SitesBLAST
Comparing WP_008498764.1 NCBI__GCF_000342445.1:WP_008498764.1 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)
Q9UHK6 Alpha-methylacyl-CoA racemase; 2-methylacyl-CoA racemase; EC 5.1.99.4 from Homo sapiens (Human) (see 5 papers)
34% identity, 97% coverage: 4:311/318 of query aligns to 2:308/382 of Q9UHK6
- V9 (≠ L11) to M: in dbSNP:rs3195676
- S52 (≠ I62) to P: in AMACRD and CBAS4; inactive enzyme; dbSNP:rs121917814
- L107 (= L117) to P: in CBAS4; inactive enzyme; dbSNP:rs121917816
- G175 (= G184) to D: in dbSNP:rs10941112
- L201 (≠ Y207) to S: in dbSNP:rs2287939
- M261 (≠ L268) to T: in dbSNP:rs3195678
- E277 (≠ S282) 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)
32% identity, 99% coverage: 1:315/318 of query aligns to 1:314/360 of O06543
- R38 (≠ P38) binding substrate
- R52 (= R58) mutation to A: 15.7% of wild-type activity.
- I56 (= I62) mutation to P: 28.8% of wild-type activity.
- ADLK 59:62 (≠ IDLK 65:68) binding substrate
- E82 (= E88) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ TFR 89:91) binding substrate
- R91 (≠ K97) binding substrate; mutation to A: 19.9% of wild-type activity.
- M111 (≠ L117) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ SHDLNY 131:136) binding substrate
- H126 (= H132) mutation to A: 4.5% of wild-type activity.
- D156 (= D162) mutation to A: 17.6 of wild-type activity.
- D190 (≠ E195) mutation to A: 3.3% of wild-type activity.
- E241 (= E244) mutation to A: 2.1% of wild-type activity.
- C297 (= C298) mutation to A: 6.2% of wild-type activity.
- H312 (≠ F313) mutation to A: 10.1% of wild-type activity.
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, 98% coverage: 5:315/318 of query aligns to 4:309/355 of 2yimA
- active site: G16 (≠ L17), D122 (= D133), D151 (= D162), G214 (= G222), G215 (≠ T223)
- binding 2-methylacetoacetyl coa: I15 (≠ Y16), R37 (≠ P38), A54 (≠ I65), L56 (= L67), K57 (= K68), G78 (≠ T89), Y79 (≠ F90), R80 (= R91), V83 (= V94), R86 (≠ K97), L87 (= L98), A119 (≠ G130), G120 (≠ S131), H121 (= H132), Y125 (= Y136), D151 (= D162)
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, 98% coverage: 5:315/318 of query aligns to 4:308/354 of 2gd6A
- active site: G16 (≠ L17), D121 (= D133), D150 (= D162), G213 (= G222), G214 (≠ T223)
- binding acetyl coenzyme *a: I15 (≠ Y16), R37 (≠ P38), A53 (≠ I65), D54 (= D66), L55 (= L67), K56 (= K68), G77 (≠ T89), Y78 (≠ F90), R79 (= R91), V82 (= V94), R85 (≠ K97), G119 (≠ S131), H120 (= H132), Y124 (= Y136), D150 (= D162), M182 (≠ L193)
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, 98% coverage: 5:315/318 of query aligns to 4:308/354 of 2gd2A
- active site: G16 (≠ L17), D121 (= D133), D150 (= D162), G213 (= G222), G214 (≠ T223)
- binding acetoacetyl-coenzyme a: I15 (≠ Y16), R37 (≠ P38), A53 (≠ I65), L55 (= L67), K56 (= K68), G77 (≠ T89), Y78 (≠ F90), R79 (= R91), V82 (= V94), R85 (≠ K97), L86 (= L98), A118 (≠ G130), G119 (≠ S131), H120 (= H132), Y124 (= Y136), D150 (= D162)
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, 98% coverage: 5:315/318 of query aligns to 4:308/354 of 2gd0A
- active site: G16 (≠ L17), D121 (= D133), D150 (= D162), G213 (= G222), G214 (≠ T223)
- binding (s)-2-methylmyristoyl-coenzyme a: D42 (≠ Q54), L55 (= L67), K56 (= K68), G77 (≠ T89), Y78 (≠ F90), R79 (= R91), V82 (= V94), R85 (≠ K97), L86 (= L98), G119 (≠ S131), H120 (= H132), D121 (= D133), Y124 (= Y136), D150 (= D162)
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, 98% coverage: 5:315/318 of query aligns to 4:308/354 of 2gciA
- active site: G16 (≠ L17), D121 (= D133), D150 (= D162), G213 (= G222), G214 (≠ T223)
- binding (r)-2-methylmyristoyl-coenzyme a: R37 (≠ P38), L55 (= L67), K56 (= K68), G77 (≠ T89), Y78 (≠ F90), R79 (= R91), V82 (= V94), G119 (≠ S131), H120 (= H132), D121 (= D133), Y124 (= Y136), D150 (= D162), Y218 (= Y227), I234 (≠ L243), E235 (= E244)
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, 98% coverage: 5:315/318 of query aligns to 4:308/354 of 2gceA
- active site: G16 (≠ L17), D121 (= D133), D150 (= D162), G213 (= G222), G214 (≠ T223)
- binding (r)-ibuprofenoyl-coenzyme a: I15 (≠ Y16), R37 (≠ P38), L55 (= L67), K56 (= K68), G77 (≠ T89), Y78 (≠ F90), R79 (= R91), V82 (= V94), R85 (≠ K97), G119 (≠ S131), H120 (= H132), D121 (= D133), Y124 (= Y136), D150 (= D162), L211 (≠ I220), Y218 (= Y227), I234 (≠ L243)
- binding (s)-ibuprofenoyl-coenzyme a: I15 (≠ Y16), G16 (≠ L17), P17 (= P18), R37 (≠ P38), L55 (= L67), K56 (= K68), G77 (≠ T89), Y78 (≠ F90), R79 (= R91), V82 (= V94), R85 (≠ K97), G119 (≠ S131), H120 (= H132), Y124 (= Y136), D150 (= D162)
9br7C Succinate--hydroxymethylglutarate CoA-transferase (see paper)
33% identity, 81% coverage: 5:262/318 of query aligns to 6:270/403 of 9br7C
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
34% identity, 93% coverage: 5:300/318 of query aligns to 6:305/360 of 5yx6A
A6W2K8 CoA-transferase/lyase DddD; EC 2.-.-.- from Marinomonas sp. (strain MWYL1) (see paper)
33% identity, 62% coverage: 5:201/318 of query aligns to 9:206/837 of A6W2K8
Sites not aligning to the query:
- 602 D→A: Abolishes ability to produce dimethyl sulfide (DMS).
Q5U921 (R)-2-hydroxy-4-methylpentanoate CoA-transferase; 2-hydroxyisocaproate-CoA transferase; EC 2.8.3.24 from Clostridioides difficile (Peptoclostridium difficile) (see paper)
29% identity, 81% coverage: 5:262/318 of query aligns to 3:271/399 of Q5U921
- D171 (= D162) mutation D->A,N: Loss of activity.
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)
25% identity, 97% coverage: 1:307/318 of query aligns to 1:343/416 of P69902
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
24% identity, 97% coverage: 1:307/318 of query aligns to 1:343/417 of 1q6yA
- active site: Q17 (≠ L17), E140 (≠ D133), D169 (= D162), G248 (≠ S226), G249 (≠ Y227)
- binding coenzyme a: V16 (≠ Y16), Q17 (≠ L17), S18 (≠ P18), R38 (≠ P38), L72 (≠ I65), N73 (≠ D66), T74 (≠ L67), K75 (= K68), N96 (≠ T89), F97 (= F90), H98 (≠ R91), M105 (≠ L98), I124 (≠ L117), K137 (≠ G130), A138 (≠ S131), Y139 (≠ H132), D169 (= D162), M200 (≠ L193)
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
25% identity, 95% coverage: 5:307/318 of query aligns to 4:342/415 of 1pt5A