SitesBLAST
Comparing PfGW456L13_1728 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_1728 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)
28% identity, 99% coverage: 5:399/399 of query aligns to 2:416/416 of P69902
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
28% identity, 99% coverage: 5:399/399 of query aligns to 1:415/415 of 1pt5A
- active site: Q16 (≠ I20), E139 (≠ G142), D168 (= D171), G247 (≠ H241), G248 (≠ T242)
- binding acetyl coenzyme *a: V15 (≠ L19), S17 (≠ A21), R37 (≠ S41), L71 (= L74), N72 (= N75), T73 (≠ L76), K74 (= K77), N95 (= N98), F96 (= F99), H97 (≠ R100), K124 (≠ S127), K136 (≠ P139), A137 (≠ G140), Y138 (≠ F141), E139 (≠ G142), D168 (= D171), M199 (≠ L203)
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
28% identity, 99% coverage: 5:399/399 of query aligns to 2:416/417 of 1q6yA
- active site: Q17 (≠ I20), E140 (≠ G142), D169 (= D171), G248 (≠ H241), G249 (≠ T242)
- binding coenzyme a: V16 (≠ L19), Q17 (≠ I20), S18 (≠ A21), R38 (≠ S41), L72 (= L74), N73 (= N75), T74 (≠ L76), K75 (= K77), N96 (= N98), F97 (= F99), H98 (≠ R100), M105 (≠ L107), I124 (≠ L126), K137 (≠ P139), A138 (≠ G140), Y139 (≠ F141), D169 (= D171), M200 (≠ L203)
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
27% identity, 98% coverage: 4:394/399 of query aligns to 1:423/430 of 3ubmB
- active site: Q17 (≠ I20), E140 (≠ G142), D182 (= D171), G261 (vs. gap), G262 (vs. gap)
- binding coenzyme a: V16 (≠ L19), R38 (≠ S41), L72 (= L74), N73 (= N75), T74 (≠ L76), K75 (= K77), N96 (= N98), F97 (= F99), R98 (= R100), A101 (≠ V103), R104 (≠ K106), K125 (≠ S127), D182 (= D171), M213 (≠ L203)
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
28% identity, 99% coverage: 5:399/399 of query aligns to 2:409/410 of 1q7eA
- active site: Q17 (≠ I20), E133 (≠ G142), D162 (= D171), G241 (≠ H241), G242 (≠ T242)
- binding methionine: N96 (= N98), F97 (= F99), H98 (≠ R100), P99 (= P101), K118 (≠ S127), K130 (≠ P139), A131 (≠ G140), W246 (vs. gap), F299 (≠ D288), A303 (≠ G292), E306 (≠ D295)
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: 5:394/399 of query aligns to 2:423/428 of O06644
- Q17 (≠ I20) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (≠ S41) binding
- W48 (= W51) 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 (≠ K106) binding
- D169 (= D171) 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: 5:394/399 of query aligns to 1:422/427 of 2vjoA
- active site: A16 (≠ I20), E139 (≠ G142), D168 (= D171), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ T18), A16 (≠ I20), A17 (= A21), R37 (≠ S41), L71 (= L74), M73 (≠ L76), N95 (= N98), F96 (= F99), G97 (≠ R100), R103 (≠ K106), M104 (≠ L107), K136 (≠ P139), V137 (≠ G140), Y138 (≠ F141), D168 (= D171), M199 (≠ L203)
- binding oxalate ion: G257 (vs. gap), G259 (vs. gap), Q261 (vs. gap)
1p5rA Formyl-coa transferase in complex with coenzyme a (see paper)
26% identity, 98% coverage: 5:394/399 of query aligns to 1:422/427 of 1p5rA
- active site: Q16 (≠ I20), E139 (≠ G142), D168 (= D171), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ T18), V15 (≠ L19), Q16 (≠ I20), A17 (= A21), R37 (≠ S41), M73 (≠ L76), K74 (= K77), N95 (= N98), F96 (= F99), A100 (≠ V103), R103 (≠ K106), K136 (≠ P139), V137 (≠ G140), D168 (= D171), M199 (≠ L203)
2vjkA Formyl-coa transferase with aspartyl-coa thioester intermediate derived from oxalyl-coa (see paper)
26% identity, 98% coverage: 5:394/399 of query aligns to 1:422/427 of 2vjkA
- active site: Q16 (≠ I20), E139 (≠ G142), D168 (= D171), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ T18), Q16 (≠ I20), A17 (= A21), R37 (≠ S41), M73 (≠ L76), K74 (= K77), N95 (= N98), F96 (= F99), G97 (≠ R100), R103 (≠ K106), M104 (≠ L107), K136 (≠ P139), V137 (≠ G140), Y138 (≠ F141), D168 (= D171), M199 (≠ L203)
- binding magnesium ion: D293 (≠ L264), D296 (≠ G267)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
26% identity, 98% coverage: 5:394/399 of query aligns to 1:422/427 of 1t4cA
- active site: Q16 (≠ I20), E139 (≠ G142), D168 (= D171), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ T18), V15 (≠ L19), Q16 (≠ I20), R37 (≠ S41), M73 (≠ L76), N95 (= N98), F96 (= F99), R103 (≠ K106), M104 (≠ L107), V137 (≠ G140), Y138 (≠ F141), D168 (= D171), M199 (≠ L203)
- binding oxalic acid: G259 (vs. gap), G260 (vs. gap)
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
26% identity, 98% coverage: 5:394/399 of query aligns to 1:422/427 of 1t3zA
- active site: Q16 (≠ I20), E139 (≠ G142), S168 (≠ D171), G259 (vs. gap), G260 (vs. gap)
- binding oxidized coenzyme a: H14 (≠ T18), V15 (≠ L19), A17 (= A21), R37 (≠ S41), K74 (= K77), N95 (= N98), F96 (= F99), A100 (≠ V103), R103 (≠ K106), M104 (≠ L107), K136 (≠ P139), V137 (≠ G140), Y138 (≠ F141), E139 (≠ G142), M199 (≠ L203)
O06543 Alpha-methylacyl-CoA racemase; AMACR; MtMCR; EC 5.1.99.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
30% identity, 89% coverage: 5:361/399 of query aligns to 2:337/360 of O06543
- R38 (≠ S41) binding
- R52 (= R67) mutation to A: 15.7% of wild-type activity.
- I56 (≠ S71) mutation to P: 28.8% of wild-type activity.
- ADLK 59:62 (≠ LNLK 74:77) binding
- E82 (= E97) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NFR 98:100) binding
- R91 (≠ K106) binding ; mutation to A: 19.9% of wild-type activity.
- M111 (≠ L126) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ GFGAVG 140:145) binding
- H126 (≠ F141) mutation to A: 4.5% of wild-type activity.
- D156 (= D171) mutation to A: 17.6 of wild-type activity.
- D190 (≠ E205) mutation to A: 3.3% of wild-type activity.
- E241 (≠ G255) mutation to A: 2.1% of wild-type activity.
- C297 (≠ P316) mutation to A: 6.2% of wild-type activity.
- H312 (≠ Q331) mutation to A: 10.1% of wild-type activity.
1xvvA Crystal structure of caib mutant d169a in complex with carnitinyl-coa (see paper)
27% identity, 98% coverage: 7:397/399 of query aligns to 8:396/402 of 1xvvA
- active site: I21 (= I20), N138 (≠ G142), A166 (≠ G166), G225 (≠ I231), K226 (≠ M232)
- binding l-carnitinyl-coa inner salt: I19 (≠ T18), E20 (≠ L19), I21 (= I20), A22 (= A21), N69 (= N75), F71 (≠ K77), A92 (≠ N98), S93 (≠ F99), K94 (≠ R100), R100 (≠ K106), R101 (≠ L107), A136 (≠ G140), Y137 (≠ F141), N138 (≠ G142), Y163 (≠ V163)
1xvtA Crystal structure of native caib in complex with coenzyme a (see paper)
27% identity, 98% coverage: 7:397/399 of query aligns to 8:396/402 of 1xvtA
- active site: I21 (= I20), N138 (≠ G142), D166 (≠ G166), G225 (≠ I231), K226 (≠ M232)
- binding coenzyme a: I21 (= I20), A22 (= A21), N42 (≠ S41), L68 (= L74), N69 (= N75), F71 (≠ K77), S93 (≠ F99), K94 (≠ R100), R100 (≠ K106), R101 (≠ L107), P135 (= P139), A136 (≠ G140), D166 (≠ G166), M197 (≠ L203)
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, 89% coverage: 5:361/399 of query aligns to 1:331/354 of 2gd6A
- active site: G16 (≠ I20), D121 (≠ G142), D150 (= D171), G213 (= G234), G214 (≠ I235)
- binding acetyl coenzyme *a: I15 (≠ L19), R37 (≠ S41), A53 (≠ L74), D54 (≠ N75), L55 (= L76), K56 (= K77), G77 (≠ N98), Y78 (≠ F99), R79 (= R100), V82 (= V103), R85 (≠ K106), G119 (= G140), H120 (≠ F141), Y124 (≠ G145), D150 (= D171), M182 (≠ L203)
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, 89% coverage: 5:361/399 of query aligns to 1:331/354 of 2gd2A
- active site: G16 (≠ I20), D121 (≠ G142), D150 (= D171), G213 (= G234), G214 (≠ I235)
- binding acetoacetyl-coenzyme a: I15 (≠ L19), R37 (≠ S41), A53 (≠ L74), L55 (= L76), K56 (= K77), G77 (≠ N98), Y78 (≠ F99), R79 (= R100), V82 (= V103), R85 (≠ K106), L86 (= L107), A118 (≠ P139), G119 (= G140), H120 (≠ F141), Y124 (≠ G145), D150 (= D171)
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, 89% coverage: 5:361/399 of query aligns to 1:331/354 of 2gd0A
- active site: G16 (≠ I20), D121 (≠ G142), D150 (= D171), G213 (= G234), G214 (≠ I235)
- binding (s)-2-methylmyristoyl-coenzyme a: D42 (= D46), L55 (= L76), K56 (= K77), G77 (≠ N98), Y78 (≠ F99), R79 (= R100), V82 (= V103), R85 (≠ K106), L86 (= L107), G119 (= G140), H120 (≠ F141), D121 (≠ G142), Y124 (≠ G145), D150 (= D171)
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, 89% coverage: 5:361/399 of query aligns to 1:331/354 of 2gciA
- active site: G16 (≠ I20), D121 (≠ G142), D150 (= D171), G213 (= G234), G214 (≠ I235)
- binding (r)-2-methylmyristoyl-coenzyme a: R37 (≠ S41), L55 (= L76), K56 (= K77), G77 (≠ N98), Y78 (≠ F99), R79 (= R100), V82 (= V103), G119 (= G140), H120 (≠ F141), D121 (≠ G142), Y124 (≠ G145), D150 (= D171), Y218 (≠ S238), I234 (≠ N254), E235 (≠ G255)
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, 89% coverage: 5:361/399 of query aligns to 1:331/354 of 2gceA
- active site: G16 (≠ I20), D121 (≠ G142), D150 (= D171), G213 (= G234), G214 (≠ I235)
- binding (r)-ibuprofenoyl-coenzyme a: I15 (≠ L19), R37 (≠ S41), L55 (= L76), K56 (= K77), G77 (≠ N98), Y78 (≠ F99), R79 (= R100), V82 (= V103), R85 (≠ K106), G119 (= G140), H120 (≠ F141), D121 (≠ G142), Y124 (≠ G145), D150 (= D171), L211 (≠ M232), Y218 (≠ S238), I234 (≠ N254)
- binding (s)-ibuprofenoyl-coenzyme a: I15 (≠ L19), G16 (≠ I20), P17 (≠ A21), R37 (≠ S41), L55 (= L76), K56 (= K77), G77 (≠ N98), Y78 (≠ F99), R79 (= R100), V82 (= V103), R85 (≠ K106), G119 (= G140), H120 (≠ F141), Y124 (≠ G145), D150 (= D171)
P31572 L-carnitine CoA-transferase; Crotonobetainyl-CoA:carnitine CoA-transferase; EC 2.8.3.21 from Escherichia coli (strain K12) (see paper)
27% identity, 98% coverage: 7:397/399 of query aligns to 11:399/405 of P31572
- K97 (≠ R100) binding
- R104 (≠ L107) binding
Query Sequence
>PfGW456L13_1728 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_1728
MPFTAKPLSGLKVIELGTLIAGPFASRICAEFGADVIKIESPDGGDPLRKWRKLYEGTSL
WWFVQARNKKSLTLNLKHPDGQAILKQLLGEADILIENFRPGVLEKLGLGWDVLHALNPK
LVMVRLSGFGQTGPMKDQPGFGAVGESMGGLRYITGFEDRPPVRTGISIGDSIAALWGVI
GALMALRHREVNGGLGQVVDVALYEAIFAMMESMVPEFDVFGFIRERTGNIMPGITPSSI
HTSADGKHVQIGANGDAIFKRFMLIIGREDLANDPQLASNDGRDARRDEIYGVIDRWVNS
LPLDRVLAQLNQAEVPASRIFSAEDMFNDPQYLAREMFLQAKLPDGKDFKMPGIVPKLSE
TPGECEWVGPQLGEHNAQVLQELGYDATQIAQLRKDGAI
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