SitesBLAST
Comparing AZOBR_RS24675 FitnessBrowser__azobra:AZOBR_RS24675 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)
31% identity, 97% coverage: 12:400/400 of query aligns to 4:416/416 of P69902
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
31% identity, 97% coverage: 12:400/400 of query aligns to 3:415/415 of 1pt5A
- active site: Q16 (≠ L25), E139 (≠ D147), D168 (= D176), G247 (vs. gap), G248 (vs. gap)
- binding acetyl coenzyme *a: V15 (≠ M24), S17 (≠ A26), R37 (= R46), L71 (= L79), N72 (= N80), T73 (≠ L81), K74 (= K82), N95 (= N103), F96 (≠ N104), H97 (≠ R105), K124 (≠ S132), K136 (≠ P144), A137 (≠ C145), Y138 (≠ F146), E139 (≠ D147), D168 (= D176), M199 (= M207)
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
31% identity, 97% coverage: 12:400/400 of query aligns to 4:416/417 of 1q6yA
- active site: Q17 (≠ L25), E140 (≠ D147), D169 (= D176), G248 (vs. gap), G249 (vs. gap)
- binding coenzyme a: V16 (≠ M24), Q17 (≠ L25), S18 (≠ A26), R38 (= R46), L72 (= L79), N73 (= N80), T74 (≠ L81), K75 (= K82), N96 (= N103), F97 (≠ N104), H98 (≠ R105), M105 (≠ L112), I124 (= I131), K137 (≠ P144), A138 (≠ C145), Y139 (≠ F146), D169 (= D176), M200 (= M207)
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
30% identity, 97% coverage: 12:400/400 of query aligns to 4:428/430 of 3ubmB
- active site: Q17 (≠ L25), E140 (≠ D147), D182 (= D176), G261 (vs. gap), G262 (vs. gap)
- binding coenzyme a: V16 (≠ M24), R38 (= R46), L72 (= L79), N73 (= N80), T74 (≠ L81), K75 (= K82), N96 (= N103), F97 (≠ N104), R98 (= R105), A101 (= A108), R104 (= R111), K125 (≠ S132), D182 (= D176), M213 (= M207)
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
31% identity, 97% coverage: 12:400/400 of query aligns to 4:409/410 of 1q7eA
- active site: Q17 (≠ L25), E133 (≠ D147), D162 (= D176), G241 (vs. gap), G242 (vs. gap)
- binding methionine: N96 (= N103), F97 (≠ N104), H98 (≠ R105), P99 (≠ A106), K118 (≠ S132), K130 (≠ P144), A131 (≠ C145), W246 (≠ L238), F299 (≠ A291), A303 (≠ L295), E306 (≠ R298)
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
30% identity, 97% coverage: 12:400/400 of query aligns to 4:428/428 of O06644
- Q17 (≠ L25) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (= R46) binding
- W48 (≠ I55) 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 (= D176) 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 (≠ H236) mutation to A: 2.5-fold decrease of the catalytic effiency.
- G260 (≠ P237) 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)
30% identity, 97% coverage: 12:400/400 of query aligns to 3:427/427 of 1p5rA
- active site: Q16 (≠ L25), E139 (≠ D147), D168 (= D176), G259 (≠ P237), G260 (≠ L238)
- binding coenzyme a: H14 (= H23), V15 (≠ M24), Q16 (≠ L25), A17 (= A26), R37 (= R46), M73 (≠ L81), K74 (= K82), N95 (= N103), F96 (≠ N104), A100 (= A108), R103 (= R111), K136 (≠ P144), V137 (≠ C145), D168 (= D176), M199 (= M207)
2vjkA Formyl-coa transferase with aspartyl-coa thioester intermediate derived from oxalyl-coa (see paper)
30% identity, 97% coverage: 12:400/400 of query aligns to 3:427/427 of 2vjkA
- active site: Q16 (≠ L25), E139 (≠ D147), D168 (= D176), G259 (≠ P237), G260 (≠ L238)
- binding coenzyme a: H14 (= H23), Q16 (≠ L25), A17 (= A26), R37 (= R46), M73 (≠ L81), K74 (= K82), N95 (= N103), F96 (≠ N104), G97 (≠ R105), R103 (= R111), M104 (≠ L112), K136 (≠ P144), V137 (≠ C145), Y138 (≠ F146), D168 (= D176), M199 (= M207)
- binding magnesium ion: D293 (≠ R267), D296 (≠ G270)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
30% identity, 97% coverage: 12:400/400 of query aligns to 3:427/427 of 1t4cA
- active site: Q16 (≠ L25), E139 (≠ D147), D168 (= D176), G259 (≠ P237), G260 (≠ L238)
- binding coenzyme a: H14 (= H23), V15 (≠ M24), Q16 (≠ L25), R37 (= R46), M73 (≠ L81), N95 (= N103), F96 (≠ N104), R103 (= R111), M104 (≠ L112), V137 (≠ C145), Y138 (≠ F146), D168 (= D176), M199 (= M207)
- binding oxalic acid: G259 (≠ P237), G260 (≠ L238)
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
30% identity, 97% coverage: 12:400/400 of query aligns to 3:427/427 of 2vjoA
- active site: A16 (≠ L25), E139 (≠ D147), D168 (= D176), G259 (≠ P237), G260 (≠ L238)
- binding coenzyme a: H14 (= H23), A16 (≠ L25), A17 (= A26), R37 (= R46), L71 (= L79), M73 (≠ L81), N95 (= N103), F96 (≠ N104), G97 (≠ R105), R103 (= R111), M104 (≠ L112), K136 (≠ P144), V137 (≠ C145), Y138 (≠ F146), D168 (= D176), M199 (= M207)
- binding oxalate ion: G257 (≠ R235), G259 (≠ P237), Q261 (≠ I239)
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
30% identity, 97% coverage: 12:400/400 of query aligns to 3:427/427 of 1t3zA
- active site: Q16 (≠ L25), E139 (≠ D147), S168 (≠ D176), G259 (≠ P237), G260 (≠ L238)
- binding oxidized coenzyme a: H14 (= H23), V15 (≠ M24), A17 (= A26), R37 (= R46), K74 (= K82), N95 (= N103), F96 (≠ N104), A100 (= A108), R103 (= R111), M104 (≠ L112), K136 (≠ P144), V137 (≠ C145), Y138 (≠ F146), E139 (≠ D147), M199 (= M207)
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
32% identity, 93% coverage: 12:381/400 of query aligns to 5:360/360 of 5yx6A
O06543 Alpha-methylacyl-CoA racemase; AMACR; MtMCR; EC 5.1.99.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
31% identity, 88% coverage: 11:363/400 of query aligns to 3:345/360 of O06543
- R38 (= R46) 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 (≠ LNLK 79:82) binding
- E82 (= E102) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NNR 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 (≠ CFDVVA 145:150) binding
- H126 (≠ F146) mutation to A: 4.5% of wild-type activity.
- D156 (= D176) mutation to A: 17.6 of wild-type activity.
- D190 (= D209) mutation to A: 3.3% of wild-type activity.
- E241 (≠ T258) mutation to A: 2.1% of wild-type activity.
- C297 (≠ P319) mutation to A: 6.2% of wild-type activity.
- H312 (≠ Q334) 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)
31% identity, 88% coverage: 11:363/400 of query aligns to 2:340/355 of 2yimA
- active site: G16 (≠ L25), D122 (= D147), D151 (= D176), G214 (≠ L238), G215 (≠ I239)
- binding 2-methylacetoacetyl coa: I15 (≠ M24), R37 (= R46), A54 (≠ L79), L56 (= L81), K57 (= K82), G78 (≠ N103), Y79 (≠ N104), R80 (= R105), V83 (≠ A108), R86 (= R111), L87 (= L112), A119 (≠ P144), G120 (≠ C145), H121 (≠ F146), Y125 (≠ A150), D151 (= D176)
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)
31% identity, 88% coverage: 11:363/400 of query aligns to 2:339/354 of 2gd6A
- active site: G16 (≠ L25), D121 (= D147), D150 (= D176), G213 (≠ L238), G214 (≠ I239)
- binding acetyl coenzyme *a: I15 (≠ M24), R37 (= R46), A53 (≠ L79), D54 (≠ N80), L55 (= L81), K56 (= K82), G77 (≠ N103), Y78 (≠ N104), R79 (= R105), V82 (≠ A108), R85 (= R111), G119 (≠ C145), H120 (≠ F146), Y124 (≠ A150), D150 (= D176), M182 (= M207)
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)
31% identity, 88% coverage: 11:363/400 of query aligns to 2:339/354 of 2gd2A
- active site: G16 (≠ L25), D121 (= D147), D150 (= D176), G213 (≠ L238), G214 (≠ I239)
- binding acetoacetyl-coenzyme a: I15 (≠ M24), R37 (= R46), A53 (≠ L79), L55 (= L81), K56 (= K82), G77 (≠ N103), Y78 (≠ N104), R79 (= R105), V82 (≠ A108), R85 (= R111), L86 (= L112), A118 (≠ P144), G119 (≠ C145), H120 (≠ F146), Y124 (≠ A150), D150 (= D176)
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)
31% identity, 88% coverage: 11:363/400 of query aligns to 2:339/354 of 2gd0A
- active site: G16 (≠ L25), D121 (= D147), D150 (= D176), G213 (≠ L238), G214 (≠ I239)
- binding (s)-2-methylmyristoyl-coenzyme a: D42 (= D51), L55 (= L81), K56 (= K82), G77 (≠ N103), Y78 (≠ N104), R79 (= R105), V82 (≠ A108), R85 (= R111), L86 (= L112), G119 (≠ C145), H120 (≠ F146), D121 (= D147), Y124 (≠ A150), D150 (= D176)
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)
31% identity, 88% coverage: 11:363/400 of query aligns to 2:339/354 of 2gciA
- active site: G16 (≠ L25), D121 (= D147), D150 (= D176), G213 (≠ L238), G214 (≠ I239)
- binding (r)-2-methylmyristoyl-coenzyme a: R37 (= R46), L55 (= L81), K56 (= K82), G77 (≠ N103), Y78 (≠ N104), R79 (= R105), V82 (≠ A108), G119 (≠ C145), H120 (≠ F146), D121 (= D147), Y124 (≠ A150), D150 (= D176), Y218 (≠ F242), I234 (≠ D257), E235 (≠ T258)
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)
31% identity, 88% coverage: 11:363/400 of query aligns to 2:339/354 of 2gceA
- active site: G16 (≠ L25), D121 (= D147), D150 (= D176), G213 (≠ L238), G214 (≠ I239)
- binding (r)-ibuprofenoyl-coenzyme a: I15 (≠ M24), R37 (= R46), L55 (= L81), K56 (= K82), G77 (≠ N103), Y78 (≠ N104), R79 (= R105), V82 (≠ A108), R85 (= R111), G119 (≠ C145), H120 (≠ F146), D121 (= D147), Y124 (≠ A150), D150 (= D176), L211 (≠ H236), Y218 (≠ F242), I234 (≠ D257)
- binding (s)-ibuprofenoyl-coenzyme a: I15 (≠ M24), G16 (≠ L25), P17 (≠ A26), R37 (= R46), L55 (= L81), K56 (= K82), G77 (≠ N103), Y78 (≠ N104), R79 (= R105), V82 (≠ A108), R85 (= R111), G119 (≠ C145), H120 (≠ F146), Y124 (≠ A150), D150 (= D176)
Q9UHK6 Alpha-methylacyl-CoA racemase; 2-methylacyl-CoA racemase; EC 5.1.99.4 from Homo sapiens (Human) (see 5 papers)
28% identity, 97% coverage: 13:400/400 of query aligns to 3:373/382 of Q9UHK6
- V9 (= V19) 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 (= G198) to D: in dbSNP:rs10941112
- L201 (= L223) to S: in dbSNP:rs2287939
- M261 (≠ R286) to T: in dbSNP:rs3195678
- E277 (≠ T303) to K: in dbSNP:rs2278008
Sites not aligning to the query:
- 380:382 Microbody targeting signal
Query Sequence
>AZOBR_RS24675 FitnessBrowser__azobra:AZOBR_RS24675
MLNTDTQRREGPLAGVRVVDLTHMLAGPYSTWLLGALGAEVIKIERPGKGDFTRIIAPFS
EEESIYFLSVNRNKRSLTLNLKEEKGKEIFKKIVATCDVLVENNRAGAMDRLGLGYTDLK
AVNPRLVYASISGFGQDGPYRHRPCFDVVAQAMSGMMSITGEPGGDPCRVGASIGDIGSS
LFAAVGILAALQKRASTGEGSFIDVAMLDCQLALMENAIARFLNAGETPRALGSRHPLIA
PFQAFPTADKPIAICVDTNEQWERMCRAMGLEHLLSDPRFPTGSARNANHAELELLLREV
FLTRGRDAWLDAMEDADVPASPINSVPDALNDPQVIHRKMVVEVPEGSGKRFAAVPITMP
EAPLPAESPAPRLGEHTDAILADLGFSPDEIGAFRRDAVV
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