168 (= D175), M199 (≠ L206)
- binding oxalate ion: G257 (vs. gap), G259 (vs. gap), Q261 (vs. gap)
2vjkA Formyl-coa transferase with aspartyl-coa thioester intermediate derived from oxalyl-coa (see paper)
29% identity, 98% coverage: 10:402/403 of query aligns to 3:427/427 of 2vjkA
- active site: Q16 (≠ L23), E139 (≠ D146), D168 (= D175), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R21), Q16 (≠ L23), A17 (= A24), R37 (≠ H44), M73 (≠ I80), K74 (≠ S81), N95 (= N102), F96 (≠ Y103), G97 (≠ K104), R103 (≠ K110), M104 (≠ F111), K136 (≠ P143), V137 (≠ G144), Y138 (= Y145), D168 (= D175), M199 (≠ L206)
- binding magnesium ion: D293 (≠ R267), D296 (= D270)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
29% identity, 98% coverage: 10:402/403 of query aligns to 3:427/427 of 1t4cA
- active site: Q16 (≠ L23), E139 (≠ D146), D168 (= D175), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R21), V15 (= V22), Q16 (≠ L23), R37 (≠ H44), M73 (≠ I80), N95 (= N102), F96 (≠ Y103), R103 (≠ K110), M104 (≠ F111), V137 (≠ G144), Y138 (= Y145), D168 (= D175), M199 (≠ L206)
- binding oxalic acid: G259 (vs. gap), G260 (vs. gap)
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
30% identity, 93% coverage: 8:383/403 of query aligns to 3:360/360 of 5yx6A
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
29% identity, 98% coverage: 10:402/403 of query aligns to 3:427/427 of 1t3zA
- active site: Q16 (≠ L23), E139 (≠ D146), S168 (≠ D175), G259 (vs. gap), G260 (vs. gap)
- binding oxidized coenzyme a: H14 (≠ R21), V15 (= V22), A17 (= A24), R37 (≠ H44), K74 (≠ S81), N95 (= N102), F96 (≠ Y103), A100 (≠ G107), R103 (≠ K110), M104 (≠ F111), K136 (≠ P143), V137 (≠ G144), Y138 (= Y145), E139 (≠ D146), M199 (≠ L206)
8apqB Camct - mesaconyl-coa c1:c4 coa transferase of chloroflexus aurantiacus (see paper)
31% identity, 98% coverage: 11:403/403 of query aligns to 5:403/406 of 8apqB
- binding coenzyme a: F16 (≠ V22), V17 (≠ L23), A18 (= A24), P38 (≠ H44), I74 (= I80), N100 (= N102), F101 (≠ Y103), L124 (≠ I130), V125 (≠ Y133), G126 (= G134), D165 (= D175)
- binding (2e)-2-methylbut-2-enedioic acid: V17 (≠ L23), R47 (≠ H53), D165 (= D175)
- binding Mesaconyl Coenzme A: T249 (≠ N257), L251 (≠ A259)
8apqA Camct - mesaconyl-coa c1:c4 coa transferase of chloroflexus aurantiacus (see paper)
31% identity, 98% coverage: 11:403/403 of query aligns to 5:403/406 of 8apqA
- binding Mesaconyl Coenzme A: G13 (≠ L19), F16 (≠ V22), V17 (≠ L23), P38 (≠ H44), R47 (≠ H53), I74 (= I80), R75 (≠ S81), N100 (= N102), F101 (≠ Y103), P102 (≠ K104), L107 (= L113), L124 (≠ I130), V125 (≠ Y133), G126 (= G134), S132 (≠ A140), E133 (= E141), V134 (≠ Y145), D135 (= D146), Y136 (= Y147), D165 (= D175)
Q9UHK6 Alpha-methylacyl-CoA racemase; 2-methylacyl-CoA racemase; EC 5.1.99.4 from Homo sapiens (Human) (see 5 papers)
25% identity, 97% coverage: 11:402/403 of query aligns to 3:373/382 of Q9UHK6
- V9 (≠ L17) to M: in dbSNP:rs3195676
- S52 (= S75) to P: in AMACRD and CBAS4; inactive enzyme; dbSNP:rs121917814
- L107 (≠ I130) to P: in CBAS4; inactive enzyme; dbSNP:rs121917816
- G175 (= G197) to D: in dbSNP:rs10941112
- L201 (≠ V223) to S: in dbSNP:rs2287939
- M261 (≠ V287) to T: in dbSNP:rs3195678
- E277 (≠ R303) to K: in dbSNP:rs2278008
Sites not aligning to the query:
- 380:382 Microbody targeting signal
O06543 Alpha-methylacyl-CoA racemase; AMACR; MtMCR; EC 5.1.99.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
29% identity, 64% coverage: 8:263/403 of query aligns to 2:246/360 of O06543
- R38 (≠ H44) binding
- R52 (= R71) mutation to A: 15.7% of wild-type activity.
- I56 (≠ S75) mutation to P: 28.8% of wild-type activity.
- ADLK 59:62 (≠ LDIS 78:81) binding
- E82 (= E101) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NYK 102:104) binding
- R91 (≠ K110) binding ; mutation to A: 19.9% of wild-type activity.
- M111 (≠ I130) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ GYDYVI 144:149) binding
- H126 (≠ Y145) mutation to A: 4.5% of wild-type activity.
- D156 (= D175) mutation to A: 17.6 of wild-type activity.
- D190 (= D208) mutation to A: 3.3% of wild-type activity.
- E241 (≠ D258) mutation to A: 2.1% of wild-type activity.
Sites not aligning to the query:
- 297 C→A: 6.2% of wild-type activity.
- 312 H→A: 10.1% of wild-type activity.
2gd6A The 1,1-proton transfer reaction mechanism by alpha-methylacyl-coa racemase is catalyzed by an aspartate/histidine pair and involves a smooth, methionine-rich surface for binding the fatty acyl moiety (see paper)
29% identity, 64% coverage: 8:263/403 of query aligns to 1:240/354 of 2gd6A
- active site: G16 (≠ L23), D121 (= D146), D150 (= D175), G213 (≠ T237), G214 (≠ V238)
- binding acetyl coenzyme *a: I15 (≠ V22), R37 (≠ H44), A53 (≠ L78), D54 (= D79), L55 (≠ I80), K56 (≠ S81), G77 (≠ N102), Y78 (= Y103), R79 (≠ K104), V82 (≠ G107), R85 (≠ K110), G119 (= G144), H120 (≠ Y145), Y124 (≠ I149), D150 (= D175), M182 (≠ L206)
2gd2A The 1,1-proton transfer reaction mechanism by alpha-methylacyl-coa racemase is catalyzed by an aspartate/histidine pair and involves a smooth, methionine-rich surface for binding the fatty acyl moiety (see paper)
29% identity, 64% coverage: 8:263/403 of query aligns to 1:240/354 of 2gd2A
- active site: G16 (≠ L23), D121 (= D146), D150 (= D175), G213 (≠ T237), G214 (≠ V238)
- binding acetoacetyl-coenzyme a: I15 (≠ V22), R37 (≠ H44), A53 (≠ L78), L55 (≠ I80), K56 (≠ S81), G77 (≠ N102), Y78 (= Y103), R79 (≠ K104), V82 (≠ G107), R85 (≠ K110), L86 (≠ F111), A118 (≠ P143), G119 (= G144), H120 (≠ Y145), Y124 (≠ I149), D150 (= D175)
2gd0A The 1,1-proton transfer reaction mechanism by alpha-methylacyl-coa racemase is catalyzed by an aspartate/histidine pair and involves a smooth, methionine-rich surface for binding the fatty acyl moiety (see paper)
29% identity, 64% coverage: 8:263/403 of query aligns to 1:240/354 of 2gd0A
- active site: G16 (≠ L23), D121 (= D146), D150 (= D175), G213 (≠ T237), G214 (≠ V238)
- binding (s)-2-methylmyristoyl-coenzyme a: D42 (= D49), L55 (≠ I80), K56 (≠ S81), G77 (≠ N102), Y78 (= Y103), R79 (≠ K104), V82 (≠ G107), R85 (≠ K110), L86 (≠ F111), G119 (= G144), H120 (≠ Y145), D121 (= D146), Y124 (≠ I149), D150 (= D175)
2gciA The 1,1-proton transfer reaction mechanism by alpha-methylacyl-coa racemase is catalyzed by an asparte/histidine pair and involves a smooth, methionine-rich surface for binding the fatty acyl moiety (see paper)
29% identity, 64% coverage: 8:263/403 of query aligns to 1:240/354 of 2gciA
- active site: G16 (≠ L23), D121 (= D146), D150 (= D175), G213 (≠ T237), G214 (≠ V238)
- binding (r)-2-methylmyristoyl-coenzyme a: R37 (≠ H44), L55 (≠ I80), K56 (≠ S81), G77 (≠ N102), Y78 (= Y103), R79 (≠ K104), V82 (≠ G107), G119 (= G144), H120 (≠ Y145), D121 (= D146), Y124 (≠ I149), D150 (= D175), Y218 (= Y241), I234 (≠ N257), E235 (≠ D258)
Query Sequence
>Ga0059261_2807 Ga0059261_2807 Predicted acyl-CoA transferases/carnitine dehydratase
MTNMNKGAAPLAGRRVLDLSRVLAGPWCTMVLADLGAEVTKVEHPRGGDDTRHWGPPYTG
GESAYYLCANRNKRSVALDISKPEGQRIVRDLAAQADVLVENYKLGGLEKFGLDYSSIAA
INPRIVYCSISGYGRRSPIAERPGYDYVIQAEGGLMSVTGPVDGEPMKVGVAVADLFTGM
AAAQAILAALIAADRDGAGQHLDMALYDCQLAMLANVGSAALVAGTEPRRYGNGHPTVVP
YQLFDTLDGQVVVAVGNDAQFTAFATRLLDRPDLATDERFAKNGSRVANRDALLAEIMPL
MRRHTTEWWLAGLRSVGVPTGAVRQVGEALAAPEATARDMVATVAHPSAGEVKLVASPLK
LGRTPVVSPVAPPMLGQHSRTVLAELGYRADEIEALFETGVIA
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