SitesBLAST
Comparing YP_427637.1 NCBI__GCF_000013085.1:YP_427637.1 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)
9br7C Succinate--hydroxymethylglutarate CoA-transferase (see paper)
30% identity, 97% coverage: 13:408/408 of query aligns to 3:397/403 of 9br7C
1p5rA Formyl-coa transferase in complex with coenzyme a (see paper)
26% identity, 97% coverage: 13:408/408 of query aligns to 1:427/427 of 1p5rA
- active site: Q16 (≠ I28), E139 (≠ A151), D168 (= D181), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ T26), V15 (≠ F27), Q16 (≠ I28), A17 (= A29), R37 (≠ H49), M73 (≠ L85), K74 (≠ R86), N95 (= N107), F96 (= F108), A100 (≠ T112), R103 (≠ K115), K136 (≠ P148), V137 (≠ G149), D168 (= D181), M199 (≠ L212)
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
26% identity, 97% coverage: 13:408/408 of query aligns to 2:428/428 of O06644
- Q17 (≠ I28) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (≠ H49) binding CoA
- W48 (≠ F59) 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 (≠ K115) binding CoA
- D169 (= D181) 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.
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
27% identity, 97% coverage: 15:408/408 of query aligns to 4:416/417 of 1q6yA
- active site: Q17 (≠ I28), E140 (≠ A151), D169 (= D181), G248 (vs. gap), G249 (vs. gap)
- binding coenzyme a: V16 (≠ F27), Q17 (≠ I28), S18 (≠ A29), R38 (≠ H49), L72 (= L83), N73 (≠ D84), T74 (≠ L85), K75 (≠ R86), N96 (= N107), F97 (= F108), H98 (≠ R109), M105 (≠ W116), I124 (≠ V135), K137 (≠ P148), A138 (≠ G149), Y139 (≠ F150), D169 (= D181), M200 (≠ L212)
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
27% identity, 97% coverage: 15:408/408 of query aligns to 3:415/415 of 1pt5A
- active site: Q16 (≠ I28), E139 (≠ A151), D168 (= D181), G247 (vs. gap), G248 (vs. gap)
- binding acetyl coenzyme *a: V15 (≠ F27), S17 (≠ A29), R37 (≠ H49), L71 (= L83), N72 (≠ D84), T73 (≠ L85), K74 (≠ R86), N95 (= N107), F96 (= F108), H97 (≠ R109), K124 (≠ S136), K136 (≠ P148), A137 (≠ G149), Y138 (≠ F150), E139 (≠ A151), D168 (= D181), M199 (≠ L212)
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)
27% identity, 97% coverage: 15:408/408 of query aligns to 4:416/416 of P69902
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
26% identity, 97% coverage: 13:408/408 of query aligns to 1:427/427 of 2vjoA
- active site: A16 (≠ I28), E139 (≠ A151), D168 (= D181), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ T26), A16 (≠ I28), A17 (= A29), R37 (≠ H49), L71 (= L83), M73 (≠ L85), N95 (= N107), F96 (= F108), G97 (≠ R109), R103 (≠ K115), M104 (≠ W116), K136 (≠ P148), V137 (≠ G149), Y138 (≠ F150), D168 (= D181), M199 (≠ L212)
- binding oxalate ion: G257 (vs. gap), G259 (vs. gap), Q261 (vs. gap)
2vjkA Formyl-coa transferase with aspartyl-coa thioester intermediate derived from oxalyl-coa (see paper)
26% identity, 97% coverage: 13:408/408 of query aligns to 1:427/427 of 2vjkA
- active site: Q16 (≠ I28), E139 (≠ A151), D168 (= D181), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ T26), Q16 (≠ I28), A17 (= A29), R37 (≠ H49), M73 (≠ L85), K74 (≠ R86), N95 (= N107), F96 (= F108), G97 (≠ R109), R103 (≠ K115), M104 (≠ W116), K136 (≠ P148), V137 (≠ G149), Y138 (≠ F150), D168 (= D181), M199 (≠ L212)
- binding magnesium ion: D293 (≠ R273), D296 (≠ G276)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
26% identity, 97% coverage: 13:408/408 of query aligns to 1:427/427 of 1t4cA
- active site: Q16 (≠ I28), E139 (≠ A151), D168 (= D181), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ T26), V15 (≠ F27), Q16 (≠ I28), R37 (≠ H49), M73 (≠ L85), N95 (= N107), F96 (= F108), R103 (≠ K115), M104 (≠ W116), V137 (≠ G149), Y138 (≠ F150), D168 (= D181), M199 (≠ L212)
- binding oxalic acid: G259 (vs. gap), G260 (vs. gap)
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
27% identity, 97% coverage: 14:408/408 of query aligns to 3:428/430 of 3ubmB
- active site: Q17 (≠ I28), E140 (≠ A151), D182 (= D181), G261 (≠ C245), G262 (≠ P246)
- binding coenzyme a: V16 (≠ F27), R38 (≠ H49), L72 (= L83), N73 (≠ D84), T74 (≠ L85), K75 (≠ R86), N96 (= N107), F97 (= F108), R98 (= R109), A101 (≠ T112), R104 (≠ K115), K125 (≠ S136), D182 (= D181), M213 (≠ L212)
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
26% identity, 97% coverage: 13:408/408 of query aligns to 1:427/427 of 1t3zA
- active site: Q16 (≠ I28), E139 (≠ A151), S168 (≠ D181), G259 (vs. gap), G260 (vs. gap)
- binding oxidized coenzyme a: H14 (≠ T26), V15 (≠ F27), A17 (= A29), R37 (≠ H49), K74 (≠ R86), N95 (= N107), F96 (= F108), A100 (≠ T112), R103 (≠ K115), M104 (≠ W116), K136 (≠ P148), V137 (≠ G149), Y138 (≠ F150), E139 (≠ A151), M199 (≠ L212)
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
27% identity, 97% coverage: 15:408/408 of query aligns to 4:409/410 of 1q7eA
- active site: Q17 (≠ I28), E133 (≠ A151), D162 (= D181), G241 (vs. gap), G242 (vs. gap)
- binding methionine: N96 (= N107), F97 (= F108), H98 (≠ R109), P99 (= P110), K118 (≠ S136), K130 (≠ P148), A131 (≠ G149), W246 (≠ F250), F299 (≠ A297), A303 (= A301), E306 (≠ S304)
1xvtA Crystal structure of native caib in complex with coenzyme a (see paper)
30% identity, 98% coverage: 9:407/408 of query aligns to 2:397/402 of 1xvtA
- active site: I21 (= I28), N138 (≠ A151), D166 (= D181), G225 (= G238), K226 (≠ A239)
- binding coenzyme a: I21 (= I28), A22 (= A29), N42 (≠ H49), L68 (= L83), N69 (≠ D84), F71 (≠ R86), S93 (≠ F108), K94 (≠ R109), R100 (≠ K115), R101 (≠ W116), P135 (= P148), A136 (≠ G149), D166 (= D181), M197 (≠ L212)
P31572 L-carnitine CoA-transferase; Crotonobetainyl-CoA:carnitine CoA-transferase; EC 2.8.3.21 from Escherichia coli (strain K12) (see paper)
30% identity, 98% coverage: 9:407/408 of query aligns to 5:400/405 of P31572
- K97 (≠ R109) binding CoA
- R104 (≠ W116) binding CoA
1xvvA Crystal structure of caib mutant d169a in complex with carnitinyl-coa (see paper)
29% identity, 98% coverage: 9:407/408 of query aligns to 2:397/402 of 1xvvA
- active site: I21 (= I28), N138 (≠ A151), A166 (≠ D181), G225 (= G238), K226 (≠ A239)
- binding l-carnitinyl-coa inner salt: I19 (≠ T26), E20 (≠ F27), I21 (= I28), A22 (= A29), N69 (≠ D84), F71 (≠ R86), A92 (≠ N107), S93 (≠ F108), K94 (≠ R109), R100 (≠ K115), R101 (≠ W116), A136 (≠ G149), Y137 (≠ F150), N138 (≠ A151), Y163 (≠ S178)
O06543 Alpha-methylacyl-CoA racemase; AMACR; MtMCR; EC 5.1.99.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
30% identity, 87% coverage: 15:370/408 of query aligns to 4:337/360 of O06543
- R38 (≠ H49) binding substrate
- R52 (= R76) mutation to A: 15.7% of wild-type activity.
- I56 (≠ S80) mutation to P: 28.8% of wild-type activity.
- ADLK 59:62 (≠ LDLR 83:86) binding substrate
- E82 (= E106) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NFR 107:109) binding substrate
- R91 (≠ K115) binding substrate; mutation to A: 19.9% of wild-type activity.
- M111 (≠ V135) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ GFARIA 149:154) binding substrate
- H126 (≠ F150) mutation to A: 4.5% of wild-type activity.
- D156 (= D181) mutation to A: 17.6 of wild-type activity.
- D190 (≠ E214) mutation to A: 3.3% of wild-type activity.
- E241 (≠ N264) mutation to A: 2.1% of wild-type activity.
- C297 (≠ P325) mutation to A: 6.2% of wild-type activity.
- H312 (= H340) 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)
27% identity, 96% coverage: 16:408/408 of query aligns to 3:373/382 of Q9UHK6
- V9 (≠ L22) to M: in dbSNP:rs3195676
- S52 (= S80) to P: in AMACRD and CBAS4; inactive enzyme; dbSNP:rs121917814
- L107 (≠ V135) to P: in CBAS4; inactive enzyme; dbSNP:rs121917816
- G175 (= G203) to D: in dbSNP:rs10941112
- L201 (≠ T230) to S: in dbSNP:rs2287939
- M261 (≠ P283) to T: in dbSNP:rs3195678
- E277 (≠ D300) to K: in dbSNP:rs2278008
Sites not aligning to the query:
- 380:382 Microbody targeting signal
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
32% identity, 76% coverage: 12:322/408 of query aligns to 2:298/360 of 5yx6A
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, 87% coverage: 15:370/408 of query aligns to 3:331/354 of 2gd6A
- active site: G16 (≠ I28), D121 (≠ A151), D150 (= D181), G213 (vs. gap), G214 (vs. gap)
- binding acetyl coenzyme *a: I15 (≠ F27), R37 (≠ H49), A53 (≠ L83), D54 (= D84), L55 (= L85), K56 (≠ R86), G77 (≠ N107), Y78 (≠ F108), R79 (= R109), V82 (≠ T112), R85 (≠ K115), G119 (= G149), H120 (≠ F150), Y124 (≠ A154), D150 (= D181), M182 (≠ L212)
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, 87% coverage: 15:370/408 of query aligns to 3:331/354 of 2gd2A
- active site: G16 (≠ I28), D121 (≠ A151), D150 (= D181), G213 (vs. gap), G214 (vs. gap)
- binding acetoacetyl-coenzyme a: I15 (≠ F27), R37 (≠ H49), A53 (≠ L83), L55 (= L85), K56 (≠ R86), G77 (≠ N107), Y78 (≠ F108), R79 (= R109), V82 (≠ T112), R85 (≠ K115), L86 (≠ W116), A118 (≠ P148), G119 (= G149), H120 (≠ F150), Y124 (≠ A154), D150 (= D181)
Query Sequence
>YP_427637.1 NCBI__GCF_000013085.1:YP_427637.1
MTVSPPPPPAAPVRPLAGLRVLDAATFIAAPFAAGLLGEFGAEVIKIEHPAGGDPFRRFG
TMTERGDSLAWLSEGRNKASLTLDLRKPQGAEVFRKLVAGADVLCENFRPGTLEKWGLGW
EVLSAINPGLVMLRVSGYGQDGPYRDYPGFARIAHAFGGLTHLAGLPGGPPVTPGSTSLG
DYMSGLFGAFGVLSALRHRDATGRGQQVDIALYESVFRVLDELAPAYAYTGAVRGPEGAG
TLNACPHGHFPCASGGWVAIACTNDKMFERLARVMGRPALASPEVWGTTARRLAERAAVD
ALVSAWTGALARTEVLALCHAGEVPCGPINAIDDIFADPHFQARQTMVTLIEAQLGAIVV
PNVLPKLSETPGRIDHLGPRLGADSGRILGELGLSEAEIADLRAQGVV
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