SitesBLAST
Comparing 3607893 FitnessBrowser__Dino:3607893 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)
8j78I Human 3-methylcrotonyl-coa carboxylase in bccp-h2 state
44% identity, 96% coverage: 4:640/661 of query aligns to 6:646/651 of 8j78I
8rthA Trypanosoma brucei 3-methylcrotonyl-coa carboxylase (see paper)
46% identity, 95% coverage: 2:630/661 of query aligns to 2:651/666 of 8rthA
P9WPQ3 Biotin-dependent 3-methylcrotonyl-coenzyme A carboxylase alpha1 subunit; EC 6.3.4.14 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
45% identity, 96% coverage: 1:634/661 of query aligns to 1:644/654 of P9WPQ3
- K322 (≠ P324) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7ybuA Human propionyl-coenzyme a carboxylase
40% identity, 97% coverage: 2:642/661 of query aligns to 5:669/670 of 7ybuA
P05165 Propionyl-CoA carboxylase alpha chain, mitochondrial; PCCase subunit alpha; Propanoyl-CoA:carbon dioxide ligase subunit alpha; EC 6.4.1.3 from Homo sapiens (Human) (see 6 papers)
40% identity, 97% coverage: 2:642/661 of query aligns to 63:727/728 of P05165
- A75 (= A14) to P: in PA-1; dbSNP:rs794727479
- R77 (= R16) to W: in PA-1; loss of function; dbSNP:rs141371306
- A138 (= A77) to T: in PA-1; loss of function; dbSNP:rs202247814
- I164 (= I103) to T: in PA-1; loss of function; dbSNP:rs202247815
- G197 (= G136) to E: in PA-1
- M229 (= M168) to K: in PA-1; dbSNP:rs375628794
- Q297 (= Q235) to R: in PA-1
- D368 (= D311) to G: in PA-1
- M373 (≠ Q316) to K: in PA-1; unstable protein; loss of function; dbSNP:rs121964958
- G379 (= G322) to V: in PA-1; dbSNP:rs794727087
- C398 (≠ A341) to R: in PA-1
- R399 (= R342) to Q: in PA-1; dbSNP:rs1301904623
- P423 (= P365) to L: in PA-1; dbSNP:rs1443858896
- L532 (vs. gap) natural variant: Missing (in PA-1)
- V551 (vs. gap) to F: in dbSNP:rs61749895
- W559 (≠ F481) to L: in PA-1; dbSNP:rs118169528
- G631 (= G553) to R: in PA-1; loss of function; dbSNP:rs796052018
- G668 (= G583) to R: in PA-1; loss of biotinylation; dbSNP:rs771438170
- K694 (= K609) modified: N6-biotinyllysine; by HLCS
- C712 (≠ V627) natural variant: Missing (in PA-1; loss of biotinylation)
Sites not aligning to the query:
- 1:52 modified: transit peptide, Mitochondrion
Q5LUF3 Propionyl-CoA carboxylase alpha chain; EC 6.4.1.3 from Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi) (see paper)
50% identity, 67% coverage: 1:446/661 of query aligns to 1:464/681 of Q5LUF3
- F348 (= F352) binding biotin
Sites not aligning to the query:
- 515 W→L: No effect on holoenzyme formation.
- 599 L→A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- 602 L→A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- 603 M→A: No effect on holoenzyme formation. Loss of holoenzyme formation; when associated with A-602 and A-603.
- 647 modified: N6-biotinyllysine
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
48% identity, 68% coverage: 1:447/661 of query aligns to 1:442/444 of 2vr1A
- active site: K116 (= K116), K159 (= K158), D194 (= D195), H207 (= H208), R233 (= R233), T272 (= T272), E274 (= E274), E286 (= E292), N288 (= N294), R290 (= R296), E294 (= E300), R336 (= R342)
- binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (= K158), R165 (≠ K166), M167 (= M168), Y201 (= Y202), L202 (≠ V203), E274 (= E274), L276 (≠ I276), E286 (= E292), N288 (= N294), I435 (≠ T440)
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
48% identity, 68% coverage: 1:447/661 of query aligns to 1:441/442 of 4mv4A
- active site: K116 (= K116), K159 (= K158), D193 (= D195), H206 (= H208), R232 (= R233), T271 (= T272), E273 (= E274), E285 (= E292), N287 (= N294), R289 (= R296), E293 (= E300), R335 (= R342)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K158), G164 (= G163), M166 (= M168), E198 (= E200), Y200 (= Y202), L201 (≠ V203), H233 (= H234), L275 (≠ I276), E285 (= E292)
- binding magnesium ion: E273 (= E274), E285 (= E292)
3n6rG Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
50% identity, 67% coverage: 2:446/661 of query aligns to 1:429/646 of 3n6rG
- active site: K115 (= K116), K157 (= K158), D180 (= D195), H193 (= H208), R219 (= R233), T258 (= T272), E260 (= E274), E273 (= E292), N275 (= N294), R277 (= R296), E281 (= E300), R323 (= R342)
Sites not aligning to the query:
4mv3A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and bicarbonate (see paper)
47% identity, 68% coverage: 1:447/661 of query aligns to 1:438/439 of 4mv3A
- active site: K116 (= K116), K159 (= K158), D190 (= D195), H203 (= H208), R229 (= R233), T268 (= T272), E270 (= E274), E282 (= E292), N284 (= N294), R286 (= R296), E290 (= E300), R332 (= R342)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K158), M163 (= M168), E195 (= E200), Y197 (= Y202), L198 (≠ V203), E270 (= E274), L272 (≠ I276), E282 (= E292)
- binding bicarbonate ion: R286 (= R296), Q288 (= Q298), V289 (= V299)
6oi8A Crystal structure of haemophilus influenzae biotin carboxylase complexed with 7-((1r,5s,6s)-6-amino-3-azabicyclo[3.1.0]hexan-3-yl)- 6-(2-chloro-6-(pyridin-3-yl)phenyl)pyrido[2,3-d]pyrimidin-2-amine (see paper)
47% identity, 68% coverage: 1:447/661 of query aligns to 1:439/440 of 6oi8A
- active site: K116 (= K116), K159 (= K158), D191 (= D195), H204 (= H208), R230 (= R233), T269 (= T272), E271 (= E274), E283 (= E292), N285 (= N294), R287 (= R296), E291 (= E300), R333 (= R342)
- binding 7-[(1R,5S,6s)-6-amino-3-azabicyclo[3.1.0]hexan-3-yl]-6-[2-chloro-6-(pyridin-3-yl)phenyl]pyrido[2,3-d]pyrimidin-2-amine: I157 (≠ L156), K159 (= K158), M164 (= M168), E196 (= E200), Y198 (= Y202), L199 (≠ V203), H204 (= H208), Q228 (= Q231), E271 (= E274), L273 (≠ I276), E283 (= E292), I432 (≠ T440)
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
47% identity, 67% coverage: 3:446/661 of query aligns to 1:443/448 of 2vpqB
- active site: V116 (≠ A118), K156 (= K158), H206 (= H208), R232 (= R233), T271 (= T272), E273 (= E274), E287 (= E292), N289 (= N294), R291 (= R296), E295 (= E300), R337 (= R342)
- binding phosphoaminophosphonic acid-adenylate ester: K114 (= K116), I154 (≠ L156), K156 (= K158), G161 (= G163), G163 (= G165), I166 (≠ M168), F200 (≠ Y202), I201 (≠ V203), E273 (= E274), I275 (= I276), M286 (= M291), E287 (= E292)
- binding magnesium ion: E273 (= E274), E287 (= E292)
6ojhA Crystal structure of haemophilus influenzae biotin carboxylase complexed with (r)-7-(3-aminopyrrolidin-1-yl)-6-(naphthalen-1-yl) pyrido[2,3-d]pyrimidin-2-amine
48% identity, 68% coverage: 1:447/661 of query aligns to 1:444/445 of 6ojhA
- active site: K116 (= K116), K159 (= K158), D196 (= D195), H209 (= H208), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E292), N290 (= N294), R292 (= R296), E296 (= E300), R338 (= R342)
- binding calcium ion: E276 (= E274), E288 (= E292), N290 (= N294)
- binding 7-[(3R)-3-aminopyrrolidin-1-yl]-6-(naphthalen-1-yl)pyrido[2,3-d]pyrimidin-2-amine: K159 (= K158), M169 (= M168), E201 (= E200), Y203 (= Y202), L204 (≠ V203), H236 (= H234), L278 (≠ I276), E288 (= E292), I437 (≠ T440)
P43873 Biotin carboxylase; Acetyl-coenzyme A carboxylase biotin carboxylase subunit A; EC 6.3.4.14 from Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) (see paper)
48% identity, 68% coverage: 1:447/661 of query aligns to 1:444/448 of P43873
- K116 (= K116) binding ATP
- K159 (= K158) binding ATP
- EKYL 201:204 (≠ EKYV 200:203) binding ATP
- E276 (= E274) binding ATP; binding Mg(2+)
- E288 (= E292) binding ATP; binding Mg(2+)
- N290 (= N294) binding Mg(2+)
3rupA Crystal structure of e.Coli biotin carboxylase in complex with two adp and two ca ions (see paper)
49% identity, 68% coverage: 1:447/661 of query aligns to 1:444/444 of 3rupA
- active site: K116 (= K116), K159 (= K158), D196 (= D195), H209 (= H208), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E292), N290 (= N294), R292 (= R296), E296 (= E300), R338 (= R342)
- binding adenosine-5'-diphosphate: Y82 (= Y82), G83 (= G83), K116 (= K116), K159 (= K158), G164 (= G163), G164 (= G163), G165 (= G164), G166 (= G165), R167 (≠ K166), M169 (= M168), F193 (= F192), E201 (= E200), K202 (= K201), Y203 (= Y202), L204 (≠ V203), H209 (= H208), Q233 (= Q231), H236 (= H234), K238 (= K236), L278 (≠ I276), E288 (= E292), R292 (= R296), V295 (= V299), E296 (= E300), R338 (= R342), D382 (= D385), I437 (≠ T440)
- binding calcium ion: E87 (= E87), E276 (= E274), E288 (= E292), E288 (= E292), N290 (= N294)
3g8cA Crystal structure of biotin carboxylase in complex with biotin, bicarbonate, adp and mg ion (see paper)
49% identity, 68% coverage: 1:447/661 of query aligns to 1:444/444 of 3g8cA
- active site: K116 (= K116), K159 (= K158), D196 (= D195), H209 (= H208), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E292), N290 (= N294), R292 (= R296), E296 (= E300), R338 (= R342)
- binding adenosine-5'-diphosphate: I157 (≠ L156), K159 (= K158), G164 (= G163), M169 (= M168), E201 (= E200), K202 (= K201), Y203 (= Y202), L204 (≠ V203), Q233 (= Q231), H236 (= H234), L278 (≠ I276), E288 (= E292), I437 (≠ T440)
- binding bicarbonate ion: K238 (= K236), R292 (= R296), Q294 (= Q298), V295 (= V299), E296 (= E300)
- binding biotin: Y82 (= Y82), F84 (= F84), R292 (= R296), V295 (= V299), R338 (= R342), D382 (= D385)
- binding magnesium ion: E276 (= E274), E288 (= E292)
3jzfB Crystal structure of biotin carboxylase from e. Coli in complex with benzimidazoles series (see paper)
49% identity, 68% coverage: 1:447/661 of query aligns to 3:446/447 of 3jzfB
- active site: K118 (= K116), K161 (= K158), D198 (= D195), H211 (= H208), R237 (= R233), T276 (= T272), E278 (= E274), E290 (= E292), N292 (= N294), R294 (= R296), E298 (= E300), R340 (= R342)
- binding 2-[(2-chlorobenzyl)amino]-1-(cyclohexylmethyl)-1H-benzimidazole-5-carboxamide: K118 (= K116), K161 (= K158), A162 (= A159), G166 (= G163), G168 (= G165), R169 (≠ K166), G170 (= G167), M171 (= M168), Y201 (≠ L198), E203 (= E200), K204 (= K201), Y205 (= Y202), H211 (= H208), H238 (= H234), L280 (≠ I276), I289 (≠ M291), E290 (= E292)
6oi9A Crystal structure of e. Coli biotin carboxylase complexed with 7-[3- (aminomethyl)pyrrolidin-1-yl]-6-(2,6-dichlorophenyl)pyrido[2,3- d]pyrimidin-2-amine (see paper)
49% identity, 68% coverage: 1:447/661 of query aligns to 1:444/446 of 6oi9A
- active site: E276 (= E274), E288 (= E292), N290 (= N294), E296 (= E300), R338 (= R342)
- binding 7-[(3S)-3-(aminomethyl)pyrrolidin-1-yl]-6-(2,6-dichlorophenyl)pyrido[2,3-d]pyrimidin-2-amine: K159 (= K158), M169 (= M168), E201 (= E200), Y203 (= Y202), L204 (≠ V203), H209 (= H208), Q233 (= Q231), H236 (= H234), E276 (= E274), L278 (≠ I276), E288 (= E292), I437 (≠ T440)
2w71A Crystal structure of biotin carboxylase from e. Coli in complex with the imidazole-pyrimidine inhibitor (see paper)
49% identity, 68% coverage: 1:447/661 of query aligns to 1:444/446 of 2w71A
- active site: K116 (= K116), K159 (= K158), D196 (= D195), H209 (= H208), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E292), N290 (= N294), R292 (= R296), E296 (= E300), R338 (= R342)
- binding 4-[1-(2,6-dichlorobenzyl)-2-methyl-1H-imidazol-4-yl]pyrimidin-2-amine: K159 (= K158), Y203 (= Y202), L204 (≠ V203), H209 (= H208), Q233 (= Q231), H236 (= H234), L278 (≠ I276), I437 (≠ T440)
2w70A Crystal structure of biotin carboxylase from e. Coli in complex with the amino-thiazole-pyrimidine fragment (see paper)
49% identity, 68% coverage: 1:447/661 of query aligns to 1:444/446 of 2w70A
- active site: K116 (= K116), K159 (= K158), D196 (= D195), H209 (= H208), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E292), N290 (= N294), R292 (= R296), E296 (= E300), R338 (= R342)
- binding 4-(2-amino-1,3-thiazol-4-yl)pyrimidin-2-amine: I157 (≠ L156), K159 (= K158), G166 (= G165), M169 (= M168), E201 (= E200), Y203 (= Y202), L204 (≠ V203), L278 (≠ I276)
Query Sequence
>3607893 FitnessBrowser__Dino:3607893
MFERILIANRGEIACRVIDTCRRLGVQTVAVHSDVDAGARHVAMADMAVNLGGAAPRDSY
LRGEAIIAAARATGAEAIHPGYGFLSENPDFVEAVAAAGLVFIGPSAAAIRAMGLKDAAK
ALMAEAGVPVVPGYQGADQDPARLAAEAEAIGYPVLIKAVAGGGGKGMRRVEGPEGFAGA
LEAARAEARGAFGNDHVLLEKYVATPRHIELQVFGDGARAVHLFERDCSLQRRHQKVIEE
APAPGMTPEMRAAMGAAAVRAAEAIGYAGAGTVEFIVDASDGLRPDRFWFMEMNTRLQVE
HPVTEAVTGVDLVAWQLRVASGEPLPARQEDLSLRGHAFEARLYAEDVPKGFLPATGRLT
HLAFPADARIETGVRAGDEISPWYDPMIAKLVVHGPTRQSALRKLDRVLAGCEVAGSVTN
LAFLRALARHGGFFAGEVDTGLIDREVETLSPAPVPCSRARALAALGAAGLHEGGPDGAG
FTLWAPLVQAQGLRFGEAEIEARIETRGAGSFRVGIGEATHEITRRGGAWWVDGAPTPAR
IVVHAAGVSVFWGNNYHFTAPDPLHRAGAAGPGAGHVEAPMPGLVKAVFVAPGDTVAQGA
RLAILEAMKMEHTLTAGRDGVVSEVLVAEGAQVSAGAPLILLAPDETPNERTDESPEEAA
E
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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