SitesBLAST
Comparing WP_011383897.1 NCBI__GCF_000009985.1:WP_011383897.1 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)
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
30% identity, 99% coverage: 5:400/401 of query aligns to 5:427/430 of 3ubmB
- active site: Q17 (≠ L17), E140 (≠ D145), D182 (= D174), G261 (≠ P235), G262 (≠ N236)
- binding coenzyme a: V16 (= V16), R38 (≠ K38), L72 (≠ I77), N73 (≠ D78), T74 (≠ F79), K75 (≠ T80), N96 (= N101), F97 (= F102), R98 (≠ K103), A101 (≠ G106), R104 (≠ K109), K125 (≠ T130), D182 (= D174), M213 (≠ L205)
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, 100% coverage: 1:401/401 of query aligns to 1:416/416 of P69902
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
28% identity, 100% coverage: 1:401/401 of query aligns to 1:416/417 of 1q6yA
- active site: Q17 (≠ L17), E140 (≠ D145), D169 (= D174), G248 (≠ P235), G249 (≠ N236)
- binding coenzyme a: V16 (= V16), Q17 (≠ L17), S18 (≠ A18), R38 (≠ K38), L72 (≠ I77), N73 (≠ D78), T74 (≠ F79), K75 (≠ T80), N96 (= N101), F97 (= F102), H98 (≠ K103), M105 (≠ Y110), I124 (= I129), K137 (≠ A142), A138 (≠ G143), Y139 (= Y144), D169 (= D174), M200 (≠ L205)
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
29% identity, 99% coverage: 5:401/401 of query aligns to 4:415/415 of 1pt5A
- active site: Q16 (≠ L17), E139 (≠ D145), D168 (= D174), G247 (≠ P235), G248 (≠ N236)
- binding acetyl coenzyme *a: V15 (= V16), S17 (≠ A18), R37 (≠ K38), L71 (≠ I77), N72 (≠ D78), T73 (≠ F79), K74 (≠ T80), N95 (= N101), F96 (= F102), H97 (≠ K103), K124 (≠ T130), K136 (≠ A142), A137 (≠ G143), Y138 (= Y144), E139 (≠ D145), D168 (= D174), M199 (≠ L205)
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
32% identity, 92% coverage: 5:374/401 of query aligns to 6:353/360 of 5yx6A
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
28% identity, 100% coverage: 1:401/401 of query aligns to 1:409/410 of 1q7eA
- active site: Q17 (≠ L17), E133 (≠ D145), D162 (= D174), G241 (≠ P235), G242 (≠ N236)
- binding methionine: N96 (= N101), F97 (= F102), H98 (≠ Y110), P99 (≠ G111), K118 (≠ T130), K130 (≠ A142), A131 (≠ G143), W246 (vs. gap), F299 (≠ A289), A303 (≠ P293), E306 (≠ V296)
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: 1:401/401 of query aligns to 1:428/428 of O06644
- Q17 (≠ L17) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (≠ K38) binding
- W48 (= W48) 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 (≠ K109) binding
- D169 (= D174) 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, 100% coverage: 2:401/401 of query aligns to 1:427/427 of 1p5rA
- active site: Q16 (≠ L17), E139 (≠ D145), D168 (= D174), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R15), V15 (= V16), Q16 (≠ L17), A17 (= A18), R37 (≠ K38), M73 (≠ F79), K74 (≠ T80), N95 (= N101), F96 (= F102), A100 (≠ G106), R103 (≠ K109), K136 (≠ A142), V137 (≠ G143), D168 (= D174), M199 (≠ L205)
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
28% identity, 100% coverage: 2:401/401 of query aligns to 1:427/427 of 2vjoA
- active site: A16 (≠ L17), E139 (≠ D145), D168 (= D174), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R15), A16 (≠ L17), A17 (= A18), R37 (≠ K38), L71 (≠ I77), M73 (≠ F79), N95 (= N101), F96 (= F102), G97 (≠ K103), R103 (≠ K109), M104 (≠ Y110), K136 (≠ A142), V137 (≠ G143), Y138 (= Y144), D168 (= D174), M199 (≠ L205)
- 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, 100% coverage: 2:401/401 of query aligns to 1:427/427 of 2vjkA
- active site: Q16 (≠ L17), E139 (≠ D145), D168 (= D174), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R15), Q16 (≠ L17), A17 (= A18), R37 (≠ K38), M73 (≠ F79), K74 (≠ T80), N95 (= N101), F96 (= F102), G97 (≠ K103), R103 (≠ K109), M104 (≠ Y110), K136 (≠ A142), V137 (≠ G143), Y138 (= Y144), D168 (= D174), M199 (≠ L205)
- binding magnesium ion: D293 (≠ E265), D296 (≠ G268)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
28% identity, 100% coverage: 2:401/401 of query aligns to 1:427/427 of 1t4cA
- active site: Q16 (≠ L17), E139 (≠ D145), D168 (= D174), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R15), V15 (= V16), Q16 (≠ L17), R37 (≠ K38), M73 (≠ F79), N95 (= N101), F96 (= F102), R103 (≠ K109), M104 (≠ Y110), V137 (≠ G143), Y138 (= Y144), D168 (= D174), M199 (≠ L205)
- binding oxalic acid: G259 (vs. gap), G260 (vs. gap)
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
28% identity, 100% coverage: 2:401/401 of query aligns to 1:427/427 of 1t3zA
- active site: Q16 (≠ L17), E139 (≠ D145), S168 (≠ D174), G259 (vs. gap), G260 (vs. gap)
- binding oxidized coenzyme a: H14 (≠ R15), V15 (= V16), A17 (= A18), R37 (≠ K38), K74 (≠ T80), N95 (= N101), F96 (= F102), A100 (≠ G106), R103 (≠ K109), M104 (≠ Y110), K136 (≠ A142), V137 (≠ G143), Y138 (= Y144), E139 (≠ D145), M199 (≠ L205)
8apqB Camct - mesaconyl-coa c1:c4 coa transferase of chloroflexus aurantiacus (see paper)
28% identity, 100% coverage: 1:401/401 of query aligns to 1:402/406 of 8apqB
- binding coenzyme a: F16 (≠ V16), V17 (≠ L17), A18 (= A18), P38 (≠ K38), I74 (≠ F79), N100 (= N101), F101 (= F102), L124 (≠ I129), V125 (≠ T130), G126 (= G131), D165 (= D174)
- binding (2e)-2-methylbut-2-enedioic acid: V17 (≠ L17), R47 (≠ A47), D165 (= D174)
- binding Mesaconyl Coenzme A: T249 (≠ N256), L251 (≠ A258)
8apqA Camct - mesaconyl-coa c1:c4 coa transferase of chloroflexus aurantiacus (see paper)
28% identity, 100% coverage: 1:401/401 of query aligns to 1:402/406 of 8apqA
- binding Mesaconyl Coenzme A: G13 (≠ L13), F16 (≠ V16), V17 (≠ L17), P38 (≠ K38), R47 (≠ A47), I74 (≠ F79), R75 (≠ T80), N100 (= N101), F101 (= F102), P102 (≠ K103), L107 (= L112), L124 (≠ I129), V125 (≠ T130), G126 (= G131), S132 (≠ A142), E133 (≠ G143), V134 (≠ Y144), D135 (= D145), Y136 (≠ F146), D165 (= D174)
Q9UHK6 Alpha-methylacyl-CoA racemase; 2-methylacyl-CoA racemase; EC 5.1.99.4 from Homo sapiens (Human) (see 5 papers)
25% identity, 99% coverage: 4:401/401 of query aligns to 2:373/382 of Q9UHK6
- V9 (≠ L11) to M: in dbSNP:rs3195676
- S52 (= S74) to P: in AMACRD and CBAS4; inactive enzyme; dbSNP:rs121917814
- L107 (≠ I129) to P: in CBAS4; inactive enzyme; dbSNP:rs121917816
- G175 (= G196) to D: in dbSNP:rs10941112
- L201 (= L221) to S: in dbSNP:rs2287939
- M261 (≠ V285) to T: in dbSNP:rs3195678
- E277 (= E301) 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, 84% coverage: 1:336/401 of query aligns to 1:316/360 of O06543
- R38 (≠ K38) binding
- R52 (= R70) mutation to A: 15.7% of wild-type activity.
- I56 (≠ S74) mutation to P: 28.8% of wild-type activity.
- ADLK 59:62 (≠ IDFT 77:80) binding
- E82 (= E100) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NFK 101:103) binding
- R91 (≠ K109) binding ; mutation to A: 19.9% of wild-type activity.
- M111 (≠ I129) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ GYDFLV 143:148) binding
- H126 (≠ Y144) mutation to A: 4.5% of wild-type activity.
- D156 (= D174) mutation to A: 17.6 of wild-type activity.
- D190 (= D207) mutation to A: 3.3% of wild-type activity.
- E241 (≠ D257) mutation to A: 2.1% of wild-type activity.
- C297 (≠ P317) mutation to A: 6.2% of wild-type activity.
- H312 (≠ Q332) 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)
26% identity, 83% coverage: 3:336/401 of query aligns to 2:311/355 of 2yimA
- active site: G16 (≠ L17), D122 (= D145), D151 (= D174), G214 (≠ N236), G215 (≠ I237)
- binding 2-methylacetoacetyl coa: I15 (≠ V16), R37 (≠ K38), A54 (≠ I77), L56 (≠ F79), K57 (≠ T80), G78 (≠ N101), Y79 (≠ F102), R80 (≠ K103), V83 (≠ G106), R86 (≠ K109), L87 (≠ Y110), A119 (= A142), G120 (= G143), H121 (≠ Y144), Y125 (≠ V148), D151 (= D174)
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, 83% coverage: 3:336/401 of query aligns to 2:310/354 of 2gd6A
- active site: G16 (≠ L17), D121 (= D145), D150 (= D174), G213 (≠ N236), G214 (≠ I237)
- binding acetyl coenzyme *a: I15 (≠ V16), R37 (≠ K38), A53 (≠ I77), D54 (= D78), L55 (≠ F79), K56 (≠ T80), G77 (≠ N101), Y78 (≠ F102), R79 (≠ K103), V82 (≠ G106), R85 (≠ K109), G119 (= G143), H120 (≠ Y144), Y124 (≠ V148), D150 (= D174), M182 (≠ L205)
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, 83% coverage: 3:336/401 of query aligns to 2:310/354 of 2gd2A
- active site: G16 (≠ L17), D121 (= D145), D150 (= D174), G213 (≠ N236), G214 (≠ I237)
- binding acetoacetyl-coenzyme a: I15 (≠ V16), R37 (≠ K38), A53 (≠ I77), L55 (≠ F79), K56 (≠ T80), G77 (≠ N101), Y78 (≠ F102), R79 (≠ K103), V82 (≠ G106), R85 (≠ K109), L86 (≠ Y110), A118 (= A142), G119 (= G143), H120 (≠ Y144), Y124 (≠ V148), D150 (= D174)
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, 83% coverage: 3:336/401 of query aligns to 2:310/354 of 2gd0A
- active site: G16 (≠ L17), D121 (= D145), D150 (= D174), G213 (≠ N236), G214 (≠ I237)
- binding (s)-2-methylmyristoyl-coenzyme a: D42 (= D43), L55 (≠ F79), K56 (≠ T80), G77 (≠ N101), Y78 (≠ F102), R79 (≠ K103), V82 (≠ G106), R85 (≠ K109), L86 (≠ Y110), G119 (= G143), H120 (≠ Y144), D121 (= D145), Y124 (≠ V148), D150 (= D174)
Query Sequence
>WP_011383897.1 NCBI__GCF_000009985.1:WP_011383897.1
MTGALSHLRILDLSRVLAGPWAGQLLADMGAEVLKIEKPGEGDDTRAWGPPFLDADEGRG
ESAYYLSANRGKHSVTIDFTQPQGQALVRRLVAQCDVVLENFKVGGLAKYGLDYDSLKAI
KPDLVYCSITGFGQDGPYAQRAGYDFLVQGMGGLMSLTGTPDGEPMKVGVALTDIFTGMY
AGFAVLAALAHRDRTGEGQHIDLALLDVQVAVLANQATNYLVGGVIPKRLGNSHPNIVPY
QAFATAEGHIILAIGNDAQFRRFCEVAGHPELGTDPLYATNADRVRHRAILVPVLVEIMT
EHDADYWIAELEKAGVPCGPINSLDRVFADPQVKHRGMAVAMEHPQREDLRLVANPIHLS
KTPVTYDRPPPLLGADTDDVLARLLGLDEGERAELRSSGVI
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