SitesBLAST
Comparing WP_012385491.1 NCBI__GCF_000019845.1:WP_012385491.1 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)
9br7C Succinate--hydroxymethylglutarate CoA-transferase (see paper)
32% identity, 95% coverage: 7:382/394 of query aligns to 4:380/403 of 9br7C
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
29% identity, 98% coverage: 7:394/394 of query aligns to 2:423/427 of 2vjoA
- active site: A16 (≠ I21), E139 (≠ D144), D168 (= D172), G259 (≠ T234), G260 (vs. gap)
- binding coenzyme a: H14 (= H19), A16 (≠ I21), A17 (= A22), R37 (= R42), L71 (≠ V76), M73 (≠ L78), N95 (= N100), F96 (≠ L101), G97 (≠ A102), R103 (= R108), M104 (≠ L109), K136 (= K141), V137 (≠ A142), Y138 (= Y143), D168 (= D172), M199 (= M203)
- binding oxalate ion: G257 (≠ H232), G259 (≠ T234), Q261 (vs. gap)
1p5rA Formyl-coa transferase in complex with coenzyme a (see paper)
29% identity, 98% coverage: 7:394/394 of query aligns to 2:423/427 of 1p5rA
- active site: Q16 (≠ I21), E139 (≠ D144), D168 (= D172), G259 (≠ T234), G260 (vs. gap)
- binding coenzyme a: H14 (= H19), V15 (≠ A20), Q16 (≠ I21), A17 (= A22), R37 (= R42), M73 (≠ L78), K74 (= K79), N95 (= N100), F96 (≠ L101), A100 (= A105), R103 (= R108), K136 (= K141), V137 (≠ A142), D168 (= D172), M199 (= 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, 98% coverage: 7:394/394 of query aligns to 3:424/428 of O06644
- Q17 (≠ I21) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (= R42) binding CoA
- W48 (≠ Y52) 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 (= R108) binding CoA
- 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 (≠ A233) mutation to A: 2.5-fold decrease of the catalytic effiency.
- G260 (≠ T234) mutation to A: 25-fold decrease of the catalytic effiency. Reduction of the affinity binding for both formyl-CoA and oxalate.
2vjkA Formyl-coa transferase with aspartyl-coa thioester intermediate derived from oxalyl-coa (see paper)
29% identity, 98% coverage: 7:394/394 of query aligns to 2:423/427 of 2vjkA
- active site: Q16 (≠ I21), E139 (≠ D144), D168 (= D172), G259 (≠ T234), G260 (vs. gap)
- binding coenzyme a: H14 (= H19), Q16 (≠ I21), A17 (= A22), R37 (= R42), M73 (≠ L78), K74 (= K79), N95 (= N100), F96 (≠ L101), G97 (≠ A102), R103 (= R108), M104 (≠ L109), K136 (= K141), V137 (≠ A142), Y138 (= Y143), D168 (= D172), M199 (= M203)
- binding magnesium ion: D293 (≠ K265), D296 (≠ E268)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
29% identity, 98% coverage: 7:394/394 of query aligns to 2:423/427 of 1t4cA
- active site: Q16 (≠ I21), E139 (≠ D144), D168 (= D172), G259 (≠ T234), G260 (vs. gap)
- binding coenzyme a: H14 (= H19), V15 (≠ A20), Q16 (≠ I21), R37 (= R42), M73 (≠ L78), N95 (= N100), F96 (≠ L101), R103 (= R108), M104 (≠ L109), V137 (≠ A142), Y138 (= Y143), D168 (= D172), M199 (= M203)
- binding oxalic acid: G259 (≠ T234), G260 (vs. gap)
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
29% identity, 98% coverage: 7:394/394 of query aligns to 2:423/427 of 1t3zA
- active site: Q16 (≠ I21), E139 (≠ D144), S168 (≠ D172), G259 (≠ T234), G260 (vs. gap)
- binding oxidized coenzyme a: H14 (= H19), V15 (≠ A20), A17 (= A22), R37 (= R42), K74 (= K79), N95 (= N100), F96 (≠ L101), A100 (= A105), R103 (= R108), M104 (≠ L109), K136 (= K141), V137 (≠ A142), Y138 (= Y143), E139 (≠ D144), M199 (= M203)
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)
31% identity, 96% coverage: 8:385/394 of query aligns to 4:403/416 of P69902
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
31% identity, 96% coverage: 8:385/394 of query aligns to 3:402/415 of 1pt5A
- active site: Q16 (≠ I21), E139 (≠ D144), D168 (= D172), G247 (≠ T234), G248 (vs. gap)
- binding acetyl coenzyme *a: V15 (≠ A20), S17 (≠ A22), R37 (= R42), L71 (≠ V76), N72 (≠ D77), T73 (≠ L78), K74 (= K79), N95 (= N100), F96 (≠ L101), H97 (≠ A102), K124 (≠ S129), K136 (= K141), A137 (= A142), Y138 (= Y143), E139 (≠ D144), D168 (= D172), M199 (= M203)
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
31% identity, 96% coverage: 8:385/394 of query aligns to 4:403/417 of 1q6yA
- active site: Q17 (≠ I21), E140 (≠ D144), D169 (= D172), G248 (≠ T234), G249 (vs. gap)
- binding coenzyme a: V16 (≠ A20), Q17 (≠ I21), S18 (≠ A22), R38 (= R42), L72 (≠ V76), N73 (≠ D77), T74 (≠ L78), K75 (= K79), N96 (= N100), F97 (≠ L101), H98 (≠ A102), M105 (≠ L109), I124 (= I128), K137 (= K141), A138 (= A142), Y139 (= Y143), D169 (= D172), M200 (= M203)
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
28% identity, 96% coverage: 7:386/394 of query aligns to 3:416/430 of 3ubmB
- active site: Q17 (≠ I21), E140 (≠ D144), D182 (= D172), G261 (≠ T234), G262 (vs. gap)
- binding coenzyme a: V16 (≠ A20), R38 (= R42), L72 (≠ V76), N73 (≠ D77), T74 (≠ L78), K75 (= K79), N96 (= N100), F97 (≠ L101), R98 (≠ A102), A101 (= A105), R104 (= R108), K125 (≠ S129), D182 (= D172), M213 (= M203)
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
30% identity, 96% coverage: 8:385/394 of query aligns to 4:396/410 of 1q7eA
- active site: Q17 (≠ I21), E133 (≠ D144), D162 (= D172), G241 (≠ T234), G242 (vs. gap)
- binding methionine: N96 (= N100), F97 (≠ L101), H98 (≠ A102), P99 (= P103), K118 (≠ S129), K130 (= K141), A131 (= A142), W246 (vs. gap), F299 (≠ D289), A303 (≠ S293), E306 (≠ V296)
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
31% identity, 95% coverage: 7:379/394 of query aligns to 4:360/360 of 5yx6A
Q9UHK6 Alpha-methylacyl-CoA racemase; 2-methylacyl-CoA racemase; EC 5.1.99.4 from Homo sapiens (Human) (see 5 papers)
30% identity, 96% coverage: 9:385/394 of query aligns to 3:360/382 of Q9UHK6
- V9 (= V15) to M: in dbSNP:rs3195676
- S52 (= S73) to P: in AMACRD and CBAS4; inactive enzyme; dbSNP:rs121917814
- L107 (≠ I128) to P: in CBAS4; inactive enzyme; dbSNP:rs121917816
- G175 (= G194) to D: in dbSNP:rs10941112
- L201 (≠ F219) to S: in dbSNP:rs2287939
- M261 (≠ N281) to T: in dbSNP:rs3195678
- E277 (≠ S301) to K: in dbSNP:rs2278008
Sites not aligning to the query:
- 380:382 Microbody targeting signal
O06543 Alpha-methylacyl-CoA racemase; AMACR; MtMCR; EC 5.1.99.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
27% identity, 87% coverage: 8:351/394 of query aligns to 4:331/360 of O06543
- R38 (= R42) binding substrate
- R52 (= R69) mutation to A: 15.7% of wild-type activity.
- I56 (≠ S73) mutation to P: 28.8% of wild-type activity.
- ADLK 59:62 (≠ VDLK 76:79) binding substrate
- E82 (≠ Q99) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NLA 100:102) binding substrate
- R91 (= R108) binding substrate; mutation to A: 19.9% of wild-type activity.
- M111 (≠ I128) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ AYDLLI 142:147) binding substrate
- H126 (≠ Y143) 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 (≠ N255) mutation to A: 2.1% of wild-type activity.
- C297 (≠ A317) mutation to A: 6.2% of wild-type activity.
- H312 (≠ Q332) mutation to 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)
26% identity, 87% coverage: 8:351/394 of query aligns to 3:325/354 of 2gd6A
- active site: G16 (≠ I21), D121 (= D144), D150 (= D172), G213 (= G221), G214 (≠ A222)
- binding acetyl coenzyme *a: I15 (≠ A20), R37 (= R42), A53 (≠ V76), D54 (= D77), L55 (= L78), K56 (= K79), G77 (≠ N100), Y78 (≠ L101), R79 (≠ A102), V82 (≠ A105), R85 (= R108), G119 (≠ A142), H120 (≠ Y143), Y124 (≠ I147), 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)
26% identity, 87% coverage: 8:351/394 of query aligns to 3:325/354 of 2gd2A
- active site: G16 (≠ I21), D121 (= D144), D150 (= D172), G213 (= G221), G214 (≠ A222)
- binding acetoacetyl-coenzyme a: I15 (≠ A20), R37 (= R42), A53 (≠ V76), L55 (= L78), K56 (= K79), G77 (≠ N100), Y78 (≠ L101), R79 (≠ A102), V82 (≠ A105), R85 (= R108), L86 (= L109), A118 (≠ K141), G119 (≠ A142), H120 (≠ Y143), Y124 (≠ I147), D150 (= D172)
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)
26% identity, 87% coverage: 8:351/394 of query aligns to 3:325/354 of 2gd0A
- active site: G16 (≠ I21), D121 (= D144), D150 (= D172), G213 (= G221), G214 (≠ A222)
- binding (s)-2-methylmyristoyl-coenzyme a: D42 (= D47), L55 (= L78), K56 (= K79), G77 (≠ N100), Y78 (≠ L101), R79 (≠ A102), V82 (≠ A105), R85 (= R108), L86 (= L109), G119 (≠ A142), H120 (≠ Y143), D121 (= D144), Y124 (≠ I147), D150 (= D172)
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)
26% identity, 87% coverage: 8:351/394 of query aligns to 3:325/354 of 2gciA
- active site: G16 (≠ I21), D121 (= D144), D150 (= D172), G213 (= G221), G214 (≠ A222)
- binding (r)-2-methylmyristoyl-coenzyme a: R37 (= R42), L55 (= L78), K56 (= K79), G77 (≠ N100), Y78 (≠ L101), R79 (≠ A102), V82 (≠ A105), G119 (≠ A142), H120 (≠ Y143), D121 (= D144), Y124 (≠ I147), D150 (= D172), Y218 (= Y238), I234 (≠ Q254), E235 (≠ N255)
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)
26% identity, 87% coverage: 8:351/394 of query aligns to 3:325/354 of 2gceA
- active site: G16 (≠ I21), D121 (= D144), D150 (= D172), G213 (= G221), G214 (≠ A222)
- binding (r)-ibuprofenoyl-coenzyme a: I15 (≠ A20), R37 (= R42), L55 (= L78), K56 (= K79), G77 (≠ N100), Y78 (≠ L101), R79 (≠ A102), V82 (≠ A105), R85 (= R108), G119 (≠ A142), H120 (≠ Y143), D121 (= D144), Y124 (≠ I147), D150 (= D172), L211 (≠ F219), Y218 (= Y238), I234 (≠ Q254)
- binding (s)-ibuprofenoyl-coenzyme a: I15 (≠ A20), G16 (≠ I21), P17 (≠ A22), R37 (= R42), L55 (= L78), K56 (= K79), G77 (≠ N100), Y78 (≠ L101), R79 (≠ A102), V82 (≠ A105), R85 (= R108), G119 (≠ A142), H120 (≠ Y143), Y124 (≠ I147), D150 (= D172)
Query Sequence
>WP_012385491.1 NCBI__GCF_000019845.1:WP_012385491.1
MATVRPRPLDGITVVTLEHAIAAPFATRQLADLGARVIKVERPDGGDFARGYDKRVRGKL
ASHFAWCNRSKESVAVDLKTPQGLEVLHALVERADVLVQNLAPGAALRLGLDPDKLRAAN
PRLILCDISGFGPGGPYSIRKAYDLLIQAEAGLLSITGTSDTMAKVGISIADIATGMYAF
TSILASLHLRDRTGQGGHIEVSMLEALGEWMGYPLYYTFDGAEPPPRTGASHATIYPYGP
FPTGDGGTVLFGLQNEREWAAFVAKVLEQPDLVTDPRFASNGDRSANRDALCSIIVSTFA
SMSREEVMRRLEQADIANASVNEMTSVWTHPQLKVRQRWQDVGSEVGPIPALLPPTGSDA
FDPRMDPVPALGEHTDAILEELGLSASGKTRLYA
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