SitesBLAST
Comparing H281DRAFT_03364 FitnessBrowser__Burk376:H281DRAFT_03364 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)
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
31% identity, 96% coverage: 8:396/407 of query aligns to 4:411/417 of 1q6yA
- active site: Q17 (≠ T21), E140 (≠ D144), D169 (= D173), G248 (vs. gap), G249 (vs. gap)
- binding coenzyme a: V16 (≠ M20), Q17 (≠ T21), S18 (≠ A22), R38 (≠ E42), L72 (= L76), N73 (≠ D77), T74 (≠ L78), K75 (= K79), N96 (= N100), F97 (= F101), H98 (≠ R102), M105 (≠ L109), I124 (≠ V128), K137 (≠ P141), A138 (= A142), Y139 (≠ N143), D169 (= D173), M200 (≠ L204)
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: 8:396/407 of query aligns to 4:411/416 of P69902
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
31% identity, 96% coverage: 8:396/407 of query aligns to 3:410/415 of 1pt5A
- active site: Q16 (≠ T21), E139 (≠ D144), D168 (= D173), G247 (vs. gap), G248 (vs. gap)
- binding acetyl coenzyme *a: V15 (≠ M20), S17 (≠ A22), R37 (≠ E42), L71 (= L76), N72 (≠ D77), T73 (≠ L78), K74 (= K79), N95 (= N100), F96 (= F101), H97 (≠ R102), K124 (≠ S129), K136 (≠ P141), A137 (= A142), Y138 (≠ N143), E139 (≠ D144), D168 (= D173), M199 (≠ L204)
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
31% identity, 97% coverage: 8:403/407 of query aligns to 4:430/430 of 3ubmB
- active site: Q17 (≠ T21), E140 (≠ D144), D182 (vs. gap), G261 (vs. gap), G262 (vs. gap)
- binding coenzyme a: V16 (≠ M20), R38 (≠ E42), L72 (= L76), N73 (≠ D77), T74 (≠ L78), K75 (= K79), N96 (= N100), F97 (= F101), R98 (= R102), A101 (≠ T105), R104 (= R108), K125 (≠ S129), D182 (vs. gap), M213 (≠ L204)
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
31% identity, 96% coverage: 8:396/407 of query aligns to 4:404/410 of 1q7eA
- active site: Q17 (≠ T21), E133 (≠ D144), D162 (= D173), G241 (vs. gap), G242 (vs. gap)
- binding methionine: N96 (= N100), F97 (= F101), H98 (≠ R102), P99 (= P103), K118 (≠ S129), K130 (≠ P141), A131 (= A142), W246 (≠ T235), F299 (≠ L291), A303 (≠ L295), E306 (= E297)
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
32% identity, 92% coverage: 8:382/407 of query aligns to 5:360/360 of 5yx6A
1p5rA Formyl-coa transferase in complex with coenzyme a (see paper)
27% identity, 97% coverage: 8:400/407 of query aligns to 3:426/427 of 1p5rA
- active site: Q16 (≠ T21), E139 (≠ D144), D168 (= D173), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ V19), V15 (≠ M20), Q16 (≠ T21), A17 (= A22), R37 (≠ E42), M73 (≠ L78), K74 (= K79), N95 (= N100), F96 (= F101), A100 (≠ T105), R103 (= R108), K136 (≠ P141), V137 (≠ A142), D168 (= D173), M199 (≠ L204)
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
27% identity, 97% coverage: 8:400/407 of query aligns to 4:427/428 of O06644
- Q17 (≠ T21) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (≠ E42) binding
- W48 (≠ L52) 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 (= R108) binding
- D169 (= D173) 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)
27% identity, 97% coverage: 8:400/407 of query aligns to 3:426/427 of 2vjkA
- active site: Q16 (≠ T21), E139 (≠ D144), D168 (= D173), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ V19), Q16 (≠ T21), A17 (= A22), R37 (≠ E42), M73 (≠ L78), K74 (= K79), N95 (= N100), F96 (= F101), G97 (≠ R102), R103 (= R108), M104 (≠ L109), K136 (≠ P141), V137 (≠ A142), Y138 (≠ N143), D168 (= D173), M199 (≠ L204)
- binding magnesium ion: D293 (≠ R265), D296 (≠ G268)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
27% identity, 97% coverage: 8:400/407 of query aligns to 3:426/427 of 1t4cA
- active site: Q16 (≠ T21), E139 (≠ D144), D168 (= D173), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ V19), V15 (≠ M20), Q16 (≠ T21), R37 (≠ E42), M73 (≠ L78), N95 (= N100), F96 (= F101), R103 (= R108), M104 (≠ L109), V137 (≠ A142), Y138 (≠ N143), D168 (= D173), M199 (≠ L204)
- 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)
27% identity, 97% coverage: 8:400/407 of query aligns to 3:426/427 of 2vjoA
- active site: A16 (≠ T21), E139 (≠ D144), D168 (= D173), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ V19), A16 (≠ T21), A17 (= A22), R37 (≠ E42), L71 (= L76), M73 (≠ L78), N95 (= N100), F96 (= F101), G97 (≠ R102), R103 (= R108), M104 (≠ L109), K136 (≠ P141), V137 (≠ A142), Y138 (≠ N143), D168 (= D173), M199 (≠ L204)
- binding oxalate ion: G257 (vs. gap), G259 (vs. gap), Q261 (vs. gap)
Q9UHK6 Alpha-methylacyl-CoA racemase; 2-methylacyl-CoA racemase; EC 5.1.99.4 from Homo sapiens (Human) (see 5 papers)
29% identity, 96% coverage: 9:400/407 of query aligns to 3:372/382 of Q9UHK6
- V9 (≠ L15) to M: in dbSNP:rs3195676
- S52 (= S73) to P: in AMACRD and CBAS4; inactive enzyme; dbSNP:rs121917814
- L107 (≠ V128) to P: in CBAS4; inactive enzyme; dbSNP:rs121917816
- G175 (= G195) to D: in dbSNP:rs10941112
- L201 (= L220) to S: in dbSNP:rs2287939
- M261 (≠ T285) to T: in dbSNP:rs3195678
- E277 (≠ L301) to K: in dbSNP:rs2278008
Sites not aligning to the query:
- 380:382 Microbody targeting signal
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
27% identity, 97% coverage: 8:400/407 of query aligns to 3:426/427 of 1t3zA
- active site: Q16 (≠ T21), E139 (≠ D144), S168 (≠ D173), G259 (vs. gap), G260 (vs. gap)
- binding oxidized coenzyme a: H14 (≠ V19), V15 (≠ M20), A17 (= A22), R37 (≠ E42), K74 (= K79), N95 (= N100), F96 (= F101), A100 (≠ T105), R103 (= R108), M104 (≠ L109), K136 (≠ P141), V137 (≠ A142), Y138 (≠ N143), E139 (≠ D144), M199 (≠ L204)
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, 76% coverage: 7:315/407 of query aligns to 2:289/354 of 2gd6A
- active site: G16 (≠ T21), D121 (= D144), D150 (= D173), G213 (≠ S231), G214 (= G232)
- binding acetyl coenzyme *a: I15 (≠ M20), R37 (≠ E42), A53 (≠ L76), D54 (= D77), L55 (= L78), K56 (= K79), G77 (≠ N100), Y78 (≠ F101), R79 (= R102), V82 (≠ T105), R85 (= R108), G119 (≠ A142), H120 (≠ N143), Y124 (≠ V147), D150 (= D173), M182 (≠ L204)
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, 76% coverage: 7:315/407 of query aligns to 2:289/354 of 2gd2A
- active site: G16 (≠ T21), D121 (= D144), D150 (= D173), G213 (≠ S231), G214 (= G232)
- binding acetoacetyl-coenzyme a: I15 (≠ M20), R37 (≠ E42), A53 (≠ L76), L55 (= L78), K56 (= K79), G77 (≠ N100), Y78 (≠ F101), R79 (= R102), V82 (≠ T105), R85 (= R108), L86 (= L109), A118 (≠ P141), G119 (≠ A142), H120 (≠ N143), Y124 (≠ V147), D150 (= D173)
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, 76% coverage: 7:315/407 of query aligns to 2:289/354 of 2gd0A
- active site: G16 (≠ T21), D121 (= D144), D150 (= D173), G213 (≠ S231), G214 (= G232)
- binding (s)-2-methylmyristoyl-coenzyme a: D42 (= D47), L55 (= L78), K56 (= K79), G77 (≠ N100), Y78 (≠ F101), R79 (= R102), V82 (≠ T105), R85 (= R108), L86 (= L109), G119 (≠ A142), H120 (≠ N143), D121 (= D144), Y124 (≠ V147), D150 (= D173)
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, 76% coverage: 7:315/407 of query aligns to 2:289/354 of 2gciA
- active site: G16 (≠ T21), D121 (= D144), D150 (= D173), G213 (≠ S231), G214 (= G232)
- binding (r)-2-methylmyristoyl-coenzyme a: R37 (≠ E42), L55 (= L78), K56 (= K79), G77 (≠ N100), Y78 (≠ F101), R79 (= R102), V82 (≠ T105), G119 (≠ A142), H120 (≠ N143), D121 (= D144), Y124 (≠ V147), D150 (= D173), Y218 (= Y239), I234 (≠ F255), E235 (≠ T256)
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, 76% coverage: 7:315/407 of query aligns to 2:289/354 of 2gceA
- active site: G16 (≠ T21), D121 (= D144), D150 (= D173), G213 (≠ S231), G214 (= G232)
- binding (r)-ibuprofenoyl-coenzyme a: I15 (≠ M20), R37 (≠ E42), L55 (= L78), K56 (= K79), G77 (≠ N100), Y78 (≠ F101), R79 (= R102), V82 (≠ T105), R85 (= R108), G119 (≠ A142), H120 (≠ N143), D121 (= D144), Y124 (≠ V147), D150 (= D173), L211 (= L229), Y218 (= Y239), I234 (≠ F255)
- binding (s)-ibuprofenoyl-coenzyme a: I15 (≠ M20), G16 (≠ T21), P17 (≠ A22), R37 (≠ E42), L55 (= L78), K56 (= K79), G77 (≠ N100), Y78 (≠ F101), R79 (= R102), V82 (≠ T105), R85 (= R108), G119 (≠ A142), H120 (≠ N143), Y124 (≠ V147), D150 (= D173)
O06543 Alpha-methylacyl-CoA racemase; AMACR; MtMCR; EC 5.1.99.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
29% identity, 76% coverage: 7:315/407 of query aligns to 3:295/360 of O06543
- R38 (≠ E42) binding
- R52 (= R69) mutation to A: 15.7% of wild-type activity.
- I56 (≠ S73) mutation to P: 28.8% of wild-type activity.
- ADLK 59:62 (≠ LDLK 76:79) binding
- E82 (= E99) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NFR 100:102) binding
- R91 (= R108) binding ; mutation to A: 19.9% of wild-type activity.
- M111 (≠ V128) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ ANDPIV 142:147) binding
- H126 (≠ N143) mutation to A: 4.5% of wild-type activity.
- D156 (= D173) mutation to A: 17.6 of wild-type activity.
- D190 (vs. gap) mutation to A: 3.3% of wild-type activity.
- E241 (≠ T256) mutation to A: 2.1% of wild-type activity.
Sites not aligning to the query:
- 297 C→A: 6.2% of wild-type activity.
- 312 H→A: 10.1% of wild-type activity.
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)
29% identity, 76% coverage: 7:315/407 of query aligns to 2:290/355 of 2yimA
- active site: G16 (≠ T21), D122 (= D144), D151 (= D173), G214 (≠ S231), G215 (= G232)
- binding 2-methylacetoacetyl coa: I15 (≠ M20), R37 (≠ E42), A54 (≠ L76), L56 (= L78), K57 (= K79), G78 (≠ N100), Y79 (≠ F101), R80 (= R102), V83 (≠ T105), R86 (= R108), L87 (= L109), A119 (≠ P141), G120 (≠ A142), H121 (≠ N143), Y125 (≠ V147), D151 (= D173)
Query Sequence
>H281DRAFT_03364 FitnessBrowser__Burk376:H281DRAFT_03364
MDKKQVGPLSGYRILDLTVMTAGPVGTVLLADLGADVVKVEEPMAGDLSRKLGNQFVQGE
SVQFLSQNRNKRSIRLDLKSPKGRDAFLRMAEQADVVVENFRPGTVDRLGIGYAAVKARN
PKIVYASVSAFGQSGPYAAWPANDPIVQAVAGLMDMTGEAGGNPVRLGAPLPDFGAAALL
AFGISAALLHRERHGEGQRIDTSLLSAALFSTIPRDGETLRSGKAPERLGSGHPTMVPYR
NYQGSDGRYFFAACFTEKFWQNLCRALGREELLSDERFIGNTARTANRHALDVILEEQFL
LHTAEYWVAHLSAADVPCAIVQDYHTALTQDPQISHNHAVVEIEHPVAGRVTNIASPVNF
HGSPVAYRRPPPTLGQHTAEVLAEYGFGEEEIAALEGRELAAAGAKS
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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