SitesBLAST
Comparing WP_068174482.1 NCBI__GCF_001592305.1:WP_068174482.1 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)
33% identity, 100% coverage: 1:393/393 of query aligns to 3:397/403 of 9br7C
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
30% identity, 98% coverage: 2:388/393 of query aligns to 3:423/430 of 3ubmB
- active site: Q17 (≠ I16), E140 (≠ D139), D182 (= D167), G261 (≠ A228), G262 (≠ T229)
- binding coenzyme a: V16 (≠ A15), R38 (= R37), L72 (= L70), N73 (≠ D71), T74 (≠ V72), K75 (= K73), N96 (= N95), F97 (≠ L96), R98 (≠ A97), A101 (= A100), R104 (= R103), K125 (≠ S124), D182 (= D167), M213 (= M198)
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
29% identity, 99% coverage: 3:393/393 of query aligns to 3:415/415 of 1pt5A
- active site: Q16 (≠ I16), E139 (≠ D139), D168 (= D167), G247 (≠ A228), G248 (≠ T229)
- binding acetyl coenzyme *a: V15 (≠ A15), S17 (≠ A17), R37 (= R37), L71 (= L70), N72 (≠ D71), T73 (≠ V72), K74 (= K73), N95 (= N95), F96 (≠ L96), H97 (≠ A97), K124 (≠ S124), K136 (= K136), A137 (= A137), Y138 (= Y138), E139 (≠ D139), D168 (= D167), M199 (= M198)
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, 99% coverage: 3:393/393 of query aligns to 4:416/416 of P69902
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
29% identity, 99% coverage: 3:393/393 of query aligns to 4:416/417 of 1q6yA
- active site: Q17 (≠ I16), E140 (≠ D139), D169 (= D167), G248 (≠ A228), G249 (≠ T229)
- binding coenzyme a: V16 (≠ A15), Q17 (≠ I16), S18 (≠ A17), R38 (= R37), L72 (= L70), N73 (≠ D71), T74 (≠ V72), K75 (= K73), N96 (= N95), F97 (≠ L96), H98 (≠ A97), M105 (≠ L104), I124 (= I123), K137 (= K136), A138 (= A137), Y139 (= Y138), D169 (= D167), M200 (= M198)
1p5rA Formyl-coa transferase in complex with coenzyme a (see paper)
36% identity, 51% coverage: 2:202/393 of query aligns to 2:203/427 of 1p5rA
- active site: Q16 (≠ I16), E139 (≠ D139), D168 (= D167)
- binding coenzyme a: H14 (= H14), V15 (≠ A15), Q16 (≠ I16), A17 (= A17), R37 (= R37), M73 (≠ V72), K74 (= K73), N95 (= N95), F96 (≠ L96), A100 (= A100), R103 (= R103), K136 (= K136), V137 (≠ A137), D168 (= D167), M199 (= M198)
Sites not aligning to the query:
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
36% identity, 51% coverage: 2:202/393 of query aligns to 3:204/428 of O06644
- Q17 (≠ I16) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (= R37) binding CoA
- W48 (≠ Y47) 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 (= R103) binding CoA
- D169 (= D167) 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.
Sites not aligning to the query:
- 259 G→A: 2.5-fold decrease of the catalytic effiency.
- 260 G→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)
36% identity, 51% coverage: 2:202/393 of query aligns to 2:203/427 of 2vjoA
- active site: A16 (≠ I16), E139 (≠ D139), D168 (= D167)
- binding coenzyme a: H14 (= H14), A16 (≠ I16), A17 (= A17), R37 (= R37), L71 (= L70), M73 (≠ V72), N95 (= N95), F96 (≠ L96), G97 (≠ A97), R103 (= R103), M104 (≠ L104), K136 (= K136), V137 (≠ A137), Y138 (= Y138), D168 (= D167), M199 (= M198)
Sites not aligning to the query:
2vjkA Formyl-coa transferase with aspartyl-coa thioester intermediate derived from oxalyl-coa (see paper)
36% identity, 51% coverage: 2:202/393 of query aligns to 2:203/427 of 2vjkA
- active site: Q16 (≠ I16), E139 (≠ D139), D168 (= D167)
- binding coenzyme a: H14 (= H14), Q16 (≠ I16), A17 (= A17), R37 (= R37), M73 (≠ V72), K74 (= K73), N95 (= N95), F96 (≠ L96), G97 (≠ A97), R103 (= R103), M104 (≠ L104), K136 (= K136), V137 (≠ A137), Y138 (= Y138), D168 (= D167), M199 (= M198)
Sites not aligning to the query:
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
36% identity, 51% coverage: 2:202/393 of query aligns to 2:203/427 of 1t4cA
- active site: Q16 (≠ I16), E139 (≠ D139), D168 (= D167)
- binding coenzyme a: H14 (= H14), V15 (≠ A15), Q16 (≠ I16), R37 (= R37), M73 (≠ V72), N95 (= N95), F96 (≠ L96), R103 (= R103), M104 (≠ L104), V137 (≠ A137), Y138 (= Y138), D168 (= D167), M199 (= M198)
Sites not aligning to the query:
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
29% identity, 99% coverage: 3:393/393 of query aligns to 4:409/410 of 1q7eA
- active site: Q17 (≠ I16), E133 (≠ D139), D162 (= D167), G241 (≠ A228), G242 (≠ T229)
- binding methionine: N96 (= N95), F97 (≠ L96), H98 (≠ A97), P99 (= P98), K118 (≠ S124), K130 (= K136), A131 (= A137), W246 (≠ Y233), F299 (≠ A284), A303 (≠ E288), E306 (≠ V291)
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
36% identity, 51% coverage: 2:202/393 of query aligns to 2:203/427 of 1t3zA
- active site: Q16 (≠ I16), E139 (≠ D139), S168 (≠ D167)
- binding oxidized coenzyme a: H14 (= H14), V15 (≠ A15), A17 (= A17), R37 (= R37), K74 (= K73), N95 (= N95), F96 (≠ L96), A100 (= A100), R103 (= R103), M104 (≠ L104), K136 (= K136), V137 (≠ A137), Y138 (= Y138), E139 (≠ D139), M199 (= M198)
Sites not aligning to the query:
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
30% identity, 82% coverage: 2:323/393 of query aligns to 4:308/360 of 5yx6A
Q9UHK6 Alpha-methylacyl-CoA racemase; 2-methylacyl-CoA racemase; EC 5.1.99.4 from Homo sapiens (Human) (see 5 papers)
27% identity, 99% coverage: 4:393/393 of query aligns to 3:373/382 of Q9UHK6
- V9 (= V10) to M: in dbSNP:rs3195676
- S52 (= S67) to P: in AMACRD and CBAS4; inactive enzyme; dbSNP:rs121917814
- L107 (≠ I123) to P: in CBAS4; inactive enzyme; dbSNP:rs121917816
- G175 (= G189) to D: in dbSNP:rs10941112
- L201 (= L202) to S: in dbSNP:rs2287939
- M261 (≠ V280) to T: in dbSNP:rs3195678
- E277 (≠ G296) to K: in dbSNP:rs2278008
Sites not aligning to the query:
- 380:382 Microbody targeting signal
P31572 L-carnitine CoA-transferase; Crotonobetainyl-CoA:carnitine CoA-transferase; EC 2.8.3.21 from Escherichia coli (strain K12) (see paper)
28% identity, 99% coverage: 3:391/393 of query aligns to 11:399/405 of P31572
- K97 (≠ A97) binding CoA
- R104 (≠ L104) binding CoA
1xvtA Crystal structure of native caib in complex with coenzyme a (see paper)
28% identity, 99% coverage: 3:391/393 of query aligns to 8:396/402 of 1xvtA
- active site: I21 (= I16), N138 (≠ D139), D166 (= D167), G225 (≠ A225), K226 (≠ S226)
- binding coenzyme a: I21 (= I16), A22 (= A17), N42 (≠ R37), L68 (= L70), N69 (≠ D71), F71 (≠ K73), S93 (≠ L96), K94 (≠ A97), R100 (= R103), R101 (≠ L104), P135 (≠ K136), A136 (= A137), D166 (= D167), M197 (= M198)
1xvvA Crystal structure of caib mutant d169a in complex with carnitinyl-coa (see paper)
28% identity, 99% coverage: 3:391/393 of query aligns to 8:396/402 of 1xvvA
- active site: I21 (= I16), N138 (≠ D139), A166 (≠ D167), G225 (≠ A225), K226 (≠ S226)
- binding l-carnitinyl-coa inner salt: I19 (≠ H14), E20 (≠ A15), I21 (= I16), A22 (= A17), N69 (≠ D71), F71 (≠ K73), A92 (≠ N95), S93 (≠ L96), K94 (≠ A97), R100 (= R103), R101 (≠ L104), A136 (= A137), Y137 (= Y138), N138 (≠ D139), Y163 (≠ S164)
8apqB Camct - mesaconyl-coa c1:c4 coa transferase of chloroflexus aurantiacus (see paper)
28% identity, 99% coverage: 4:393/393 of query aligns to 5:402/406 of 8apqB
- binding coenzyme a: F16 (≠ A15), V17 (≠ I16), A18 (= A17), P38 (≠ R37), I74 (≠ V72), N100 (= N95), F101 (≠ L96), L124 (≠ I123), V125 (≠ S124), G126 (= G125), D165 (= D167)
- binding (2e)-2-methylbut-2-enedioic acid: V17 (≠ I16), R47 (≠ G46), D165 (= D167)
- binding Mesaconyl Coenzme A: T249 (≠ N250), L251 (≠ R252)
8apqA Camct - mesaconyl-coa c1:c4 coa transferase of chloroflexus aurantiacus (see paper)
28% identity, 99% coverage: 4:393/393 of query aligns to 5:402/406 of 8apqA
- binding Mesaconyl Coenzme A: G13 (≠ L12), F16 (≠ A15), V17 (≠ I16), P38 (≠ R37), R47 (≠ G46), I74 (≠ V72), R75 (≠ K73), N100 (= N95), F101 (≠ L96), P102 (≠ A97), L107 (= L106), L124 (≠ I123), V125 (≠ S124), G126 (= G125), S132 (≠ K136), E133 (≠ A137), V134 (≠ Y138), D135 (= D139), Y136 (≠ L140), D165 (= D167)
O06543 Alpha-methylacyl-CoA racemase; AMACR; MtMCR; EC 5.1.99.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
33% identity, 50% coverage: 3:200/393 of query aligns to 4:190/360 of O06543
- R38 (= R37) binding substrate
- R52 (≠ T61) mutation to A: 15.7% of wild-type activity.
- I56 (≠ S67) mutation to P: 28.8% of wild-type activity.
- ADLK 59:62 (≠ LDVK 70:73) binding substrate
- E82 (≠ Q94) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NLA 95:97) binding substrate
- R91 (= R103) binding substrate; mutation to A: 19.9% of wild-type activity.
- M111 (≠ I123) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ AYDLLI 137:142) binding substrate
- H126 (≠ Y138) mutation to A: 4.5% of wild-type activity.
- D156 (= D167) mutation to A: 17.6 of wild-type activity.
- D190 (≠ E200) 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.
Query Sequence
>WP_068174482.1 NCBI__GCF_001592305.1:WP_068174482.1
MQPLQGITVVTLEHAIAAPFATRQLADLGARVIKIERPGVGDFARGYDTRVRGIASHFVW
TNRSKESLTLDVKHPEAQAILKCIIEEEADVVVQNLAPGATARLGLSYEALSKTKPGIIV
CDISGYGGSGPYRDKKAYDLLIQSEAGFVSVTGTEDTPSKAGPSIADIAAGMYAYTNILA
ALLHRQRTGEGQHIDISMLEALTEWMGYPLYYSIDGAAPPKRTGASHATIYPYGPFPAGD
GKTVMLGLQNEREWKAFCEQVLQQPALAADERFASNPQRVAARASLDEIIVNAFAGLSAA
EVVQRLETAQIANAQVNTMAEVWAHPQLQARQRWTTVGTPAGTVPALLPPGSWSQGAPRM
DAVPALGQHTDRILRGLGYGAEQVQALRAEGAV
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