SitesBLAST
Comparing WP_050462144.1 NCBI__GCF_001189915.1:WP_050462144.1 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)
31% identity, 99% coverage: 6:396/396 of query aligns to 4:397/403 of 9br7C
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
30% identity, 99% coverage: 5:396/396 of query aligns to 1:415/415 of 1pt5A
- active site: Q16 (≠ I20), E139 (≠ D142), D168 (= D170), G247 (vs. gap), G248 (vs. gap)
- binding acetyl coenzyme *a: V15 (≠ A19), S17 (≠ A21), R37 (= R41), L71 (= L74), N72 (= N75), T73 (≠ L76), K74 (= K77), N95 (= N98), F96 (≠ L99), H97 (≠ A100), K124 (≠ S127), K136 (= K139), A137 (= A140), Y138 (= Y141), E139 (≠ D142), D168 (= D170), M199 (= M201)
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
30% identity, 99% coverage: 5:396/396 of query aligns to 2:416/417 of 1q6yA
- active site: Q17 (≠ I20), E140 (≠ D142), D169 (= D170), G248 (vs. gap), G249 (vs. gap)
- binding coenzyme a: V16 (≠ A19), Q17 (≠ I20), S18 (≠ A21), R38 (= R41), L72 (= L74), N73 (= N75), T74 (≠ L76), K75 (= K77), N96 (= N98), F97 (≠ L99), H98 (≠ A100), M105 (≠ L107), I124 (= I126), K137 (= K139), A138 (= A140), Y139 (= Y141), D169 (= D170), M200 (= M201)
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, 99% coverage: 5:396/396 of query aligns to 2:416/416 of P69902
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
28% identity, 98% coverage: 5:393/396 of query aligns to 2:425/430 of 3ubmB
- active site: Q17 (≠ I20), E140 (≠ D142), D182 (= D170), G261 (≠ A231), G262 (≠ T232)
- binding coenzyme a: V16 (≠ A19), R38 (= R41), L72 (= L74), N73 (= N75), T74 (≠ L76), K75 (= K77), N96 (= N98), F97 (≠ L99), R98 (≠ A100), A101 (= A103), R104 (≠ G106), K125 (≠ S127), D182 (= D170), M213 (= M201)
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
29% identity, 99% coverage: 5:396/396 of query aligns to 2:409/410 of 1q7eA
- active site: Q17 (≠ I20), E133 (≠ D142), D162 (= D170), G241 (vs. gap), G242 (vs. gap)
- binding methionine: N96 (= N98), F97 (≠ L99), H98 (≠ A100), P99 (= P101), K118 (≠ S127), K130 (= K139), A131 (= A140), W246 (vs. gap), F299 (≠ A287), A303 (= A291), E306 (≠ L294)
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
27% identity, 99% coverage: 5:396/396 of query aligns to 2:428/428 of O06644
- Q17 (≠ I20) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (= R41) binding CoA
- W48 (≠ Y51) 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 (≠ G106) binding CoA
- D169 (= D170) 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)
27% identity, 99% coverage: 5:396/396 of query aligns to 1:427/427 of 1p5rA
- active site: Q16 (≠ I20), E139 (≠ D142), D168 (= D170), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (= H18), V15 (≠ A19), Q16 (≠ I20), A17 (= A21), R37 (= R41), M73 (≠ L76), K74 (= K77), N95 (= N98), F96 (≠ L99), A100 (= A103), R103 (≠ G106), K136 (= K139), V137 (≠ A140), D168 (= D170), M199 (= M201)
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
27% identity, 99% coverage: 5:396/396 of query aligns to 1:427/427 of 2vjoA
- active site: A16 (≠ I20), E139 (≠ D142), D168 (= D170), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (= H18), A16 (≠ I20), A17 (= A21), R37 (= R41), L71 (= L74), M73 (≠ L76), N95 (= N98), F96 (≠ L99), G97 (≠ A100), R103 (≠ G106), M104 (≠ L107), K136 (= K139), V137 (≠ A140), Y138 (= Y141), D168 (= D170), M199 (= M201)
- 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)
27% identity, 99% coverage: 5:396/396 of query aligns to 1:427/427 of 2vjkA
- active site: Q16 (≠ I20), E139 (≠ D142), D168 (= D170), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (= H18), Q16 (≠ I20), A17 (= A21), R37 (= R41), M73 (≠ L76), K74 (= K77), N95 (= N98), F96 (≠ L99), G97 (≠ A100), R103 (≠ G106), M104 (≠ L107), K136 (= K139), V137 (≠ A140), Y138 (= Y141), D168 (= D170), M199 (= M201)
- binding magnesium ion: D293 (≠ E262), D296 (≠ Q266)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
27% identity, 99% coverage: 5:396/396 of query aligns to 1:427/427 of 1t4cA
- active site: Q16 (≠ I20), E139 (≠ D142), D168 (= D170), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (= H18), V15 (≠ A19), Q16 (≠ I20), R37 (= R41), M73 (≠ L76), N95 (= N98), F96 (≠ L99), R103 (≠ G106), M104 (≠ L107), V137 (≠ A140), Y138 (= Y141), D168 (= D170), M199 (= M201)
- binding oxalic acid: G259 (vs. gap), G260 (vs. gap)
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
26% identity, 99% coverage: 5:396/396 of query aligns to 1:427/427 of 1t3zA
- active site: Q16 (≠ I20), E139 (≠ D142), S168 (≠ D170), G259 (vs. gap), G260 (vs. gap)
- binding oxidized coenzyme a: H14 (= H18), V15 (≠ A19), A17 (= A21), R37 (= R41), K74 (= K77), N95 (= N98), F96 (≠ L99), A100 (= A103), R103 (≠ G106), M104 (≠ L107), K136 (= K139), V137 (≠ A140), Y138 (= Y141), E139 (≠ D142), M199 (= M201)
Q9UHK6 Alpha-methylacyl-CoA racemase; 2-methylacyl-CoA racemase; EC 5.1.99.4 from Homo sapiens (Human) (see 5 papers)
27% identity, 98% coverage: 8:396/396 of query aligns to 3:373/382 of Q9UHK6
- V9 (= V14) to M: in dbSNP:rs3195676
- S52 (= S71) to P: in AMACRD and CBAS4; inactive enzyme; dbSNP:rs121917814
- L107 (≠ I126) to P: in CBAS4; inactive enzyme; dbSNP:rs121917816
- G175 (= G192) to D: in dbSNP:rs10941112
- L201 (≠ G219) to S: in dbSNP:rs2287939
- M261 (≠ H283) to T: in dbSNP:rs3195678
- E277 (≠ K299) to K: in dbSNP:rs2278008
Sites not aligning to the query:
- 380:382 Microbody targeting signal
1xvtA Crystal structure of native caib in complex with coenzyme a (see paper)
28% identity, 98% coverage: 7:394/396 of query aligns to 8:396/402 of 1xvtA
- active site: I21 (= I20), N138 (≠ D142), D166 (= D170), G225 (≠ A228), K226 (≠ E229)
- binding coenzyme a: I21 (= I20), A22 (= A21), N42 (≠ R41), L68 (= L74), N69 (= N75), F71 (≠ K77), S93 (≠ L99), K94 (≠ A100), R100 (≠ G106), R101 (≠ L107), P135 (≠ K139), A136 (= A140), D166 (= D170), M197 (= M201)
P31572 L-carnitine CoA-transferase; Crotonobetainyl-CoA:carnitine CoA-transferase; EC 2.8.3.21 from Escherichia coli (strain K12) (see paper)
28% identity, 98% coverage: 7:394/396 of query aligns to 11:399/405 of P31572
- K97 (≠ A100) binding CoA
- R104 (≠ L107) binding CoA
1xvvA Crystal structure of caib mutant d169a in complex with carnitinyl-coa (see paper)
27% identity, 98% coverage: 7:394/396 of query aligns to 8:396/402 of 1xvvA
- active site: I21 (= I20), N138 (≠ D142), A166 (≠ D170), G225 (≠ A228), K226 (≠ E229)
- binding l-carnitinyl-coa inner salt: I19 (≠ H18), E20 (≠ A19), I21 (= I20), A22 (= A21), N69 (= N75), F71 (≠ K77), A92 (≠ N98), S93 (≠ L99), K94 (≠ A100), R100 (≠ G106), R101 (≠ L107), A136 (= A140), Y137 (= Y141), N138 (≠ D142), Y163 (≠ S167)
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
27% identity, 85% coverage: 6:342/396 of query aligns to 4:328/360 of 5yx6A
O06543 Alpha-methylacyl-CoA racemase; AMACR; MtMCR; EC 5.1.99.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
26% identity, 87% coverage: 7:349/396 of query aligns to 4:331/360 of O06543
- R38 (= R41) binding substrate
- R52 (≠ T65) mutation to A: 15.7% of wild-type activity.
- I56 (≠ S71) mutation to P: 28.8% of wild-type activity.
- ADLK 59:62 (≠ LNLK 74:77) binding substrate
- E82 (≠ Q97) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NLA 98:100) binding substrate
- R91 (≠ G106) binding substrate; mutation to A: 19.9% of wild-type activity.
- M111 (≠ I126) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ AYDLLI 140:145) binding substrate
- H126 (≠ Y141) mutation to A: 4.5% of wild-type activity.
- D156 (= D170) mutation to A: 17.6 of wild-type activity.
- D190 (≠ E203) mutation to A: 3.3% of wild-type activity.
- E241 (≠ N253) mutation to A: 2.1% of wild-type activity.
- C297 (≠ A315) mutation to A: 6.2% of wild-type activity.
- H312 (≠ Q330) 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)
25% identity, 87% coverage: 7:349/396 of query aligns to 3:326/355 of 2yimA
- active site: G16 (≠ I20), D122 (= D142), D151 (= D170), G214 (≠ T232), G215 (≠ I233)
- binding 2-methylacetoacetyl coa: I15 (≠ A19), R37 (= R41), A54 (≠ L74), L56 (= L76), K57 (= K77), G78 (≠ N98), Y79 (≠ L99), R80 (≠ A100), V83 (≠ A103), R86 (≠ G106), L87 (= L107), A119 (≠ K139), G120 (≠ A140), H121 (≠ Y141), Y125 (≠ I145), D151 (= D170)
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)
25% identity, 87% coverage: 7:349/396 of query aligns to 3:325/354 of 2gd6A
- active site: G16 (≠ I20), D121 (= D142), D150 (= D170), G213 (≠ T232), G214 (≠ I233)
- binding acetyl coenzyme *a: I15 (≠ A19), R37 (= R41), A53 (≠ L74), D54 (≠ N75), L55 (= L76), K56 (= K77), G77 (≠ N98), Y78 (≠ L99), R79 (≠ A100), V82 (≠ A103), R85 (≠ G106), G119 (≠ A140), H120 (≠ Y141), Y124 (≠ I145), D150 (= D170), M182 (= M201)
Query Sequence
>WP_050462144.1 NCBI__GCF_001189915.1:WP_050462144.1
MMQATRPLEGITVVSLEHAIAAPFCTRQLADMGARVIKIERPGVGDFARGYDERVNGMSS
HFVWTNRSKESLSLNLKDAEGQAIIDKLLAQADVLVQNLAPGAAAGLGLSAAVLHAKYPR
LIVCDISGYGENGPYRDKKAYDLLIQSEAGFLSVTGSADEPAKAGCSIADIAAGMYAYSN
ILAALIKRGRDGVGSHIDLSMLEALTEWMSFPMYYAYEGASAPKRSGAEHATIYPYGPFA
AGDGNVVMLGLQNEREWKVFCEQVLQDAALTDDPRFSSNSRRHENRAVLRAQILESFSKL
TAQQVVERLDQAQIANARVNTMQDLWQHPQLAARQRWTEVGSPVGPLPALLPPGVSNTWD
YRMDAVPALGEHTDAILAGLGYAPQQIGDLRARGAI
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