SitesBLAST
Comparing BPHYT_RS19985 FitnessBrowser__BFirm:BPHYT_RS19985 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)
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
31% identity, 99% coverage: 4:399/399 of query aligns to 4:428/430 of 3ubmB
- active site: Q17 (≠ L17), E140 (≠ D143), D182 (vs. gap), G261 (vs. gap), G262 (vs. gap)
- binding coenzyme a: V16 (= V16), R38 (≠ H38), L72 (= L75), N73 (= N76), T74 (≠ L77), K75 (= K78), N96 (= N99), F97 (= F100), R98 (= R101), A101 (≠ V104), R104 (= R107), K125 (≠ S128), D182 (vs. gap), M213 (= M203)
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
29% identity, 100% coverage: 1:399/399 of query aligns to 1:428/428 of O06644
- Q17 (≠ L17) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (≠ H38) binding
- W48 (≠ L48) 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 (= R107) binding
- D169 (= D172) 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.
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
29% identity, 100% coverage: 2:399/399 of query aligns to 1:427/427 of 2vjoA
- active site: A16 (≠ L17), E139 (≠ D143), D168 (= D172), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ N15), A16 (≠ L17), A17 (= A18), R37 (≠ H38), L71 (= L75), M73 (≠ L77), N95 (= N99), F96 (= F100), G97 (≠ R101), R103 (= R107), M104 (≠ L108), K136 (≠ P140), V137 (≠ A141), Y138 (= Y142), D168 (= D172), M199 (= M203)
- 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)
29% identity, 100% coverage: 2:399/399 of query aligns to 1:427/427 of 2vjkA
- active site: Q16 (≠ L17), E139 (≠ D143), D168 (= D172), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ N15), Q16 (≠ L17), A17 (= A18), R37 (≠ H38), M73 (≠ L77), K74 (= K78), N95 (= N99), F96 (= F100), G97 (≠ R101), R103 (= R107), M104 (≠ L108), K136 (≠ P140), V137 (≠ A141), Y138 (= Y142), D168 (= D172), M199 (= M203)
- binding magnesium ion: D293 (≠ Q263), D296 (≠ G266)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
29% identity, 100% coverage: 2:399/399 of query aligns to 1:427/427 of 1t4cA
- active site: Q16 (≠ L17), E139 (≠ D143), D168 (= D172), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ N15), V15 (= V16), Q16 (≠ L17), R37 (≠ H38), M73 (≠ L77), N95 (= N99), F96 (= F100), R103 (= R107), M104 (≠ L108), V137 (≠ A141), Y138 (= Y142), D168 (= D172), M199 (= M203)
- binding oxalic acid: G259 (vs. gap), G260 (vs. gap)
1p5rA Formyl-coa transferase in complex with coenzyme a (see paper)
29% identity, 100% coverage: 2:399/399 of query aligns to 1:427/427 of 1p5rA
- active site: Q16 (≠ L17), E139 (≠ D143), D168 (= D172), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ N15), V15 (= V16), Q16 (≠ L17), A17 (= A18), R37 (≠ H38), M73 (≠ L77), K74 (= K78), N95 (= N99), F96 (= F100), A100 (≠ V104), R103 (= R107), K136 (≠ P140), V137 (≠ A141), D168 (= D172), M199 (= M203)
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
29% identity, 100% coverage: 2:399/399 of query aligns to 1:427/427 of 1t3zA
- active site: Q16 (≠ L17), E139 (≠ D143), S168 (≠ D172), G259 (vs. gap), G260 (vs. gap)
- binding oxidized coenzyme a: H14 (≠ N15), V15 (= V16), A17 (= A18), R37 (≠ H38), K74 (= K78), N95 (= N99), F96 (= F100), A100 (≠ V104), R103 (= R107), M104 (≠ L108), K136 (≠ P140), V137 (≠ A141), Y138 (= Y142), E139 (≠ D143), M199 (= M203)
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
35% identity, 76% coverage: 4:305/399 of query aligns to 5:291/360 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)
29% identity, 99% coverage: 1:394/399 of query aligns to 1:411/416 of P69902
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
29% identity, 99% coverage: 1:394/399 of query aligns to 1:411/417 of 1q6yA
- active site: Q17 (≠ L17), E140 (≠ D143), D169 (= D172), G248 (vs. gap), G249 (vs. gap)
- binding coenzyme a: V16 (= V16), Q17 (≠ L17), S18 (≠ A18), R38 (≠ H38), L72 (= L75), N73 (= N76), T74 (≠ L77), K75 (= K78), N96 (= N99), F97 (= F100), H98 (≠ R101), M105 (≠ L108), I124 (= I127), K137 (≠ P140), A138 (= A141), Y139 (= Y142), D169 (= D172), M200 (= M203)
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
29% identity, 98% coverage: 2:394/399 of query aligns to 1:410/415 of 1pt5A
- active site: Q16 (≠ L17), E139 (≠ D143), D168 (= D172), G247 (vs. gap), G248 (vs. gap)
- binding acetyl coenzyme *a: V15 (= V16), S17 (≠ A18), R37 (≠ H38), L71 (= L75), N72 (= N76), T73 (≠ L77), K74 (= K78), N95 (= N99), F96 (= F100), H97 (≠ R101), K124 (≠ S128), K136 (≠ P140), A137 (= A141), Y138 (= Y142), E139 (≠ D143), D168 (= D172), M199 (= M203)
Q9UHK6 Alpha-methylacyl-CoA racemase; 2-methylacyl-CoA racemase; EC 5.1.99.4 from Homo sapiens (Human) (see 5 papers)
31% identity, 99% coverage: 3:399/399 of query aligns to 1:373/382 of Q9UHK6
- V9 (≠ L11) to M: in dbSNP:rs3195676
- S52 (= S72) to P: in AMACRD and CBAS4; inactive enzyme; dbSNP:rs121917814
- L107 (≠ I127) to P: in CBAS4; inactive enzyme; dbSNP:rs121917816
- G175 (= G194) to D: in dbSNP:rs10941112
- L201 (= L219) to S: in dbSNP:rs2287939
- M261 (≠ A281) to T: in dbSNP:rs3195678
- E277 (≠ R299) to K: in dbSNP:rs2278008
Sites not aligning to the query:
- 380:382 Microbody targeting signal
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
28% identity, 99% coverage: 1:394/399 of query aligns to 1:404/410 of 1q7eA
- active site: Q17 (≠ L17), E133 (≠ D143), D162 (= D172), G241 (vs. gap), G242 (vs. gap)
- binding methionine: N96 (= N99), F97 (= F100), H98 (≠ R101), P99 (= P102), K118 (≠ S128), K130 (≠ P140), A131 (= A141), W246 (vs. gap), F299 (≠ A287), A303 (= A291), E306 (= E294)
1xvtA Crystal structure of native caib in complex with coenzyme a (see paper)
28% identity, 99% coverage: 4:398/399 of query aligns to 8:397/402 of 1xvtA
- active site: I21 (≠ L17), N138 (≠ D143), D166 (= D172), G225 (≠ N230), K226 (≠ E231)
- binding coenzyme a: I21 (≠ L17), A22 (= A18), N42 (≠ H38), L68 (= L75), N69 (= N76), F71 (≠ K78), S93 (≠ F100), K94 (≠ R101), R100 (= R107), R101 (≠ L108), P135 (= P140), A136 (= A141), D166 (= D172), M197 (= M203)
P31572 L-carnitine CoA-transferase; Crotonobetainyl-CoA:carnitine CoA-transferase; EC 2.8.3.21 from Escherichia coli (strain K12) (see paper)
28% identity, 99% coverage: 4:398/399 of query aligns to 11:400/405 of P31572
- K97 (≠ R101) binding
- R104 (≠ L108) binding
1xvvA Crystal structure of caib mutant d169a in complex with carnitinyl-coa (see paper)
28% identity, 99% coverage: 4:398/399 of query aligns to 8:397/402 of 1xvvA
- active site: I21 (≠ L17), N138 (≠ D143), A166 (≠ D172), G225 (≠ N230), K226 (≠ E231)
- binding l-carnitinyl-coa inner salt: I19 (≠ N15), E20 (≠ V16), I21 (≠ L17), A22 (= A18), N69 (= N76), F71 (≠ K78), A92 (≠ N99), S93 (≠ F100), K94 (≠ R101), R100 (= R107), R101 (≠ L108), A136 (= A141), Y137 (= Y142), N138 (≠ D143), Y163 (≠ P169)
O06543 Alpha-methylacyl-CoA racemase; AMACR; MtMCR; EC 5.1.99.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
29% identity, 85% coverage: 1:339/399 of query aligns to 1:321/360 of O06543
- R38 (≠ H38) binding
- R52 (= R57) mutation to A: 15.7% of wild-type activity.
- I56 (≠ S72) mutation to P: 28.8% of wild-type activity.
- ADLK 59:62 (≠ LNLK 75:78) binding
- E82 (= E98) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NFR 99:101) binding
- R91 (= R107) binding ; mutation to A: 19.9% of wild-type activity.
- M111 (≠ I127) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ AYDQII 141:146) binding
- H126 (≠ Y142) mutation to A: 4.5% of wild-type activity.
- D156 (= D172) mutation to A: 17.6 of wild-type activity.
- D190 (≠ E205) mutation to A: 3.3% of wild-type activity.
- E241 (= E254) mutation to A: 2.1% of wild-type activity.
- C297 (≠ P315) mutation to A: 6.2% of wild-type activity.
- H312 (= H330) 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)
28% identity, 84% coverage: 4:339/399 of query aligns to 3:316/355 of 2yimA
- active site: G16 (≠ L17), D122 (= D143), D151 (= D172), G214 (≠ T234), G215 (≠ A235)
- binding 2-methylacetoacetyl coa: I15 (≠ V16), R37 (≠ H38), A54 (≠ L75), L56 (= L77), K57 (= K78), G78 (≠ N99), Y79 (≠ F100), R80 (= R101), V83 (= V104), R86 (= R107), L87 (= L108), A119 (≠ P140), G120 (≠ A141), H121 (≠ Y142), Y125 (≠ I146), D151 (= D172)
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, 84% coverage: 4:339/399 of query aligns to 3:315/354 of 2gd6A
- active site: G16 (≠ L17), D121 (= D143), D150 (= D172), G213 (≠ T234), G214 (≠ A235)
- binding acetyl coenzyme *a: I15 (≠ V16), R37 (≠ H38), A53 (≠ L75), D54 (≠ N76), L55 (= L77), K56 (= K78), G77 (≠ N99), Y78 (≠ F100), R79 (= R101), V82 (= V104), R85 (= R107), G119 (≠ A141), H120 (≠ Y142), Y124 (≠ I146), D150 (= D172), M182 (= M203)
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, 84% coverage: 4:339/399 of query aligns to 3:315/354 of 2gd2A
- active site: G16 (≠ L17), D121 (= D143), D150 (= D172), G213 (≠ T234), G214 (≠ A235)
- binding acetoacetyl-coenzyme a: I15 (≠ V16), R37 (≠ H38), A53 (≠ L75), L55 (= L77), K56 (= K78), G77 (≠ N99), Y78 (≠ F100), R79 (= R101), V82 (= V104), R85 (= R107), L86 (= L108), A118 (≠ P140), G119 (≠ A141), H120 (≠ Y142), Y124 (≠ I146), D150 (= D172)
Query Sequence
>BPHYT_RS19985 FitnessBrowser__BFirm:BPHYT_RS19985
MTLPLAGVRVLDLSNVLAGPFCAYQLALLGAEVIKVEHPEGGDLARRLGADKDASARNMG
ASFVAVNAGKQSVTLNLKDPRGKAILRELVKTADVLVENFRPGVMTRLGLDFEALREVNP
KLVYCAISGFGMDGEFSKRPAYDQIIQGISGVMSVTGDADSAPLRVGYPVSDTVGGLTAA
FGICAALLDARATGHGRMLDVSMLEATLATMGWVVSNFLNAGVTPTPMGNENFTAAPSGT
FKTGDGPLNIAANENKQFVSLCQLIGRADLLDDPRFSERNARKMNRAALKAEIEAALARD
SAANWEARFFEAGVPAGRVMSVPEILAHPHLESRGFIREFAADATTERQRVTRAGFRLHD
ADTAPGTPAPVLSAHTREQLAALGYDDAHIDQLRAEGVV
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