SitesBLAST
Comparing BPHYT_RS07105 FitnessBrowser__BFirm:BPHYT_RS07105 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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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)
30% identity, 95% coverage: 14:393/401 of query aligns to 5:422/428 of O06644
- Q17 (≠ L26) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (≠ P47) binding
- W48 (= W56) 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 (= R112) binding
- D169 (= D178) 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.
1p5rA Formyl-coa transferase in complex with coenzyme a (see paper)
30% identity, 95% coverage: 14:393/401 of query aligns to 4:421/427 of 1p5rA
- active site: Q16 (≠ L26), E139 (≠ D149), D168 (= D178), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R24), V15 (= V25), Q16 (≠ L26), A17 (≠ G27), R37 (≠ P47), M73 (≠ L82), K74 (≠ S83), N95 (= N104), F96 (= F105), A100 (≠ T109), R103 (= R112), K136 (≠ P146), V137 (≠ G147), D168 (= D178), M199 (≠ L209)
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
30% identity, 95% coverage: 14:393/401 of query aligns to 4:421/427 of 2vjoA
- active site: A16 (≠ L26), E139 (≠ D149), D168 (= D178), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R24), A16 (≠ L26), A17 (≠ G27), R37 (≠ P47), L71 (≠ V80), M73 (≠ L82), N95 (= N104), F96 (= F105), G97 (≠ K106), R103 (= R112), M104 (≠ W113), K136 (≠ P146), V137 (≠ G147), Y138 (= Y148), D168 (= D178), M199 (≠ L209)
- 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)
30% identity, 95% coverage: 14:393/401 of query aligns to 4:421/427 of 2vjkA
- active site: Q16 (≠ L26), E139 (≠ D149), D168 (= D178), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R24), Q16 (≠ L26), A17 (≠ G27), R37 (≠ P47), M73 (≠ L82), K74 (≠ S83), N95 (= N104), F96 (= F105), G97 (≠ K106), R103 (= R112), M104 (≠ W113), K136 (≠ P146), V137 (≠ G147), Y138 (= Y148), D168 (= D178), M199 (≠ L209)
- binding magnesium ion: D293 (≠ A269), D296 (≠ G272)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
30% identity, 95% coverage: 14:393/401 of query aligns to 4:421/427 of 1t4cA
- active site: Q16 (≠ L26), E139 (≠ D149), D168 (= D178), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R24), V15 (= V25), Q16 (≠ L26), R37 (≠ P47), M73 (≠ L82), N95 (= N104), F96 (= F105), R103 (= R112), M104 (≠ W113), V137 (≠ G147), Y138 (= Y148), D168 (= D178), M199 (≠ L209)
- binding oxalic acid: G259 (vs. gap), G260 (vs. gap)
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
30% identity, 95% coverage: 14:393/401 of query aligns to 4:421/427 of 1t3zA
- active site: Q16 (≠ L26), E139 (≠ D149), S168 (≠ D178), G259 (vs. gap), G260 (vs. gap)
- binding oxidized coenzyme a: H14 (≠ R24), V15 (= V25), A17 (≠ G27), R37 (≠ P47), K74 (≠ S83), N95 (= N104), F96 (= F105), A100 (≠ T109), R103 (= R112), M104 (≠ W113), K136 (≠ P146), V137 (≠ G147), Y138 (= Y148), E139 (≠ D149), M199 (≠ L209)
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
31% identity, 96% coverage: 14:398/401 of query aligns to 5:427/430 of 3ubmB
- active site: Q17 (≠ L26), E140 (≠ D149), D182 (= D178), G261 (≠ P239), G262 (≠ N240)
- binding coenzyme a: V16 (= V25), R38 (≠ P47), L72 (≠ V80), N73 (≠ D81), T74 (≠ L82), K75 (≠ S83), N96 (= N104), F97 (= F105), R98 (≠ K106), A101 (≠ T109), R104 (= R112), K125 (≠ S134), D182 (= D178), M213 (≠ L209)
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, 93% coverage: 14:384/401 of query aligns to 5:401/416 of P69902
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
32% identity, 93% coverage: 14:384/401 of query aligns to 4:400/415 of 1pt5A
- active site: Q16 (≠ L26), E139 (≠ D149), D168 (= D178), G247 (≠ P239), G248 (≠ N240)
- binding acetyl coenzyme *a: V15 (= V25), S17 (≠ G27), R37 (≠ P47), L71 (≠ V80), N72 (≠ D81), T73 (≠ L82), K74 (≠ S83), N95 (= N104), F96 (= F105), H97 (≠ K106), K124 (≠ S134), K136 (≠ P146), A137 (≠ G147), Y138 (= Y148), E139 (≠ D149), D168 (= D178), M199 (≠ L209)
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
32% identity, 93% coverage: 14:384/401 of query aligns to 5:401/417 of 1q6yA
- active site: Q17 (≠ L26), E140 (≠ D149), D169 (= D178), G248 (≠ P239), G249 (≠ N240)
- binding coenzyme a: V16 (= V25), Q17 (≠ L26), S18 (≠ G27), R38 (≠ P47), L72 (≠ V80), N73 (≠ D81), T74 (≠ L82), K75 (≠ S83), N96 (= N104), F97 (= F105), H98 (≠ K106), M105 (≠ W113), I124 (≠ V133), K137 (≠ P146), A138 (≠ G147), Y139 (= Y148), D169 (= D178), M200 (≠ L209)
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
29% identity, 90% coverage: 14:373/401 of query aligns to 6:353/360 of 5yx6A
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
31% identity, 93% coverage: 14:384/401 of query aligns to 5:394/410 of 1q7eA
- active site: Q17 (≠ L26), E133 (≠ D149), D162 (= D178), G241 (≠ P239), G242 (≠ N240)
- binding methionine: N96 (= N104), F97 (= F105), H98 (≠ K106), P99 (= P107), K118 (≠ S134), K130 (≠ P146), A131 (≠ G147), W246 (vs. gap), F299 (≠ E293), A303 (= A297), E306 (= E300)
P31572 L-carnitine CoA-transferase; Crotonobetainyl-CoA:carnitine CoA-transferase; EC 2.8.3.21 from Escherichia coli (strain K12) (see paper)
26% identity, 97% coverage: 12:401/401 of query aligns to 10:403/405 of P31572
- K97 (= K106) binding
- R104 (≠ W113) binding
Q9UHK6 Alpha-methylacyl-CoA racemase; 2-methylacyl-CoA racemase; EC 5.1.99.4 from Homo sapiens (Human) (see 5 papers)
27% identity, 97% coverage: 13:401/401 of query aligns to 2:380/382 of Q9UHK6
- V9 (≠ I20) to M: in dbSNP:rs3195676
- S52 (≠ G77) to P: in AMACRD and CBAS4; inactive enzyme; dbSNP:rs121917814
- L107 (≠ V133) to P: in CBAS4; inactive enzyme; dbSNP:rs121917816
- G175 (= G200) to D: in dbSNP:rs10941112
- L201 (≠ F225) to S: in dbSNP:rs2287939
- M261 (≠ N285) to T: in dbSNP:rs3195678
- E277 (≠ S301) to K: in dbSNP:rs2278008
Sites not aligning to the query:
- 380:382 Microbody targeting signal
1xvtA Crystal structure of native caib in complex with coenzyme a (see paper)
26% identity, 97% coverage: 12:401/401 of query aligns to 7:400/402 of 1xvtA
- active site: I21 (≠ L26), N138 (≠ D149), D166 (= D178), G225 (≠ N236), K226 (≠ A237)
- binding coenzyme a: I21 (≠ L26), A22 (≠ G27), N42 (≠ P47), L68 (≠ V80), N69 (≠ D81), F71 (≠ S83), S93 (≠ F105), K94 (= K106), R100 (= R112), R101 (≠ W113), P135 (= P146), A136 (≠ G147), D166 (= D178), M197 (≠ L209)
1xvvA Crystal structure of caib mutant d169a in complex with carnitinyl-coa (see paper)
25% identity, 97% coverage: 12:401/401 of query aligns to 7:400/402 of 1xvvA
- active site: I21 (≠ L26), N138 (≠ D149), A166 (≠ V177), G225 (≠ N236), K226 (≠ A237)
- binding l-carnitinyl-coa inner salt: I19 (≠ R24), E20 (≠ V25), I21 (≠ L26), A22 (≠ G27), N69 (≠ D81), F71 (≠ S83), A92 (≠ N104), S93 (≠ F105), K94 (= K106), R100 (= R112), R101 (≠ W113), A136 (≠ G147), Y137 (= Y148), N138 (≠ D149), Y163 (≠ L174)
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)
28% identity, 92% coverage: 12:380/401 of query aligns to 2:349/354 of 2gd6A
- active site: G16 (≠ L26), D121 (= D149), D150 (= D178), G213 (≠ N240), G214 (≠ I241)
- binding acetyl coenzyme *a: I15 (≠ V25), R37 (≠ P47), A53 (≠ V80), D54 (= D81), L55 (= L82), K56 (≠ S83), G77 (≠ N104), Y78 (≠ F105), R79 (≠ K106), V82 (≠ T109), R85 (= R112), G119 (= G147), H120 (≠ Y148), Y124 (≠ I152), D150 (= D178), M182 (≠ L209)
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)
28% identity, 92% coverage: 12:380/401 of query aligns to 2:349/354 of 2gd2A
- active site: G16 (≠ L26), D121 (= D149), D150 (= D178), G213 (≠ N240), G214 (≠ I241)
- binding acetoacetyl-coenzyme a: I15 (≠ V25), R37 (≠ P47), A53 (≠ V80), L55 (= L82), K56 (≠ S83), G77 (≠ N104), Y78 (≠ F105), R79 (≠ K106), V82 (≠ T109), R85 (= R112), L86 (≠ W113), A118 (≠ P146), G119 (= G147), H120 (≠ Y148), Y124 (≠ I152), D150 (= D178)
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)
28% identity, 92% coverage: 12:380/401 of query aligns to 2:349/354 of 2gd0A
- active site: G16 (≠ L26), D121 (= D149), D150 (= D178), G213 (≠ N240), G214 (≠ I241)
- binding (s)-2-methylmyristoyl-coenzyme a: D42 (≠ E52), L55 (= L82), K56 (≠ S83), G77 (≠ N104), Y78 (≠ F105), R79 (≠ K106), V82 (≠ T109), R85 (= R112), L86 (≠ W113), G119 (= G147), H120 (≠ Y148), D121 (= D149), Y124 (≠ I152), D150 (= D178)
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)
28% identity, 92% coverage: 12:380/401 of query aligns to 2:349/354 of 2gciA
- active site: G16 (≠ L26), D121 (= D149), D150 (= D178), G213 (≠ N240), G214 (≠ I241)
- binding (r)-2-methylmyristoyl-coenzyme a: R37 (≠ P47), L55 (= L82), K56 (≠ S83), G77 (≠ N104), Y78 (≠ F105), R79 (≠ K106), V82 (≠ T109), G119 (= G147), H120 (≠ Y148), D121 (= D149), Y124 (≠ I152), D150 (= D178), Y218 (= Y244), I234 (vs. gap), E235 (≠ N260)
Query Sequence
>BPHYT_RS07105 FitnessBrowser__BFirm:BPHYT_RS07105
MTAPLQNDGAKGALQGLKVIDLSRVLGGPYCTQALADHGAQVIKLEPPNGDETRGWGPPF
YGDTAWYFAGVNRNKQGIAVDLSREEGRAILWKLLEDADVLVENFKPGTLERWGMDYERD
LRERFPKLIHCAVSGFGPDGPLGGLPGYDAAIQAMTGLMSVNGERDGPATRVGLPVVDMV
TGLNALAGILLALAERAKSGRGQSIDIALYDCGVSLLHPHLPNYFGSGRTPQRSGNAHPN
ITPYDSYRTATAPIFLAVGNDRQFAKLCAHLGAPELADDPRYVDNRSRCAHREPLKAALE
SLLTAHECEPLAHALINAGVPCGPVQTVDVVARHPHTLHRGLVVEMGEYRGTASPIKLSR
TPATYRSAPPSLGADTRDVLDKLGIDAATQQRLLESGVLRA
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