SitesBLAST
Comparing WP_068174644.1 NCBI__GCF_001592305.1:WP_068174644.1 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)
43% identity, 100% coverage: 1:421/421 of query aligns to 3:397/403 of 9br7C
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
31% identity, 98% coverage: 4:417/421 of query aligns to 4:411/415 of 1pt5A
- active site: Q16 (≠ L16), E139 (≠ D151), D168 (= D184), G247 (vs. gap), G248 (vs. gap)
- binding acetyl coenzyme *a: V15 (= V15), S17 (≠ A17), R37 (= R37), L71 (≠ C83), N72 (≠ D84), T73 (≠ I85), K74 (≠ A86), N95 (= N107), F96 (≠ Y108), H97 (≠ K109), K124 (≠ T136), K136 (≠ A148), A137 (≠ G149), Y138 (= Y150), E139 (≠ D151), D168 (= D184), M199 (≠ L215)
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
31% identity, 98% coverage: 4:417/421 of query aligns to 5:412/417 of 1q6yA
- active site: Q17 (≠ L16), E140 (≠ D151), D169 (= D184), G248 (vs. gap), G249 (vs. gap)
- binding coenzyme a: V16 (= V15), Q17 (≠ L16), S18 (≠ A17), R38 (= R37), L72 (≠ C83), N73 (≠ D84), T74 (≠ I85), K75 (≠ A86), N96 (= N107), F97 (≠ Y108), H98 (≠ K109), M105 (≠ Y116), I124 (= I135), K137 (≠ A148), A138 (≠ G149), Y139 (= Y150), D169 (= D184), M200 (≠ L215)
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, 98% coverage: 4:417/421 of query aligns to 5:412/416 of P69902
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
31% identity, 98% coverage: 4:417/421 of query aligns to 5:405/410 of 1q7eA
- active site: Q17 (≠ L16), E133 (≠ D151), D162 (= D184), G241 (vs. gap), G242 (vs. gap)
- binding methionine: N96 (= N107), F97 (≠ Y108), H98 (≠ Y116), P99 (≠ G117), K118 (≠ T136), K130 (≠ A148), A131 (≠ G149), W246 (≠ N250), F299 (≠ D309), A303 (≠ P313), E306 (≠ A316)
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
30% identity, 99% coverage: 4:421/421 of query aligns to 5:428/430 of 3ubmB
- active site: Q17 (≠ L16), E140 (≠ D151), D182 (= D184), G261 (≠ N250), G262 (≠ I251)
- binding coenzyme a: V16 (= V15), R38 (= R37), L72 (≠ C83), N73 (≠ D84), T74 (≠ I85), K75 (≠ A86), N96 (= N107), F97 (≠ Y108), R98 (≠ K109), A101 (≠ D112), R104 (= R115), K125 (≠ T136), D182 (= D184), M213 (≠ L215)
1p5rA Formyl-coa transferase in complex with coenzyme a (see paper)
29% identity, 99% coverage: 4:421/421 of query aligns to 4:427/427 of 1p5rA
- active site: Q16 (≠ L16), E139 (≠ D151), D168 (= D184), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R14), V15 (= V15), Q16 (≠ L16), A17 (= A17), R37 (= R37), M73 (≠ I85), K74 (≠ A86), N95 (= N107), F96 (≠ Y108), A100 (≠ D112), R103 (= R115), K136 (≠ A148), V137 (≠ G149), D168 (= D184), M199 (≠ L215)
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
29% identity, 99% coverage: 4:421/421 of query aligns to 5:428/428 of O06644
- Q17 (≠ L16) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (= R37) binding CoA
- W48 (= W52) 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 (= R115) binding CoA
- D169 (= D184) 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)
29% identity, 99% coverage: 4:421/421 of query aligns to 4:427/427 of 2vjoA
- active site: A16 (≠ L16), E139 (≠ D151), D168 (= D184), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R14), A16 (≠ L16), A17 (= A17), R37 (= R37), L71 (≠ C83), M73 (≠ I85), N95 (= N107), F96 (≠ Y108), G97 (≠ K109), R103 (= R115), M104 (≠ Y116), K136 (≠ A148), V137 (≠ G149), Y138 (= Y150), D168 (= D184), M199 (≠ L215)
- 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)
29% identity, 99% coverage: 4:421/421 of query aligns to 4:427/427 of 2vjkA
- active site: Q16 (≠ L16), E139 (≠ D151), D168 (= D184), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R14), Q16 (≠ L16), A17 (= A17), R37 (= R37), M73 (≠ I85), K74 (≠ A86), N95 (= N107), F96 (≠ Y108), G97 (≠ K109), R103 (= R115), M104 (≠ Y116), K136 (≠ A148), V137 (≠ G149), Y138 (= Y150), D168 (= D184), M199 (≠ L215)
- binding magnesium ion: D293 (≠ E285), D296 (≠ G288)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
29% identity, 99% coverage: 4:421/421 of query aligns to 4:427/427 of 1t4cA
- active site: Q16 (≠ L16), E139 (≠ D151), D168 (= D184), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R14), V15 (= V15), Q16 (≠ L16), R37 (= R37), M73 (≠ I85), N95 (= N107), F96 (≠ Y108), R103 (= R115), M104 (≠ Y116), V137 (≠ G149), Y138 (= Y150), D168 (= D184), M199 (≠ L215)
- binding oxalic acid: G259 (vs. gap), G260 (vs. gap)
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
28% identity, 99% coverage: 4:421/421 of query aligns to 4:427/427 of 1t3zA
- active site: Q16 (≠ L16), E139 (≠ D151), S168 (≠ D184), G259 (vs. gap), G260 (vs. gap)
- binding oxidized coenzyme a: H14 (≠ R14), V15 (= V15), A17 (= A17), R37 (= R37), K74 (≠ A86), N95 (= N107), F96 (≠ Y108), A100 (≠ D112), R103 (= R115), M104 (≠ Y116), K136 (≠ A148), V137 (≠ G149), Y138 (= Y150), E139 (≠ D151), M199 (≠ L215)
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
28% identity, 95% coverage: 4:401/421 of query aligns to 6:360/360 of 5yx6A
Q9UHK6 Alpha-methylacyl-CoA racemase; 2-methylacyl-CoA racemase; EC 5.1.99.4 from Homo sapiens (Human) (see 5 papers)
28% identity, 100% coverage: 3:421/421 of query aligns to 2:373/382 of Q9UHK6
- V9 (≠ L10) to M: in dbSNP:rs3195676
- S52 (= S80) to P: in AMACRD and CBAS4; inactive enzyme; dbSNP:rs121917814
- L107 (≠ I135) to P: in CBAS4; inactive enzyme; dbSNP:rs121917816
- G175 (= G206) to D: in dbSNP:rs10941112
- L201 (≠ V232) to S: in dbSNP:rs2287939
- M261 (≠ V305) to T: in dbSNP:rs3195678
- E277 (≠ T321) to K: in dbSNP:rs2278008
Sites not aligning to the query:
- 380:382 Microbody targeting signal
8apqB Camct - mesaconyl-coa c1:c4 coa transferase of chloroflexus aurantiacus (see paper)
29% identity, 99% coverage: 4:421/421 of query aligns to 5:402/406 of 8apqB
- binding coenzyme a: F16 (≠ V15), V17 (≠ L16), A18 (= A17), P38 (= P38), I74 (= I85), N100 (= N107), F101 (≠ Y108), L124 (≠ I135), V125 (≠ T136), G126 (= G137), D165 (= D184)
- binding (2e)-2-methylbut-2-enedioic acid: V17 (≠ L16), R47 (≠ G51), D165 (= D184)
- binding Mesaconyl Coenzme A: T249 (≠ N276), L251 (≠ G278)
8apqA Camct - mesaconyl-coa c1:c4 coa transferase of chloroflexus aurantiacus (see paper)
29% identity, 99% coverage: 4:421/421 of query aligns to 5:402/406 of 8apqA
- binding Mesaconyl Coenzme A: G13 (≠ L12), F16 (≠ V15), V17 (≠ L16), P38 (= P38), R47 (≠ G51), I74 (= I85), R75 (≠ A86), N100 (= N107), F101 (≠ Y108), P102 (≠ K109), L107 (= L118), L124 (≠ I135), V125 (≠ T136), G126 (= G137), S132 (≠ A148), E133 (≠ G149), V134 (≠ Y150), D135 (= D151), Y136 (≠ F152), D165 (= D184)
O06543 Alpha-methylacyl-CoA racemase; AMACR; MtMCR; EC 5.1.99.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
31% identity, 53% coverage: 4:228/421 of query aligns to 5:201/360 of O06543
- R38 (= R37) binding substrate
- R52 (= R76) mutation to A: 15.7% of wild-type activity.
- I56 (≠ S80) mutation to P: 28.8% of wild-type activity.
- ADLK 59:62 (≠ CDIA 83:86) binding substrate
- E82 (= E106) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NYK 107:109) binding substrate
- R91 (= R115) binding substrate; mutation to A: 19.9% of wild-type activity.
- M111 (≠ I135) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ GYDFAI 149:154) binding substrate
- H126 (≠ Y150) mutation to A: 4.5% of wild-type activity.
- D156 (= D184) mutation to A: 17.6 of wild-type activity.
- D190 (= D217) 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.
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)
31% identity, 53% coverage: 4:228/421 of query aligns to 4:196/355 of 2yimA
- active site: G16 (≠ L16), D122 (= D151), D151 (= D184)
- binding 2-methylacetoacetyl coa: I15 (≠ V15), R37 (= R37), A54 (≠ C83), L56 (≠ I85), K57 (≠ A86), G78 (≠ N107), Y79 (= Y108), R80 (≠ K109), V83 (≠ D112), R86 (= R115), L87 (≠ Y116), A119 (= A148), G120 (= G149), H121 (≠ Y150), Y125 (≠ I154), D151 (= D184)
Sites not aligning to the query:
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)
31% identity, 53% coverage: 4:228/421 of query aligns to 4:195/354 of 2gd6A
- active site: G16 (≠ L16), D121 (= D151), D150 (= D184)
- binding acetyl coenzyme *a: I15 (≠ V15), R37 (= R37), A53 (≠ C83), D54 (= D84), L55 (≠ I85), K56 (≠ A86), G77 (≠ N107), Y78 (= Y108), R79 (≠ K109), V82 (≠ D112), R85 (= R115), G119 (= G149), H120 (≠ Y150), Y124 (≠ I154), D150 (= D184), M182 (≠ L215)
Sites not aligning to the query:
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)
31% identity, 53% coverage: 4:228/421 of query aligns to 4:195/354 of 2gd2A
- active site: G16 (≠ L16), D121 (= D151), D150 (= D184)
- binding acetoacetyl-coenzyme a: I15 (≠ V15), R37 (= R37), A53 (≠ C83), L55 (≠ I85), K56 (≠ A86), G77 (≠ N107), Y78 (= Y108), R79 (≠ K109), V82 (≠ D112), R85 (= R115), L86 (≠ Y116), A118 (= A148), G119 (= G149), H120 (≠ Y150), Y124 (≠ I154), D150 (= D184)
Sites not aligning to the query:
Query Sequence
>WP_068174644.1 NCBI__GCF_001592305.1:WP_068174644.1
MNALDGIRILDLSRVLAGPWCTQTLADLGADVVKVERPPGPQHPGGDDTRGWGPPFLRGH
DGADTAEAAYYLGANRNKRSITCDIAQPEGQALIRELAAKADVFVENYKVGDMARYGLDY
ERLRAINPRLVYCSITGFGQTGPYQDRAGYDFAIQAMGGLMSVTGERDDLPGGGPQKVGV
AVADLFTGLYATVAIQAALRHAERTGEGQHIDMALLDTQVAMLANLGANYLVRGREDGKV
PGRAGNAHANIVPYQVFEVAPDAQGAPQHIILAVGNDGQFAKFCEVAGRPELAADALFAR
NQDRVRHRDTLVPELASLMKTRGKADWLGALEAAKVPCGPINNLAEVFADEHVRSRGMVH
TWAHPLADTLDLVASPLKLSATPVRNDLPPPLLGQHTAEVLNDWLGDSPQRLSELQRRGI
V
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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