SitesBLAST
Comparing AZOBR_RS29180 FitnessBrowser__azobra:AZOBR_RS29180 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)
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
33% identity, 92% coverage: 3:382/413 of query aligns to 6:355/360 of 5yx6A
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
28% identity, 97% coverage: 3:402/413 of query aligns to 5:423/430 of 3ubmB
- active site: Q17 (≠ L15), E140 (≠ D147), D182 (= D180), G261 (vs. gap), G262 (vs. gap)
- binding coenzyme a: F13 (≠ L11), V16 (= V14), S18 (≠ A16), E37 (= E35), R38 (≠ H36), L72 (≠ I79), N73 (≠ D80), T74 (≠ I81), K75 (≠ A82), N96 (= N103), F97 (= F104), R98 (≠ K105), A101 (≠ G108), R104 (= R111), M105 (≠ Y112), V124 (≠ I131), K125 (≠ T132), G126 (= G133), A138 (≠ G145), D182 (= D180), M213 (≠ L211)
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
28% identity, 94% coverage: 3:390/413 of query aligns to 4:399/415 of 1pt5A
- active site: Q16 (≠ L15), E139 (≠ D147), D168 (= D180), G247 (≠ P241), G248 (≠ N242)
- binding acetyl coenzyme *a: F12 (≠ L11), V15 (= V14), S17 (≠ A16), E36 (= E35), R37 (≠ H36), L71 (≠ I79), N72 (≠ D80), T73 (≠ I81), K74 (≠ A82), N95 (= N103), F96 (= F104), H97 (≠ K105), A100 (≠ G108), I123 (= I131), K124 (≠ T132), K136 (≠ G144), A137 (≠ G145), Y138 (= Y146), E139 (≠ D147), D168 (= D180), M199 (≠ L211)
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
28% identity, 94% coverage: 3:390/413 of query aligns to 5:400/417 of 1q6yA
- active site: Q17 (≠ L15), E140 (≠ D147), D169 (= D180), G248 (≠ P241), G249 (≠ N242)
- binding coenzyme a: F13 (≠ L11), V16 (= V14), Q17 (≠ L15), S18 (≠ A16), E37 (= E35), R38 (≠ H36), L72 (≠ I79), N73 (≠ D80), T74 (≠ I81), K75 (≠ A82), N96 (= N103), F97 (= F104), H98 (≠ K105), A101 (≠ G108), M105 (≠ Y112), I124 (= I131), K125 (≠ T132), G126 (= G133), K137 (≠ G144), A138 (≠ G145), Y139 (= Y146), D169 (= D180), M200 (≠ L211)
1pt8A Crystal structure of the yfdw gene product of e. Coli, in complex with oxalate and acetyl-coa (see paper)
28% identity, 94% coverage: 3:390/413 of query aligns to 5:400/416 of 1pt8A
- active site: Q17 (≠ L15), E140 (≠ D147), D169 (= D180), G248 (≠ P241), G249 (≠ N242)
- binding acetyl coenzyme *a: V16 (= V14), Q17 (≠ L15), S18 (≠ A16), E37 (= E35), R38 (≠ H36), L72 (≠ I79), N73 (≠ D80), T74 (≠ I81), K75 (≠ A82), N96 (= N103), F97 (= F104), H98 (≠ K105), A101 (≠ G108), I124 (= I131), K137 (≠ G144), A138 (≠ G145), Y139 (= Y146), D169 (= D180), M200 (≠ L211), G248 (≠ P241), G249 (≠ N242), Q273 (≠ N262)
- binding oxalate ion: Q48 (≠ N50), L49 (= L51), E226 (vs. gap), G249 (≠ N242), Q250 (≠ V243), P251 (≠ V244)
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)
28% identity, 94% coverage: 3:390/413 of query aligns to 5:400/416 of P69902
1p5rA Formyl-coa transferase in complex with coenzyme a (see paper)
26% identity, 98% coverage: 3:407/413 of query aligns to 4:427/427 of 1p5rA
- active site: Q16 (≠ L15), E139 (≠ D147), D168 (= D180), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R13), V15 (= V14), Q16 (≠ L15), A17 (= A16), E36 (= E35), R37 (≠ H36), L71 (≠ I79), D72 (= D80), M73 (≠ I81), K74 (≠ A82), N95 (= N103), F96 (= F104), A100 (≠ G108), R103 (= R111), M104 (≠ Y112), V123 (≠ I131), K136 (≠ G144), V137 (≠ G145), Y138 (= Y146), D168 (= D180), M199 (≠ L211)
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
26% identity, 98% coverage: 3:407/413 of query aligns to 5:428/428 of O06644
- Q17 (≠ L15) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (≠ H36) binding
- W48 (= W46) 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.
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
26% identity, 98% coverage: 3:407/413 of query aligns to 4:427/427 of 2vjoA
- active site: A16 (≠ L15), E139 (≠ D147), D168 (= D180), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R13), V15 (= V14), A16 (≠ L15), A17 (= A16), E36 (= E35), R37 (≠ H36), M43 (≠ D42), L71 (≠ I79), D72 (= D80), M73 (≠ I81), K74 (≠ A82), N95 (= N103), F96 (= F104), G97 (≠ K105), A100 (≠ G108), R103 (= R111), M104 (≠ Y112), V123 (≠ I131), K124 (≠ T132), K136 (≠ G144), V137 (≠ G145), Y138 (= Y146), D168 (= D180), M199 (≠ L211)
- binding oxalate ion: G257 (vs. gap), G258 (vs. gap), G259 (vs. gap), G260 (vs. gap), Q261 (vs. gap)
2vjkA Formyl-coa transferase with aspartyl-coa thioester intermediate derived from oxalyl-coa (see paper)
26% identity, 98% coverage: 3:407/413 of query aligns to 4:427/427 of 2vjkA
- active site: Q16 (≠ L15), E139 (≠ D147), D168 (= D180), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R13), V15 (= V14), Q16 (≠ L15), A17 (= A16), E36 (= E35), R37 (≠ H36), L71 (≠ I79), D72 (= D80), M73 (≠ I81), K74 (≠ A82), N95 (= N103), F96 (= F104), G97 (≠ K105), A100 (≠ G108), R103 (= R111), M104 (≠ Y112), V123 (≠ I131), K136 (≠ G144), V137 (≠ G145), Y138 (= Y146), D168 (= D180), M199 (≠ L211), G259 (vs. gap), G260 (vs. gap)
- binding magnesium ion: D293 (≠ R271), D296 (≠ N274)
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
26% identity, 98% coverage: 3:407/413 of query aligns to 4:427/427 of 1t3zA