SitesBLAST
Comparing AZOBR_RS27630 FitnessBrowser__azobra:AZOBR_RS27630 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)
1p5rA Formyl-coa transferase in complex with coenzyme a (see paper)
31% identity, 98% coverage: 7:397/397 of query aligns to 1:427/427 of 1p5rA
- active site: Q16 (≠ R22), E139 (≠ D142), D168 (= D171), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R20), V15 (= V21), Q16 (≠ R22), A17 (= A23), R37 (≠ A43), M73 (≠ L76), K74 (≠ R77), N95 (= N98), F96 (≠ Y99), A100 (≠ V103), R103 (= R106), K136 (≠ A139), V137 (≠ G140), D168 (= D171), M199 (≠ L202)
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
31% identity, 98% coverage: 7:397/397 of query aligns to 2:428/428 of O06644
- Q17 (≠ R22) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (≠ A43) binding
- W48 (≠ M53) 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 (= R106) 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.
2vjkA Formyl-coa transferase with aspartyl-coa thioester intermediate derived from oxalyl-coa (see paper)
31% identity, 98% coverage: 7:397/397 of query aligns to 1:427/427 of 2vjkA
- active site: Q16 (≠ R22), E139 (≠ D142), D168 (= D171), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R20), Q16 (≠ R22), A17 (= A23), R37 (≠ A43), M73 (≠ L76), K74 (≠ R77), N95 (= N98), F96 (≠ Y99), G97 (≠ R100), R103 (= R106), M104 (≠ L107), K136 (≠ A139), V137 (≠ G140), Y138 (≠ F141), D168 (= D171), M199 (≠ L202)
- binding magnesium ion: D293 (≠ R262), D296 (≠ E265)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
31% identity, 98% coverage: 7:397/397 of query aligns to 1:427/427 of 1t4cA
- active site: Q16 (≠ R22), E139 (≠ D142), D168 (= D171), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R20), V15 (= V21), Q16 (≠ R22), R37 (≠ A43), M73 (≠ L76), N95 (= N98), F96 (≠ Y99), R103 (= R106), M104 (≠ L107), V137 (≠ G140), Y138 (≠ F141), D168 (= D171), M199 (≠ L202)
- binding oxalic acid: G259 (vs. gap), G260 (vs. gap)
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
31% identity, 98% coverage: 7:397/397 of query aligns to 1:427/427 of 2vjoA
- active site: A16 (≠ R22), E139 (≠ D142), D168 (= D171), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R20), A16 (≠ R22), A17 (= A23), R37 (≠ A43), L71 (= L74), M73 (≠ L76), N95 (= N98), F96 (≠ Y99), G97 (≠ R100), R103 (= R106), M104 (≠ L107), K136 (≠ A139), V137 (≠ G140), Y138 (≠ F141), D168 (= D171), M199 (≠ L202)
- binding oxalate ion: G257 (vs. gap), G259 (vs. gap), Q261 (vs. gap)
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
31% identity, 98% coverage: 7:397/397 of query aligns to 1:427/427 of 1t3zA
- active site: Q16 (≠ R22), E139 (≠ D142), S168 (≠ D171), G259 (vs. gap), G260 (vs. gap)
- binding oxidized coenzyme a: H14 (≠ R20), V15 (= V21), A17 (= A23), R37 (≠ A43), K74 (≠ R77), N95 (= N98), F96 (≠ Y99), A100 (≠ V103), R103 (= R106), M104 (≠ L107), K136 (≠ A139), V137 (≠ G140), Y138 (≠ F141), E139 (≠ D142), M199 (≠ L202)
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
31% identity, 96% coverage: 10:392/397 of query aligns to 4:410/415 of 1pt5A
- active site: Q16 (≠ R22), E139 (≠ D142), D168 (= D171), G247 (vs. gap), G248 (vs. gap)
- binding acetyl coenzyme *a: V15 (= V21), S17 (≠ A23), R37 (≠ A43), L71 (= L74), N72 (= N75), T73 (≠ L76), K74 (≠ R77), N95 (= N98), F96 (≠ Y99), H97 (≠ R100), K124 (≠ S127), K136 (≠ A139), A137 (≠ G140), Y138 (≠ F141), E139 (≠ D142), D168 (= D171), M199 (≠ L202)
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
31% identity, 96% coverage: 10:392/397 of query aligns to 5:411/417 of 1q6yA
- active site: Q17 (≠ R22), E140 (≠ D142), D169 (= D171), G248 (vs. gap), G249 (vs. gap)
- binding coenzyme a: V16 (= V21), Q17 (≠ R22), S18 (≠ A23), R38 (≠ A43), L72 (= L74), N73 (= N75), T74 (≠ L76), K75 (≠ R77), N96 (= N98), F97 (≠ Y99), H98 (≠ R100), M105 (≠ L107), I124 (= I126), K137 (≠ A139), A138 (≠ G140), Y139 (≠ F141), D169 (= D171), M200 (≠ L202)
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)
31% identity, 96% coverage: 10:392/397 of query aligns to 5:411/416 of P69902
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
31% identity, 96% coverage: 10:392/397 of query aligns to 5:404/410 of 1q7eA
- active site: Q17 (≠ R22), E133 (≠ D142), D162 (= D171), G241 (vs. gap), G242 (vs. gap)
- binding methionine: N96 (= N98), F97 (≠ Y99), H98 (≠ R100), P99 (= P101), K118 (≠ S127), K130 (≠ A139), A131 (≠ G140), W246 (vs. gap), F299 (≠ K289), A303 (≠ E293), E306 (≠ F296)
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
29% identity, 98% coverage: 7:397/397 of query aligns to 2:428/430 of 3ubmB
- active site: Q17 (≠ R22), E140 (≠ D142), D182 (= D171), G261 (vs. gap), G262 (vs. gap)
- binding coenzyme a: V16 (= V21), R38 (vs. gap), L72 (= L74), N73 (= N75), T74 (≠ L76), K75 (≠ R77), N96 (= N98), F97 (≠ Y99), R98 (= R100), A101 (≠ V103), R104 (= R106), K125 (≠ S127), D182 (= D171), M213 (≠ L202)
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
31% identity, 94% coverage: 5:378/397 of query aligns to 1:360/360 of 5yx6A
Q9UHK6 Alpha-methylacyl-CoA racemase; 2-methylacyl-CoA racemase; EC 5.1.99.4 from Homo sapiens (Human) (see 5 papers)
30% identity, 98% coverage: 9:397/397 of query aligns to 2:373/382 of Q9UHK6
- V9 (≠ L16) to M: in dbSNP:rs3195676
- S52 (= S71) to P: in AMACRD and CBAS4; inactive enzyme; dbSNP:rs121917814
- L107 (≠ I126) to P: in CBAS4; inactive enzyme; dbSNP:rs121917816
- G175 (= G193) to D: in dbSNP:rs10941112
- L201 (= L218) to S: in dbSNP:rs2287939
- M261 (≠ F282) to T: in dbSNP:rs3195678
- E277 (≠ T298) to K: in dbSNP:rs2278008
Sites not aligning to the query:
- 380:382 Microbody targeting signal
O06543 Alpha-methylacyl-CoA racemase; AMACR; MtMCR; EC 5.1.99.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
31% identity, 82% coverage: 7:330/397 of query aligns to 2:313/360 of O06543
- R38 (≠ A43) 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 (≠ LNLR 74:77) binding
- E82 (= E97) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NYR 98:100) binding
- R91 (= R106) binding ; mutation to A: 19.9% of wild-type activity.
- M111 (≠ I126) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ GFDQIA 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 (≠ E204) mutation to A: 3.3% of wild-type activity.
- E241 (≠ G255) 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.
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, 82% coverage: 7:330/397 of query aligns to 1:307/354 of 2gd6A
- active site: G16 (≠ R22), D121 (= D142), D150 (= D171), G213 (≠ Y233), G214 (≠ S234)
- binding acetyl coenzyme *a: I15 (≠ V21), R37 (≠ A43), A53 (≠ L74), D54 (≠ N75), L55 (= L76), K56 (≠ R77), G77 (≠ N98), Y78 (= Y99), R79 (= R100), V82 (= V103), R85 (= R106), G119 (= G140), H120 (≠ F141), Y124 (≠ A145), D150 (= D171), M182 (≠ L202)
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, 82% coverage: 7:330/397 of query aligns to 1:307/354 of 2gd2A
- active site: G16 (≠ R22), D121 (= D142), D150 (= D171), G213 (≠ Y233), G214 (≠ S234)
- binding acetoacetyl-coenzyme a: I15 (≠ V21), R37 (≠ A43), A53 (≠ L74), L55 (= L76), K56 (≠ R77), G77 (≠ N98), Y78 (= Y99), R79 (= R100), V82 (= V103), R85 (= R106), L86 (= L107), A118 (= A139), G119 (= G140), H120 (≠ F141), Y124 (≠ A145), 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)
30% identity, 82% coverage: 7:330/397 of query aligns to 1:307/354 of 2gd0A
- active site: G16 (≠ R22), D121 (= D142), D150 (= D171), G213 (≠ Y233), G214 (≠ S234)
- binding (s)-2-methylmyristoyl-coenzyme a: D42 (= D48), L55 (= L76), K56 (≠ R77), G77 (≠ N98), Y78 (= Y99), R79 (= R100), V82 (= V103), R85 (= R106), L86 (= L107), G119 (= G140), H120 (≠ F141), D121 (= D142), Y124 (≠ A145), 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)
30% identity, 82% coverage: 7:330/397 of query aligns to 1:307/354 of 2gciA
- active site: G16 (≠ R22), D121 (= D142), D150 (= D171), G213 (≠ Y233), G214 (≠ S234)
- binding (r)-2-methylmyristoyl-coenzyme a: R37 (≠ A43), L55 (= L76), K56 (≠ R77), G77 (≠ N98), Y78 (= Y99), R79 (= R100), V82 (= V103), G119 (= G140), H120 (≠ F141), D121 (= D142), Y124 (≠ A145), D150 (= D171), Y218 (≠ M237), I234 (≠ D254), 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)
30% identity, 82% coverage: 7:330/397 of query aligns to 1:307/354 of 2gceA
- active site: G16 (≠ R22), D121 (= D142), D150 (= D171), G213 (≠ Y233), G214 (≠ S234)
- binding (r)-ibuprofenoyl-coenzyme a: I15 (≠ V21), R37 (≠ A43), L55 (= L76), K56 (≠ R77), G77 (≠ N98), Y78 (= Y99), R79 (= R100), V82 (= V103), R85 (= R106), G119 (= G140), H120 (≠ F141), D121 (= D142), Y124 (≠ A145), D150 (= D171), L211 (≠ H231), Y218 (≠ M237), I234 (≠ D254)
- binding (s)-ibuprofenoyl-coenzyme a: I15 (≠ V21), G16 (≠ R22), P17 (≠ A23), R37 (≠ A43), L55 (= L76), K56 (≠ R77), G77 (≠ N98), Y78 (= Y99), R79 (= R100), V82 (= V103), R85 (= R106), G119 (= G140), H120 (≠ F141), Y124 (≠ A145), D150 (= D171)
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, 82% coverage: 7:330/397 of query aligns to 1:308/355 of 2yimA
- active site: G16 (≠ R22), D122 (= D142), D151 (= D171), G214 (≠ Y233), G215 (≠ S234)
- binding 2-methylacetoacetyl coa: I15 (≠ V21), R37 (≠ A43), A54 (≠ L74), L56 (= L76), K57 (≠ R77), G78 (≠ N98), Y79 (= Y99), R80 (= R100), V83 (= V103), R86 (= R106), L87 (= L107), A119 (= A139), G120 (= G140), H121 (≠ F141), Y125 (≠ A145), D151 (= D171)
Query Sequence
>AZOBR_RS27630 FitnessBrowser__azobra:AZOBR_RS27630
MTRSEPAKALEHIRVLDLTRVRAGPTCCRVLADFGADVIKVEAPPGVDRNEGMSGPRHGY
DMLNLHRNKRSLSLNLRTPQGRDLFLELVRTADVVVENYRPDVKDRLGIGYDALRAVNPR
IILASISGYGQTGPYRERAGFDQIAQGMGGLMSVTGLPGQGPVRAGIAVADSASGLYAAI
GILVALSERDRSGEGQWVQTSLLESQIALMDFQAARYLVEGEVPQPAGNDHPYSTPMGVM
ATADGHLNIGVGGDGQWQSFCRAIEREDLADAPEFATQEQRFRNRPTLKPLLEEVFRTRK
TADWLARLEEEGVPAGPIYRMDEVFADPQVGHLGIAVPCEHPARGAMRLVGQPVGLSRTP
ARIERPAPDAGEHTAEVLGAIGLSPADVAALKAQGIV
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