SitesBLAST
Comparing CCNA_03677 FitnessBrowser__Caulo:CCNA_03677 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)
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
28% identity, 97% coverage: 7:398/403 of query aligns to 1:411/415 of 1pt5A
- active site: Q16 (≠ I22), E139 (≠ A145), D168 (= D174), G247 (vs. gap), G248 (vs. gap)
- binding acetyl coenzyme *a: V15 (≠ L21), S17 (≠ A23), R37 (≠ D43), L71 (≠ V77), N72 (≠ D78), T73 (≠ L79), K74 (≠ R80), N95 (= N101), F96 (= F102), H97 (≠ R103), K124 (≠ S130), K136 (≠ A142), A137 (≠ G143), Y138 (= Y144), E139 (≠ A145), D168 (= D174), M199 (≠ I205)
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, 97% coverage: 7:398/403 of query aligns to 2:412/416 of P69902
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
28% identity, 97% coverage: 7:398/403 of query aligns to 2:412/417 of 1q6yA
- active site: Q17 (≠ I22), E140 (≠ A145), D169 (= D174), G248 (vs. gap), G249 (vs. gap)
- binding coenzyme a: V16 (≠ L21), Q17 (≠ I22), S18 (≠ A23), R38 (≠ D43), L72 (≠ V77), N73 (≠ D78), T74 (≠ L79), K75 (≠ R80), N96 (= N101), F97 (= F102), H98 (≠ R103), M105 (≠ W110), I124 (≠ V129), K137 (≠ A142), A138 (≠ G143), Y139 (= Y144), D169 (= D174), M200 (≠ I205)
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
28% identity, 98% coverage: 7:401/403 of query aligns to 2:427/430 of 3ubmB
- active site: Q17 (≠ I22), E140 (≠ A145), D182 (= D174), G261 (vs. gap), G262 (vs. gap)
- binding coenzyme a: V16 (≠ L21), R38 (≠ D43), L72 (≠ V77), N73 (≠ D78), T74 (≠ L79), K75 (≠ R80), N96 (= N101), F97 (= F102), R98 (= R103), A101 (≠ T106), R104 (≠ K109), K125 (≠ S130), D182 (= D174), M213 (≠ I205)
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
27% identity, 98% coverage: 7:402/403 of query aligns to 1:427/427 of 2vjoA
- active site: A16 (≠ I22), E139 (≠ A145), D168 (= D174), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ S20), A16 (≠ I22), A17 (= A23), R37 (≠ D43), L71 (≠ V77), M73 (≠ L79), N95 (= N101), F96 (= F102), G97 (≠ R103), R103 (≠ K109), M104 (≠ W110), K136 (≠ A142), V137 (≠ G143), Y138 (= Y144), D168 (= D174), M199 (≠ I205)
- binding oxalate ion: G257 (vs. gap), G259 (vs. gap), Q261 (vs. gap)
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: 7:402/403 of query aligns to 2:428/428 of O06644
- Q17 (≠ I22) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (≠ D43) binding
- W48 (= W53) 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.
1p5rA Formyl-coa transferase in complex with coenzyme a (see paper)
27% identity, 98% coverage: 7:402/403 of query aligns to 1:427/427 of 1p5rA
- active site: Q16 (≠ I22), E139 (≠ A145), D168 (= D174), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ S20), V15 (≠ L21), Q16 (≠ I22), A17 (= A23), R37 (≠ D43), M73 (≠ L79), K74 (≠ R80), N95 (= N101), F96 (= F102), A100 (≠ T106), R103 (≠ K109), K136 (≠ A142), V137 (≠ G143), D168 (= D174), M199 (≠ I205)
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
33% identity, 94% coverage: 5:382/403 of query aligns to 1:360/360 of 5yx6A
2vjkA Formyl-coa transferase with aspartyl-coa thioester intermediate derived from oxalyl-coa (see paper)
27% identity, 98% coverage: 7:402/403 of query aligns to 1:427/427 of 2vjkA
- active site: Q16 (≠ I22), E139 (≠ A145), D168 (= D174), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ S20), Q16 (≠ I22), A17 (= A23), R37 (≠ D43), M73 (≠ L79), K74 (≠ R80), N95 (= N101), F96 (= F102), G97 (≠ R103), R103 (≠ K109), M104 (≠ W110), K136 (≠ A142), V137 (≠ G143), Y138 (= Y144), D168 (= D174), M199 (≠ I205)
- binding magnesium ion: D293 (≠ E266), D296 (≠ G269)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
27% identity, 98% coverage: 7:402/403 of query aligns to 1:427/427 of 1t4cA
- active site: Q16 (≠ I22), E139 (≠ A145), D168 (= D174), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ S20), V15 (≠ L21), Q16 (≠ I22), R37 (≠ D43), M73 (≠ L79), N95 (= N101), F96 (= F102), R103 (≠ K109), M104 (≠ W110), V137 (≠ G143), Y138 (= Y144), D168 (= D174), M199 (≠ I205)
- binding oxalic acid: G259 (vs. gap), G260 (vs. gap)
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
27% identity, 98% coverage: 7:402/403 of query aligns to 1:427/427 of 1t3zA
- active site: Q16 (≠ I22), E139 (≠ A145), S168 (≠ D174), G259 (vs. gap), G260 (vs. gap)
- binding oxidized coenzyme a: H14 (≠ S20), V15 (≠ L21), A17 (= A23), R37 (≠ D43), K74 (≠ R80), N95 (= N101), F96 (= F102), A100 (≠ T106), R103 (≠ K109), M104 (≠ W110), K136 (≠ A142), V137 (≠ G143), Y138 (= Y144), E139 (≠ A145), M199 (≠ I205)
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
27% identity, 97% coverage: 7:398/403 of query aligns to 2:405/410 of 1q7eA
- active site: Q17 (≠ I22), E133 (≠ A145), D162 (= D174), G241 (vs. gap), G242 (vs. gap)
- binding methionine: N96 (= N101), F97 (= F102), H98 (≠ R103), P99 (= P104), K118 (≠ S130), K130 (≠ A142), A131 (≠ G143), W246 (≠ G236), F299 (≠ A290), A303 (= A294), E306 (≠ A297)
P31572 L-carnitine CoA-transferase; Crotonobetainyl-CoA:carnitine CoA-transferase; EC 2.8.3.21 from Escherichia coli (strain K12) (see paper)
30% identity, 98% coverage: 8:401/403 of query aligns to 10:400/405 of P31572
- K97 (≠ R103) binding
- R104 (≠ W110) binding
1xvtA Crystal structure of native caib in complex with coenzyme a (see paper)
30% identity, 98% coverage: 8:401/403 of query aligns to 7:397/402 of 1xvtA
- active site: I21 (= I22), N138 (≠ A145), D166 (= D174), G225 (≠ A232), K226 (≠ V233)
- binding coenzyme a: I21 (= I22), A22 (= A23), N42 (≠ D43), L68 (≠ V77), N69 (≠ D78), F71 (≠ R80), S93 (≠ F102), K94 (≠ R103), R100 (≠ K109), R101 (≠ W110), P135 (≠ A142), A136 (≠ G143), D166 (= D174), M197 (≠ I205)
1xvvA Crystal structure of caib mutant d169a in complex with carnitinyl-coa (see paper)
29% identity, 98% coverage: 8:401/403 of query aligns to 7:397/402 of 1xvvA
- active site: I21 (= I22), N138 (≠ A145), A166 (≠ D174), G225 (≠ A232), K226 (≠ V233)
- binding l-carnitinyl-coa inner salt: I19 (≠ S20), E20 (≠ L21), I21 (= I22), A22 (= A23), N69 (≠ D78), F71 (≠ R80), A92 (≠ N101), S93 (≠ F102), K94 (≠ R103), R100 (≠ K109), R101 (≠ W110), A136 (≠ G143), Y137 (= Y144), N138 (≠ A145), Y163 (≠ S171)
O06543 Alpha-methylacyl-CoA racemase; AMACR; MtMCR; EC 5.1.99.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
35% identity, 68% coverage: 8:283/403 of query aligns to 3:266/360 of O06543
- R38 (≠ D43) 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 (≠ VDLR 77:80) binding
- E82 (= E100) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NFR 101:103) binding
- R91 (≠ K109) binding ; mutation to A: 19.9% of wild-type activity.
- M111 (≠ V129) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ GYALVG 143:148) binding
- H126 (≠ Y144) mutation to A: 4.5% of wild-type activity.
- D156 (= D174) mutation to A: 17.6 of wild-type activity.
- D190 (≠ E207) mutation to A: 3.3% of wild-type activity.
- E241 (≠ Q257) 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.
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)
34% identity, 68% coverage: 8:283/403 of query aligns to 2:260/354 of 2gd6A
- active site: G16 (≠ I22), D121 (≠ A145), D150 (= D174), G213 (= G236), G214 (≠ I237)
- binding acetyl coenzyme *a: I15 (≠ L21), R37 (≠ D43), A53 (≠ V77), D54 (= D78), L55 (= L79), K56 (≠ R80), G77 (≠ N101), Y78 (≠ F102), R79 (= R103), V82 (≠ T106), R85 (≠ K109), G119 (= G143), H120 (≠ Y144), Y124 (≠ G148), D150 (= D174), M182 (≠ I205)
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)
34% identity, 68% coverage: 8:283/403 of query aligns to 2:260/354 of 2gd2A
- active site: G16 (≠ I22), D121 (≠ A145), D150 (= D174), G213 (= G236), G214 (≠ I237)
- binding acetoacetyl-coenzyme a: I15 (≠ L21), R37 (≠ D43), A53 (≠ V77), L55 (= L79), K56 (≠ R80), G77 (≠ N101), Y78 (≠ F102), R79 (= R103), V82 (≠ T106), R85 (≠ K109), L86 (≠ W110), A118 (= A142), G119 (= G143), H120 (≠ Y144), 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)
34% identity, 68% coverage: 8:283/403 of query aligns to 2:260/354 of 2gd0A
- active site: G16 (≠ I22), D121 (≠ A145), D150 (= D174), G213 (= G236), G214 (≠ I237)
- binding (s)-2-methylmyristoyl-coenzyme a: D42 (= D48), L55 (= L79), K56 (≠ R80), G77 (≠ N101), Y78 (≠ F102), R79 (= R103), V82 (≠ T106), R85 (≠ K109), L86 (≠ W110), G119 (= G143), H120 (≠ Y144), D121 (≠ A145), Y124 (≠ G148), D150 (= D174)
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)
34% identity, 68% coverage: 8:283/403 of query aligns to 2:260/354 of 2gciA
- active site: G16 (≠ I22), D121 (≠ A145), D150 (= D174), G213 (= G236), G214 (≠ I237)
- binding (r)-2-methylmyristoyl-coenzyme a: R37 (≠ D43), L55 (= L79), K56 (≠ R80), G77 (≠ N101), Y78 (≠ F102), R79 (= R103), V82 (≠ T106), G119 (= G143), H120 (≠ Y144), D121 (≠ A145), Y124 (≠ G148), D150 (= D174), Y218 (≠ S240), I234 (≠ N256), E235 (≠ Q257)
Query Sequence
>CCNA_03677 FitnessBrowser__Caulo:CCNA_03677
MADPSPTGPLQGLRVIEMGSLIAGPFCGQVLGDFGAEVIKLEDPKVGDPMRQWGRSKPKG
LSPWWPVIGRNKKSVTVDLRSEAGRDIARALIAKADVVVENFRPGTLEKWGMGYEALAKT
NPGLVMARVSGFGQTGPYASRAGYALVGEAMGGLRHITGEPDRPPARAGISIGDSLSGLN
AALGVMMALHARQRTGKGQVVDTAIYESVLTVMENLVTEYDLTGYVRERSGAVLPGIAPS
NVYPTRSGELVLIGANQDTLFRRLCELMGRPDLADDPRYRDHAARGAHQAELDARIAAWT
ADQDIEDLLPKLEGAGLATGRIYRAPDMLTDPQYAARESIVTVPHPVFGEIKMQNAFPRL
TETPGGVRWPGPTLGEHTDAVLADVAGMSAEAIEGLRKAGVLG
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