SitesBLAST
Comparing HSERO_RS18350 FitnessBrowser__HerbieS:HSERO_RS18350 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)
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)
28% identity, 98% coverage: 10:415/415 of query aligns to 4:416/416 of P69902
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
28% identity, 98% coverage: 10:415/415 of query aligns to 4:416/417 of 1q6yA
- active site: Q17 (≠ I23), E140 (≠ G145), D169 (= D174), G248 (vs. gap), G249 (vs. gap)
- binding coenzyme a: V16 (≠ L22), Q17 (≠ I23), S18 (≠ A24), R38 (≠ A44), L72 (= L77), N73 (= N78), T74 (≠ M79), K75 (= K80), N96 (= N101), F97 (≠ Y102), H98 (≠ R103), M105 (≠ W110), I124 (≠ L129), K137 (≠ P142), A138 (≠ G143), Y139 (≠ F144), D169 (= D174), M200 (≠ L219)
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
28% identity, 98% coverage: 10:415/415 of query aligns to 3:415/415 of 1pt5A
- active site: Q16 (≠ I23), E139 (≠ G145), D168 (= D174), G247 (vs. gap), G248 (vs. gap)
- binding acetyl coenzyme *a: V15 (≠ L22), S17 (≠ A24), R37 (≠ A44), L71 (= L77), N72 (= N78), T73 (≠ M79), K74 (= K80), N95 (= N101), F96 (≠ Y102), H97 (≠ R103), K124 (≠ S130), K136 (≠ P142), A137 (≠ G143), Y138 (≠ F144), E139 (≠ G145), D168 (= D174), M199 (≠ L219)
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
28% identity, 98% coverage: 10:415/415 of query aligns to 4:409/410 of 1q7eA
- active site: Q17 (≠ I23), E133 (≠ G145), D162 (= D174), G241 (vs. gap), G242 (vs. gap)
- binding methionine: N96 (= N101), F97 (≠ Y102), H98 (≠ R103), P99 (= P104), K118 (≠ S130), K130 (≠ P142), A131 (≠ G143), W246 (vs. gap), F299 (≠ E304), A303 (= A308), E306 (≠ Q311)
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
27% identity, 98% coverage: 10:415/415 of query aligns to 4:428/430 of 3ubmB
- active site: Q17 (≠ I23), E140 (≠ G145), D182 (= D174), G261 (vs. gap), G262 (vs. gap)
- binding coenzyme a: V16 (≠ L22), R38 (≠ A44), L72 (= L77), N73 (= N78), T74 (≠ M79), K75 (= K80), N96 (= N101), F97 (≠ Y102), R98 (= R103), A101 (≠ V106), R104 (≠ K109), K125 (≠ S130), D182 (= D174), M213 (≠ L219)
1p5rA Formyl-coa transferase in complex with coenzyme a (see paper)
27% identity, 98% coverage: 10:415/415 of query aligns to 3:427/427 of 1p5rA
- active site: Q16 (≠ I23), E139 (≠ G145), D168 (= D174), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ T21), V15 (≠ L22), Q16 (≠ I23), A17 (= A24), R37 (≠ A44), M73 (= M79), K74 (= K80), N95 (= N101), F96 (≠ Y102), A100 (≠ V106), R103 (≠ K109), K136 (≠ P142), V137 (≠ G143), D168 (= D174), M199 (≠ L219)
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: 10:415/415 of query aligns to 4:428/428 of O06644
- Q17 (≠ I23) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (≠ A44) binding
- W48 (= W54) 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 (≠ K109) binding
- D169 (= D174) 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)
27% identity, 98% coverage: 10:415/415 of query aligns to 3:427/427 of 2vjoA
- active site: A16 (≠ I23), E139 (≠ G145), D168 (= D174), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ T21), A16 (≠ I23), A17 (= A24), R37 (≠ A44), L71 (= L77), M73 (= M79), N95 (= N101), F96 (≠ Y102), G97 (≠ R103), R103 (≠ K109), M104 (≠ W110), K136 (≠ P142), V137 (≠ G143), Y138 (≠ F144), D168 (= D174), M199 (≠ L219)
- 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)
27% identity, 98% coverage: 10:415/415 of query aligns to 3:427/427 of 2vjkA
- active site: Q16 (≠ I23), E139 (≠ G145), D168 (= D174), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ T21), Q16 (≠ I23), A17 (= A24), R37 (≠ A44), M73 (= M79), K74 (= K80), N95 (= N101), F96 (≠ Y102), G97 (≠ R103), R103 (≠ K109), M104 (≠ W110), K136 (≠ P142), V137 (≠ G143), Y138 (≠ F144), D168 (= D174), M199 (≠ L219)
- binding magnesium ion: D293 (≠ S280), D296 (≠ G283)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
27% identity, 98% coverage: 10:415/415 of query aligns to 3:427/427 of 1t4cA
- active site: Q16 (≠ I23), E139 (≠ G145), D168 (= D174), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ T21), V15 (≠ L22), Q16 (≠ I23), R37 (≠ A44), M73 (= M79), N95 (= N101), F96 (≠ Y102), R103 (≠ K109), M104 (≠ W110), V137 (≠ G143), Y138 (≠ F144), D168 (= D174), M199 (≠ L219)
- binding oxalic acid: G259 (vs. gap), G260 (vs. gap)
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
27% identity, 98% coverage: 10:415/415 of query aligns to 3:427/427 of 1t3zA
- active site: Q16 (≠ I23), E139 (≠ G145), S168 (≠ D174), G259 (vs. gap), G260 (vs. gap)
- binding oxidized coenzyme a: H14 (≠ T21), V15 (≠ L22), A17 (= A24), R37 (≠ A44), K74 (= K80), N95 (= N101), F96 (≠ Y102), A100 (≠ V106), R103 (≠ K109), M104 (≠ W110), K136 (≠ P142), V137 (≠ G143), Y138 (≠ F144), E139 (≠ G145), M199 (≠ L219)
1xvvA Crystal structure of caib mutant d169a in complex with carnitinyl-coa (see paper)
26% identity, 98% coverage: 7:414/415 of query aligns to 5:397/402 of 1xvvA
- active site: I21 (= I23), N138 (≠ G145), A166 (≠ G173), G225 (= G246), K226 (≠ A247)
- binding l-carnitinyl-coa inner salt: I19 (≠ T21), E20 (≠ L22), I21 (= I23), A22 (= A24), N69 (= N78), F71 (≠ K80), A92 (≠ N101), S93 (≠ Y102), K94 (≠ R103), R100 (≠ K109), R101 (≠ W110), A136 (≠ G143), Y137 (≠ F144), N138 (≠ G145), Y163 (≠ I170)
1xvtA Crystal structure of native caib in complex with coenzyme a (see paper)
26% identity, 98% coverage: 7:414/415 of query aligns to 5:397/402 of 1xvtA
- active site: I21 (= I23), N138 (≠ G145), D166 (≠ G173), G225 (= G246), K226 (≠ A247)
- binding coenzyme a: I21 (= I23), A22 (= A24), N42 (≠ A44), L68 (= L77), N69 (= N78), F71 (≠ K80), S93 (≠ Y102), K94 (≠ R103), R100 (≠ K109), R101 (≠ W110), P135 (= P142), A136 (≠ G143), D166 (≠ G173), M197 (≠ L219)
P31572 L-carnitine CoA-transferase; Crotonobetainyl-CoA:carnitine CoA-transferase; EC 2.8.3.21 from Escherichia coli (strain K12) (see paper)
26% identity, 98% coverage: 7:414/415 of query aligns to 8:400/405 of P31572
- K97 (≠ R103) binding
- R104 (≠ W110) binding
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
29% identity, 83% coverage: 10:353/415 of query aligns to 5:322/360 of 5yx6A
O06543 Alpha-methylacyl-CoA racemase; AMACR; MtMCR; EC 5.1.99.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
26% identity, 89% coverage: 9:377/415 of query aligns to 3:337/360 of O06543
- R38 (≠ A44) binding
- R52 (= R70) mutation to A: 15.7% of wild-type activity.
- I56 (≠ S74) mutation to P: 28.8% of wild-type activity.
- ADLK 59:62 (≠ LNMK 77:80) binding
- E82 (= E100) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NYR 101:103) binding
- R91 (≠ K109) binding ; mutation to A: 19.9% of wild-type activity.
- M111 (≠ L129) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ GFGAIG 143:148) binding
- H126 (≠ F144) mutation to A: 4.5% of wild-type activity.
- D156 (= D174) mutation to A: 17.6 of wild-type activity.
- D190 (≠ E221) mutation to A: 3.3% of wild-type activity.
- E241 (≠ G271) mutation to A: 2.1% of wild-type activity.
- C297 (≠ P332) mutation to A: 6.2% of wild-type activity.
- H312 (≠ Q347) mutation to A: 10.1% of wild-type activity.
Q9UHK6 Alpha-methylacyl-CoA racemase; 2-methylacyl-CoA racemase; EC 5.1.99.4 from Homo sapiens (Human) (see 5 papers)
25% identity, 98% coverage: 11:415/415 of query aligns to 3:373/382 of Q9UHK6
- V9 (≠ L17) to M: in dbSNP:rs3195676
- S52 (= S74) to P: in AMACRD and CBAS4; inactive enzyme; dbSNP:rs121917814
- L107 (= L129) to P: in CBAS4; inactive enzyme; dbSNP:rs121917816
- G175 (= G210) to D: in dbSNP:rs10941112
- L201 (≠ F236) to S: in dbSNP:rs2287939
- M261 (≠ R295) to T: in dbSNP:rs3195678
- E277 (≠ Q311) to K: in dbSNP:rs2278008
Sites not aligning to the query:
- 380:382 Microbody targeting signal
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)
25% identity, 89% coverage: 9:377/415 of query aligns to 2:331/354 of 2gd6A
- active site: G16 (≠ I23), D121 (≠ G145), D150 (= D174), G213 (= G250), G214 (≠ I251)
- binding acetyl coenzyme *a: I15 (≠ L22), R37 (≠ A44), A53 (≠ L77), D54 (≠ N78), L55 (≠ M79), K56 (= K80), G77 (≠ N101), Y78 (= Y102), R79 (= R103), V82 (= V106), R85 (≠ K109), G119 (= G143), H120 (≠ F144), Y124 (≠ G148), D150 (= D174), M182 (≠ L219)
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)
25% identity, 89% coverage: 9:377/415 of query aligns to 2:331/354 of 2gd2A
- active site: G16 (≠ I23), D121 (≠ G145), D150 (= D174), G213 (= G250), G214 (≠ I251)
- binding acetoacetyl-coenzyme a: I15 (≠ L22), R37 (≠ A44), A53 (≠ L77), L55 (≠ M79), K56 (= K80), G77 (≠ N101), Y78 (= Y102), R79 (= R103), V82 (= V106), R85 (≠ K109), L86 (≠ W110), A118 (≠ P142), G119 (= G143), H120 (≠ F144), Y124 (≠ G148), D150 (= D174)
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)
25% identity, 89% coverage: 9:377/415 of query aligns to 2:331/354 of 2gd0A
- active site: G16 (≠ I23), D121 (≠ G145), D150 (= D174), G213 (= G250), G214 (≠ I251)
- binding (s)-2-methylmyristoyl-coenzyme a: D42 (= D49), L55 (≠ M79), K56 (= K80), G77 (≠ N101), Y78 (= Y102), R79 (= R103), V82 (= V106), R85 (≠ K109), L86 (≠ W110), G119 (= G143), H120 (≠ F144), D121 (≠ G145), Y124 (≠ G148), D150 (= D174)
Query Sequence
>HSERO_RS18350 FitnessBrowser__HerbieS:HSERO_RS18350
MTTGTSKPGPLAGIKVLELGTLIAGPFCSRMLAEFGADVIKVEAPGNGDPLRQWRVLKDG
TSLWWSVQARNKKSITLNMKDERAQEIARKLALEADVIIENYRPGVLEKWKLGYEDLKQL
NPATIMVRLSGYGQTGPLRDLPGFGAIGESMGGIRYVSGHPDRPPVRIGISIGDSIAALH
GVIGAMMALRHRDVTGGRWNGKQGADCVAGQGQMVDVALYEAVFNMMESMVPEFDFAGVV
RERTGGALPGIVPSNTYTTGEGMNIVIAGNGDAIFKRLMSAIGREDMANDPGLARNDGRV
PRTEEIDAAIQQWCSTQTIETALATLQAADVPVGKIYSVKDMMNDAQFLARDMFEQHQFA
DGTPVKLPGITPKMSETPGQTKWLGPELGAHSDEILQSLGYDEAHIKMLRDQGVV
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