SitesBLAST
Comparing RR42_RS29900 FitnessBrowser__Cup4G11:RR42_RS29900 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)
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)
29% identity, 100% coverage: 1:407/407 of query aligns to 1:416/416 of P69902
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
28% identity, 98% coverage: 4:402/407 of query aligns to 4:423/430 of 3ubmB
- active site: Q17 (≠ L17), E140 (≠ D147), D182 (= D180), G261 (≠ P241), G262 (≠ N242)
- binding coenzyme a: V16 (≠ I16), R38 (= R38), L72 (= L79), N73 (≠ D80), T74 (≠ V81), K75 (≠ S82), N96 (= N103), F97 (≠ Y104), R98 (≠ K105), A101 (≠ D108), R104 (= R111), K125 (≠ T132), D182 (= D180), M213 (≠ L211)
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
29% identity, 100% coverage: 1:407/407 of query aligns to 1:416/417 of 1q6yA
- active site: Q17 (≠ L17), E140 (≠ D147), D169 (= D180), G248 (≠ P241), G249 (≠ N242)
- binding coenzyme a: V16 (≠ I16), Q17 (≠ L17), S18 (≠ A18), R38 (= R38), L72 (= L79), N73 (≠ D80), T74 (≠ V81), K75 (≠ S82), N96 (= N103), F97 (≠ Y104), H98 (≠ K105), M105 (≠ Y112), I124 (= I131), K137 (≠ A144), A138 (≠ G145), Y139 (= Y146), D169 (= D180), M200 (≠ L211)
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
29% identity, 99% coverage: 4:407/407 of query aligns to 3:415/415 of 1pt5A
- active site: Q16 (≠ L17), E139 (≠ D147), D168 (= D180), G247 (≠ P241), G248 (≠ N242)
- binding acetyl coenzyme *a: V15 (≠ I16), S17 (≠ A18), R37 (= R38), L71 (= L79), N72 (≠ D80), T73 (≠ V81), K74 (≠ S82), N95 (= N103), F96 (≠ Y104), H97 (≠ K105), K124 (≠ T132), K136 (≠ A144), A137 (≠ G145), Y138 (= Y146), E139 (≠ D147), D168 (= D180), M199 (≠ L211)
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
29% identity, 100% coverage: 1:407/407 of query aligns to 1:409/410 of 1q7eA
- active site: Q17 (≠ L17), E133 (≠ D147), D162 (= D180), G241 (≠ P241), G242 (≠ N242)
- binding methionine: N96 (= N103), F97 (≠ Y104), H98 (≠ Y112), P99 (≠ G113), K118 (≠ T132), K130 (≠ A144), A131 (≠ G145), W246 (≠ Y246), F299 (≠ E295), A303 (≠ E299), E306 (≠ S302)
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
28% identity, 99% coverage: 1:402/407 of query aligns to 1:423/428 of O06644
- Q17 (≠ L17) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (= R38) binding
- W48 (= W48) 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 (= R111) binding
- D169 (= D180) 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)
28% identity, 98% coverage: 4:402/407 of query aligns to 3:422/427 of 1p5rA
- active site: Q16 (≠ L17), E139 (≠ D147), D168 (= D180), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R15), V15 (≠ I16), Q16 (≠ L17), A17 (= A18), R37 (= R38), M73 (≠ V81), K74 (≠ S82), N95 (= N103), F96 (≠ Y104), A100 (≠ D108), R103 (= R111), K136 (≠ A144), V137 (≠ G145), D168 (= D180), M199 (≠ L211)
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
28% identity, 98% coverage: 4:402/407 of query aligns to 3:422/427 of 2vjoA
- active site: A16 (≠ L17), E139 (≠ D147), D168 (= D180), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R15), A16 (≠ L17), A17 (= A18), R37 (= R38), L71 (= L79), M73 (≠ V81), N95 (= N103), F96 (≠ Y104), G97 (≠ K105), R103 (= R111), M104 (≠ Y112), K136 (≠ A144), V137 (≠ G145), Y138 (= Y146), D168 (= D180), M199 (≠ L211)
- 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)
28% identity, 98% coverage: 4:402/407 of query aligns to 3:422/427 of 2vjkA
- active site: Q16 (≠ L17), E139 (≠ D147), D168 (= D180), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R15), Q16 (≠ L17), A17 (= A18), R37 (= R38), M73 (≠ V81), K74 (≠ S82), N95 (= N103), F96 (≠ Y104), G97 (≠ K105), R103 (= R111), M104 (≠ Y112), K136 (≠ A144), V137 (≠ G145), Y138 (= Y146), D168 (= D180), M199 (≠ L211)
- binding magnesium ion: D293 (≠ E271), D296 (≠ G274)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
28% identity, 98% coverage: 4:402/407 of query aligns to 3:422/427 of 1t4cA
- active site: Q16 (≠ L17), E139 (≠ D147), D168 (= D180), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R15), V15 (≠ I16), Q16 (≠ L17), R37 (= R38), M73 (≠ V81), N95 (= N103), F96 (≠ Y104), R103 (= R111), M104 (≠ Y112), V137 (≠ G145), Y138 (= Y146), D168 (= D180), M199 (≠ L211)
- binding oxalic acid: G259 (vs. gap), G260 (vs. gap)
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
27% identity, 98% coverage: 4:402/407 of query aligns to 3:422/427 of 1t3zA
- active site: Q16 (≠ L17), E139 (≠ D147), S168 (≠ D180), G259 (vs. gap), G260 (vs. gap)
- binding oxidized coenzyme a: H14 (≠ R15), V15 (≠ I16), A17 (= A18), R37 (= R38), K74 (≠ S82), N95 (= N103), F96 (≠ Y104), A100 (≠ D108), R103 (= R111), M104 (≠ Y112), K136 (≠ A144), V137 (≠ G145), Y138 (= Y146), E139 (≠ D147), M199 (≠ L211)
O06543 Alpha-methylacyl-CoA racemase; AMACR; MtMCR; EC 5.1.99.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
29% identity, 96% coverage: 1:389/407 of query aligns to 1:357/360 of O06543
- R38 (= R38) binding
- R52 (= R72) mutation to A: 15.7% of wild-type activity.
- I56 (≠ S76) mutation to P: 28.8% of wild-type activity.
- ADLK 59:62 (≠ LDVS 79:82) binding
- E82 (= E102) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NYK 103:105) binding
- R91 (= R111) binding ; mutation to A: 19.9% of wild-type activity.
- M111 (≠ I131) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ GYDFVV 145:150) binding
- H126 (≠ Y146) mutation to A: 4.5% of wild-type activity.
- D156 (= D180) mutation to A: 17.6 of wild-type activity.
- D190 (= D213) mutation to A: 3.3% of wild-type activity.
- E241 (≠ D263) mutation to A: 2.1% of wild-type activity.
- C297 (≠ P323) mutation to A: 6.2% of wild-type activity.
- H312 (= H338) 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)
29% identity, 95% coverage: 2:389/407 of query aligns to 1:352/355 of 2yimA
- active site: G16 (≠ L17), D122 (= D147), D151 (= D180), G214 (≠ N242), G215 (≠ L243)
- binding 2-methylacetoacetyl coa: I15 (= I16), R37 (= R38), A54 (≠ L79), L56 (≠ V81), K57 (≠ S82), G78 (≠ N103), Y79 (= Y104), R80 (≠ K105), V83 (≠ D108), R86 (= R111), L87 (≠ Y112), A119 (= A144), G120 (= G145), H121 (≠ Y146), Y125 (≠ V150), D151 (= D180)
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, 95% coverage: 2:389/407 of query aligns to 1:351/354 of 2gd6A
- active site: G16 (≠ L17), D121 (= D147), D150 (= D180), G213 (≠ N242), G214 (≠ L243)
- binding acetyl coenzyme *a: I15 (= I16), R37 (= R38), A53 (≠ L79), D54 (= D80), L55 (≠ V81), K56 (≠ S82), G77 (≠ N103), Y78 (= Y104), R79 (≠ K105), V82 (≠ D108), R85 (= R111), G119 (= G145), H120 (≠ Y146), Y124 (≠ V150), D150 (= D180), M182 (≠ L211)
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, 95% coverage: 2:389/407 of query aligns to 1:351/354 of 2gd2A
- active site: G16 (≠ L17), D121 (= D147), D150 (= D180), G213 (≠ N242), G214 (≠ L243)
- binding acetoacetyl-coenzyme a: I15 (= I16), R37 (= R38), A53 (≠ L79), L55 (≠ V81), K56 (≠ S82), G77 (≠ N103), Y78 (= Y104), R79 (≠ K105), V82 (≠ D108), R85 (= R111), L86 (≠ Y112), A118 (= A144), G119 (= G145), H120 (≠ Y146), Y124 (≠ V150), D150 (= D180)
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, 95% coverage: 2:389/407 of query aligns to 1:351/354 of 2gd0A
- active site: G16 (≠ L17), D121 (= D147), D150 (= D180), G213 (≠ N242), G214 (≠ L243)
- binding (s)-2-methylmyristoyl-coenzyme a: D42 (= D43), L55 (≠ V81), K56 (≠ S82), G77 (≠ N103), Y78 (= Y104), R79 (≠ K105), V82 (≠ D108), R85 (= R111), L86 (≠ Y112), G119 (= G145), H120 (≠ Y146), D121 (= D147), Y124 (≠ V150), D150 (= D180)
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, 95% coverage: 2:389/407 of query aligns to 1:351/354 of 2gciA
- active site: G16 (≠ L17), D121 (= D147), D150 (= D180), G213 (≠ N242), G214 (≠ L243)
- binding (r)-2-methylmyristoyl-coenzyme a: R37 (= R38), L55 (≠ V81), K56 (≠ S82), G77 (≠ N103), Y78 (= Y104), R79 (≠ K105), V82 (≠ D108), G119 (= G145), H120 (≠ Y146), D121 (= D147), Y124 (≠ V150), D150 (= D180), Y218 (= Y246), I234 (≠ N262), E235 (≠ D263)
2gceA 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, 95% coverage: 2:389/407 of query aligns to 1:351/354 of 2gceA
- active site: G16 (≠ L17), D121 (= D147), D150 (= D180), G213 (≠ N242), G214 (≠ L243)
- binding (r)-ibuprofenoyl-coenzyme a: I15 (= I16), R37 (= R38), L55 (≠ V81), K56 (≠ S82), G77 (≠ N103), Y78 (= Y104), R79 (≠ K105), V82 (≠ D108), R85 (= R111), G119 (= G145), H120 (≠ Y146), D121 (= D147), Y124 (≠ V150), D150 (= D180), L211 (≠ H240), Y218 (= Y246), I234 (≠ N262)
- binding (s)-ibuprofenoyl-coenzyme a: I15 (= I16), G16 (≠ L17), P17 (≠ A18), R37 (= R38), L55 (≠ V81), K56 (≠ S82), G77 (≠ N103), Y78 (= Y104), R79 (≠ K105), V82 (≠ D108), R85 (= R111), G119 (= G145), H120 (≠ Y146), Y124 (≠ V150), D150 (= D180)
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
27% identity, 95% coverage: 2:387/407 of query aligns to 3:360/360 of 5yx6A
Q9UHK6 Alpha-methylacyl-CoA racemase; 2-methylacyl-CoA racemase; EC 5.1.99.4 from Homo sapiens (Human) (see 5 papers)
27% identity, 99% coverage: 5:407/407 of query aligns to 3:373/382 of Q9UHK6
- V9 (≠ L11) to M: in dbSNP:rs3195676
- S52 (= S76) to P: in AMACRD and CBAS4; inactive enzyme; dbSNP:rs121917814
- L107 (≠ I131) to P: in CBAS4; inactive enzyme; dbSNP:rs121917816
- G175 (= G202) to D: in dbSNP:rs10941112
- L201 (vs. gap) to S: in dbSNP:rs2287939
- M261 (vs. gap) to T: in dbSNP:rs3195678
- E277 (= E307) to K: in dbSNP:rs2278008
Sites not aligning to the query:
- 380:382 Microbody targeting signal
Query Sequence
>RR42_RS29900 FitnessBrowser__Cup4G11:RR42_RS29900
MAGPLAGIKVLDLSRILAGPWSTQLLSDLGADVMKVERPGTGDDTRAWGPPFLTREDGTT
TEESAYFLCANRGKRSITLDVSSKVGQDLLHELVKDCDVFVENYKFGDMQRYGLDFKTLS
EINPRLVYCSITGFGQTGPYRKRAGYDFVVQAMGGLMSITGERDGVPGGGPQKCGVPISD
LMTGMYASVAIVSALFERVGSGRGQYIDMSLLDTQVAWLANQASNYLVGGSHPRRWGNAH
PNLAPYQSFPASDGSLIVAVGNDRQFRAMCEALGLINLPDDDRYRRNADRLKNRESLVEV
LSARFEEEERDTWLKLLESVGVPCGPIQSIPEALEDPHIRAREMVFSLPHSSGASAPQVA
NPIKFSRSSIDYLRAPPALGEHTETILKNELGKSVEQIEAMRRDGTI
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