SitesBLAST
Comparing WP_086509637.1 NCBI__GCF_002151265.1:WP_086509637.1 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)
42% identity, 99% coverage: 3:400/401 of query aligns to 4:397/403 of 9br7C
Q9HAC7 Succinyl-CoA:glutarate CoA-transferase; Dermal papilla-derived protein 13; Dicarboxyl-CoA:dicarboxylic acid coenzyme A transferase SUGCT; Succinate--hydroxymethylglutarate CoA-transferase; EC 2.8.3.-; EC 2.8.3.13 from Homo sapiens (Human) (see 3 papers)
42% identity, 99% coverage: 3:400/401 of query aligns to 39:432/438 of Q9HAC7
- D205 (= D175) mutation to A: Loss of CoA transferase activity toward glutaryl-CoA and 3-hydroxy-3-methylglutarate substrates.
- R329 (≠ I299) to W: in GA3; severely decreased protein stability and processing; dbSNP:rs137852860
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
30% identity, 100% coverage: 1:400/401 of query aligns to 1:428/428 of O06644
- Q17 (≠ L17) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (≠ H38) binding CoA
- 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 (≠ K110) binding CoA
- D169 (= D175) 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)
30% identity, 100% coverage: 2:400/401 of query aligns to 1:427/427 of 1p5rA
- active site: Q16 (≠ L17), E139 (≠ D146), D168 (= D175), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R15), V15 (= V16), Q16 (≠ L17), A17 (= A18), R37 (≠ H38), M73 (≠ V80), K74 (≠ A81), N95 (= N102), F96 (= F103), A100 (≠ G107), R103 (≠ K110), K136 (≠ A143), V137 (≠ G144), D168 (= D175), M199 (≠ L206)
2vjkA Formyl-coa transferase with aspartyl-coa thioester intermediate derived from oxalyl-coa (see paper)
30% identity, 100% coverage: 2:400/401 of query aligns to 1:427/427 of 2vjkA
- active site: Q16 (≠ L17), E139 (≠ D146), D168 (= D175), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R15), Q16 (≠ L17), A17 (= A18), R37 (≠ H38), M73 (≠ V80), K74 (≠ A81), N95 (= N102), F96 (= F103), G97 (≠ K104), R103 (≠ K110), M104 (≠ Y111), K136 (≠ A143), V137 (≠ G144), Y138 (= Y145), D168 (= D175), M199 (≠ L206)
- binding magnesium ion: D293 (≠ E266), D296 (≠ G269)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
30% identity, 100% coverage: 2:400/401 of query aligns to 1:427/427 of 1t4cA
- active site: Q16 (≠ L17), E139 (≠ D146), D168 (= D175), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R15), V15 (= V16), Q16 (≠ L17), R37 (≠ H38), M73 (≠ V80), N95 (= N102), F96 (= F103), R103 (≠ K110), M104 (≠ Y111), V137 (≠ G144), Y138 (= Y145), D168 (= D175), M199 (≠ L206)
- binding oxalic acid: G259 (vs. gap), G260 (vs. gap)
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
30% identity, 100% coverage: 2:400/401 of query aligns to 1:427/427 of 2vjoA
- active site: A16 (≠ L17), E139 (≠ D146), D168 (= D175), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R15), A16 (≠ L17), A17 (= A18), R37 (≠ H38), L71 (≠ V78), M73 (≠ V80), N95 (= N102), F96 (= F103), G97 (≠ K104), R103 (≠ K110), M104 (≠ Y111), K136 (≠ A143), V137 (≠ G144), Y138 (= Y145), D168 (= D175), M199 (≠ L206)
- binding oxalate ion: G257 (vs. gap), G259 (vs. gap), Q261 (vs. gap)
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
30% identity, 100% coverage: 2:400/401 of query aligns to 1:427/427 of 1t3zA
- active site: Q16 (≠ L17), E139 (≠ D146), S168 (≠ D175), G259 (vs. gap), G260 (vs. gap)
- binding oxidized coenzyme a: H14 (≠ R15), V15 (= V16), A17 (= A18), R37 (≠ H38), K74 (≠ A81), N95 (= N102), F96 (= F103), A100 (≠ G107), R103 (≠ K110), M104 (≠ Y111), K136 (≠ A143), V137 (≠ G144), Y138 (= Y145), E139 (≠ D146), M199 (≠ L206)
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, 99% coverage: 1:396/401 of query aligns to 1:412/416 of P69902
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
29% identity, 100% coverage: 2:400/401 of query aligns to 2:428/430 of 3ubmB
- active site: Q17 (≠ L17), E140 (≠ D146), D182 (= D175), G261 (vs. gap), G262 (vs. gap)
- binding coenzyme a: V16 (= V16), R38 (≠ H38), L72 (≠ V78), N73 (≠ D79), T74 (≠ V80), K75 (≠ A81), N96 (= N102), F97 (= F103), R98 (≠ K104), A101 (≠ G107), R104 (≠ K110), K125 (≠ T131), D182 (= D175), M213 (vs. gap)
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
31% identity, 99% coverage: 1:396/401 of query aligns to 1:412/417 of 1q6yA
- active site: Q17 (≠ L17), E140 (≠ D146), D169 (= D175), G248 (vs. gap), G249 (vs. gap)
- binding coenzyme a: V16 (= V16), Q17 (≠ L17), S18 (≠ A18), R38 (≠ H38), L72 (≠ V78), N73 (≠ D79), T74 (≠ V80), K75 (≠ A81), N96 (= N102), F97 (= F103), H98 (≠ K104), M105 (≠ Y111), I124 (= I130), K137 (≠ A143), A138 (≠ G144), Y139 (= Y145), D169 (= D175), M200 (≠ L206)
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
31% identity, 99% coverage: 2:396/401 of query aligns to 1:411/415 of 1pt5A
- active site: Q16 (≠ L17), E139 (≠ D146), D168 (= D175), G247 (vs. gap), G248 (vs. gap)
- binding acetyl coenzyme *a: V15 (= V16), S17 (≠ A18), R37 (≠ H38), L71 (≠ V78), N72 (≠ D79), T73 (≠ V80), K74 (≠ A81), N95 (= N102), F96 (= F103), H97 (≠ K104), K124 (≠ T131), K136 (≠ A143), A137 (≠ G144), Y138 (= Y145), E139 (≠ D146), D168 (= D175), M199 (≠ L206)
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
33% identity, 95% coverage: 2:381/401 of query aligns to 3:360/360 of 5yx6A
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
30% identity, 99% coverage: 1:396/401 of query aligns to 1:405/410 of 1q7eA
- active site: Q17 (≠ L17), E133 (≠ D146), D162 (= D175), G241 (vs. gap), G242 (vs. gap)
- binding methionine: N96 (= N102), F97 (= F103), H98 (≠ Y111), P99 (≠ G112), K118 (≠ T131), K130 (≠ A143), A131 (≠ G144), W246 (vs. gap), F299 (≠ E290), A303 (≠ P294), E306 (≠ Q297)
Q5U921 (R)-2-hydroxy-4-methylpentanoate CoA-transferase; 2-hydroxyisocaproate-CoA transferase; EC 2.8.3.24 from Clostridioides difficile (Peptoclostridium difficile) (see paper)
28% identity, 99% coverage: 5:401/401 of query aligns to 3:398/399 of Q5U921
- D171 (= D175) mutation D->A,N: Loss of activity.
Q9UHK6 Alpha-methylacyl-CoA racemase; 2-methylacyl-CoA racemase; EC 5.1.99.4 from Homo sapiens (Human) (see 5 papers)
26% identity, 99% coverage: 5:400/401 of query aligns to 3:373/382 of Q9UHK6
- V9 (≠ L11) to M: in dbSNP:rs3195676
- S52 (= S75) to P: in AMACRD and CBAS4; inactive enzyme; dbSNP:rs121917814
- L107 (≠ I130) to P: in CBAS4; inactive enzyme; dbSNP:rs121917816
- G175 (= G197) to D: in dbSNP:rs10941112
- L201 (≠ V223) to S: in dbSNP:rs2287939
- M261 (≠ V286) to T: in dbSNP:rs3195678
- E277 (≠ T302) 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)
26% identity, 96% coverage: 1:383/401 of query aligns to 1:357/360 of O06543
- R38 (≠ H38) binding substrate
- R52 (= R71) mutation to A: 15.7% of wild-type activity.
- I56 (≠ S75) mutation to P: 28.8% of wild-type activity.
- ADLK 59:62 (≠ VDVA 78:81) binding substrate
- E82 (= E101) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NFK 102:104) binding substrate
- R91 (≠ K110) binding substrate; mutation to A: 19.9% of wild-type activity.
- M111 (≠ I130) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ GYDFMI 144:149) binding substrate
- H126 (≠ Y145) mutation to A: 4.5% of wild-type activity.
- D156 (= D175) mutation to A: 17.6 of wild-type activity.
- D190 (= D208) mutation to A: 3.3% of wild-type activity.
- E241 (≠ D258) mutation to A: 2.1% of wild-type activity.
- C297 (≠ P318) mutation to A: 6.2% of wild-type activity.
- H312 (≠ Q333) 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, 95% coverage: 4:383/401 of query aligns to 3:352/355 of 2yimA
- active site: G16 (≠ L17), D122 (= D146), D151 (= D175), G214 (≠ N237), G215 (≠ I238)
- binding 2-methylacetoacetyl coa: I15 (≠ V16), R37 (≠ H38), A54 (≠ V78), L56 (≠ V80), K57 (≠ A81), G78 (≠ N102), Y79 (≠ F103), R80 (≠ K104), V83 (≠ G107), R86 (≠ K110), L87 (≠ Y111), A119 (= A143), G120 (= G144), H121 (≠ Y145), Y125 (≠ I149), D151 (= D175)
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, 95% coverage: 4:383/401 of query aligns to 3:351/354 of 2gd6A
- active site: G16 (≠ L17), D121 (= D146), D150 (= D175), G213 (≠ N237), G214 (≠ I238)
- binding acetyl coenzyme *a: I15 (≠ V16), R37 (≠ H38), A53 (≠ V78), D54 (= D79), L55 (≠ V80), K56 (≠ A81), G77 (≠ N102), Y78 (≠ F103), R79 (≠ K104), V82 (≠ G107), R85 (≠ K110), G119 (= G144), H120 (≠ Y145), Y124 (≠ I149), D150 (= D175), M182 (≠ L206)
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, 95% coverage: 4:383/401 of query aligns to 3:351/354 of 2gd2A
- active site: G16 (≠ L17), D121 (= D146), D150 (= D175), G213 (≠ N237), G214 (≠ I238)
- binding acetoacetyl-coenzyme a: I15 (≠ V16), R37 (≠ H38), A53 (≠ V78), L55 (≠ V80), K56 (≠ A81), G77 (≠ N102), Y78 (≠ F103), R79 (≠ K104), V82 (≠ G107), R85 (≠ K110), L86 (≠ Y111), A118 (= A143), G119 (= G144), H120 (≠ Y145), Y124 (≠ I149), D150 (= D175)
Query Sequence
>WP_086509637.1 NCBI__GCF_002151265.1:WP_086509637.1
MSRPLEGITVLDMSRVLAGPWAGQLLADLGARVIKIEHPERGDDTRGWGPPWLAEDDEAE
RVAAYFLCANRGKQSLAVDVASERGQALIRQLAAGADVMLENFKVGGLAKYGLDYASLKA
LNPRLIGCSITGFGQDGPYAHRAGYDFMIQAMGGLMSIGGEPDGMPMKTGVAITDVMTGL
YATIGVLSALHERERTGQGRHVDVALLDVQVATLANQALNALVSGVSPERHGNAHPNIVP
YQAFACADGHLVLTVGNDAQFSRLAELLGHPEWARDPAYATNAARVGNREVLVPLIQSIF
LTRGRDEWLAELEARGIPAGPINTISEVFDDPQVKHRGMQRTLARGELEVPQVACPLRFD
SEPALSEVAPPRLGQDSDAILAEMGLTEDDIARLRREGIVR
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