SitesBLAST
Comparing CCNA_02410 FitnessBrowser__Caulo:CCNA_02410 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)
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
29% identity, 99% coverage: 2:395/396 of query aligns to 5:415/417 of 1q6yA
- active site: Q17 (≠ I14), E140 (≠ W143), D169 (= D168), G248 (≠ T239), G249 (≠ S240)
- binding coenzyme a: V16 (≠ Y13), Q17 (≠ I14), S18 (≠ A15), R38 (≠ S35), L72 (= L70), N73 (≠ D71), T74 (≠ I72), K75 (≠ R73), N96 (= N94), F97 (≠ V95), H98 (≠ R96), M105 (≠ A103), I124 (≠ L122), K137 (≠ A140), A138 (= A141), Y139 (≠ F142), D169 (= D168), M200 (≠ L199)
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
28% identity, 99% coverage: 2:395/396 of query aligns to 4:414/415 of 1pt5A
- active site: Q16 (≠ I14), E139 (≠ W143), D168 (= D168), G247 (vs. gap), G248 (vs. gap)
- binding acetyl coenzyme *a: V15 (≠ Y13), S17 (≠ A15), R37 (≠ S35), L71 (= L70), N72 (≠ D71), T73 (≠ I72), K74 (≠ R73), N95 (= N94), F96 (≠ V95), H97 (≠ R96), K124 (≠ S123), K136 (≠ A140), A137 (= A141), Y138 (≠ F142), E139 (≠ W143), D168 (= D168), M199 (≠ L199)
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: 2:395/396 of query aligns to 5:415/416 of P69902
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
28% identity, 98% coverage: 2:390/396 of query aligns to 5:422/430 of 3ubmB
- active site: Q17 (≠ I14), E140 (≠ D138), D182 (= D168), G261 (≠ L233), G262 (vs. gap)
- binding coenzyme a: V16 (≠ Y13), R38 (≠ S35), L72 (= L70), N73 (≠ D71), T74 (≠ I72), K75 (≠ R73), N96 (= N94), F97 (≠ V95), R98 (= R96), A101 (= A99), R104 (= R102), K125 (≠ S123), D182 (= D168), M213 (≠ L199)
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
27% identity, 99% coverage: 2:395/396 of query aligns to 5:408/410 of 1q7eA
- active site: Q17 (≠ I14), E133 (≠ W143), D162 (= D168), G241 (vs. gap), G242 (vs. gap)
- binding methionine: N96 (= N94), F97 (≠ V95), H98 (≠ R96), P99 (≠ S97), K118 (≠ S123), K130 (≠ A140), A131 (= A141), W246 (vs. gap), F299 (≠ V288), A303 (≠ D292), E306 (≠ F295)
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
29% identity, 75% coverage: 2:299/396 of query aligns to 6:287/360 of 5yx6A
1p5rA Formyl-coa transferase in complex with coenzyme a (see paper)
27% identity, 98% coverage: 2:390/396 of query aligns to 4:421/427 of 1p5rA
- active site: Q16 (≠ I14), E139 (≠ D138), D168 (= D168), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ T12), V15 (≠ Y13), Q16 (≠ I14), A17 (= A15), R37 (≠ S35), M73 (≠ I72), K74 (≠ R73), N95 (= N94), F96 (≠ V95), A100 (= A99), R103 (= R102), K136 (≠ P135), V137 (≠ G136), D168 (= D168), M199 (≠ L199)
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: 2:390/396 of query aligns to 5:422/428 of O06644
- Q17 (≠ I14) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (≠ S35) binding
- W48 (≠ S50) 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 (= R102) binding
- D169 (= D168) 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: 2:390/396 of query aligns to 4:421/427 of 2vjoA
- active site: A16 (≠ I14), E139 (≠ D138), D168 (= D168), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ T12), A16 (≠ I14), A17 (= A15), R37 (≠ S35), L71 (= L70), M73 (≠ I72), N95 (= N94), F96 (≠ V95), G97 (≠ R96), R103 (= R102), M104 (≠ A103), K136 (≠ P135), V137 (≠ G136), Y138 (≠ M137), D168 (= D168), M199 (≠ L199)
- binding oxalate ion: G257 (≠ D255), 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: 2:390/396 of query aligns to 4:421/427 of 2vjkA
- active site: Q16 (≠ I14), E139 (≠ D138), D168 (= D168), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ T12), Q16 (≠ I14), A17 (= A15), R37 (≠ S35), M73 (≠ I72), K74 (≠ R73), N95 (= N94), F96 (≠ V95), G97 (≠ R96), R103 (= R102), M104 (≠ A103), K136 (≠ P135), V137 (≠ G136), Y138 (≠ M137), D168 (= D168), M199 (≠ L199)
- binding magnesium ion: D293 (≠ A261), D296 (≠ G264)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
27% identity, 98% coverage: 2:390/396 of query aligns to 4:421/427 of 1t4cA
- active site: Q16 (≠ I14), E139 (≠ D138), D168 (= D168), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ T12), V15 (≠ Y13), Q16 (≠ I14), R37 (≠ S35), M73 (≠ I72), N95 (= N94), F96 (≠ V95), R103 (= R102), M104 (≠ A103), V137 (≠ G136), Y138 (≠ M137), D168 (= D168), M199 (≠ L199)
- binding oxalic acid: G259 (vs. gap), G260 (vs. gap)
Q9UHK6 Alpha-methylacyl-CoA racemase; 2-methylacyl-CoA racemase; EC 5.1.99.4 from Homo sapiens (Human) (see 5 papers)
24% identity, 98% coverage: 2:391/396 of query aligns to 3:368/382 of Q9UHK6
- V9 (= V8) to M: in dbSNP:rs3195676
- S52 (≠ A67) to P: in AMACRD and CBAS4; inactive enzyme; dbSNP:rs121917814
- L107 (= L122) to P: in CBAS4; inactive enzyme; dbSNP:rs121917816
- G175 (= G190) to D: in dbSNP:rs10941112
- L201 (≠ F217) to S: in dbSNP:rs2287939
- M261 (≠ V254) to T: in dbSNP:rs3195678
- E277 (≠ S297) to K: in dbSNP:rs2278008
Sites not aligning to the query:
- 380:382 Microbody targeting signal
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
26% identity, 98% coverage: 2:390/396 of query aligns to 4:421/427 of 1t3zA
- active site: Q16 (≠ I14), E139 (≠ D138), S168 (≠ D168), G259 (vs. gap), G260 (vs. gap)
- binding oxidized coenzyme a: H14 (≠ T12), V15 (≠ Y13), A17 (= A15), R37 (≠ S35), K74 (≠ R73), N95 (= N94), F96 (≠ V95), A100 (= A99), R103 (= R102), M104 (≠ A103), K136 (≠ P135), V137 (≠ G136), Y138 (≠ M137), E139 (≠ D138), M199 (≠ L199)
O06543 Alpha-methylacyl-CoA racemase; AMACR; MtMCR; EC 5.1.99.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
28% identity, 95% coverage: 2:379/396 of query aligns to 5:357/360 of O06543
- R38 (≠ S35) binding
- R52 (= R63) mutation to A: 15.7% of wild-type activity.
- I56 (≠ A67) mutation to P: 28.8% of wild-type activity.
- ADLK 59:62 (≠ LDIR 70:73) binding
- E82 (≠ T93) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NVR 94:96) binding
- R91 (= R102) binding ; mutation to A: 19.9% of wild-type activity.
- M111 (≠ L122) mutation to P: 5.2% of wild-type activity.
- GHDI-NY 125:130 (≠ GMDVAAF 136:142) binding
- H126 (≠ M137) mutation to A: 4.5% of wild-type activity.
- D156 (= D168) mutation to A: 17.6 of wild-type activity.
- D190 (≠ R201) mutation to A: 3.3% of wild-type activity.
- E241 (≠ D255) mutation to A: 2.1% of wild-type activity.
- C297 (≠ T313) mutation to A: 6.2% of wild-type activity.
- H312 (≠ Q328) mutation to A: 10.1% of wild-type activity.
8apqB Camct - mesaconyl-coa c1:c4 coa transferase of chloroflexus aurantiacus (see paper)
29% identity, 98% coverage: 1:390/396 of query aligns to 4:396/406 of 8apqB
- binding coenzyme a: F16 (≠ Y13), V17 (≠ I14), A18 (= A15), P38 (≠ T47), I74 (= I72), N100 (= N94), F101 (≠ V95), L124 (= L122), V125 (≠ S123), G126 (= G124), D165 (= D168)
- binding (2e)-2-methylbut-2-enedioic acid: V17 (≠ I14), R47 (vs. gap), D165 (= D168)
- binding Mesaconyl Coenzme A: T249 (≠ Q251), L251 (≠ V254)
8apqA Camct - mesaconyl-coa c1:c4 coa transferase of chloroflexus aurantiacus (see paper)
29% identity, 98% coverage: 1:390/396 of query aligns to 4:396/406 of 8apqA
- binding Mesaconyl Coenzme A: G13 (≠ L10), F16 (≠ Y13), V17 (≠ I14), P38 (≠ T47), R47 (vs. gap), I74 (= I72), R75 (= R73), N100 (= N94), F101 (≠ V95), P102 (≠ R96), L107 (= L105), L124 (= L122), V125 (≠ S123), G126 (= G124), S132 (≠ P130), E133 (≠ D131), V134 (≠ A132), D135 (= D133), Y136 (≠ K134), D165 (= D168)
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, 95% coverage: 2:379/396 of query aligns to 4:352/355 of 2yimA
- active site: G16 (≠ I14), D122 (= D138), D151 (= D168), G214 (≠ A229), G215 (≠ V230)
- binding 2-methylacetoacetyl coa: I15 (≠ Y13), R37 (≠ S35), A54 (≠ L70), L56 (≠ I72), K57 (≠ R73), G78 (≠ N94), Y79 (≠ V95), R80 (= R96), V83 (≠ A99), R86 (= R102), L87 (≠ A103), A119 (≠ P135), G120 (= G136), H121 (≠ M137), Y125 (≠ F142), D151 (= D168)
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, 95% coverage: 2:379/396 of query aligns to 4:351/354 of 2gd6A
- active site: G16 (≠ I14), D121 (= D138), D150 (= D168), G213 (≠ A229), G214 (≠ V230)
- binding acetyl coenzyme *a: I15 (≠ Y13), R37 (≠ S35), A53 (≠ L70), D54 (= D71), L55 (≠ I72), K56 (≠ R73), G77 (≠ N94), Y78 (≠ V95), R79 (= R96), V82 (≠ A99), R85 (= R102), G119 (= G136), H120 (≠ M137), Y124 (≠ F142), D150 (= D168), M182 (≠ L199)
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, 95% coverage: 2:379/396 of query aligns to 4:351/354 of 2gd2A
- active site: G16 (≠ I14), D121 (= D138), D150 (= D168), G213 (≠ A229), G214 (≠ V230)
- binding acetoacetyl-coenzyme a: I15 (≠ Y13), R37 (≠ S35), A53 (≠ L70), L55 (≠ I72), K56 (≠ R73), G77 (≠ N94), Y78 (≠ V95), R79 (= R96), V82 (≠ A99), R85 (= R102), L86 (≠ A103), A118 (≠ P135), G119 (= G136), H120 (≠ M137), Y124 (≠ F142), D150 (= D168)
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)
28% identity, 95% coverage: 2:379/396 of query aligns to 4:351/354 of 2gd0A
- active site: G16 (≠ I14), D121 (= D138), D150 (= D168), G213 (≠ A229), G214 (≠ V230)
- binding (s)-2-methylmyristoyl-coenzyme a: D42 (= D51), L55 (≠ I72), K56 (≠ R73), G77 (≠ N94), Y78 (≠ V95), R79 (= R96), V82 (≠ A99), R85 (= R102), L86 (≠ A103), G119 (= G136), H120 (≠ M137), D121 (= D138), Y124 (≠ F142), D150 (= D168)
Query Sequence
>CCNA_02410 FitnessBrowser__Caulo:CCNA_02410
MLEGLRVVELATYIAAPGAAGVMADWGADVIKVESPEGDPMRRFFDTIGSDQDANPVFEL
DNRGKRAVVLDIRSDLGREALKALVATADIFLTNVRSAALARAGLDYEALKAVNPRLIYC
SLSGYGLTGPDADKPGMDVAAFWSRAGVGAITAPKGTEPFPIRTGMGDHVTSLATVSAIL
AAVHERTRTGVGRLVETSLLRTGVYAIGSDMAIQLRFGKLASTRGRREAVQPLANFYKTS
DGRWICLLPRQGSVDWPQIAAAAGRPELVDDPRFATAKARREHGQALVDIFDEAFGSMTY
DAAAAALDAGDITWAPYQTPRELALDAQAEAAGCFVDTPDGAGGTFKAPAAPARFPGAPN
GPRGPAPKLGADTAAVFRELGFSEDQVAALTRVSAA
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