SitesBLAST
Comparing RR42_RS32705 FitnessBrowser__Cup4G11:RR42_RS32705 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)
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, 99% coverage: 1:400/405 of query aligns to 1:411/416 of P69902
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
30% identity, 99% coverage: 1:400/405 of query aligns to 1:411/417 of 1q6yA
- active site: Q17 (≠ V17), E140 (≠ D146), D169 (= D179), G248 (vs. gap), G249 (vs. gap)
- binding coenzyme a: V16 (= V16), Q17 (≠ V17), S18 (≠ A18), R38 (≠ K38), L72 (≠ I78), N73 (≠ D79), T74 (≠ I80), K75 (≠ S81), N96 (= N102), F97 (≠ Y103), H98 (≠ K104), M105 (≠ Y111), I124 (≠ V130), K137 (≠ P143), A138 (= A144), Y139 (= Y145), D169 (= D179), M200 (= M210)
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
30% identity, 99% coverage: 2:400/405 of query aligns to 1:410/415 of 1pt5A
- active site: Q16 (≠ V17), E139 (≠ D146), D168 (= D179), G247 (vs. gap), G248 (vs. gap)
- binding acetyl coenzyme *a: V15 (= V16), S17 (≠ A18), R37 (≠ K38), L71 (≠ I78), N72 (≠ D79), T73 (≠ I80), K74 (≠ S81), N95 (= N102), F96 (≠ Y103), H97 (≠ K104), K124 (≠ T131), K136 (≠ P143), A137 (= A144), Y138 (= Y145), E139 (≠ D146), D168 (= D179), M199 (= M210)
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
29% identity, 100% coverage: 2:404/405 of query aligns to 2:427/430 of 3ubmB
- active site: Q17 (≠ V17), E140 (≠ D146), D182 (= D179), G261 (≠ V241), G262 (≠ A242)
- binding coenzyme a: V16 (= V16), R38 (≠ K38), L72 (≠ I78), N73 (≠ D79), T74 (≠ I80), K75 (≠ S81), N96 (= N102), F97 (≠ Y103), R98 (≠ K104), A101 (≠ S107), R104 (≠ K110), K125 (≠ T131), D182 (= D179), M213 (= M210)
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
29% identity, 100% coverage: 1:405/405 of query aligns to 1:428/428 of O06644
- Q17 (≠ V17) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (≠ K38) binding
- W48 (≠ F51) 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 (= D179) 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, 99% coverage: 5:405/405 of query aligns to 4:427/427 of 1p5rA
- active site: Q16 (≠ V17), E139 (≠ D146), D168 (= D179), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R15), V15 (= V16), Q16 (≠ V17), A17 (= A18), R37 (≠ K38), M73 (≠ I80), K74 (≠ S81), N95 (= N102), F96 (≠ Y103), A100 (≠ S107), R103 (≠ K110), K136 (≠ P143), V137 (≠ A144), D168 (= D179), M199 (= M210)
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
29% identity, 99% coverage: 5:405/405 of query aligns to 4:427/427 of 2vjoA
- active site: A16 (≠ V17), E139 (≠ D146), D168 (= D179), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R15), A16 (≠ V17), A17 (= A18), R37 (≠ K38), L71 (≠ I78), M73 (≠ I80), N95 (= N102), F96 (≠ Y103), G97 (≠ K104), R103 (≠ K110), M104 (≠ Y111), K136 (≠ P143), V137 (≠ A144), Y138 (= Y145), D168 (= D179), M199 (= M210)
- 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, 99% coverage: 5:405/405 of query aligns to 4:427/427 of 2vjkA
- active site: Q16 (≠ V17), E139 (≠ D146), D168 (= D179), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R15), Q16 (≠ V17), A17 (= A18), R37 (≠ K38), M73 (≠ I80), K74 (≠ S81), N95 (= N102), F96 (≠ Y103), G97 (≠ K104), R103 (≠ K110), M104 (≠ Y111), K136 (≠ P143), V137 (≠ A144), Y138 (= Y145), D168 (= D179), M199 (= M210)
- binding magnesium ion: D293 (≠ K270), D296 (≠ G273)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
29% identity, 99% coverage: 5:405/405 of query aligns to 4:427/427 of 1t4cA
- active site: Q16 (≠ V17), E139 (≠ D146), D168 (= D179), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R15), V15 (= V16), Q16 (≠ V17), R37 (≠ K38), M73 (≠ I80), N95 (= N102), F96 (≠ Y103), R103 (≠ K110), M104 (≠ Y111), V137 (≠ A144), Y138 (= Y145), D168 (= D179), M199 (= M210)
- 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: 5:380/405 of query aligns to 6:355/360 of 5yx6A
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
28% identity, 99% coverage: 5:405/405 of query aligns to 4:427/427 of 1t3zA
- active site: Q16 (≠ V17), E139 (≠ D146), S168 (≠ D179), G259 (vs. gap), G260 (vs. gap)
- binding oxidized coenzyme a: H14 (≠ R15), V15 (= V16), A17 (= A18), R37 (≠ K38), K74 (≠ S81), N95 (= N102), F96 (≠ Y103), A100 (≠ S107), R103 (≠ K110), M104 (≠ Y111), K136 (≠ P143), V137 (≠ A144), Y138 (= Y145), E139 (≠ D146), M199 (= M210)
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
29% identity, 99% coverage: 1:400/405 of query aligns to 1:404/410 of 1q7eA
- active site: Q17 (≠ V17), E133 (≠ D146), D162 (= D179), G241 (vs. gap), G242 (vs. gap)
- binding methionine: N96 (= N102), F97 (≠ Y103), H98 (≠ Y111), P99 (≠ G112), K118 (≠ T131), K130 (≠ P143), A131 (= A144), W246 (vs. gap), F299 (≠ D294), A303 (≠ E298), E306 (≠ A301)
8apqB Camct - mesaconyl-coa c1:c4 coa transferase of chloroflexus aurantiacus (see paper)
28% identity, 100% coverage: 1:405/405 of query aligns to 1:402/406 of 8apqB
- binding coenzyme a: F16 (≠ V16), V17 (= V17), A18 (= A18), P38 (≠ K38), I74 (= I80), N100 (= N102), F101 (≠ Y103), L124 (≠ V130), V125 (≠ T131), G126 (= G132), D165 (= D179)
- binding (2e)-2-methylbut-2-enedioic acid: V17 (= V17), R47 (≠ K47), D165 (= D179)
- binding Mesaconyl Coenzme A: T249 (≠ N261), L251 (≠ G263)
8apqA Camct - mesaconyl-coa c1:c4 coa transferase of chloroflexus aurantiacus (see paper)
28% identity, 100% coverage: 1:405/405 of query aligns to 1:402/406 of 8apqA
- binding Mesaconyl Coenzme A: G13 (≠ L13), F16 (≠ V16), V17 (= V17), P38 (≠ K38), R47 (≠ K47), I74 (= I80), R75 (≠ S81), N100 (= N102), F101 (≠ Y103), P102 (≠ K104), L107 (= L113), L124 (≠ V130), V125 (≠ T131), G126 (= G132), S132 (≠ P138), E133 (≠ A144), V134 (≠ Y145), D135 (= D146), Y136 (≠ F147), D165 (= D179)
Q9UHK6 Alpha-methylacyl-CoA racemase; 2-methylacyl-CoA racemase; EC 5.1.99.4 from Homo sapiens (Human) (see 5 papers)
25% identity, 99% coverage: 5:405/405 of query aligns to 3:373/382 of Q9UHK6
- V9 (≠ L11) to M: in dbSNP:rs3195676
- S52 (= S75) to P: in AMACRD and CBAS4; inactive enzyme; dbSNP:rs121917814
- L107 (≠ V130) to P: in CBAS4; inactive enzyme; dbSNP:rs121917816
- G175 (= G201) to D: in dbSNP:rs10941112
- L201 (≠ M227) to S: in dbSNP:rs2287939
- M261 (≠ V290) to T: in dbSNP:rs3195678
- E277 (≠ T306) 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)
26% identity, 93% coverage: 1:375/405 of query aligns to 1:345/360 of O06543
- R38 (≠ K38) 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 (≠ IDIS 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 (≠ V130) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ AYDFIL 144:149) binding
- H126 (≠ Y145) mutation to A: 4.5% of wild-type activity.
- D156 (vs. gap) mutation to A: 17.6 of wild-type activity.
- D190 (= D212) mutation to A: 3.3% of wild-type activity.
- E241 (≠ N262) mutation to A: 2.1% of wild-type activity.
- C297 (≠ P322) mutation to A: 6.2% of wild-type activity.
- H312 (≠ Q337) mutation to A: 10.1% of wild-type activity.
2yimA The enolisation chemistry of a thioester-dependent racemase: the 1.4 a crystal structure of a complex with a planar reaction intermediate analogue (see paper)
26% identity, 92% coverage: 5:375/405 of query aligns to 4:340/355 of 2yimA
- active site: G16 (≠ V17), D122 (= D146), D151 (vs. gap), G214 (≠ V241), G215 (≠ A242)
- binding 2-methylacetoacetyl coa: I15 (≠ V16), R37 (≠ K38), A54 (≠ I78), L56 (≠ I80), K57 (≠ S81), G78 (≠ N102), Y79 (= Y103), R80 (≠ K104), V83 (≠ S107), R86 (≠ K110), L87 (≠ Y111), A119 (≠ P143), G120 (≠ A144), H121 (≠ Y145), Y125 (≠ L149), D151 (vs. gap)
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)
26% identity, 92% coverage: 5:375/405 of query aligns to 4:339/354 of 2gd6A
- active site: G16 (≠ V17), D121 (= D146), D150 (vs. gap), G213 (≠ V241), G214 (≠ A242)
- binding acetyl coenzyme *a: I15 (≠ V16), R37 (≠ K38), A53 (≠ I78), D54 (= D79), L55 (≠ I80), K56 (≠ S81), G77 (≠ N102), Y78 (= Y103), R79 (≠ K104), V82 (≠ S107), R85 (≠ K110), G119 (≠ A144), H120 (≠ Y145), Y124 (≠ L149), D150 (vs. gap), M182 (= M210)
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)
26% identity, 92% coverage: 5:375/405 of query aligns to 4:339/354 of 2gd2A
- active site: G16 (≠ V17), D121 (= D146), D150 (vs. gap), G213 (≠ V241), G214 (≠ A242)
- binding acetoacetyl-coenzyme a: I15 (≠ V16), R37 (≠ K38), A53 (≠ I78), L55 (≠ I80), K56 (≠ S81), G77 (≠ N102), Y78 (= Y103), R79 (≠ K104), V82 (≠ S107), R85 (≠ K110), L86 (≠ Y111), A118 (≠ P143), G119 (≠ A144), H120 (≠ Y145), Y124 (≠ L149), D150 (vs. gap)
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)
26% identity, 92% coverage: 5:375/405 of query aligns to 4:339/354 of 2gd0A
- active site: G16 (≠ V17), D121 (= D146), D150 (vs. gap), G213 (≠ V241), G214 (≠ A242)
- binding (s)-2-methylmyristoyl-coenzyme a: D42 (= D43), L55 (≠ I80), K56 (≠ S81), G77 (≠ N102), Y78 (= Y103), R79 (≠ K104), V82 (≠ S107), R85 (≠ K110), L86 (≠ Y111), G119 (≠ A144), H120 (≠ Y145), D121 (= D146), Y124 (≠ L149), D150 (vs. gap)
Query Sequence
>RR42_RS32705 FitnessBrowser__Cup4G11:RR42_RS32705
MSAILDGIKVLDLTRVVAGPWATQNLADMGATVYKIEKPGDGDDTRKMGPFLNDAQGAAT
NDSAFYLACNRGKQSLTIDISQPEGAELVRQLAARCDVVVENYKAGSLKKYGLDYESIRA
VRPDVIYCSVTGFGPDGPYAARPAYDFILQGMAGLMSTCGQPDGSPGGEPMRTAIPITDI
LTGLYATVSLLGALYHRQATGEGQYIDAAMLDASVAVNGHLALGYQMTGKLPRRAGNSNP
VAAPSEVFACRDGHLIIASGNNGQFAALCKLLGIPELAADPRYTQNANRVANRDALRETI
AERVATWNAADLLASLERAGVPGGPINELDEVFEDAQVKHRGLLVQLPHGRGVDVPSLRS
PMRFSATPVAMRCPPMLGEHTDAALRAELGLSDGDVAGLRARGIL
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