SitesBLAST
Comparing GFF2615 FitnessBrowser__psRCH2:GFF2615 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)
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
30% identity, 97% coverage: 9:398/401 of query aligns to 3:425/430 of 3ubmB
- active site: Q17 (≠ I23), E140 (≠ D145), D182 (= D175), G261 (≠ T237), G262 (vs. gap)
- binding coenzyme a: V16 (≠ A22), R38 (= R44), L72 (= L77), N73 (≠ D78), T74 (≠ V79), K75 (= K80), N96 (= N101), F97 (≠ L102), R98 (≠ A103), A101 (= A106), R104 (= R109), K125 (≠ S130), D182 (= D175), M213 (= M206)
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
30% identity, 98% coverage: 9:401/401 of query aligns to 2:427/427 of 2vjoA
- active site: A16 (≠ I23), E139 (≠ D145), D168 (= D175), G259 (≠ T237), G260 (≠ I238)
- binding coenzyme a: H14 (= H21), A16 (≠ I23), A17 (= A24), R37 (= R44), L71 (= L77), M73 (≠ V79), N95 (= N101), F96 (≠ L102), G97 (≠ A103), R103 (= R109), M104 (= M110), K136 (= K142), V137 (≠ A143), Y138 (= Y144), D168 (= D175), M199 (= M206)
- binding oxalate ion: G257 (≠ H235), G259 (≠ T237), Q261 (≠ Y239)
1p5rA Formyl-coa transferase in complex with coenzyme a (see paper)
30% identity, 98% coverage: 9:401/401 of query aligns to 2:427/427 of 1p5rA
- active site: Q16 (≠ I23), E139 (≠ D145), D168 (= D175), G259 (≠ T237), G260 (≠ I238)
- binding coenzyme a: H14 (= H21), V15 (≠ A22), Q16 (≠ I23), A17 (= A24), R37 (= R44), M73 (≠ V79), K74 (= K80), N95 (= N101), F96 (≠ L102), A100 (= A106), R103 (= R109), K136 (= K142), V137 (≠ A143), D168 (= D175), M199 (= M206)
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
30% identity, 98% coverage: 9:401/401 of query aligns to 3:428/428 of O06644
- Q17 (≠ I23) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (= R44) binding
- W48 (≠ Y54) 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 (= R109) binding
- D169 (= D175) 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 (≠ A236) mutation to A: 2.5-fold decrease of the catalytic effiency.
- G260 (≠ T237) 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)
30% identity, 98% coverage: 9:401/401 of query aligns to 2:427/427 of 2vjkA
- active site: Q16 (≠ I23), E139 (≠ D145), D168 (= D175), G259 (≠ T237), G260 (≠ I238)
- binding coenzyme a: H14 (= H21), Q16 (≠ I23), A17 (= A24), R37 (= R44), M73 (≠ V79), K74 (= K80), N95 (= N101), F96 (≠ L102), G97 (≠ A103), R103 (= R109), M104 (= M110), K136 (= K142), V137 (≠ A143), Y138 (= Y144), D168 (= D175), M199 (= M206)
- binding magnesium ion: D293 (= D267), D296 (≠ L271)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
30% identity, 98% coverage: 9:401/401 of query aligns to 2:427/427 of 1t4cA
- active site: Q16 (≠ I23), E139 (≠ D145), D168 (= D175), G259 (≠ T237), G260 (≠ I238)
- binding coenzyme a: H14 (= H21), V15 (≠ A22), Q16 (≠ I23), R37 (= R44), M73 (≠ V79), N95 (= N101), F96 (≠ L102), R103 (= R109), M104 (= M110), V137 (≠ A143), Y138 (= Y144), D168 (= D175), M199 (= M206)
- binding oxalic acid: G259 (≠ T237), G260 (≠ I238)
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
30% identity, 98% coverage: 9:401/401 of query aligns to 2:427/427 of 1t3zA
- active site: Q16 (≠ I23), E139 (≠ D145), S168 (≠ C171), G259 (≠ T237), G260 (≠ I238)
- binding oxidized coenzyme a: H14 (= H21), V15 (≠ A22), A17 (= A24), R37 (= R44), K74 (= K80), N95 (= N101), F96 (≠ L102), A100 (= A106), R103 (= R109), M104 (= M110), K136 (= K142), V137 (≠ A143), Y138 (= Y144), E139 (≠ D145), M199 (= M206)
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, 98% coverage: 10:401/401 of query aligns to 4:416/416 of P69902
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
32% identity, 98% coverage: 10:401/401 of query aligns to 4:416/417 of 1q6yA
- active site: Q17 (≠ I23), E140 (≠ D145), D169 (= D175), G248 (≠ T237), G249 (vs. gap)
- binding coenzyme a: V16 (≠ A22), Q17 (≠ I23), S18 (≠ A24), R38 (= R44), L72 (= L77), N73 (≠ D78), T74 (≠ V79), K75 (= K80), N96 (= N101), F97 (≠ L102), H98 (≠ A103), M105 (= M110), I124 (= I129), K137 (= K142), A138 (= A143), Y139 (= Y144), D169 (= D175), M200 (= M206)
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
32% identity, 98% coverage: 10:401/401 of query aligns to 3:415/415 of 1pt5A
- active site: Q16 (≠ I23), E139 (≠ D145), D168 (= D175), G247 (≠ T237), G248 (vs. gap)
- binding acetyl coenzyme *a: V15 (≠ A22), S17 (≠ A24), R37 (= R44), L71 (= L77), N72 (≠ D78), T73 (≠ V79), K74 (= K80), N95 (= N101), F96 (≠ L102), H97 (≠ A103), K124 (≠ S130), K136 (= K142), A137 (= A143), Y138 (= Y144), E139 (≠ D145), D168 (= D175), M199 (= M206)
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
31% identity, 98% coverage: 10:401/401 of query aligns to 4:409/410 of 1q7eA
- active site: Q17 (≠ I23), E133 (≠ D145), D162 (= D175), G241 (≠ T237), G242 (vs. gap)
- binding methionine: N96 (= N101), F97 (≠ L102), H98 (≠ A103), P99 (= P104), K118 (≠ S130), K130 (= K142), A131 (= A143), W246 (vs. gap), F299 (≠ T292), A303 (= A296), E306 (≠ V299)
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
30% identity, 93% coverage: 9:382/401 of query aligns to 4:360/360 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, 98% coverage: 11:401/401 of query aligns to 3:373/382 of Q9UHK6
- V9 (= V17) to M: in dbSNP:rs3195676
- S52 (= S74) to P: in AMACRD and CBAS4; inactive enzyme; dbSNP:rs121917814
- L107 (≠ I129) to P: in CBAS4; inactive enzyme; dbSNP:rs121917816
- G175 (= G197) to D: in dbSNP:rs10941112
- L201 (≠ K223) to S: in dbSNP:rs2287939
- M261 (≠ S288) to T: in dbSNP:rs3195678
- E277 (≠ R304) 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)
26% identity, 97% coverage: 10:399/401 of query aligns to 8:396/402 of 1xvtA
- active site: I21 (= I23), N138 (≠ D145), D166 (= D175), G225 (≠ A234), K226 (≠ H235)
- binding coenzyme a: I21 (= I23), A22 (= A24), N42 (≠ R44), L68 (= L77), N69 (≠ D78), F71 (≠ K80), S93 (≠ L102), K94 (≠ A103), R100 (= R109), R101 (≠ M110), P135 (≠ K142), A136 (= A143), D166 (= D175), M197 (= M206)
P31572 L-carnitine CoA-transferase; Crotonobetainyl-CoA:carnitine CoA-transferase; EC 2.8.3.21 from Escherichia coli (strain K12) (see paper)
26% identity, 97% coverage: 10:399/401 of query aligns to 11:399/405 of P31572
- K97 (≠ A103) binding
- R104 (≠ M110) binding
1xvvA Crystal structure of caib mutant d169a in complex with carnitinyl-coa (see paper)
25% identity, 97% coverage: 10:399/401 of query aligns to 8:396/402 of 1xvvA
- active site: I21 (= I23), N138 (≠ D145), A166 (= A174), G225 (≠ A234), K226 (≠ H235)
- binding l-carnitinyl-coa inner salt: I19 (≠ H21), E20 (≠ A22), I21 (= I23), A22 (= A24), N69 (≠ D78), F71 (≠ K80), A92 (≠ N101), S93 (≠ L102), K94 (≠ A103), R100 (= R109), R101 (≠ M110), A136 (= A143), Y137 (= Y144), N138 (≠ D145), Y163 (≠ C171)
O06543 Alpha-methylacyl-CoA racemase; AMACR; MtMCR; EC 5.1.99.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
31% identity, 50% coverage: 10:208/401 of query aligns to 4:190/360 of O06543
- R38 (= R44) binding
- R52 (≠ T68) mutation to A: 15.7% of wild-type activity.
- I56 (≠ S74) mutation to P: 28.8% of wild-type activity.
- ADLK 59:62 (≠ LDVK 77:80) binding
- E82 (≠ Q100) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NLA 101:103) binding
- R91 (= R109) binding ; mutation to A: 19.9% of wild-type activity.
- M111 (≠ I129) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ AYDLLI 143:148) binding
- H126 (≠ Y144) mutation to A: 4.5% of wild-type activity.
- D156 (= D175) mutation to A: 17.6 of wild-type activity.
- D190 (≠ E208) 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.
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)
30% identity, 50% coverage: 10:208/401 of query aligns to 3:184/354 of 2gd6A
- active site: G16 (≠ I23), D121 (= D145), D150 (= D175)
- binding acetyl coenzyme *a: I15 (≠ A22), R37 (= R44), A53 (≠ L77), D54 (= D78), L55 (≠ V79), K56 (= K80), G77 (≠ N101), Y78 (≠ L102), R79 (≠ A103), V82 (≠ A106), R85 (= R109), G119 (≠ A143), H120 (≠ Y144), Y124 (≠ I148), D150 (= D175), M182 (= M206)
Sites not aligning to the query:
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)
30% identity, 50% coverage: 10:208/401 of query aligns to 3:184/354 of 2gd2A
- active site: G16 (≠ I23), D121 (= D145), D150 (= D175)
- binding acetoacetyl-coenzyme a: I15 (≠ A22), R37 (= R44), A53 (≠ L77), L55 (≠ V79), K56 (= K80), G77 (≠ N101), Y78 (≠ L102), R79 (≠ A103), V82 (≠ A106), R85 (= R109), L86 (≠ M110), A118 (≠ K142), G119 (≠ A143), H120 (≠ Y144), Y124 (≠ I148), D150 (= D175)
Sites not aligning to the query:
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)
30% identity, 50% coverage: 10:208/401 of query aligns to 3:184/354 of 2gd0A
- active site: G16 (≠ I23), D121 (= D145), D150 (= D175)
- binding (s)-2-methylmyristoyl-coenzyme a: D42 (= D49), L55 (≠ V79), K56 (= K80), G77 (≠ N101), Y78 (≠ L102), R79 (≠ A103), V82 (≠ A106), R85 (= R109), L86 (≠ M110), G119 (≠ A143), H120 (≠ Y144), D121 (= D145), Y124 (≠ I148), D150 (= D175)
Sites not aligning to the query:
Query Sequence
>GFF2615 FitnessBrowser__psRCH2:GFF2615
MNKSQAKPRPLDGITVVSLEHAIAAPFCTRQLADLGARVIKVERPGAGDFARGYDERVDG
LASHFVWTNRSKESLTLDVKQDAAARVLDQLLAGADVLVQNLAPGAAARMGLSFDALHER
FPRLIVCDISGYGEGGPYEQKKAYDLLIQSEGGFLSVTGGPGETEMAKAGCSIADIAAGM
YAYTGVLSALMLRDKTGEGSRVDVSMLESLVEWMGYPLYYAYKGATPPPRAGAAHATIYP
YGPFPTGDGGTVMLGLQNEREWLAFCDKVLLQPELAQDERFSSNARRSEHRTELRALIVE
AFSRLSAEEVIARLDAAPIANAHVNDMAGVWAHPQLKARQRWSEVDSPAGRLPALLPPGR
NSAFAPRMDPIPALGQHTDSLLAELGYAPGDIQRLHEQGAV
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