SitesBLAST
Comparing N515DRAFT_0927 FitnessBrowser__Dyella79:N515DRAFT_0927 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)
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, 100% coverage: 1:663/665 of query aligns to 1:652/654 of P9WPQ3
- K322 (≠ A320) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
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)
43% identity, 100% coverage: 1:663/665 of query aligns to 1:680/681 of Q5LUF3
- F348 (= F348) binding
- W515 (≠ G502) mutation to L: No effect on holoenzyme formation.
- L599 (≠ A582) mutation to A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- L602 (≠ F585) mutation to A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- M603 (≠ A586) mutation to A: No effect on holoenzyme formation. Loss of holoenzyme formation; when associated with A-602 and A-603.
- K647 (= K630) modified: N6-biotinyllysine
7ybuA Human propionyl-coenzyme a carboxylase
41% identity, 100% coverage: 2:663/665 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)
41% identity, 100% coverage: 2:663/665 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 (= Q236) to R: in PA-1
- D368 (= D307) to G: in PA-1
- M373 (≠ Q312) to K: in PA-1; unstable protein; loss of function; dbSNP:rs121964958
- G379 (= G318) to V: in PA-1; dbSNP:rs794727087
- C398 (≠ V337) to R: in PA-1
- R399 (= R338) to Q: in PA-1; dbSNP:rs1301904623
- P423 (= P361) to L: in PA-1; dbSNP:rs1443858896
- L532 (= L470) natural variant: Missing (in PA-1)
- V551 (≠ W490) to F: in dbSNP:rs61749895
- W559 (= W496) to L: in PA-1; dbSNP:rs118169528
- G631 (≠ A562) to R: in PA-1; loss of function; dbSNP:rs796052018
- G668 (= G604) to R: in PA-1; loss of biotinylation; dbSNP:rs771438170
- K694 (= K630) modified: N6-biotinyllysine; by HLCS
- C712 (≠ A648) natural variant: Missing (in PA-1; loss of biotinylation)
Sites not aligning to the query:
- 1:52 modified: transit peptide, Mitochondrion
8sgxX Leishmania tarentolae propionyl-coa carboxylase (alpha-4-beta-6) (see paper)
40% identity, 99% coverage: 5:663/665 of query aligns to 1:656/657 of 8sgxX
3n6rG Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
42% identity, 100% coverage: 2:663/665 of query aligns to 1:645/646 of 3n6rG
- active site: K115 (= K116), K157 (= K158), D180 (≠ T195), H193 (= H208), R219 (= R234), T258 (= T273), E260 (= E275), E273 (= E288), N275 (= N290), R277 (= R292), E281 (= E296), R323 (= R338), G519 (= G544)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: M611 (= M629), K612 (= K630)
7kctA Crystal structure of the hydrogenobacter thermophilus 2-oxoglutarate carboxylase (ogc) biotin carboxylase (bc) domain dimer in complex with adenosine 5'-diphosphate magnesium salt (mgadp), adenosine 5'- diphosphate (adp, and bicarbonate anion (hydrogen carbonate/hco3-) (see paper)
48% identity, 67% coverage: 1:445/665 of query aligns to 3:445/453 of 7kctA
- active site: E276 (= E275), E289 (= E288), N291 (= N290), E297 (= E296), R339 (= R338)
- binding adenosine-5'-diphosphate: K117 (= K116), L157 (≠ M156), K159 (= K158), G164 (= G163), G165 (= G164), G166 (= G165), I169 (≠ M168), E201 (= E200), Y203 (= Y202), I204 (≠ V203), H209 (= H208), Q233 (= Q232), Q237 (= Q236), K238 (= K237), I278 (= I277), E289 (= E288), R293 (= R292), Q295 (= Q294), V296 (= V295), E297 (= E296), R339 (= R338)
- binding bicarbonate ion: D116 (≠ S115), R119 (≠ A118)
- binding magnesium ion: E276 (= E275), E289 (= E288)
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
47% identity, 67% coverage: 3:445/665 of query aligns to 1:443/448 of 2vpqB
- active site: V116 (≠ A118), K156 (= K158), H206 (= H208), R232 (= R234), T271 (= T273), E273 (= E275), E287 (= E288), N289 (= N290), R291 (= R292), E295 (= E296), R337 (= R338)
- binding phosphoaminophosphonic acid-adenylate ester: K114 (= K116), I154 (≠ M156), K156 (= K158), G161 (= G163), G163 (= G165), I166 (≠ M168), F200 (≠ Y202), I201 (≠ V203), E273 (= E275), I275 (= I277), M286 (= M287), E287 (= E288)
- binding magnesium ion: E273 (= E275), E287 (= E288)
8hz4A The tetrameric structure of biotin carboxylase from chloroflexus aurantiacus in complex with bicarbonate
49% identity, 68% coverage: 1:449/665 of query aligns to 1:444/456 of 8hz4A
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
46% identity, 67% coverage: 1:446/665 of query aligns to 1:442/444 of 2vr1A
- active site: K116 (= K116), K159 (= K158), D194 (≠ T195), H207 (= H208), R233 (= R234), T272 (= T273), E274 (= E275), E286 (= E288), N288 (= N290), R290 (= R292), E294 (= E296), R336 (= R338)
- binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (= K158), R165 (≠ K166), M167 (= M168), Y201 (= Y202), L202 (≠ V203), E274 (= E275), L276 (≠ I277), E286 (= E288), N288 (= N290), I435 (≠ T439)
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
47% identity, 67% coverage: 1:446/665 of query aligns to 1:441/442 of 4mv4A
- active site: K116 (= K116), K159 (= K158), D193 (≠ T195), H206 (= H208), R232 (= R234), T271 (= T273), E273 (= E275), E285 (= E288), N287 (= N290), R289 (= R292), E293 (= E296), R335 (= R338)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K158), G164 (= G163), M166 (= M168), E198 (= E200), Y200 (= Y202), L201 (≠ V203), H233 (≠ Y235), L275 (≠ I277), E285 (= E288)
- binding magnesium ion: E273 (= E275), E285 (= E288)
3rupA Crystal structure of e.Coli biotin carboxylase in complex with two adp and two ca ions (see paper)
46% identity, 67% coverage: 1:446/665 of query aligns to 1:444/444 of 3rupA
- active site: K116 (= K116), K159 (= K158), D196 (≠ T195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R338)
- 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 (≠ R201), Y203 (= Y202), L204 (≠ V203), H209 (= H208), Q233 (= Q232), H236 (≠ Y235), K238 (= K237), L278 (≠ I277), E288 (= E288), R292 (= R292), V295 (= V295), E296 (= E296), R338 (= R338), D382 (= D384), I437 (≠ T439)
- binding calcium ion: E87 (= E87), E276 (= E275), E288 (= E288), E288 (= E288), N290 (= N290)
3g8cA Crystal structure of biotin carboxylase in complex with biotin, bicarbonate, adp and mg ion (see paper)
46% identity, 67% coverage: 1:446/665 of query aligns to 1:444/444 of 3g8cA
- active site: K116 (= K116), K159 (= K158), D196 (≠ T195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R338)
- binding adenosine-5'-diphosphate: I157 (≠ M156), K159 (= K158), G164 (= G163), M169 (= M168), E201 (= E200), K202 (≠ R201), Y203 (= Y202), L204 (≠ V203), Q233 (= Q232), H236 (≠ Y235), L278 (≠ I277), E288 (= E288), I437 (≠ T439)
- binding bicarbonate ion: K238 (= K237), R292 (= R292), Q294 (= Q294), V295 (= V295), E296 (= E296)
- binding biotin: Y82 (= Y82), F84 (= F84), R292 (= R292), V295 (= V295), R338 (= R338), D382 (= D384)
- binding magnesium ion: E276 (= E275), E288 (= E288)
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)
46% identity, 67% coverage: 1:446/665 of query aligns to 1:444/446 of 6oi9A
- active site: E276 (= E275), E288 (= E288), N290 (= N290), E296 (= E296), R338 (= R338)
- 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 (= Q232), H236 (≠ Y235), E276 (= E275), L278 (≠ I277), E288 (= E288), I437 (≠ T439)
2w71A Crystal structure of biotin carboxylase from e. Coli in complex with the imidazole-pyrimidine inhibitor (see paper)
46% identity, 67% coverage: 1:446/665 of query aligns to 1:444/446 of 2w71A
- active site: K116 (= K116), K159 (= K158), D196 (≠ T195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R338)
- binding 4-[1-(2,6-dichlorobenzyl)-2-methyl-1H-imidazol-4-yl]pyrimidin-2-amine: K159 (= K158), Y203 (= Y202), L204 (≠ V203), H209 (= H208), Q233 (= Q232), H236 (≠ Y235), L278 (≠ I277), I437 (≠ T439)
2w70A Crystal structure of biotin carboxylase from e. Coli in complex with the amino-thiazole-pyrimidine fragment (see paper)
46% identity, 67% coverage: 1:446/665 of query aligns to 1:444/446 of 2w70A
- active site: K116 (= K116), K159 (= K158), D196 (≠ T195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R338)
- binding 4-(2-amino-1,3-thiazol-4-yl)pyrimidin-2-amine: I157 (≠ M156), K159 (= K158), G166 (= G165), M169 (= M168), E201 (= E200), Y203 (= Y202), L204 (≠ V203), L278 (≠ I277)
2w6zA Crystal structure of biotin carboxylase from e. Coli in complex with the 3-(3-methyl-but-2-enyl)-3h-purin-6-ylamine fragment (see paper)
46% identity, 67% coverage: 1:446/665 of query aligns to 1:444/446 of 2w6zA
- active site: K116 (= K116), K159 (= K158), D196 (≠ T195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R338)
- binding 3-(3-methylbut-2-en-1-yl)-3H-purin-6-amine: K159 (= K158), Y203 (= Y202), L204 (≠ V203), L278 (≠ I277)
2w6qA Crystal structure of biotin carboxylase from e. Coli in complex with the triazine-2,4-diamine fragment (see paper)
46% identity, 67% coverage: 1:446/665 of query aligns to 1:444/446 of 2w6qA
- active site: K116 (= K116), K159 (= K158), D196 (≠ T195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R338)
- binding 6-(2-phenoxyethoxy)-1,3,5-triazine-2,4-diamine: I157 (≠ M156), K159 (= K158), E201 (= E200), K202 (≠ R201), Y203 (= Y202), L204 (≠ V203), H236 (≠ Y235), L278 (≠ I277)
2w6pA Crystal structure of biotin carboxylase from e. Coli in complex with 5-methyl-6-phenyl-quinazoline-2,4-diamine (see paper)
46% identity, 67% coverage: 1:446/665 of query aligns to 1:444/446 of 2w6pA
- active site: K116 (= K116), K159 (= K158), D196 (≠ T195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R338)
- binding 5-methyl-6-phenylquinazoline-2,4-diamine: K159 (= K158), Y203 (= Y202), L204 (≠ V203), Q233 (= Q232), H236 (≠ Y235), L278 (≠ I277), I437 (≠ T439)
2w6mA Crystal structure of biotin carboxylase from e. Coli in complex with amino-oxazole fragment series (see paper)
46% identity, 67% coverage: 1:446/665 of query aligns to 1:444/446 of 2w6mA
- active site: K116 (= K116), K159 (= K158), D196 (≠ T195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R338)
- binding (2-amino-1,3-oxazol-5-yl)-(3-bromophenyl)methanone: I157 (≠ M156), K159 (= K158), M169 (= M168), E201 (= E200), K202 (≠ R201), Y203 (= Y202), H236 (≠ Y235), L278 (≠ I277), I437 (≠ T439)
Query Sequence
>N515DRAFT_0927 FitnessBrowser__Dyella79:N515DRAFT_0927
MFERVLIANRGEIACRVIRTCRRLGIRTIAVYSEADADAQHVRLADEAWPIGGPRPADSY
LRGETILEVARRSGAQAIHPGYGFLSENTAFARACTEAGIAFIGPRPASIDAMGSKAAAK
ALMEKHAVPLVPGYHGDNQDADFLAGQARSTGFPLMIKAAAGGGGKGMRIVRAEREFADA
LASAQREAANAFGDTRVILERYVEHPRHIEFQVFGDTHGNVIHLNERECSAQRRYQKVLE
ETPSPFLTPARRAAMGAAAVAAARAVDYVGAGTVEFIVGQDGEFFFMEMNTRLQVEHPVT
EETLGLDLVEWQLRVAAGEALPLRQEDVHAQGHAIEVRLYAEDPEQNFLPGSGKLLRLRL
PETSRHVRLDGGVIEGDTVTIFYDPMIAKLIVHDRDRAQALQRLREALMACEIAGPKSNI
AFLERLVRHPVVVEGRIDTGYLDRHLDEFLAGDAAPAPQLLFAAAVAALLHDERTVVAQA
AHGVDPHSPWARADAWRIGHAGKRIVALSLREQRYEVEAHGHDGDYQLCHGDASCHVQGA
RHDGAALSARFDGQSLRLPLHADAQRVLLHDSDGRRHSFARAAAFAWEARQGAGGNQVLA
PMPGRIVLVKARPGDQVEEGQELLVMEAMKMELALKAPRAGTIDSIGATQGDFVEADAVL
VRFAT
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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