SitesBLAST
Comparing CA265_RS08550 FitnessBrowser__Pedo557:CA265_RS08550 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)
34% identity, 54% coverage: 2:209/383 of query aligns to 2:220/430 of 3ubmB
- active site: Q17 (≠ L17), E140 (≠ D142), D182 (= D171)
- binding coenzyme a: V16 (≠ F16), R38 (= R38), L72 (≠ A74), N73 (≠ D75), T74 (≠ L76), K75 (= K77), N96 (= N98), F97 (= F99), R98 (= R100), A101 (≠ V103), R104 (≠ K106), K125 (≠ T127), D182 (= D171), M213 (≠ L202)
Sites not aligning to the query:
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
28% identity, 96% coverage: 3:370/383 of query aligns to 4:353/360 of 5yx6A
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
28% identity, 100% coverage: 1:383/383 of query aligns to 1:415/428 of O06644
- Q17 (≠ L17) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (= R38) 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 (≠ K106) binding
- D169 (= D171) 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)
28% identity, 99% coverage: 3:383/383 of query aligns to 2:414/427 of 1p5rA
- active site: Q16 (≠ L17), E139 (≠ D142), D168 (= D171), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ Q15), V15 (≠ F16), Q16 (≠ L17), A17 (= A18), R37 (= R38), M73 (≠ L76), K74 (= K77), N95 (= N98), F96 (= F99), A100 (≠ V103), R103 (≠ K106), K136 (≠ P139), V137 (≠ G140), D168 (= D171), M199 (≠ L202)
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
28% identity, 99% coverage: 3:383/383 of query aligns to 2:414/427 of 2vjoA
- active site: A16 (≠ L17), E139 (≠ D142), D168 (= D171), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ Q15), A16 (≠ L17), A17 (= A18), R37 (= R38), L71 (≠ A74), M73 (≠ L76), N95 (= N98), F96 (= F99), G97 (≠ R100), R103 (≠ K106), M104 (≠ I107), K136 (≠ P139), V137 (≠ G140), Y138 (≠ Q141), D168 (= D171), M199 (≠ L202)
- 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)
28% identity, 99% coverage: 3:383/383 of query aligns to 2:414/427 of 2vjkA
- active site: Q16 (≠ L17), E139 (≠ D142), D168 (= D171), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ Q15), Q16 (≠ L17), A17 (= A18), R37 (= R38), M73 (≠ L76), K74 (= K77), N95 (= N98), F96 (= F99), G97 (≠ R100), R103 (≠ K106), M104 (≠ I107), K136 (≠ P139), V137 (≠ G140), Y138 (≠ Q141), D168 (= D171), M199 (≠ L202)
- binding magnesium ion: D293 (≠ A264), D296 (≠ N267)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
28% identity, 99% coverage: 3:383/383 of query aligns to 2:414/427 of 1t4cA
- active site: Q16 (≠ L17), E139 (≠ D142), D168 (= D171), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ Q15), V15 (≠ F16), Q16 (≠ L17), R37 (= R38), M73 (≠ L76), N95 (= N98), F96 (= F99), R103 (≠ K106), M104 (≠ I107), V137 (≠ G140), Y138 (≠ Q141), D168 (= D171), M199 (≠ L202)
- binding oxalic acid: G259 (vs. gap), G260 (vs. gap)
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
28% identity, 99% coverage: 3:383/383 of query aligns to 2:414/427 of 1t3zA
- active site: Q16 (≠ L17), E139 (≠ D142), S168 (≠ D171), G259 (vs. gap), G260 (vs. gap)
- binding oxidized coenzyme a: H14 (≠ Q15), V15 (≠ F16), A17 (= A18), R37 (= R38), K74 (= K77), N95 (= N98), F96 (= F99), A100 (≠ V103), R103 (≠ K106), M104 (≠ I107), K136 (≠ P139), V137 (≠ G140), Y138 (≠ Q141), E139 (≠ D142), M199 (≠ L202)
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)
34% identity, 55% coverage: 1:209/383 of query aligns to 1:207/416 of P69902
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
33% identity, 55% coverage: 1:209/383 of query aligns to 1:207/417 of 1q6yA
- active site: Q17 (≠ L17), E140 (≠ D142), D169 (= D171)
- binding coenzyme a: V16 (≠ F16), Q17 (≠ L17), S18 (≠ A18), R38 (= R38), L72 (≠ A74), N73 (≠ D75), T74 (≠ L76), K75 (= K77), N96 (= N98), F97 (= F99), H98 (≠ R100), M105 (≠ I107), I124 (≠ V126), K137 (≠ P139), A138 (≠ G140), Y139 (≠ Q141), D169 (= D171), M200 (≠ L202)
Sites not aligning to the query:
O06543 Alpha-methylacyl-CoA racemase; AMACR; MtMCR; EC 5.1.99.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
33% identity, 66% coverage: 1:254/383 of query aligns to 1:237/360 of O06543
- R38 (= R38) binding
- R52 (= R67) mutation to A: 15.7% of wild-type activity.
- I56 (≠ S71) mutation to P: 28.8% of wild-type activity.
- ADLK 59:62 (= ADLK 74:77) binding
- E82 (≠ H97) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NFR 98:100) binding
- R91 (≠ K106) binding ; mutation to A: 19.9% of wild-type activity.
- M111 (≠ V126) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ GQDLLV 140:145) binding
- H126 (≠ Q141) mutation to A: 4.5% of wild-type activity.
- D156 (= D171) mutation to A: 17.6 of wild-type activity.
- D190 (≠ E204) 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.
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
34% identity, 54% coverage: 4:209/383 of query aligns to 3:206/415 of 1pt5A
- active site: Q16 (≠ L17), E139 (≠ D142), D168 (= D171)
- binding acetyl coenzyme *a: V15 (≠ F16), S17 (≠ A18), R37 (= R38), L71 (≠ A74), N72 (≠ D75), T73 (≠ L76), K74 (= K77), N95 (= N98), F96 (= F99), H97 (≠ R100), K124 (≠ T127), K136 (≠ P139), A137 (≠ G140), Y138 (≠ Q141), E139 (≠ D142), D168 (= D171), M199 (≠ L202)
Sites not aligning to the query:
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, 66% coverage: 4:254/383 of query aligns to 3:232/355 of 2yimA
- active site: G16 (≠ L17), D122 (= D142), D151 (= D171), G214 (= G232), G215 (≠ S233)
- binding 2-methylacetoacetyl coa: I15 (≠ F16), R37 (= R38), A54 (= A74), L56 (= L76), K57 (= K77), G78 (≠ N98), Y79 (≠ F99), R80 (= R100), V83 (= V103), R86 (≠ K106), L87 (≠ I107), A119 (≠ P139), G120 (= G140), H121 (≠ Q141), Y125 (≠ V145), D151 (= D171)
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)
32% identity, 66% coverage: 4:254/383 of query aligns to 3:231/354 of 2gd6A
- active site: G16 (≠ L17), D121 (= D142), D150 (= D171), G213 (= G232), G214 (≠ S233)
- binding acetyl coenzyme *a: I15 (≠ F16), R37 (= R38), A53 (= A74), D54 (= D75), L55 (= L76), K56 (= K77), G77 (≠ N98), Y78 (≠ F99), R79 (= R100), V82 (= V103), R85 (≠ K106), G119 (= G140), H120 (≠ Q141), Y124 (≠ V145), D150 (= D171), M182 (≠ L202)
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)
32% identity, 66% coverage: 4:254/383 of query aligns to 3:231/354 of 2gd2A
- active site: G16 (≠ L17), D121 (= D142), D150 (= D171), G213 (= G232), G214 (≠ S233)
- binding acetoacetyl-coenzyme a: I15 (≠ F16), R37 (= R38), A53 (= A74), L55 (= L76), K56 (= K77), G77 (≠ N98), Y78 (≠ F99), R79 (= R100), V82 (= V103), R85 (≠ K106), L86 (≠ I107), A118 (≠ P139), G119 (= G140), H120 (≠ Q141), Y124 (≠ V145), D150 (= D171)
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)
32% identity, 66% coverage: 4:254/383 of query aligns to 3:231/354 of 2gd0A
- active site: G16 (≠ L17), D121 (= D142), D150 (= D171), G213 (= G232), G214 (≠ S233)
- binding (s)-2-methylmyristoyl-coenzyme a: D42 (= D58), L55 (= L76), K56 (= K77), G77 (≠ N98), Y78 (≠ F99), R79 (= R100), V82 (= V103), R85 (≠ K106), L86 (≠ I107), G119 (= G140), H120 (≠ Q141), D121 (= D142), Y124 (≠ V145), D150 (= D171)
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)
32% identity, 66% coverage: 4:254/383 of query aligns to 3:231/354 of 2gciA
- active site: G16 (≠ L17), D121 (= D142), D150 (= D171), G213 (= G232), G214 (≠ S233)
- binding (r)-2-methylmyristoyl-coenzyme a: R37 (= R38), L55 (= L76), K56 (= K77), G77 (≠ N98), Y78 (≠ F99), R79 (= R100), V82 (= V103), G119 (= G140), H120 (≠ Q141), D121 (= D142), Y124 (≠ V145), D150 (= D171), Y218 (= Y237)
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)
32% identity, 66% coverage: 4:254/383 of query aligns to 3:231/354 of 2gceA
- active site: G16 (≠ L17), D121 (= D142), D150 (= D171), G213 (= G232), G214 (≠ S233)
- binding (r)-ibuprofenoyl-coenzyme a: I15 (≠ F16), R37 (= R38), L55 (= L76), K56 (= K77), G77 (≠ N98), Y78 (≠ F99), R79 (= R100), V82 (= V103), R85 (≠ K106), G119 (= G140), H120 (≠ Q141), D121 (= D142), Y124 (≠ V145), D150 (= D171), L211 (vs. gap), Y218 (= Y237)
- binding (s)-ibuprofenoyl-coenzyme a: I15 (≠ F16), G16 (≠ L17), P17 (≠ A18), R37 (= R38), L55 (= L76), K56 (= K77), G77 (≠ N98), Y78 (≠ F99), R79 (= R100), V82 (= V103), R85 (≠ K106), G119 (= G140), H120 (≠ Q141), Y124 (≠ V145), D150 (= D171)
Sites not aligning to the query:
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: 5:380/383 of query aligns to 3:357/382 of Q9UHK6
- V9 (≠ L11) to M: in dbSNP:rs3195676
- S52 (= S71) to P: in AMACRD and CBAS4; inactive enzyme; dbSNP:rs121917814
- L107 (≠ V126) to P: in CBAS4; inactive enzyme; dbSNP:rs121917816
- G175 (≠ N193) to D: in dbSNP:rs10941112
- L201 (= L224) to S: in dbSNP:rs2287939
- M261 (≠ F281) to T: in dbSNP:rs3195678
- E277 (≠ K297) 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)
33% identity, 55% coverage: 1:209/383 of query aligns to 1:200/410 of 1q7eA
Sites not aligning to the query:
Query Sequence
>CA265_RS08550 FitnessBrowser__Pedo557:CA265_RS08550
MNRPLEGLLVLEFCQFLAGPSAGLKLADLGARVIKIERPKTGDACRQLSIKNLFVDEDSL
LFHTINRNKESYAADLKNPEDLEKLKKLISKADVMTHNFRPGVMEKIGLDYQTVQNINPK
IVYGVVTGYGNEGPWKNKPGQDLLVQSVSGLTFLSGVDVDGPVPFGLSVSDIMCGNHLVQ
GIMAALIKRAKTNKSVLVEVSLLESILDVQFEVLTTYLNDGGKLPDRSGAKGSAHAYLSA
PYGMYETADGYIAMAMGNLPNICAIINCDITDLYVEAGSAFENRDQLIVRLAATFKKENT
KTWVELLENHGIWCAEVLNYQKATALSTYKKLDIAQELNLDGGKTIKTTVSPIRLDREKL
FASKAAPKLGGNTSDINKEFELN
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