SitesBLAST
Comparing GFF2609 FitnessBrowser__psRCH2:GFF2609 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)
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
31% identity, 98% coverage: 10:399/400 of query aligns to 4:427/430 of 3ubmB
- active site: Q17 (≠ I23), E140 (≠ G145), D182 (= D174), G261 (vs. gap), G262 (vs. gap)
- binding coenzyme a: V16 (≠ L22), R38 (≠ P44), L72 (= L77), N73 (≠ D78), T74 (≠ L79), K75 (= K80), N96 (= N101), F97 (= F102), R98 (= R103), A101 (≠ T106), R104 (≠ E109), K125 (≠ S130), D182 (= D174), M213 (≠ L205)
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
28% identity, 98% coverage: 8:400/400 of query aligns to 2:416/417 of 1q6yA
- active site: Q17 (≠ I23), E140 (≠ G145), D169 (= D174), G248 (vs. gap), G249 (vs. gap)
- binding coenzyme a: V16 (≠ L22), Q17 (≠ I23), S18 (≠ A24), R38 (≠ P44), L72 (= L77), N73 (≠ D78), T74 (≠ L79), K75 (= K80), N96 (= N101), F97 (= F102), H98 (≠ R103), M105 (≠ W110), I124 (= I129), K137 (≠ P142), A138 (≠ G143), Y139 (≠ F144), D169 (= D174), M200 (≠ L205)
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, 98% coverage: 8:400/400 of query aligns to 2:416/416 of P69902
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
28% identity, 98% coverage: 8:400/400 of query aligns to 1:415/415 of 1pt5A
- active site: Q16 (≠ I23), E139 (≠ G145), D168 (= D174), G247 (vs. gap), G248 (vs. gap)
- binding acetyl coenzyme *a: V15 (≠ L22), S17 (≠ A24), R37 (≠ P44), L71 (= L77), N72 (≠ D78), T73 (≠ L79), K74 (= K80), N95 (= N101), F96 (= F102), H97 (≠ R103), K124 (≠ S130), K136 (≠ P142), A137 (≠ G143), Y138 (≠ F144), E139 (≠ G145), D168 (= D174), M199 (≠ L205)
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
27% identity, 98% coverage: 10:400/400 of query aligns to 3:427/427 of 2vjoA
- active site: A16 (≠ I23), E139 (≠ G145), D168 (= D174), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ Q21), A16 (≠ I23), A17 (= A24), R37 (≠ P44), L71 (= L77), M73 (≠ L79), N95 (= N101), F96 (= F102), G97 (≠ R103), R103 (≠ E109), M104 (≠ W110), K136 (≠ P142), V137 (≠ G143), Y138 (≠ F144), D168 (= D174), M199 (≠ L205)
- binding oxalate ion: G257 (vs. gap), G259 (vs. gap), Q261 (vs. gap)
1p5rA Formyl-coa transferase in complex with coenzyme a (see paper)
27% identity, 98% coverage: 10:400/400 of query aligns to 3:427/427 of 1p5rA
- active site: Q16 (≠ I23), E139 (≠ G145), D168 (= D174), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ Q21), V15 (≠ L22), Q16 (≠ I23), A17 (= A24), R37 (≠ P44), M73 (≠ L79), K74 (= K80), N95 (= N101), F96 (= F102), A100 (≠ T106), R103 (≠ E109), K136 (≠ P142), V137 (≠ G143), D168 (= D174), M199 (≠ L205)
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
27% identity, 98% coverage: 10:400/400 of query aligns to 4:428/428 of O06644
- Q17 (≠ I23) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (≠ P44) 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 (≠ E109) binding
- D169 (= D174) 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.
2vjkA Formyl-coa transferase with aspartyl-coa thioester intermediate derived from oxalyl-coa (see paper)
27% identity, 98% coverage: 10:400/400 of query aligns to 3:427/427 of 2vjkA
- active site: Q16 (≠ I23), E139 (≠ G145), D168 (= D174), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ Q21), Q16 (≠ I23), A17 (= A24), R37 (≠ P44), M73 (≠ L79), K74 (= K80), N95 (= N101), F96 (= F102), G97 (≠ R103), R103 (≠ E109), M104 (≠ W110), K136 (≠ P142), V137 (≠ G143), Y138 (≠ F144), D168 (= D174), M199 (≠ L205)
- binding magnesium ion: D293 (≠ T266), D296 (≠ G269)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
27% identity, 98% coverage: 10:400/400 of query aligns to 3:427/427 of 1t4cA
- active site: Q16 (≠ I23), E139 (≠ G145), D168 (= D174), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ Q21), V15 (≠ L22), Q16 (≠ I23), R37 (≠ P44), M73 (≠ L79), N95 (= N101), F96 (= F102), R103 (≠ E109), M104 (≠ W110), V137 (≠ G143), Y138 (≠ F144), D168 (= D174), M199 (≠ L205)
- binding oxalic acid: G259 (vs. gap), G260 (vs. gap)
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
27% identity, 98% coverage: 10:400/400 of query aligns to 3:427/427 of 1t3zA
- active site: Q16 (≠ I23), E139 (≠ G145), S168 (≠ D174), G259 (vs. gap), G260 (vs. gap)
- binding oxidized coenzyme a: H14 (≠ Q21), V15 (≠ L22), A17 (= A24), R37 (≠ P44), K74 (= K80), N95 (= N101), F96 (= F102), A100 (≠ T106), R103 (≠ E109), M104 (≠ W110), K136 (≠ P142), V137 (≠ G143), Y138 (≠ F144), E139 (≠ G145), M199 (≠ L205)
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
28% identity, 98% coverage: 8:400/400 of query aligns to 2:409/410 of 1q7eA
- active site: Q17 (≠ I23), E133 (≠ G145), D162 (= D174), G241 (vs. gap), G242 (vs. gap)
- binding methionine: N96 (= N101), F97 (= F102), H98 (≠ R103), P99 (= P104), K118 (≠ S130), K130 (≠ P142), A131 (≠ G143), W246 (≠ G236), F299 (≠ E290), A303 (= A294), E306 (≠ G297)
O06543 Alpha-methylacyl-CoA racemase; AMACR; MtMCR; EC 5.1.99.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
30% identity, 88% coverage: 10:362/400 of query aligns to 4:337/360 of O06543
- R38 (≠ P44) binding
- R52 (= R70) mutation to A: 15.7% of wild-type activity.
- I56 (≠ S74) mutation to P: 28.8% of wild-type activity.
- ADLK 59:62 (≠ LDLK 77:80) binding
- E82 (= E100) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NFR 101:103) binding
- R91 (≠ E109) binding ; mutation to A: 19.9% of wild-type activity.
- M111 (≠ I129) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ GFGVIG 143:148) binding
- H126 (≠ F144) mutation to A: 4.5% of wild-type activity.
- D156 (= D174) mutation to A: 17.6 of wild-type activity.
- D190 (≠ E207) mutation to A: 3.3% of wild-type activity.
- E241 (≠ G257) mutation to A: 2.1% of wild-type activity.
- C297 (≠ P318) mutation to A: 6.2% of wild-type activity.
- H312 (= H333) 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)
30% identity, 88% coverage: 10:362/400 of query aligns to 3:332/355 of 2yimA
- active site: G16 (≠ I23), D122 (≠ G145), D151 (= D174), G214 (= G236), G215 (≠ I237)
- binding 2-methylacetoacetyl coa: I15 (≠ L22), R37 (≠ P44), A54 (≠ L77), L56 (= L79), K57 (= K80), G78 (≠ N101), Y79 (≠ F102), R80 (= R103), V83 (≠ T106), R86 (≠ E109), L87 (≠ W110), A119 (≠ P142), G120 (= G143), H121 (≠ F144), Y125 (≠ G148), D151 (= D174)
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)
30% identity, 88% coverage: 10:362/400 of query aligns to 3:331/354 of 2gd6A
- active site: G16 (≠ I23), D121 (≠ G145), D150 (= D174), G213 (= G236), G214 (≠ I237)
- binding acetyl coenzyme *a: I15 (≠ L22), R37 (≠ P44), A53 (≠ L77), D54 (= D78), L55 (= L79), K56 (= K80), G77 (≠ N101), Y78 (≠ F102), R79 (= R103), V82 (≠ T106), R85 (≠ E109), G119 (= G143), H120 (≠ F144), Y124 (≠ G148), D150 (= D174), M182 (≠ L205)
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)
30% identity, 88% coverage: 10:362/400 of query aligns to 3:331/354 of 2gd2A
- active site: G16 (≠ I23), D121 (≠ G145), D150 (= D174), G213 (= G236), G214 (≠ I237)
- binding acetoacetyl-coenzyme a: I15 (≠ L22), R37 (≠ P44), A53 (≠ L77), L55 (= L79), K56 (= K80), G77 (≠ N101), Y78 (≠ F102), R79 (= R103), V82 (≠ T106), R85 (≠ E109), L86 (≠ W110), A118 (≠ P142), G119 (= G143), H120 (≠ F144), Y124 (≠ G148), D150 (= D174)
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)
30% identity, 88% coverage: 10:362/400 of query aligns to 3:331/354 of 2gd0A
- active site: G16 (≠ I23), D121 (≠ G145), D150 (= D174), G213 (= G236), G214 (≠ I237)
- binding (s)-2-methylmyristoyl-coenzyme a: D42 (= D49), L55 (= L79), K56 (= K80), G77 (≠ N101), Y78 (≠ F102), R79 (= R103), V82 (≠ T106), R85 (≠ E109), L86 (≠ W110), G119 (= G143), H120 (≠ F144), D121 (≠ G145), Y124 (≠ G148), D150 (= D174)
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)
30% identity, 88% coverage: 10:362/400 of query aligns to 3:331/354 of 2gciA
- active site: G16 (≠ I23), D121 (≠ G145), D150 (= D174), G213 (= G236), G214 (≠ I237)
- binding (r)-2-methylmyristoyl-coenzyme a: R37 (≠ P44), L55 (= L79), K56 (= K80), G77 (≠ N101), Y78 (≠ F102), R79 (= R103), V82 (≠ T106), G119 (= G143), H120 (≠ F144), D121 (≠ G145), Y124 (≠ G148), D150 (= D174), Y218 (≠ S240), I234 (≠ N256), E235 (≠ G257)
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)
30% identity, 88% coverage: 10:362/400 of query aligns to 3:331/354 of 2gceA
- active site: G16 (≠ I23), D121 (≠ G145), D150 (= D174), G213 (= G236), G214 (≠ I237)
- binding (r)-ibuprofenoyl-coenzyme a: I15 (≠ L22), R37 (≠ P44), L55 (= L79), K56 (= K80), G77 (≠ N101), Y78 (≠ F102), R79 (= R103), V82 (≠ T106), R85 (≠ E109), G119 (= G143), H120 (≠ F144), D121 (≠ G145), Y124 (≠ G148), D150 (= D174), L211 (= L234), Y218 (≠ S240), I234 (≠ N256)
- binding (s)-ibuprofenoyl-coenzyme a: I15 (≠ L22), G16 (≠ I23), P17 (≠ A24), R37 (≠ P44), L55 (= L79), K56 (= K80), G77 (≠ N101), Y78 (≠ F102), R79 (= R103), V82 (≠ T106), R85 (≠ E109), G119 (= G143), H120 (≠ F144), Y124 (≠ G148), D150 (= D174)
P31572 L-carnitine CoA-transferase; Crotonobetainyl-CoA:carnitine CoA-transferase; EC 2.8.3.21 from Escherichia coli (strain K12) (see paper)
28% identity, 98% coverage: 10:399/400 of query aligns to 11:400/405 of P31572
- K97 (≠ R103) binding
- R104 (≠ W110) binding
1xvtA Crystal structure of native caib in complex with coenzyme a (see paper)
28% identity, 98% coverage: 10:399/400 of query aligns to 8:397/402 of 1xvtA
- active site: I21 (= I23), N138 (≠ G145), D166 (= D174), G225 (= G231), K226 (≠ S232)
- binding coenzyme a: I21 (= I23), A22 (= A24), N42 (≠ P44), L68 (= L77), N69 (≠ D78), F71 (≠ K80), S93 (≠ F102), K94 (≠ R103), R100 (≠ E109), R101 (≠ W110), P135 (= P142), A136 (≠ G143), D166 (= D174), M197 (≠ L205)
Query Sequence
>GFF2609 FitnessBrowser__psRCH2:GFF2609
MSEQTDKNLPLQGLKVIEMGQLIAGPFASKLLGEFGADVIKIEPPKVGDPLRKWRKLKDG
TSLWWHVQSRNKRSVTLDLKAAEGQAIVRQLVAEADILVENFRPGTLEEWGLGWDELSKL
NPRLIMLRISGYGQTGPYRDLPGFGVIGEAMGGLRHLSGYPGQPPVRVGVSIGDSLSSLY
GVIGVLLALQERNRSGQGQEIDVALYESVFAMMESLVPEYDAFGYVREPAGSALPGITPS
NSYPCNDGAYVLIAGNGDSIYKRLMTLMGRQDLADDPRFAHNDGRAQHAELIDAAIGEWT
IQHGRDEVIEALKGARVPAGYPYTAADIVKDPHYLARQMIEQVQTFAGPLKVPGVLPKLS
RTPGRIGEGGPQLGEHTDDVLAGLGLTDEQRQGLRERGII
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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