SitesBLAST
Comparing PP_3001 FitnessBrowser__Putida:PP_3001 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)
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
30% identity, 96% coverage: 6:398/410 of query aligns to 4:423/430 of 3ubmB
- active site: Q17 (≠ L19), E140 (≠ G142), D182 (= D171), G261 (≠ P234), G262 (≠ T235)
- binding coenzyme a: V16 (≠ F18), R38 (= R40), L72 (≠ V74), N73 (= N75), T74 (≠ M76), K75 (= K77), N96 (= N98), F97 (≠ Y99), R98 (= R100), A101 (= A103), R104 (≠ K106), K125 (≠ S127), D182 (= D171), M213 (≠ 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)
29% identity, 97% coverage: 4:400/410 of query aligns to 2:413/416 of P69902
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
29% identity, 97% coverage: 4:400/410 of query aligns to 1:412/415 of 1pt5A
- active site: Q16 (≠ L19), E139 (≠ G142), D168 (= D171), G247 (≠ P234), G248 (≠ T235)
- binding acetyl coenzyme *a: V15 (≠ F18), S17 (≠ A20), R37 (= R40), L71 (≠ V74), N72 (= N75), T73 (≠ M76), K74 (= K77), N95 (= N98), F96 (≠ Y99), H97 (≠ R100), K124 (≠ S127), K136 (≠ A139), A137 (≠ G140), Y138 (≠ F141), E139 (≠ G142), D168 (= D171), M199 (≠ L202)
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
29% identity, 97% coverage: 4:400/410 of query aligns to 2:413/417 of 1q6yA
- active site: Q17 (≠ L19), E140 (≠ G142), D169 (= D171), G248 (≠ P234), G249 (≠ T235)
- binding coenzyme a: V16 (≠ F18), Q17 (≠ L19), S18 (≠ A20), R38 (= R40), L72 (≠ V74), N73 (= N75), T74 (≠ M76), K75 (= K77), N96 (= N98), F97 (≠ Y99), H98 (≠ R100), M105 (≠ L107), I124 (= I126), K137 (≠ A139), A138 (≠ G140), Y139 (≠ F141), D169 (= D171), M200 (≠ L202)
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
31% identity, 92% coverage: 6:381/410 of query aligns to 5:357/360 of 5yx6A
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
28% identity, 97% coverage: 4:400/410 of query aligns to 2:406/410 of 1q7eA
- active site: Q17 (≠ L19), E133 (≠ G142), D162 (= D171), G241 (≠ P234), G242 (≠ T235)
- binding methionine: N96 (= N98), F97 (≠ Y99), H98 (≠ R100), P99 (= P101), K118 (≠ S127), K130 (≠ A139), A131 (≠ G140), W246 (≠ Y239), F299 (≠ E292), A303 (= A296), E306 (≠ R299)
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
27% identity, 98% coverage: 4:403/410 of query aligns to 2:428/428 of O06644
- Q17 (≠ L19) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (= R40) binding
- W48 (≠ H50) 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 (≠ K106) binding
- 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)
27% identity, 98% coverage: 4:403/410 of query aligns to 1:427/427 of 1p5rA
- active site: Q16 (≠ L19), E139 (≠ G142), D168 (= D171), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (= H17), V15 (≠ F18), Q16 (≠ L19), A17 (= A20), R37 (= R40), M73 (= M76), K74 (= K77), N95 (= N98), F96 (≠ Y99), A100 (= A103), R103 (≠ K106), K136 (≠ A139), V137 (≠ G140), D168 (= D171), M199 (≠ L202)
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
27% identity, 98% coverage: 4:403/410 of query aligns to 1:427/427 of 2vjoA
- active site: A16 (≠ L19), E139 (≠ G142), D168 (= D171), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (= H17), A16 (≠ L19), A17 (= A20), R37 (= R40), L71 (≠ V74), M73 (= M76), N95 (= N98), F96 (≠ Y99), G97 (≠ R100), R103 (≠ K106), M104 (≠ L107), K136 (≠ A139), V137 (≠ G140), Y138 (≠ F141), D168 (= D171), M199 (≠ L202)
- 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, 98% coverage: 4:403/410 of query aligns to 1:427/427 of 2vjkA
- active site: Q16 (≠ L19), E139 (≠ G142), D168 (= D171), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (= H17), Q16 (≠ L19), A17 (= A20), R37 (= R40), M73 (= M76), K74 (= K77), N95 (= N98), F96 (≠ Y99), G97 (≠ R100), R103 (≠ K106), M104 (≠ L107), K136 (≠ A139), V137 (≠ G140), Y138 (≠ F141), D168 (= D171), M199 (≠ L202)
- binding magnesium ion: D293 (≠ A264), D296 (≠ E267)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
27% identity, 98% coverage: 4:403/410 of query aligns to 1:427/427 of 1t4cA
- active site: Q16 (≠ L19), E139 (≠ G142), D168 (= D171), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (= H17), V15 (≠ F18), Q16 (≠ L19), R37 (= R40), M73 (= M76), N95 (= N98), F96 (≠ Y99), R103 (≠ K106), M104 (≠ L107), V137 (≠ G140), Y138 (≠ F141), D168 (= D171), M199 (≠ L202)
- binding oxalic acid: G259 (vs. gap), G260 (vs. gap)
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
27% identity, 98% coverage: 4:403/410 of query aligns to 1:427/427 of 1t3zA
- active site: Q16 (≠ L19), E139 (≠ G142), S168 (≠ D171), G259 (vs. gap), G260 (vs. gap)
- binding oxidized coenzyme a: H14 (= H17), V15 (≠ F18), A17 (= A20), R37 (= R40), K74 (= K77), N95 (= N98), F96 (≠ Y99), A100 (= A103), R103 (≠ K106), M104 (≠ L107), K136 (≠ A139), V137 (≠ G140), Y138 (≠ F141), E139 (≠ G142), M199 (≠ L202)
Q9UHK6 Alpha-methylacyl-CoA racemase; 2-methylacyl-CoA racemase; EC 5.1.99.4 from Homo sapiens (Human) (see 5 papers)
27% identity, 97% coverage: 5:403/410 of query aligns to 1:373/382 of Q9UHK6
- V9 (= V13) to M: in dbSNP:rs3195676
- S52 (≠ G71) to P: in AMACRD and CBAS4; inactive enzyme; dbSNP:rs121917814
- L107 (≠ I126) to P: in CBAS4; inactive enzyme; dbSNP:rs121917816
- G175 (= G193) to D: in dbSNP:rs10941112
- L201 (= L219) to S: in dbSNP:rs2287939
- M261 (≠ G286) to T: in dbSNP:rs3195678
- E277 (≠ A304) 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)
26% identity, 98% coverage: 1:402/410 of query aligns to 6:400/405 of P31572
- K97 (≠ R100) binding
- R104 (≠ L107) binding
1xvtA Crystal structure of native caib in complex with coenzyme a (see paper)
26% identity, 98% coverage: 1:402/410 of query aligns to 3:397/402 of 1xvtA
- active site: I21 (≠ L19), N138 (≠ G142), D166 (= D171), G225 (≠ H231), K226 (≠ D232)
- binding coenzyme a: I21 (≠ L19), A22 (= A20), N42 (≠ R40), L68 (= L65), N69 (= N66), F71 (≠ M76), S93 (≠ Y99), K94 (≠ R100), R100 (≠ K106), R101 (≠ L107), P135 (≠ A139), A136 (≠ G140), D166 (= D171), M197 (≠ L202)
1xvvA Crystal structure of caib mutant d169a in complex with carnitinyl-coa (see paper)
26% identity, 98% coverage: 1:402/410 of query aligns to 3:397/402 of 1xvvA
- active site: I21 (≠ L19), N138 (≠ G142), A166 (≠ G170), G225 (≠ H231), K226 (≠ D232)
- binding l-carnitinyl-coa inner salt: I19 (≠ H17), E20 (≠ F18), I21 (≠ L19), A22 (= A20), N69 (= N66), F71 (≠ M76), A92 (≠ N98), S93 (≠ Y99), K94 (≠ R100), R100 (≠ K106), R101 (≠ L107), A136 (≠ G140), Y137 (≠ F141), N138 (≠ G142), Y163 (≠ I167)
O06543 Alpha-methylacyl-CoA racemase; AMACR; MtMCR; EC 5.1.99.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
30% identity, 83% coverage: 6:344/410 of query aligns to 4:321/360 of O06543
- R38 (= R40) binding
- R52 (≠ L54) mutation to A: 15.7% of wild-type activity.
- I56 (≠ G71) mutation to P: 28.8% of wild-type activity.
- ADLK 59:62 (≠ VNMK 74:77) binding
- E82 (= E97) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NYR 98:100) binding
- R91 (≠ K106) binding ; mutation to A: 19.9% of wild-type activity.
- M111 (≠ I126) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ GFGLIA 140:145) binding
- H126 (≠ F141) mutation to A: 4.5% of wild-type activity.
- D156 (= D171) mutation to A: 17.6 of wild-type activity.
- D190 (= D204) mutation to A: 3.3% of wild-type activity.
- E241 (≠ D256) mutation to A: 2.1% of wild-type activity.
- C297 (≠ I317) mutation to A: 6.2% of wild-type activity.
- H312 (≠ Q335) mutation to A: 10.1% of wild-type activity.
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)
31% identity, 65% coverage: 6:270/410 of query aligns to 3:247/354 of 2gd6A
- active site: G16 (≠ L19), D121 (≠ G142), D150 (= D171), G213 (vs. gap), G214 (vs. gap)
- binding acetyl coenzyme *a: I15 (≠ F18), R37 (= R40), A53 (≠ V74), D54 (≠ N75), L55 (≠ M76), K56 (= K77), G77 (≠ N98), Y78 (= Y99), R79 (= R100), V82 (≠ A103), R85 (≠ K106), G119 (= G140), H120 (≠ F141), 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)
31% identity, 65% coverage: 6:270/410 of query aligns to 3:247/354 of 2gd2A
- active site: G16 (≠ L19), D121 (≠ G142), D150 (= D171), G213 (vs. gap), G214 (vs. gap)
- binding acetoacetyl-coenzyme a: I15 (≠ F18), R37 (= R40), A53 (≠ V74), L55 (≠ M76), K56 (= K77), G77 (≠ N98), Y78 (= Y99), R79 (= R100), V82 (≠ A103), R85 (≠ K106), L86 (= L107), A118 (= A139), G119 (= G140), H120 (≠ F141), 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)
31% identity, 65% coverage: 6:270/410 of query aligns to 3:247/354 of 2gd0A
- active site: G16 (≠ L19), D121 (≠ G142), D150 (= D171), G213 (vs. gap), G214 (vs. gap)
- binding (s)-2-methylmyristoyl-coenzyme a: D42 (= D45), L55 (≠ M76), K56 (= K77), G77 (≠ N98), Y78 (= Y99), R79 (= R100), V82 (≠ A103), R85 (≠ K106), L86 (= L107), G119 (= G140), H120 (≠ F141), D121 (≠ G142), Y124 (≠ A145), D150 (= D171)
Query Sequence
>PP_3001 FitnessBrowser__Putida:PP_3001
MSQTLPLAGIRVVDYSHFLAGPYVGRCLAALGAEVIKVERPGSGDAGRQHAFTLDDQQSG
YFLQLNMGKQGVSVNMKDPRGKAFMQRLTDSADVFIENYRPGALDKLGLGYAELSARNPR
LVYCSISAYGHTGPDAHRAGFGLIAEAKSGIMQMVGVPGEAPPLLRISLGDMYTGIHAVA
AINAALLGRVSSGRGQHIDMALYDTLVSMHEYAVQCYTLSGGTVLPQQTGHDMPTSTLYG
VFRATDGDLVIAAQVDDAWQRFAAMLEANGGPPGFGSDRRYHGLNGRNAHREAILAVVRD
WVGARRVAEILALLDGIDIPSAKVQRIDEVLADPQIQARNMVIEQQHPRYGTLRLANLPF
RFSDCDTTIHQVAPDLGQHNAEVAAGLGFSPEEITALQADGVLFTHGDAR
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