SitesBLAST
Comparing 16479 FitnessBrowser__Keio:16479 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)
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)
100% identity, 100% coverage: 1:416/416 of query aligns to 1:416/416 of P69902
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
100% identity, 100% coverage: 1:416/416 of query aligns to 1:416/417 of 1q6yA
- active site: Q17 (= Q17), E140 (= E140), D169 (= D169), G248 (= G248), G249 (= G249)
- binding coenzyme a: V16 (= V16), Q17 (= Q17), S18 (= S18), R38 (= R38), L72 (= L72), N73 (= N73), T74 (= T74), K75 (= K75), N96 (= N96), F97 (= F97), H98 (= H98), M105 (= M105), I124 (= I124), K137 (= K137), A138 (= A138), Y139 (= Y139), D169 (= D169), M200 (= M200)
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
100% identity, 100% coverage: 2:416/416 of query aligns to 1:415/415 of 1pt5A
- active site: Q16 (= Q17), E139 (= E140), D168 (= D169), G247 (= G248), G248 (= G249)
- binding acetyl coenzyme *a: V15 (= V16), S17 (= S18), R37 (= R38), L71 (= L72), N72 (= N73), T73 (= T74), K74 (= K75), N95 (= N96), F96 (= F97), H97 (= H98), K124 (= K125), K136 (= K137), A137 (= A138), Y138 (= Y139), E139 (= E140), D168 (= D169), M199 (= M200)
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
98% identity, 100% coverage: 1:416/416 of query aligns to 1:409/410 of 1q7eA
- active site: Q17 (= Q17), E133 (= E140), D162 (= D169), G241 (= G248), G242 (= G249)
- binding methionine: N96 (= N96), F97 (= F97), H98 (= H98), P99 (= P99), K118 (= K125), K130 (= K137), A131 (= A138), W246 (= W253), F299 (= F306), A303 (= A310), E306 (= E313)
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
70% identity, 99% coverage: 2:411/416 of query aligns to 2:423/430 of 3ubmB
- active site: Q17 (= Q17), E140 (= E140), D182 (= D169), G261 (= G248), G262 (= G249)
- binding coenzyme a: V16 (= V16), R38 (= R38), L72 (= L72), N73 (= N73), T74 (= T74), K75 (= K75), N96 (= N96), F97 (= F97), R98 (≠ H98), A101 (= A101), R104 (≠ H104), K125 (= K125), D182 (= D169), M213 (= M200)
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
60% identity, 100% coverage: 1:415/416 of query aligns to 1:424/428 of O06644
- Q17 (= Q17) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (= R38) binding
- W48 (≠ Q48) 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 (≠ H104) binding
- D169 (= D169) 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 (= G247) mutation to A: 2.5-fold decrease of the catalytic effiency.
- G260 (= G248) 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)
60% identity, 100% coverage: 2:415/416 of query aligns to 1:423/427 of 1p5rA
- active site: Q16 (= Q17), E139 (= E140), D168 (= D169), G259 (= G248), G260 (= G249)
- binding coenzyme a: H14 (≠ G15), V15 (= V16), Q16 (= Q17), A17 (≠ S18), R37 (= R38), M73 (≠ T74), K74 (= K75), N95 (= N96), F96 (= F97), A100 (= A101), R103 (≠ H104), K136 (= K137), V137 (≠ A138), D168 (= D169), M199 (= M200)
2vjkA Formyl-coa transferase with aspartyl-coa thioester intermediate derived from oxalyl-coa (see paper)
60% identity, 100% coverage: 2:415/416 of query aligns to 1:423/427 of 2vjkA
- active site: Q16 (= Q17), E139 (= E140), D168 (= D169), G259 (= G248), G260 (= G249)
- binding coenzyme a: H14 (≠ G15), Q16 (= Q17), A17 (≠ S18), R37 (= R38), M73 (≠ T74), K74 (= K75), N95 (= N96), F96 (= F97), G97 (≠ H98), R103 (≠ H104), M104 (= M105), K136 (= K137), V137 (≠ A138), Y138 (= Y139), D168 (= D169), M199 (= M200)
- binding magnesium ion: D293 (≠ K282), D296 (≠ G285)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
60% identity, 100% coverage: 2:415/416 of query aligns to 1:423/427 of 1t4cA
- active site: Q16 (= Q17), E139 (= E140), D168 (= D169), G259 (= G248), G260 (= G249)
- binding coenzyme a: H14 (≠ G15), V15 (= V16), Q16 (= Q17), R37 (= R38), M73 (≠ T74), N95 (= N96), F96 (= F97), R103 (≠ H104), M104 (= M105), V137 (≠ A138), Y138 (= Y139), D168 (= D169), M199 (= M200)
- binding oxalic acid: G259 (= G248), G260 (= G249)
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
60% identity, 100% coverage: 2:415/416 of query aligns to 1:423/427 of 1t3zA
- active site: Q16 (= Q17), E139 (= E140), S168 (≠ D169), G259 (= G248), G260 (= G249)
- binding oxidized coenzyme a: H14 (≠ G15), V15 (= V16), A17 (≠ S18), R37 (= R38), K74 (= K75), N95 (= N96), F96 (= F97), A100 (= A101), R103 (≠ H104), M104 (= M105), K136 (= K137), V137 (≠ A138), Y138 (= Y139), E139 (= E140), M199 (= M200)
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
60% identity, 100% coverage: 2:415/416 of query aligns to 1:423/427 of 2vjoA
- active site: A16 (≠ Q17), E139 (= E140), D168 (= D169), G259 (= G248), G260 (= G249)
- binding coenzyme a: H14 (≠ G15), A16 (≠ Q17), A17 (≠ S18), R37 (= R38), L71 (= L72), M73 (≠ T74), N95 (= N96), F96 (= F97), G97 (≠ H98), R103 (≠ H104), M104 (= M105), K136 (= K137), V137 (≠ A138), Y138 (= Y139), D168 (= D169), M199 (= M200)
- binding oxalate ion: G257 (= G246), G259 (= G248), Q261 (= Q250)
Q9UHK6 Alpha-methylacyl-CoA racemase; 2-methylacyl-CoA racemase; EC 5.1.99.4 from Homo sapiens (Human) (see 5 papers)
26% identity, 99% coverage: 5:416/416 of query aligns to 3:373/382 of Q9UHK6
- V9 (≠ L11) to M: in dbSNP:rs3195676
- S52 (= S69) to P: in AMACRD and CBAS4; inactive enzyme; dbSNP:rs121917814
- L107 (≠ I124) to P: in CBAS4; inactive enzyme; dbSNP:rs121917816
- G175 (= G191) to D: in dbSNP:rs10941112
- L201 (= L221) to S: in dbSNP:rs2287939
- M261 (≠ Y295) to T: in dbSNP:rs3195678
- E277 (= E311) 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)
26% identity, 95% coverage: 2:397/416 of query aligns to 3:360/360 of 5yx6A
O06543 Alpha-methylacyl-CoA racemase; AMACR; MtMCR; EC 5.1.99.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
30% identity, 49% coverage: 1:202/416 of query aligns to 1:190/360 of O06543
- R38 (= R38) binding
- R52 (≠ S65) mutation to A: 15.7% of wild-type activity.
- I56 (≠ S69) mutation to P: 28.8% of wild-type activity.
- ADLK 59:62 (≠ LNTK 72:75) binding
- E82 (= E95) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NFH 96:98) binding
- R91 (≠ H104) binding ; mutation to A: 19.9% of wild-type activity.
- M111 (≠ I124) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ AYENVA 138:143) binding
- H126 (≠ Y139) mutation to A: 4.5% of wild-type activity.
- D156 (= D169) mutation to A: 17.6 of wild-type activity.
- D190 (= D202) mutation to A: 3.3% of wild-type activity.
Sites not aligning to the query:
- 241 E→A: 2.1% of wild-type activity.
- 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)
32% identity, 48% coverage: 4:202/416 of query aligns to 3:185/355 of 2yimA
- active site: G16 (≠ Q17), D122 (≠ E140), D151 (= D169)
- binding 2-methylacetoacetyl coa: I15 (≠ V16), R37 (= R38), A54 (≠ L72), L56 (≠ T74), K57 (= K75), G78 (≠ N96), Y79 (≠ F97), R80 (≠ H98), V83 (≠ A101), R86 (≠ H104), L87 (≠ M105), A119 (≠ K137), G120 (≠ A138), H121 (≠ Y139), Y125 (≠ A143), D151 (= D169)
Sites not aligning to the query:
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)
31% identity, 48% coverage: 4:202/416 of query aligns to 3:184/354 of 2gd6A
- active site: G16 (≠ Q17), D121 (≠ E140), D150 (= D169)
- binding acetyl coenzyme *a: I15 (≠ V16), R37 (= R38), A53 (≠ L72), D54 (≠ N73), L55 (≠ T74), K56 (= K75), G77 (≠ N96), Y78 (≠ F97), R79 (≠ H98), V82 (≠ A101), R85 (≠ H104), G119 (≠ A138), H120 (≠ Y139), Y124 (≠ A143), D150 (= D169), M182 (= M200)
Sites not aligning to the query:
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)
31% identity, 48% coverage: 4:202/416 of query aligns to 3:184/354 of 2gd2A
- active site: G16 (≠ Q17), D121 (≠ E140), D150 (= D169)
- binding acetoacetyl-coenzyme a: I15 (≠ V16), R37 (= R38), A53 (≠ L72), L55 (≠ T74), K56 (= K75), G77 (≠ N96), Y78 (≠ F97), R79 (≠ H98), V82 (≠ A101), R85 (≠ H104), L86 (≠ M105), A118 (≠ K137), G119 (≠ A138), H120 (≠ Y139), Y124 (≠ A143), D150 (= D169)
Sites not aligning to the query:
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)
31% identity, 48% coverage: 4:202/416 of query aligns to 3:184/354 of 2gd0A
- active site: G16 (≠ Q17), D121 (≠ E140), D150 (= D169)
- binding (s)-2-methylmyristoyl-coenzyme a: D42 (= D56), L55 (≠ T74), K56 (= K75), G77 (≠ N96), Y78 (≠ F97), R79 (≠ H98), V82 (≠ A101), R85 (≠ H104), L86 (≠ M105), G119 (≠ A138), H120 (≠ Y139), D121 (≠ E140), Y124 (≠ A143), D150 (= D169)
Sites not aligning to the query:
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)
31% identity, 48% coverage: 4:202/416 of query aligns to 3:184/354 of 2gciA
- active site: G16 (≠ Q17), D121 (≠ E140), D150 (= D169)
- binding (r)-2-methylmyristoyl-coenzyme a: R37 (= R38), L55 (≠ T74), K56 (= K75), G77 (≠ N96), Y78 (≠ F97), R79 (≠ H98), V82 (≠ A101), G119 (≠ A138), H120 (≠ Y139), D121 (≠ E140), Y124 (≠ A143), D150 (= D169)
Sites not aligning to the query:
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)
31% identity, 48% coverage: 4:202/416 of query aligns to 3:184/354 of 2gceA
- active site: G16 (≠ Q17), D121 (≠ E140), D150 (= D169)
- binding (r)-ibuprofenoyl-coenzyme a: I15 (≠ V16), R37 (= R38), L55 (≠ T74), K56 (= K75), G77 (≠ N96), Y78 (≠ F97), R79 (≠ H98), V82 (≠ A101), R85 (≠ H104), G119 (≠ A138), H120 (≠ Y139), D121 (≠ E140), Y124 (≠ A143), D150 (= D169)
- binding (s)-ibuprofenoyl-coenzyme a: I15 (≠ V16), G16 (≠ Q17), P17 (≠ S18), R37 (= R38), L55 (≠ T74), K56 (= K75), G77 (≠ N96), Y78 (≠ F97), R79 (≠ H98), V82 (≠ A101), R85 (≠ H104), G119 (≠ A138), H120 (≠ Y139), Y124 (≠ A143), D150 (= D169)
Sites not aligning to the query:
Query Sequence
>16479 FitnessBrowser__Keio:16479
MSTPLQGIKVLDFTGVQSGPSCTQMLAWFGADVIKIERPGVGDVTRHQLRDIPDIDALYF
TMLNSNKRSIELNTKTAEGKEVMEKLIREADILVENFHPGAIDHMGFTWEHIQEINPRLI
FGSIKGFDECSPYVNVKAYENVAQAAGGAASTTGFWDGPPLVSAAALGDSNTGMHLLIGL
LAALLHREKTGRGQRVTMSMQDAVLNLCRVKLRDQQRLDKLGYLEEYPQYPNGTFGDAVP
RGGNAGGGGQPGWILKCKGWETDPNAYIYFTIQEQNWENTCKAIGKPEWITDPAYSTAHA
RQPHIFDIFAEIEKYTVTIDKHEAVAYLTQFDIPCAPVLSMKEISLDPSLRQSGSVVEVE
QPLRGKYLTVGCPMKFSAFTPDIKAAPLLGEHTAAVLQELGYSDDEIAAMKQNHAI
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