SitesBLAST
Comparing WP_092347644.1 NCBI__GCF_900107645.1:WP_092347644.1 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)
9br7C Succinate--hydroxymethylglutarate CoA-transferase (see paper)
33% identity, 90% coverage: 26:407/423 of query aligns to 4:380/403 of 9br7C
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
31% identity, 94% coverage: 25:423/423 of query aligns to 2:428/430 of 3ubmB
- active site: Q17 (≠ L40), E140 (≠ D166), D182 (vs. gap), G261 (vs. gap), G262 (vs. gap)
- binding coenzyme a: V16 (= V39), R38 (≠ V61), L72 (≠ I98), N73 (= N99), T74 (≠ L100), K75 (= K101), N96 (= N122), F97 (= F123), R98 (= R124), A101 (≠ V127), R104 (= R130), K125 (≠ S151), D182 (vs. gap), M213 (= M227)
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
34% identity, 89% coverage: 25:399/423 of query aligns to 3:355/360 of 5yx6A
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
30% identity, 95% coverage: 24:423/423 of query aligns to 1:416/417 of 1q6yA
- active site: Q17 (≠ L40), E140 (≠ D166), D169 (= D195), G248 (vs. gap), G249 (vs. gap)
- binding coenzyme a: V16 (= V39), Q17 (≠ L40), S18 (= S41), R38 (≠ V61), L72 (≠ I98), N73 (= N99), T74 (≠ L100), K75 (= K101), N96 (= N122), F97 (= F123), H98 (≠ R124), M105 (≠ L131), I124 (= I150), K137 (≠ P163), A138 (= A164), Y139 (= Y165), D169 (= D195), M200 (= M227)
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
30% identity, 94% coverage: 25:423/423 of query aligns to 1:415/415 of 1pt5A
- active site: Q16 (≠ L40), E139 (≠ D166), D168 (= D195), G247 (vs. gap), G248 (vs. gap)
- binding acetyl coenzyme *a: V15 (= V39), S17 (= S41), R37 (≠ V61), L71 (≠ I98), N72 (= N99), T73 (≠ L100), K74 (= K101), N95 (= N122), F96 (= F123), H97 (≠ R124), K124 (≠ S151), K136 (≠ P163), A137 (= A164), Y138 (= Y165), E139 (≠ D166), D168 (= D195), M199 (= M227)
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)
30% identity, 94% coverage: 25:423/423 of query aligns to 2:416/416 of P69902
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
27% identity, 94% coverage: 25:423/423 of query aligns to 2:428/428 of O06644
- Q17 (≠ L40) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (≠ V61) binding CoA
- W48 (≠ Q70) 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 (= R130) binding CoA
- D169 (= D195) 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)
27% identity, 94% coverage: 25:423/423 of query aligns to 1:427/427 of 2vjoA
- active site: A16 (≠ L40), E139 (≠ D166), D168 (= D195), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ N38), A16 (≠ L40), A17 (≠ S41), R37 (≠ V61), L71 (≠ I98), M73 (≠ L100), N95 (= N122), F96 (= F123), G97 (≠ R124), R103 (= R130), M104 (≠ L131), K136 (≠ P163), V137 (≠ A164), Y138 (= Y165), D168 (= D195), M199 (= M227)
- binding oxalate ion: G257 (vs. gap), G259 (vs. gap), Q261 (vs. gap)
1p5rA Formyl-coa transferase in complex with coenzyme a (see paper)
27% identity, 94% coverage: 25:423/423 of query aligns to 1:427/427 of 1p5rA
- active site: Q16 (≠ L40), E139 (≠ D166), D168 (= D195), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ N38), V15 (= V39), Q16 (≠ L40), A17 (≠ S41), R37 (≠ V61), M73 (≠ L100), K74 (= K101), N95 (= N122), F96 (= F123), A100 (≠ V127), R103 (= R130), K136 (≠ P163), V137 (≠ A164), D168 (= D195), M199 (= M227)
2vjkA Formyl-coa transferase with aspartyl-coa thioester intermediate derived from oxalyl-coa (see paper)
27% identity, 94% coverage: 25:423/423 of query aligns to 1:427/427 of 2vjkA
- active site: Q16 (≠ L40), E139 (≠ D166), D168 (= D195), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ N38), Q16 (≠ L40), A17 (≠ S41), R37 (≠ V61), M73 (≠ L100), K74 (= K101), N95 (= N122), F96 (= F123), G97 (≠ R124), R103 (= R130), M104 (≠ L131), K136 (≠ P163), V137 (≠ A164), Y138 (= Y165), D168 (= D195), M199 (= M227)
- binding magnesium ion: D293 (≠ E287), D296 (≠ G290)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
27% identity, 94% coverage: 25:423/423 of query aligns to 1:427/427 of 1t4cA
- active site: Q16 (≠ L40), E139 (≠ D166), D168 (= D195), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ N38), V15 (= V39), Q16 (≠ L40), R37 (≠ V61), M73 (≠ L100), N95 (= N122), F96 (= F123), R103 (= R130), M104 (≠ L131), V137 (≠ A164), Y138 (= Y165), D168 (= D195), M199 (= M227)
- binding oxalic acid: G259 (vs. gap), G260 (vs. gap)
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
27% identity, 94% coverage: 25:423/423 of query aligns to 1:427/427 of 1t3zA
- active site: Q16 (≠ L40), E139 (≠ D166), S168 (≠ D195), G259 (vs. gap), G260 (vs. gap)
- binding oxidized coenzyme a: H14 (≠ N38), V15 (= V39), A17 (≠ S41), R37 (≠ V61), K74 (= K101), N95 (= N122), F96 (= F123), A100 (≠ V127), R103 (= R130), M104 (≠ L131), K136 (≠ P163), V137 (≠ A164), Y138 (= Y165), E139 (≠ D166), M199 (= M227)
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
29% identity, 95% coverage: 24:423/423 of query aligns to 1:409/410 of 1q7eA
- active site: Q17 (≠ L40), E133 (≠ D166), D162 (= D195), G241 (vs. gap), G242 (vs. gap)
- binding methionine: N96 (= N122), F97 (= F123), H98 (≠ R124), P99 (= P125), K118 (≠ S151), K130 (≠ P163), A131 (= A164), W246 (vs. gap), F299 (≠ Q311), A303 (≠ Q315), E306 (= E318)
Q9UHK6 Alpha-methylacyl-CoA racemase; 2-methylacyl-CoA racemase; EC 5.1.99.4 from Homo sapiens (Human) (see 5 papers)
28% identity, 94% coverage: 28:423/423 of query aligns to 3:373/382 of Q9UHK6
- V9 (≠ I34) to M: in dbSNP:rs3195676
- S52 (= S95) to P: in AMACRD and CBAS4; inactive enzyme; dbSNP:rs121917814
- L107 (≠ I150) to P: in CBAS4; inactive enzyme; dbSNP:rs121917816
- G175 (≠ D218) to D: in dbSNP:rs10941112
- L201 (≠ Y242) to S: in dbSNP:rs2287939
- M261 (≠ L307) to T: in dbSNP:rs3195678
- E277 (≠ S323) 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, 78% coverage: 27:358/423 of query aligns to 4:316/360 of O06543
- R38 (≠ V61) binding substrate
- R52 (≠ A91) mutation to A: 15.7% of wild-type activity.
- I56 (≠ S95) mutation to P: 28.8% of wild-type activity.
- ADLK 59:62 (≠ INLK 98:101) binding substrate
- E82 (= E121) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NFR 122:124) binding substrate
- R91 (= R130) binding substrate; mutation to A: 19.9% of wild-type activity.
- M111 (≠ I150) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ AYDQII 164:169) binding substrate
- H126 (≠ Y165) mutation to A: 4.5% of wild-type activity.
- D156 (= D195) mutation to A: 17.6 of wild-type activity.
- D190 (= D229) mutation to A: 3.3% of wild-type activity.
- E241 (≠ K278) mutation to A: 2.1% of wild-type activity.
- C297 (≠ P339) mutation to A: 6.2% of wild-type activity.
- H312 (= H354) mutation to A: 10.1% of wild-type activity.
1xvtA Crystal structure of native caib in complex with coenzyme a (see paper)
26% identity, 92% coverage: 27:417/423 of query aligns to 8:392/402 of 1xvtA
- active site: I21 (≠ L40), N138 (≠ D166), D166 (= D195), G225 (= G253), K226 (≠ N254)
- binding coenzyme a: I21 (≠ L40), A22 (≠ S41), N42 (≠ V61), L68 (≠ I98), N69 (= N99), F71 (≠ K101), S93 (≠ F123), K94 (≠ R124), R100 (= R130), R101 (≠ L131), P135 (= P163), A136 (= A164), D166 (= D195), M197 (= M227)
P31572 L-carnitine CoA-transferase; Crotonobetainyl-CoA:carnitine CoA-transferase; EC 2.8.3.21 from Escherichia coli (strain K12) (see paper)
26% identity, 92% coverage: 27:417/423 of query aligns to 11:395/405 of P31572
- K97 (≠ R124) binding CoA
- R104 (≠ L131) binding CoA
1xvvA Crystal structure of caib mutant d169a in complex with carnitinyl-coa (see paper)
27% identity, 92% coverage: 27:417/423 of query aligns to 8:392/402 of 1xvvA
- active site: I21 (≠ L40), N138 (≠ D166), A166 (= A194), G225 (= G253), K226 (≠ N254)
- binding l-carnitinyl-coa inner salt: I19 (≠ N38), E20 (≠ V39), I21 (≠ L40), A22 (≠ S41), N69 (= N99), F71 (≠ K101), A92 (≠ N122), S93 (≠ F123), K94 (≠ R124), R100 (= R130), R101 (≠ L131), A136 (= A164), Y137 (= Y165), N138 (≠ D166), Y163 (= Y191)
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, 78% coverage: 27:358/423 of query aligns to 3:310/354 of 2gd6A
- active site: G16 (≠ L40), D121 (= D166), D150 (= D195), G213 (≠ M252), G214 (= G253)
- binding acetyl coenzyme *a: I15 (≠ V39), R37 (≠ V61), A53 (≠ I98), D54 (≠ N99), L55 (= L100), K56 (= K101), G77 (≠ N122), Y78 (≠ F123), R79 (= R124), V82 (= V127), R85 (= R130), G119 (≠ A164), H120 (≠ Y165), Y124 (≠ I169), D150 (= D195), M182 (= M227)
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, 78% coverage: 27:358/423 of query aligns to 3:310/354 of 2gd2A
- active site: G16 (≠ L40), D121 (= D166), D150 (= D195), G213 (≠ M252), G214 (= G253)
- binding acetoacetyl-coenzyme a: I15 (≠ V39), R37 (≠ V61), A53 (≠ I98), L55 (= L100), K56 (= K101), G77 (≠ N122), Y78 (≠ F123), R79 (= R124), V82 (= V127), R85 (= R130), L86 (= L131), A118 (≠ P163), G119 (≠ A164), H120 (≠ Y165), Y124 (≠ I169), D150 (= D195)
Query Sequence
>WP_092347644.1 NCBI__GCF_900107645.1:WP_092347644.1
MQFCLREPHYLNTLPDKSKGAYVFSRPLKKFRVIDLTNVLSGPFCGYLLANMGAQVIKVE
VPESGDLARQLGASPELNKNKMGASFLAQNAGKKSLTINLKTAAGKKLFEKLIRTADVLI
ENFRPGVMTRLGLGFDDLKLINPKLIYCAISGFGATGPLRYLPAYDQIIQGLSGVMSITG
DSSSAPLRVGYPIADTIGGMSAAFAIAATLAGRNGETDEAVFIDVSMLDSTMSTMGWVVS
NYLIAGKDPIPMGNDNFTASPSGTFQTGDGPLNIAANKQEQFEKLCELLGLPELTTDPHF
SQRQLRLQNRQELKQLLEQALKSKSAEAWEEELSSAGVPAGRVLSVPEALNHPHMRDRGM
IGHFDNVPRVGNVDVFRPGFKLNGLSPQVDTPPPLLGQHTDEMLTDLGLTAEDIAALRQE
KVV
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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