SitesBLAST
Comparing WP_012116683.1 NCBI__GCF_000017645.1:WP_012116683.1 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)
42% identity, 97% coverage: 4:382/391 of query aligns to 5:377/403 of 9br7C
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
32% identity, 97% coverage: 4:382/391 of query aligns to 5:360/360 of 5yx6A
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, 98% coverage: 1:385/391 of query aligns to 1:400/416 of P69902
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
31% identity, 98% coverage: 1:385/391 of query aligns to 1:400/417 of 1q6yA
- active site: Q17 (≠ L17), E140 (≠ D146), D169 (= D175), G248 (≠ N237), G249 (≠ I238)
- binding coenzyme a: V16 (≠ I16), Q17 (≠ L17), S18 (≠ A18), R38 (= R38), L72 (≠ V78), N73 (≠ D79), T74 (≠ F80), K75 (≠ E81), N96 (= N102), F97 (= F103), H98 (≠ K104), M105 (≠ Y111), I124 (≠ V130), K137 (≠ A143), A138 (≠ G144), Y139 (= Y145), D169 (= D175), M200 (≠ L206)
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
31% identity, 98% coverage: 2:385/391 of query aligns to 1:399/415 of 1pt5A
- active site: Q16 (≠ L17), E139 (≠ D146), D168 (= D175), G247 (≠ N237), G248 (≠ I238)
- binding acetyl coenzyme *a: V15 (≠ I16), S17 (≠ A18), R37 (= R38), L71 (≠ V78), N72 (≠ D79), T73 (≠ F80), K74 (≠ E81), N95 (= N102), F96 (= F103), H97 (≠ K104), K124 (≠ T131), K136 (≠ A143), A137 (≠ G144), Y138 (= Y145), E139 (≠ D146), D168 (= D175), M199 (≠ L206)
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
30% identity, 98% coverage: 1:385/391 of query aligns to 1:393/410 of 1q7eA
- active site: Q17 (≠ L17), E133 (≠ D146), D162 (= D175), G241 (≠ N237), G242 (≠ I238)
- binding methionine: N96 (= N102), F97 (= F103), H98 (≠ Y111), P99 (≠ G112), K118 (≠ T131), K130 (≠ A143), A131 (≠ G144), W246 (≠ Q242), F299 (≠ A290), A303 (≠ P294), E306 (≠ S297)
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
27% identity, 98% coverage: 1:385/391 of query aligns to 1:412/428 of O06644
- Q17 (≠ L17) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (= R38) binding CoA
- W48 (= W48) 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 (≠ K110) binding CoA
- D169 (= D175) 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 (≠ H235) mutation to A: 2.5-fold decrease of the catalytic effiency.
- G260 (≠ P236) mutation to A: 25-fold decrease of the catalytic effiency. Reduction of the affinity binding for both formyl-CoA and oxalate.
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
29% identity, 98% coverage: 2:385/391 of query aligns to 2:412/430 of 3ubmB
- active site: Q17 (≠ L17), E140 (≠ D146), D182 (= D175), G261 (vs. gap), G262 (vs. gap)
- binding coenzyme a: V16 (≠ I16), R38 (= R38), L72 (≠ V78), N73 (≠ D79), T74 (≠ F80), K75 (≠ E81), N96 (= N102), F97 (= F103), R98 (≠ K104), A101 (≠ G107), R104 (≠ K110), K125 (≠ T131), D182 (= D175), M213 (≠ L206)
1p5rA Formyl-coa transferase in complex with coenzyme a (see paper)
27% identity, 98% coverage: 2:385/391 of query aligns to 1:411/427 of 1p5rA
- active site: Q16 (≠ L17), E139 (≠ D146), D168 (= D175), G259 (≠ P236), G260 (≠ N237)
- binding coenzyme a: H14 (≠ R15), V15 (≠ I16), Q16 (≠ L17), A17 (= A18), R37 (= R38), M73 (≠ F80), K74 (≠ E81), N95 (= N102), F96 (= F103), A100 (≠ G107), R103 (≠ K110), K136 (≠ A143), V137 (≠ G144), D168 (= D175), M199 (≠ L206)
2vjkA Formyl-coa transferase with aspartyl-coa thioester intermediate derived from oxalyl-coa (see paper)
27% identity, 98% coverage: 2:385/391 of query aligns to 1:411/427 of 2vjkA
- active site: Q16 (≠ L17), E139 (≠ D146), D168 (= D175), G259 (≠ P236), G260 (≠ N237)
- binding coenzyme a: H14 (≠ R15), Q16 (≠ L17), A17 (= A18), R37 (= R38), M73 (≠ F80), K74 (≠ E81), N95 (= N102), F96 (= F103), G97 (≠ K104), R103 (≠ K110), M104 (≠ Y111), K136 (≠ A143), V137 (≠ G144), Y138 (= Y145), D168 (= D175), M199 (≠ L206)
- binding magnesium ion: D293 (≠ A266), D296 (≠ G269)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
27% identity, 98% coverage: 2:385/391 of query aligns to 1:411/427 of 1t4cA
- active site: Q16 (≠ L17), E139 (≠ D146), D168 (= D175), G259 (≠ P236), G260 (≠ N237)
- binding coenzyme a: H14 (≠ R15), V15 (≠ I16), Q16 (≠ L17), R37 (= R38), M73 (≠ F80), N95 (= N102), F96 (= F103), R103 (≠ K110), M104 (≠ Y111), V137 (≠ G144), Y138 (= Y145), D168 (= D175), M199 (≠ L206)
- binding oxalic acid: G259 (≠ P236), G260 (≠ N237)
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
27% identity, 98% coverage: 2:385/391 of query aligns to 1:411/427 of 2vjoA
- active site: A16 (≠ L17), E139 (≠ D146), D168 (= D175), G259 (≠ P236), G260 (≠ N237)
- binding coenzyme a: H14 (≠ R15), A16 (≠ L17), A17 (= A18), R37 (= R38), L71 (≠ V78), M73 (≠ F80), N95 (= N102), F96 (= F103), G97 (≠ K104), R103 (≠ K110), M104 (≠ Y111), K136 (≠ A143), V137 (≠ G144), Y138 (= Y145), D168 (= D175), M199 (≠ L206)
- binding oxalate ion: G257 (≠ A234), G259 (≠ P236), Q261 (≠ I238)
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
27% identity, 98% coverage: 2:385/391 of query aligns to 1:411/427 of 1t3zA
- active site: Q16 (≠ L17), E139 (≠ D146), S168 (≠ D175), G259 (≠ P236), G260 (≠ N237)
- binding oxidized coenzyme a: H14 (≠ R15), V15 (≠ I16), A17 (= A18), R37 (= R38), K74 (≠ E81), N95 (= N102), F96 (= F103), A100 (≠ G107), R103 (≠ K110), M104 (≠ Y111), K136 (≠ A143), V137 (≠ G144), Y138 (= Y145), E139 (≠ D146), M199 (≠ L206)
O06543 Alpha-methylacyl-CoA racemase; AMACR; MtMCR; EC 5.1.99.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
29% identity, 90% coverage: 1:352/391 of query aligns to 1:328/360 of O06543
- R38 (= R38) binding substrate
- R52 (= R71) mutation to A: 15.7% of wild-type activity.
- I56 (≠ S75) mutation to P: 28.8% of wild-type activity.
- ADLK 59:62 (≠ VDFE 78:81) binding substrate
- E82 (= E101) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NFK 102:104) binding substrate
- R91 (≠ K110) binding substrate; mutation to A: 19.9% of wild-type activity.
- M111 (≠ V130) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ GYDFLV 144:149) binding substrate
- H126 (≠ Y145) mutation to A: 4.5% of wild-type activity.
- D156 (= D175) mutation to A: 17.6 of wild-type activity.
- D190 (= D208) mutation to A: 3.3% of wild-type activity.
- E241 (≠ D258) mutation to A: 2.1% of wild-type activity.
- C297 (≠ P318) mutation to A: 6.2% of wild-type activity.
- H312 (≠ Q333) mutation to 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, 89% coverage: 4:352/391 of query aligns to 3:323/355 of 2yimA
- active site: G16 (≠ L17), D122 (= D146), D151 (= D175), G214 (≠ N233), G215 (≠ A234)
- binding 2-methylacetoacetyl coa: I15 (= I16), R37 (= R38), A54 (≠ V78), L56 (≠ F80), K57 (≠ E81), G78 (≠ N102), Y79 (≠ F103), R80 (≠ K104), V83 (≠ G107), R86 (≠ K110), L87 (≠ Y111), A119 (= A143), G120 (= G144), H121 (≠ Y145), Y125 (≠ V149), D151 (= D175)
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: 4:352/391 of query aligns to 3:322/354 of 2gd6A
- active site: G16 (≠ L17), D121 (= D146), D150 (= D175), G213 (≠ N233), G214 (≠ A234)
- binding acetyl coenzyme *a: I15 (= I16), R37 (= R38), A53 (≠ V78), D54 (= D79), L55 (≠ F80), K56 (≠ E81), G77 (≠ N102), Y78 (≠ F103), R79 (≠ K104), V82 (≠ G107), R85 (≠ K110), G119 (= G144), H120 (≠ Y145), Y124 (≠ V149), D150 (= D175), M182 (≠ L206)
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: 4:352/391 of query aligns to 3:322/354 of 2gd2A
- active site: G16 (≠ L17), D121 (= D146), D150 (= D175), G213 (≠ N233), G214 (≠ A234)
- binding acetoacetyl-coenzyme a: I15 (= I16), R37 (= R38), A53 (≠ V78), L55 (≠ F80), K56 (≠ E81), G77 (≠ N102), Y78 (≠ F103), R79 (≠ K104), V82 (≠ G107), R85 (≠ K110), L86 (≠ Y111), A118 (= A143), G119 (= G144), H120 (≠ Y145), Y124 (≠ V149), D150 (= D175)
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: 4:352/391 of query aligns to 3:322/354 of 2gd0A
- active site: G16 (≠ L17), D121 (= D146), D150 (= D175), G213 (≠ N233), G214 (≠ A234)
- binding (s)-2-methylmyristoyl-coenzyme a: D42 (= D43), L55 (≠ F80), K56 (≠ E81), G77 (≠ N102), Y78 (≠ F103), R79 (≠ K104), V82 (≠ G107), R85 (≠ K110), L86 (≠ Y111), G119 (= G144), H120 (≠ Y145), D121 (= D146), Y124 (≠ V149), D150 (= D175)
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: 4:352/391 of query aligns to 3:322/354 of 2gciA
- active site: G16 (≠ L17), D121 (= D146), D150 (= D175), G213 (≠ N233), G214 (≠ A234)
- binding (r)-2-methylmyristoyl-coenzyme a: R37 (= R38), L55 (≠ F80), K56 (≠ E81), G77 (≠ N102), Y78 (≠ F103), R79 (≠ K104), V82 (≠ G107), G119 (= G144), H120 (≠ Y145), D121 (= D146), Y124 (≠ V149), D150 (= D175), Y218 (= Y241), I234 (≠ N257), E235 (≠ D258)
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: 4:352/391 of query aligns to 3:322/354 of 2gceA
- active site: G16 (≠ L17), D121 (= D146), D150 (= D175), G213 (≠ N233), G214 (≠ A234)
- binding (r)-ibuprofenoyl-coenzyme a: I15 (= I16), R37 (= R38), L55 (≠ F80), K56 (≠ E81), G77 (≠ N102), Y78 (≠ F103), R79 (≠ K104), V82 (≠ G107), R85 (≠ K110), G119 (= G144), H120 (≠ Y145), D121 (= D146), Y124 (≠ V149), D150 (= D175), L211 (≠ M231), Y218 (= Y241), I234 (≠ N257)
- binding (s)-ibuprofenoyl-coenzyme a: I15 (= I16), G16 (≠ L17), P17 (≠ A18), R37 (= R38), L55 (≠ F80), K56 (≠ E81), G77 (≠ N102), Y78 (≠ F103), R79 (≠ K104), V82 (≠ G107), R85 (≠ K110), G119 (= G144), H120 (≠ Y145), Y124 (≠ V149), D150 (= D175)
Query Sequence
>WP_012116683.1 NCBI__GCF_000017645.1:WP_012116683.1
MSPPLAGLRVLELARILAGPWCGQLLADLGAEVIKVERPGGGDDTRTWGPPFLTGEDGAD
LGAAYFHATNRGKRSVAVDFETAEGQETIRALARQSDVVIENFKVGGLKKYGLDYASLKA
ENPRLVYCSVTGFGQDGPYAPRAGYDFLVQGMGGIMDLTGAPEGEPQKVGVAFADIFTGL
YATVGILAALRRREETGTGGHVDMALLDTQVGVLANQAMNYLTSGKAPRRMGNAHPNIVP
YQVFPCADGYFIAAVGNDGQFARFCAVLGAPELAQEADFGTNPARVAHRAALVPQLSALT
AAFRRDDLLAALEAKGVPAGPINTVAQVFDDPQVKARGLRVDLKEAGGGTIPAVASPIVL
DGERQVAKAASPRLGADTQAVLAALKALAKG
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