SitesBLAST
Comparing Pf1N1B4_5611 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_5611 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)
32% identity, 99% coverage: 7:400/400 of query aligns to 3:397/403 of 9br7C
Q9HAC7 Succinyl-CoA:glutarate CoA-transferase; Dermal papilla-derived protein 13; Dicarboxyl-CoA:dicarboxylic acid coenzyme A transferase SUGCT; Succinate--hydroxymethylglutarate CoA-transferase; EC 2.8.3.-; EC 2.8.3.13 from Homo sapiens (Human) (see 3 papers)
32% identity, 100% coverage: 2:400/400 of query aligns to 33:432/438 of Q9HAC7
- D205 (= D174) mutation to A: Loss of CoA transferase activity toward glutaryl-CoA and 3-hydroxy-3-methylglutarate substrates.
- R329 (≠ A300) to W: in GA3; severely decreased protein stability and processing; dbSNP:rs137852860
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
29% identity, 98% coverage: 8:400/400 of query aligns to 2:427/427 of 2vjoA
- active site: A16 (≠ I22), E139 (≠ D144), D168 (= D174), G259 (≠ T236), G260 (≠ I237)
- binding coenzyme a: H14 (= H20), A16 (≠ I22), A17 (= A23), R37 (= R43), L71 (= L76), M73 (≠ L78), N95 (= N100), F96 (≠ L101), G97 (≠ A102), R103 (= R108), M104 (= M109), K136 (= K141), V137 (≠ A142), Y138 (= Y143), D168 (= D174), M199 (= M205)
- binding oxalate ion: G257 (≠ H234), G259 (≠ T236), Q261 (≠ Y238)
1p5rA Formyl-coa transferase in complex with coenzyme a (see paper)
29% identity, 98% coverage: 8:400/400 of query aligns to 2:427/427 of 1p5rA
- active site: Q16 (≠ I22), E139 (≠ D144), D168 (= D174), G259 (≠ T236), G260 (≠ I237)
- binding coenzyme a: H14 (= H20), V15 (≠ A21), Q16 (≠ I22), A17 (= A23), R37 (= R43), M73 (≠ L78), K74 (= K79), N95 (= N100), F96 (≠ L101), A100 (= A105), R103 (= R108), K136 (= K141), V137 (≠ A142), D168 (= D174), M199 (= M205)
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
29% identity, 98% coverage: 8:400/400 of query aligns to 3:428/428 of O06644
- Q17 (≠ I22) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (= R43) binding CoA
- W48 (≠ Y53) 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 (= R108) binding CoA
- D169 (= D174) 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 (≠ A235) mutation to A: 2.5-fold decrease of the catalytic effiency.
- G260 (≠ T236) mutation to A: 25-fold decrease of the catalytic effiency. Reduction of the affinity binding for both formyl-CoA and oxalate.
2vjkA Formyl-coa transferase with aspartyl-coa thioester intermediate derived from oxalyl-coa (see paper)
29% identity, 98% coverage: 8:400/400 of query aligns to 2:427/427 of 2vjkA
- active site: Q16 (≠ I22), E139 (≠ D144), D168 (= D174), G259 (≠ T236), G260 (≠ I237)
- binding coenzyme a: H14 (= H20), Q16 (≠ I22), A17 (= A23), R37 (= R43), M73 (≠ L78), K74 (= K79), N95 (= N100), F96 (≠ L101), G97 (≠ A102), R103 (= R108), M104 (= M109), K136 (= K141), V137 (≠ A142), Y138 (= Y143), D168 (= D174), M199 (= M205)
- binding magnesium ion: D293 (≠ E266), D296 (≠ L270)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
29% identity, 98% coverage: 8:400/400 of query aligns to 2:427/427 of 1t4cA
- active site: Q16 (≠ I22), E139 (≠ D144), D168 (= D174), G259 (≠ T236), G260 (≠ I237)
- binding coenzyme a: H14 (= H20), V15 (≠ A21), Q16 (≠ I22), R37 (= R43), M73 (≠ L78), N95 (= N100), F96 (≠ L101), R103 (= R108), M104 (= M109), V137 (≠ A142), Y138 (= Y143), D168 (= D174), M199 (= M205)
- binding oxalic acid: G259 (≠ T236), G260 (≠ I237)
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
29% identity, 98% coverage: 8:400/400 of query aligns to 2:427/427 of 1t3zA
- active site: Q16 (≠ I22), E139 (≠ D144), S168 (≠ D174), G259 (≠ T236), G260 (≠ I237)
- binding oxidized coenzyme a: H14 (= H20), V15 (≠ A21), A17 (= A23), R37 (= R43), K74 (= K79), N95 (= N100), F96 (≠ L101), A100 (= A105), R103 (= R108), M104 (= M109), K136 (= K141), V137 (≠ A142), Y138 (= Y143), E139 (≠ D144), M199 (= M205)
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
28% identity, 97% coverage: 8:395/400 of query aligns to 3:423/430 of 3ubmB
- active site: Q17 (≠ I22), E140 (≠ D144), D182 (= D174), G261 (≠ T236), G262 (vs. gap)
- binding coenzyme a: V16 (≠ A21), R38 (= R43), L72 (= L76), N73 (≠ D77), T74 (≠ L78), K75 (= K79), N96 (= N100), F97 (≠ L101), R98 (≠ A102), A101 (= A105), R104 (= R108), K125 (≠ S129), D182 (= D174), M213 (= M205)
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)
31% identity, 98% coverage: 9:400/400 of query aligns to 4:416/416 of P69902
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
31% identity, 98% coverage: 9:400/400 of query aligns to 4:416/417 of 1q6yA
- active site: Q17 (≠ I22), E140 (≠ D144), D169 (= D174), G248 (≠ T236), G249 (vs. gap)
- binding coenzyme a: V16 (≠ A21), Q17 (≠ I22), S18 (≠ A23), R38 (= R43), L72 (= L76), N73 (≠ D77), T74 (≠ L78), K75 (= K79), N96 (= N100), F97 (≠ L101), H98 (≠ A102), M105 (= M109), I124 (= I128), K137 (= K141), A138 (= A142), Y139 (= Y143), D169 (= D174), M200 (= M205)
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
31% identity, 98% coverage: 9:400/400 of query aligns to 3:415/415 of 1pt5A
- active site: Q16 (≠ I22), E139 (≠ D144), D168 (= D174), G247 (≠ T236), G248 (vs. gap)
- binding acetyl coenzyme *a: V15 (≠ A21), S17 (≠ A23), R37 (= R43), L71 (= L76), N72 (≠ D77), T73 (≠ L78), K74 (= K79), N95 (= N100), F96 (≠ L101), H97 (≠ A102), K124 (≠ S129), K136 (= K141), A137 (= A142), Y138 (= Y143), E139 (≠ D144), D168 (= D174), M199 (= M205)
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
30% identity, 98% coverage: 9:400/400 of query aligns to 4:409/410 of 1q7eA
- active site: Q17 (≠ I22), E133 (≠ D144), D162 (= D174), G241 (≠ T236), G242 (vs. gap)
- binding methionine: N96 (= N100), F97 (≠ L101), H98 (≠ A102), P99 (= P103), K118 (≠ S129), K130 (= K141), A131 (= A142), W246 (vs. gap), F299 (≠ H291), A303 (≠ Q295), E306 (≠ V298)
Q5U921 (R)-2-hydroxy-4-methylpentanoate CoA-transferase; 2-hydroxyisocaproate-CoA transferase; EC 2.8.3.24 from Clostridioides difficile (Peptoclostridium difficile) (see paper)
27% identity, 98% coverage: 10:400/400 of query aligns to 3:397/399 of Q5U921
- D171 (≠ A181) mutation D->A,N: Loss of activity.
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
28% identity, 93% coverage: 8:377/400 of query aligns to 4:356/360 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, 98% coverage: 10:400/400 of query aligns to 3:373/382 of Q9UHK6
- V9 (≠ I16) to M: in dbSNP:rs3195676
- S52 (= S73) to P: in AMACRD and CBAS4; inactive enzyme; dbSNP:rs121917814
- L107 (≠ I128) to P: in CBAS4; inactive enzyme; dbSNP:rs121917816
- G175 (= G196) to D: in dbSNP:rs10941112
- L201 (≠ D222) to S: in dbSNP:rs2287939
- M261 (≠ S281) to T: in dbSNP:rs3195678
- E277 (= E299) 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)
25% identity, 98% coverage: 9:398/400 of query aligns to 8:396/402 of 1xvtA
- active site: I21 (= I22), N138 (≠ D144), D166 (= D174), G225 (≠ A233), K226 (≠ H234)
- binding coenzyme a: I21 (= I22), A22 (= A23), N42 (≠ R43), L68 (= L76), N69 (≠ D77), F71 (≠ K79), S93 (≠ L101), K94 (≠ A102), R100 (= R108), R101 (≠ M109), P135 (≠ K141), A136 (= A142), D166 (= D174), M197 (= M205)
P31572 L-carnitine CoA-transferase; Crotonobetainyl-CoA:carnitine CoA-transferase; EC 2.8.3.21 from Escherichia coli (strain K12) (see paper)
25% identity, 98% coverage: 9:398/400 of query aligns to 11:399/405 of P31572
- K97 (≠ A102) binding CoA
- R104 (≠ M109) binding CoA
1xvvA Crystal structure of caib mutant d169a in complex with carnitinyl-coa (see paper)
24% identity, 98% coverage: 9:398/400 of query aligns to 8:396/402 of 1xvvA
- active site: I21 (= I22), N138 (≠ D144), A166 (= A173), G225 (≠ A233), K226 (≠ H234)
- binding l-carnitinyl-coa inner salt: I19 (≠ H20), E20 (≠ A21), I21 (= I22), A22 (= A23), N69 (≠ D77), F71 (≠ K79), A92 (≠ N100), S93 (≠ L101), K94 (≠ A102), R100 (= R108), R101 (≠ M109), A136 (= A142), Y137 (= Y143), N138 (≠ D144), Y163 (≠ C170)
O06543 Alpha-methylacyl-CoA racemase; AMACR; MtMCR; EC 5.1.99.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
32% identity, 50% coverage: 9:207/400 of query aligns to 4:190/360 of O06543
- R38 (= R43) binding substrate
- R52 (≠ T67) mutation to A: 15.7% of wild-type activity.
- I56 (≠ S73) mutation to P: 28.8% of wild-type activity.
- ADLK 59:62 (≠ LDLK 76:79) binding substrate
- E82 (≠ Q99) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NLA 100:102) binding substrate
- R91 (= R108) binding substrate; mutation to A: 19.9% of wild-type activity.
- M111 (≠ I128) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ AYDLLI 142:147) binding substrate
- H126 (≠ Y143) mutation to A: 4.5% of wild-type activity.
- D156 (= D174) mutation to A: 17.6 of wild-type activity.
- D190 (≠ E207) 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
>Pf1N1B4_5611 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_5611
MSQPKGLRPLDGITVISLEHAIAAPFCTRQLADLGARVIKVERPGTGDFARGYDQRVNGL
ASHFVWTNRSKESVTLDLKQDSATEVLDSLLATADVLVQNLAPGAAARMGLSFEALHQRF
PRLIVCDISGYGVGGPYEKKKAYDLLIQSEGGFLSVTGGPGEEEMAKAGCSIADIAAGMY
AYTAILSALLLRERTGEGSHLDVSMLESLVEWMNYPMYYAYDGAPPPPRAGAAHATIYPY
GPFPIGDGTTVMLGLQNEREWQLFCEKVLLAPELAKDERFSANFKRVENRHALRQLIVEA
FSTLNFDAVFDRLEHAQIANARVNDMQGVWDHPQLQARDRWREVETSAGSVPSLLPPGSN
SAFEPRMDAVPALGQHTEQVLRELGLGTDRIEQMRAAGAI
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