SitesBLAST
Comparing WP_003548337.1 NCBI__GCF_000009265.1:WP_003548337.1 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)
31% identity, 99% coverage: 3:384/385 of query aligns to 3:387/403 of 9br7C
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
31% identity, 97% coverage: 5:378/385 of query aligns to 4:413/430 of 3ubmB
- active site: Q17 (≠ M18), E140 (≠ D142), D182 (= D171), G261 (vs. gap), G262 (vs. gap)
- binding coenzyme a: V16 (= V17), R38 (≠ K39), L72 (= L74), N73 (≠ D75), T74 (≠ L76), K75 (= K77), N96 (= N98), F97 (= F99), R98 (= R100), A101 (≠ V103), R104 (= R106), K125 (≠ T127), D182 (= D171), M213 (≠ L202)
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
28% identity, 97% coverage: 5:378/385 of query aligns to 4:413/428 of O06644
- Q17 (≠ M18) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (≠ K39) binding CoA
- W48 (≠ S49) 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 (= R106) binding CoA
- D169 (= D171) 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, 97% coverage: 5:378/385 of query aligns to 3:412/427 of 1p5rA
- active site: Q16 (≠ M18), E139 (≠ D142), D168 (= D171), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ Q16), V15 (= V17), Q16 (≠ M18), A17 (≠ L19), R37 (≠ K39), M73 (≠ L76), K74 (= K77), N95 (= N98), F96 (= F99), A100 (≠ V103), R103 (= R106), K136 (≠ G139), V137 (≠ G140), D168 (= D171), M199 (≠ L202)
2vjkA Formyl-coa transferase with aspartyl-coa thioester intermediate derived from oxalyl-coa (see paper)
28% identity, 97% coverage: 5:378/385 of query aligns to 3:412/427 of 2vjkA
- active site: Q16 (≠ M18), E139 (≠ D142), D168 (= D171), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ Q16), Q16 (≠ M18), A17 (≠ L19), R37 (≠ K39), M73 (≠ L76), K74 (= K77), N95 (= N98), F96 (= F99), G97 (≠ R100), R103 (= R106), M104 (= M107), K136 (≠ G139), V137 (≠ G140), Y138 (≠ Q141), D168 (= D171), M199 (≠ L202)
- binding magnesium ion: D293 (≠ N258), D296 (≠ E261)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
28% identity, 97% coverage: 5:378/385 of query aligns to 3:412/427 of 1t4cA
- active site: Q16 (≠ M18), E139 (≠ D142), D168 (= D171), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ Q16), V15 (= V17), Q16 (≠ M18), R37 (≠ K39), M73 (≠ L76), N95 (= N98), F96 (= F99), R103 (= R106), M104 (= M107), V137 (≠ G140), Y138 (≠ Q141), D168 (= D171), M199 (≠ L202)
- binding oxalic acid: G259 (vs. gap), G260 (vs. gap)
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
32% identity, 97% coverage: 5:378/385 of query aligns to 4:401/417 of 1q6yA
- active site: Q17 (≠ M18), E140 (≠ D142), D169 (= D171), G248 (vs. gap), G249 (vs. gap)
- binding coenzyme a: V16 (= V17), Q17 (≠ M18), S18 (≠ L19), R38 (≠ K39), L72 (= L74), N73 (≠ D75), T74 (≠ L76), K75 (= K77), N96 (= N98), F97 (= F99), H98 (≠ R100), M105 (= M107), I124 (≠ G126), K137 (≠ G139), A138 (≠ G140), Y139 (≠ Q141), D169 (= D171), M200 (≠ L202)
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
28% identity, 97% coverage: 5:378/385 of query aligns to 3:412/427 of 2vjoA
- active site: A16 (≠ M18), E139 (≠ D142), D168 (= D171), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ Q16), A16 (≠ M18), A17 (≠ L19), R37 (≠ K39), L71 (= L74), M73 (≠ L76), N95 (= N98), F96 (= F99), G97 (≠ R100), R103 (= R106), M104 (= M107), K136 (≠ G139), V137 (≠ G140), Y138 (≠ Q141), D168 (= D171), M199 (≠ L202)
- binding oxalate ion: G257 (vs. gap), G259 (vs. gap), Q261 (vs. gap)
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
32% identity, 97% coverage: 5:378/385 of query aligns to 3:400/415 of 1pt5A
- active site: Q16 (≠ M18), E139 (≠ D142), D168 (= D171), G247 (vs. gap), G248 (vs. gap)
- binding acetyl coenzyme *a: V15 (= V17), S17 (≠ L19), R37 (≠ K39), L71 (= L74), N72 (≠ D75), T73 (≠ L76), K74 (= K77), N95 (= N98), F96 (= F99), H97 (≠ R100), K124 (≠ T127), K136 (≠ G139), A137 (≠ G140), Y138 (≠ Q141), E139 (≠ D142), D168 (= D171), M199 (≠ L202)
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)
32% identity, 97% coverage: 5:378/385 of query aligns to 4:401/416 of P69902
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
28% identity, 97% coverage: 5:378/385 of query aligns to 3:412/427 of 1t3zA
- active site: Q16 (≠ M18), E139 (≠ D142), S168 (≠ D171), G259 (vs. gap), G260 (vs. gap)
- binding oxidized coenzyme a: H14 (≠ Q16), V15 (= V17), A17 (≠ L19), R37 (≠ K39), K74 (= K77), N95 (= N98), F96 (= F99), A100 (≠ V103), R103 (= R106), M104 (= M107), K136 (≠ G139), V137 (≠ G140), Y138 (≠ Q141), E139 (≠ D142), M199 (≠ L202)
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
31% identity, 97% coverage: 5:378/385 of query aligns to 4:394/410 of 1q7eA
- active site: Q17 (≠ M18), E133 (≠ D142), D162 (= D171), G241 (vs. gap), G242 (vs. gap)
- binding methionine: N96 (= N98), F97 (= F99), H98 (≠ R100), P99 (= P101), K118 (≠ T127), K130 (≠ G139), A131 (≠ G140), W246 (vs. gap), F299 (≠ Q285), A303 (≠ H289), E306 (≠ D290)
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
31% identity, 96% coverage: 5:374/385 of query aligns to 5:360/360 of 5yx6A
Q9UHK6 Alpha-methylacyl-CoA racemase; 2-methylacyl-CoA racemase; EC 5.1.99.4 from Homo sapiens (Human) (see 5 papers)
28% identity, 97% coverage: 4:378/385 of query aligns to 1:358/382 of Q9UHK6
- V9 (≠ I12) to M: in dbSNP:rs3195676
- S52 (= S71) to P: in AMACRD and CBAS4; inactive enzyme; dbSNP:rs121917814
- L107 (≠ G126) to P: in CBAS4; inactive enzyme; dbSNP:rs121917816
- G175 (= G193) to D: in dbSNP:rs10941112
- L201 (≠ E213) to S: in dbSNP:rs2287939
- M261 (≠ F274) to T: in dbSNP:rs3195678
- E277 (≠ K294) 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)
29% identity, 86% coverage: 5:335/385 of query aligns to 4:322/360 of O06543
- R38 (≠ K39) binding substrate
- R52 (= R67) mutation to A: 15.7% of wild-type activity.
- I56 (≠ S71) mutation to P: 28.8% of wild-type activity.
- ADLK 59:62 (≠ LDLK 74:77) binding substrate
- E82 (≠ N97) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NFR 98:100) binding substrate
- R91 (= R106) binding substrate; mutation to A: 19.9% of wild-type activity.
- M111 (≠ G126) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ GQDVLA 140:145) binding substrate
- H126 (≠ Q141) mutation to A: 4.5% of wild-type activity.
- D156 (= D171) mutation to A: 17.6 of wild-type activity.
- D190 (≠ N204) mutation to A: 3.3% of wild-type activity.
- E241 (≠ K249) mutation to A: 2.1% of wild-type activity.
- C297 (≠ L310) mutation to A: 6.2% of wild-type activity.
- H312 (≠ Q325) 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)
29% identity, 86% coverage: 5:335/385 of query aligns to 3:317/355 of 2yimA
- active site: G16 (≠ M18), D122 (= D142), D151 (= D171), G214 (≠ W226), G215 (= G227)
- binding 2-methylacetoacetyl coa: I15 (≠ V17), R37 (≠ K39), A54 (≠ L74), L56 (= L76), K57 (= K77), G78 (≠ N98), Y79 (≠ F99), R80 (= R100), V83 (= V103), R86 (= R106), L87 (≠ M107), A119 (≠ G139), G120 (= G140), H121 (≠ Q141), Y125 (≠ A145), D151 (= D171)
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)
29% identity, 86% coverage: 5:335/385 of query aligns to 3:316/354 of 2gd6A
- active site: G16 (≠ M18), D121 (= D142), D150 (= D171), G213 (≠ W226), G214 (= G227)
- binding acetyl coenzyme *a: I15 (≠ V17), R37 (≠ K39), A53 (≠ L74), D54 (= D75), L55 (= L76), K56 (= K77), G77 (≠ N98), Y78 (≠ F99), R79 (= R100), V82 (= V103), R85 (= R106), G119 (= G140), H120 (≠ Q141), Y124 (≠ A145), D150 (= D171), M182 (≠ L202)
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)
29% identity, 86% coverage: 5:335/385 of query aligns to 3:316/354 of 2gd2A
- active site: G16 (≠ M18), D121 (= D142), D150 (= D171), G213 (≠ W226), G214 (= G227)
- binding acetoacetyl-coenzyme a: I15 (≠ V17), R37 (≠ K39), A53 (≠ L74), L55 (= L76), K56 (= K77), G77 (≠ N98), Y78 (≠ F99), R79 (= R100), V82 (= V103), R85 (= R106), L86 (≠ M107), A118 (≠ G139), G119 (= G140), H120 (≠ Q141), Y124 (≠ A145), D150 (= D171)
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)
29% identity, 86% coverage: 5:335/385 of query aligns to 3:316/354 of 2gd0A
- active site: G16 (≠ M18), D121 (= D142), D150 (= D171), G213 (≠ W226), G214 (= G227)
- binding (s)-2-methylmyristoyl-coenzyme a: D42 (≠ C63), L55 (= L76), K56 (= K77), G77 (≠ N98), Y78 (≠ F99), R79 (= R100), V82 (= V103), R85 (= R106), L86 (≠ M107), G119 (= G140), H120 (≠ Q141), D121 (= D142), Y124 (≠ A145), D150 (= D171)
2gciA The 1,1-proton transfer reaction mechanism by alpha-methylacyl-coa racemase is catalyzed by an asparte/histidine pair and involves a smooth, methionine-rich surface for binding the fatty acyl moiety (see paper)
29% identity, 86% coverage: 5:335/385 of query aligns to 3:316/354 of 2gciA
- active site: G16 (≠ M18), D121 (= D142), D150 (= D171), G213 (≠ W226), G214 (= G227)
- binding (r)-2-methylmyristoyl-coenzyme a: R37 (≠ K39), L55 (= L76), K56 (= K77), G77 (≠ N98), Y78 (≠ F99), R79 (= R100), V82 (= V103), G119 (= G140), H120 (≠ Q141), D121 (= D142), Y124 (≠ A145), D150 (= D171), Y218 (≠ T232), I234 (≠ F248), E235 (≠ K249)
Query Sequence
>WP_003548337.1 NCBI__GCF_000009265.1:WP_003548337.1
MTILPLDGIRVIDFTQVMLGPSCTQVLADYGAEVIKIEKVRIGDLSRWSLGSDPDGLNNP
VFCSLNRNKKSLALDLKQPEARETVLTLLETADVVVNNFRPGVMERMGFGFEDLKKINKK
LIYAVGTGFGLTGPYQHKGGQDVLAQAVSGVMRRKSDSSHPTSIYATPLADYSAGMHLVQ
GILLALLQRDKTGEGQQVAVSLYNSMLAMQMQEGTTHLMRQKDLNWGAFPLTGVFETTDG
AIVMVGAFKQNPLQDICNALEIEDLSQYPHYKDFDAQMARRPELQTIFHDNFAKNTTAHW
LQRLEDVDILCAPVRSLPEALKDEQTIINKMILEAGETAAGPIRLIGSPIDMSAAEVAVR
ISPPQLGQHNDEILGSLGRLQGNAA
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