SitesBLAST
Comparing GFF2665 FitnessBrowser__Marino:GFF2665 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)
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
28% identity, 100% coverage: 1:397/398 of query aligns to 1:428/428 of O06644
- Q17 (≠ L17) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (≠ P38) binding
- W48 (≠ L47) 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 (≠ K107) binding
- D169 (= D172) 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.
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
31% identity, 98% coverage: 2:392/398 of query aligns to 2:423/430 of 3ubmB
- active site: Q17 (≠ L17), E140 (≠ D143), D182 (= D172), G261 (vs. gap), G262 (vs. gap)
- binding coenzyme a: V16 (≠ M16), R38 (≠ P38), L72 (≠ I75), N73 (≠ D76), T74 (≠ L77), K75 (= K78), N96 (= N99), F97 (= F100), R98 (≠ S101), A101 (≠ V104), R104 (≠ K107), K125 (≠ T128), D182 (= D172), M213 (= M203)
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)
32% identity, 100% coverage: 1:397/398 of query aligns to 1:416/416 of P69902
1p5rA Formyl-coa transferase in complex with coenzyme a (see paper)
28% identity, 99% coverage: 2:397/398 of query aligns to 1:427/427 of 1p5rA
- active site: Q16 (≠ L17), E139 (≠ D143), D168 (= D172), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (= H15), V15 (≠ M16), Q16 (≠ L17), A17 (≠ S18), R37 (≠ P38), M73 (≠ L77), K74 (= K78), N95 (= N99), F96 (= F100), A100 (≠ V104), R103 (≠ K107), K136 (≠ P140), V137 (≠ A141), D168 (= D172), M199 (= M203)
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
28% identity, 99% coverage: 2:397/398 of query aligns to 1:427/427 of 2vjoA
- active site: A16 (≠ L17), E139 (≠ D143), D168 (= D172), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (= H15), A16 (≠ L17), A17 (≠ S18), R37 (≠ P38), L71 (≠ I75), M73 (≠ L77), N95 (= N99), F96 (= F100), G97 (≠ S101), R103 (≠ K107), M104 (≠ L108), K136 (≠ P140), V137 (≠ A141), Y138 (≠ F142), D168 (= D172), M199 (= M203)
- binding oxalate ion: G257 (vs. gap), G259 (vs. gap), Q261 (vs. gap)
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
32% identity, 100% coverage: 1:397/398 of query aligns to 1:416/417 of 1q6yA
- active site: Q17 (≠ L17), E140 (≠ D143), D169 (= D172), G248 (vs. gap), G249 (vs. gap)
- binding coenzyme a: V16 (≠ M16), Q17 (≠ L17), S18 (= S18), R38 (vs. gap), L72 (≠ I75), N73 (≠ D76), T74 (≠ L77), K75 (= K78), N96 (= N99), F97 (= F100), H98 (≠ S101), M105 (≠ L108), I124 (≠ V127), K137 (≠ P140), A138 (= A141), Y139 (≠ F142), D169 (= D172), M200 (= M203)
2vjkA Formyl-coa transferase with aspartyl-coa thioester intermediate derived from oxalyl-coa (see paper)
28% identity, 99% coverage: 2:397/398 of query aligns to 1:427/427 of 2vjkA
- active site: Q16 (≠ L17), E139 (≠ D143), D168 (= D172), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (= H15), Q16 (≠ L17), A17 (≠ S18), R37 (≠ P38), M73 (≠ L77), K74 (= K78), N95 (= N99), F96 (= F100), G97 (≠ S101), R103 (≠ K107), M104 (≠ L108), K136 (≠ P140), V137 (≠ A141), Y138 (≠ F142), D168 (= D172), M199 (= M203)
- binding magnesium ion: D293 (≠ E263), D296 (≠ G266)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
28% identity, 99% coverage: 2:397/398 of query aligns to 1:427/427 of 1t4cA
- active site: Q16 (≠ L17), E139 (≠ D143), D168 (= D172), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (= H15), V15 (≠ M16), Q16 (≠ L17), R37 (≠ P38), M73 (≠ L77), N95 (= N99), F96 (= F100), R103 (≠ K107), M104 (≠ L108), V137 (≠ A141), Y138 (≠ F142), D168 (= D172), M199 (= M203)
- binding oxalic acid: G259 (vs. gap), G260 (vs. gap)
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
32% identity, 99% coverage: 2:397/398 of query aligns to 1:415/415 of 1pt5A
- active site: Q16 (≠ L17), E139 (≠ D143), D168 (= D172), G247 (vs. gap), G248 (vs. gap)
- binding acetyl coenzyme *a: V15 (≠ M16), S17 (= S18), R37 (vs. gap), L71 (≠ I75), N72 (≠ D76), T73 (≠ L77), K74 (= K78), N95 (= N99), F96 (= F100), H97 (≠ S101), K124 (≠ T128), K136 (≠ P140), A137 (= A141), Y138 (≠ F142), E139 (≠ D143), D168 (= D172), M199 (= M203)
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
27% identity, 99% coverage: 2:397/398 of query aligns to 1:427/427 of 1t3zA
- active site: Q16 (≠ L17), E139 (≠ D143), S168 (≠ D172), G259 (vs. gap), G260 (vs. gap)
- binding oxidized coenzyme a: H14 (= H15), V15 (≠ M16), A17 (≠ S18), R37 (≠ P38), K74 (= K78), N95 (= N99), F96 (= F100), A100 (≠ V104), R103 (≠ K107), M104 (≠ L108), K136 (≠ P140), V137 (≠ A141), Y138 (≠ F142), E139 (≠ D143), M199 (= M203)
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
32% identity, 100% coverage: 1:397/398 of query aligns to 1:409/410 of 1q7eA
- active site: Q17 (≠ L17), E133 (≠ D143), D162 (= D172), G241 (vs. gap), G242 (vs. gap)
- binding methionine: N96 (= N99), F97 (= F100), H98 (≠ S101), P99 (≠ A102), K118 (≠ T128), K130 (≠ P140), A131 (= A141), W246 (vs. gap), F299 (≠ N289), A303 (≠ T293), E306 (≠ L296)
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
29% identity, 93% coverage: 3:373/398 of query aligns to 4:355/360 of 5yx6A
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)
27% identity, 83% coverage: 4:334/398 of query aligns to 3:312/355 of 2yimA
- active site: G16 (≠ L17), D122 (= D143), D151 (= D172), G214 (≠ V234), G215 (≠ H235)
- binding 2-methylacetoacetyl coa: I15 (≠ M16), R37 (= R45), A54 (≠ I75), L56 (= L77), K57 (= K78), G78 (≠ N99), Y79 (≠ F100), R80 (≠ S101), V83 (= V104), R86 (≠ K107), L87 (= L108), A119 (≠ P140), G120 (≠ A141), H121 (≠ F142), Y125 (≠ V146), D151 (= D172)
O06543 Alpha-methylacyl-CoA racemase; AMACR; MtMCR; EC 5.1.99.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
28% identity, 84% coverage: 1:334/398 of query aligns to 1:317/360 of O06543
- R38 (vs. gap) binding
- R52 (= R68) mutation to A: 15.7% of wild-type activity.
- I56 (≠ S72) mutation to P: 28.8% of wild-type activity.
- ADLK 59:62 (≠ IDLK 75:78) binding
- E82 (≠ D98) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NFS 99:101) binding
- R91 (≠ K107) binding ; mutation to A: 19.9% of wild-type activity.
- M111 (≠ V127) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ AFDQVV 141:146) binding
- H126 (≠ F142) mutation to A: 4.5% of wild-type activity.
- D156 (= D172) mutation to A: 17.6 of wild-type activity.
- D190 (= D205) mutation to A: 3.3% of wild-type activity.
- E241 (≠ F254) mutation to A: 2.1% of wild-type activity.
- C297 (≠ P314) mutation to A: 6.2% of wild-type activity.
- H312 (≠ Q329) mutation to A: 10.1% of wild-type activity.
Q9UHK6 Alpha-methylacyl-CoA racemase; 2-methylacyl-CoA racemase; EC 5.1.99.4 from Homo sapiens (Human) (see 5 papers)
26% identity, 99% coverage: 5:397/398 of query aligns to 3:373/382 of Q9UHK6
- V9 (≠ I11) to M: in dbSNP:rs3195676
- S52 (= S72) to P: in AMACRD and CBAS4; inactive enzyme; dbSNP:rs121917814
- L107 (≠ V127) to P: in CBAS4; inactive enzyme; dbSNP:rs121917816
- G175 (= G194) to D: in dbSNP:rs10941112
- L201 (= L220) to S: in dbSNP:rs2287939
- M261 (vs. gap) to T: in dbSNP:rs3195678
- E277 (≠ T298) to K: in dbSNP:rs2278008
Sites not aligning to the query:
- 380:382 Microbody targeting signal
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)
27% identity, 83% coverage: 4:334/398 of query aligns to 3:311/354 of 2gd6A
- active site: G16 (≠ L17), D121 (= D143), D150 (= D172), G213 (≠ V234), G214 (≠ H235)
- binding acetyl coenzyme *a: I15 (≠ M16), R37 (≠ S46), A53 (≠ I75), D54 (= D76), L55 (= L77), K56 (= K78), G77 (≠ N99), Y78 (≠ F100), R79 (≠ S101), V82 (= V104), R85 (≠ K107), G119 (≠ A141), H120 (≠ F142), Y124 (≠ V146), D150 (= D172), M182 (= M203)
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)
27% identity, 83% coverage: 4:334/398 of query aligns to 3:311/354 of 2gd2A
- active site: G16 (≠ L17), D121 (= D143), D150 (= D172), G213 (≠ V234), G214 (≠ H235)
- binding acetoacetyl-coenzyme a: I15 (≠ M16), R37 (≠ S46), A53 (≠ I75), L55 (= L77), K56 (= K78), G77 (≠ N99), Y78 (≠ F100), R79 (≠ S101), V82 (= V104), R85 (≠ K107), L86 (= L108), A118 (≠ P140), G119 (≠ A141), H120 (≠ F142), Y124 (≠ V146), D150 (= D172)
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)
27% identity, 83% coverage: 4:334/398 of query aligns to 3:311/354 of 2gd0A
- active site: G16 (≠ L17), D121 (= D143), D150 (= D172), G213 (≠ V234), G214 (≠ H235)
- binding (s)-2-methylmyristoyl-coenzyme a: D42 (= D51), L55 (= L77), K56 (= K78), G77 (≠ N99), Y78 (≠ F100), R79 (≠ S101), V82 (= V104), R85 (≠ K107), L86 (= L108), G119 (≠ A141), H120 (≠ F142), D121 (= D143), Y124 (≠ V146), D150 (= D172)
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)
27% identity, 83% coverage: 4:334/398 of query aligns to 3:311/354 of 2gciA
- active site: G16 (≠ L17), D121 (= D143), D150 (= D172), G213 (≠ V234), G214 (≠ H235)
- binding (r)-2-methylmyristoyl-coenzyme a: R37 (≠ S46), L55 (= L77), K56 (= K78), G77 (≠ N99), Y78 (≠ F100), R79 (≠ S101), V82 (= V104), G119 (≠ A141), H120 (≠ F142), D121 (= D143), Y124 (≠ V146), D150 (= D172), Y218 (= Y238), I234 (= I253), E235 (≠ F254)
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)
27% identity, 83% coverage: 4:334/398 of query aligns to 3:311/354 of 2gceA
- active site: G16 (≠ L17), D121 (= D143), D150 (= D172), G213 (≠ V234), G214 (≠ H235)
- binding (r)-ibuprofenoyl-coenzyme a: I15 (≠ M16), R37 (≠ S46), L55 (= L77), K56 (= K78), G77 (≠ N99), Y78 (≠ F100), R79 (≠ S101), V82 (= V104), R85 (≠ K107), G119 (≠ A141), H120 (≠ F142), D121 (= D143), Y124 (≠ V146), D150 (= D172), L211 (≠ H232), Y218 (= Y238), I234 (= I253)
- binding (s)-ibuprofenoyl-coenzyme a: I15 (≠ M16), G16 (≠ L17), P17 (≠ S18), R37 (≠ S46), L55 (= L77), K56 (= K78), G77 (≠ N99), Y78 (≠ F100), R79 (≠ S101), V82 (= V104), R85 (≠ K107), G119 (≠ A141), H120 (≠ F142), Y124 (≠ V146), D150 (= D172)
Query Sequence
>GFF2665 FitnessBrowser__Marino:GFF2665
MTKPLEGVRIIDLTHMLSGPYAGMLLADMGAESIKVEPLKGEGTRSLLAKDPRNSYNGHG
AYFITLNRNKKSVCIDLKSEAGLQTFYDLVKDADIVLDNFSAGVPAKLKIDHEHLSRVNP
RIITCSVTGFGQAGPNFKRPAFDQVVQGIGGGMSITGHDAEHPARAGIPIGDLGGGMFAV
MGVLAALHSRAVNGYGQHVDISMLDCQISMLNYMATMYFLSGDNPSPIGNGHFVHVPYDA
FRTSNGFVIIAVIFDSFWDNLVELLGIDELRDPAYKTQPGRFADKHKINGILTDLLKTNT
TEHWVELLSSARIPCAPVNKFSDALSDPQVLFRNMVVDIPQFDGGTVKAPGNPIKLSVDS
SDSYTAPPLLGQHTEDVLKSLGYSDERIAELKAMQAIG
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