SitesBLAST
Comparing WP_024328274.1 NCBI__GCF_001995255.1:WP_024328274.1 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)
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
68% identity, 99% coverage: 1:444/447 of query aligns to 1:441/442 of 4mv4A
- active site: K116 (= K116), K159 (= K159), D193 (= D196), H206 (= H209), R232 (= R235), T271 (= T274), E273 (= E276), E285 (= E288), N287 (= N290), R289 (= R292), E293 (= E296), R335 (= R338)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K159), G164 (= G164), M166 (= M169), E198 (= E201), Y200 (≠ F203), L201 (= L204), H233 (= H236), L275 (= L278), E285 (= E288)
- binding magnesium ion: E273 (= E276), E285 (= E288)
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
68% identity, 99% coverage: 1:444/447 of query aligns to 1:442/444 of 2vr1A
- active site: K116 (= K116), K159 (= K159), D194 (= D196), H207 (= H209), R233 (= R235), T272 (= T274), E274 (= E276), E286 (= E288), N288 (= N290), R290 (= R292), E294 (= E296), R336 (= R338)
- binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (= K159), R165 (= R167), M167 (= M169), Y201 (≠ F203), L202 (= L204), E274 (= E276), L276 (= L278), E286 (= E288), N288 (= N290), I435 (= I437)
4mv3A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and bicarbonate (see paper)
67% identity, 99% coverage: 1:444/447 of query aligns to 1:438/439 of 4mv3A
- active site: K116 (= K116), K159 (= K159), D190 (= D196), H203 (= H209), R229 (= R235), T268 (= T274), E270 (= E276), E282 (= E288), N284 (= N290), R286 (= R292), E290 (= E296), R332 (= R338)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K159), M163 (= M169), E195 (= E201), Y197 (≠ F203), L198 (= L204), E270 (= E276), L272 (= L278), E282 (= E288)
- binding bicarbonate ion: R286 (= R292), Q288 (= Q294), V289 (= V295)
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)
67% identity, 99% coverage: 1:444/447 of query aligns to 1:439/440 of 6oi8A
- active site: K116 (= K116), K159 (= K159), D191 (= D196), H204 (= H209), R230 (= R235), T269 (= T274), E271 (= E276), E283 (= E288), N285 (= N290), R287 (= R292), E291 (= E296), R333 (= R338)
- 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 (= I157), K159 (= K159), M164 (= M169), E196 (= E201), Y198 (≠ F203), L199 (= L204), H204 (= H209), Q228 (= Q233), E271 (= E276), L273 (= L278), E283 (= E288), I432 (= I437)
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)
68% identity, 99% coverage: 1:444/447 of query aligns to 1:444/448 of P43873
- K116 (= K116) binding ATP
- K159 (= K159) binding ATP
- EKYL 201:204 (≠ EKFL 201:204) binding ATP
- E276 (= E276) binding ATP; binding Mg(2+)
- E288 (= E288) binding ATP; binding Mg(2+)
- N290 (= N290) binding Mg(2+)
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
68% identity, 99% coverage: 1:444/447 of query aligns to 1:444/445 of 6ojhA
- active site: K116 (= K116), K159 (= K159), D196 (= D196), H209 (= H209), R235 (= R235), T274 (= T274), E276 (= E276), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R338)
- binding calcium ion: E276 (= E276), E288 (= E288), N290 (= N290)
- binding 7-[(3R)-3-aminopyrrolidin-1-yl]-6-(naphthalen-1-yl)pyrido[2,3-d]pyrimidin-2-amine: K159 (= K159), M169 (= M169), E201 (= E201), Y203 (≠ F203), L204 (= L204), H236 (= H236), L278 (= L278), E288 (= E288), I437 (= I437)
4mv1A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with adp and phosphate (see paper)
67% identity, 99% coverage: 1:444/447 of query aligns to 1:430/430 of 4mv1A
- active site: K116 (= K116), K159 (= K159), D182 (= D196), H195 (= H209), R221 (= R235), T260 (= T274), E262 (= E276), E274 (= E288), N276 (= N290), R278 (= R292), E282 (= E296), R324 (= R338)
- binding adenosine-5'-diphosphate: K159 (= K159), E187 (= E201), K188 (= K202), Y189 (≠ F203), L190 (= L204), L264 (= L278)
- binding phosphate ion: K224 (= K238), R278 (= R292), Q280 (= Q294), V281 (= V295), E282 (= E296)
P24182 Biotin carboxylase; Acetyl-coenzyme A carboxylase biotin carboxylase subunit A; EC 6.3.4.14 from Escherichia coli (strain K12) (see 3 papers)
68% identity, 99% coverage: 1:444/447 of query aligns to 1:444/449 of P24182
- R19 (= R19) mutation to E: Loss of homodimerization. No effect on ATP binding.
- E23 (= E23) mutation to R: Loss of homodimerization. No effect on ATP binding.
- K116 (= K116) binding ATP
- K159 (= K159) binding ATP
- GG 165:166 (= GG 165:166) binding ATP
- EKYL 201:204 (≠ EKFL 201:204) binding ATP
- H209 (= H209) binding ATP
- H236 (= H236) binding ATP
- K238 (= K238) binding hydrogencarbonate
- E276 (= E276) binding ATP; binding Mg(2+)
- E288 (= E288) binding ATP; binding Mg(2+)
- R292 (= R292) active site; binding hydrogencarbonate
- V295 (= V295) binding hydrogencarbonate
- E296 (= E296) mutation to A: Severe reduction in catalytic activity.
- R338 (= R338) binding biotin; binding hydrogencarbonate; mutation to A: Severe reduction in catalytic activity.
- F363 (≠ P363) mutation to A: Loss of homodimerization. No effect on ATP binding.
- R366 (= R366) mutation to E: Loss of homodimerization. No effect on ATP binding.
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)
68% identity, 99% coverage: 1:444/447 of query aligns to 1:444/446 of 6oi9A
- active site: E276 (= E276), 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 (= K159), M169 (= M169), E201 (= E201), Y203 (≠ F203), L204 (= L204), H209 (= H209), Q233 (= Q233), H236 (= H236), E276 (= E276), L278 (= L278), E288 (= E288), I437 (= I437)
2w71A Crystal structure of biotin carboxylase from e. Coli in complex with the imidazole-pyrimidine inhibitor (see paper)
68% identity, 99% coverage: 1:444/447 of query aligns to 1:444/446 of 2w71A
- active site: K116 (= K116), K159 (= K159), D196 (= D196), H209 (= H209), R235 (= R235), T274 (= T274), E276 (= E276), 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 (= K159), Y203 (≠ F203), L204 (= L204), H209 (= H209), Q233 (= Q233), H236 (= H236), L278 (= L278), I437 (= I437)
2w70A Crystal structure of biotin carboxylase from e. Coli in complex with the amino-thiazole-pyrimidine fragment (see paper)
68% identity, 99% coverage: 1:444/447 of query aligns to 1:444/446 of 2w70A
- active site: K116 (= K116), K159 (= K159), D196 (= D196), H209 (= H209), R235 (= R235), T274 (= T274), E276 (= E276), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R338)
- binding 4-(2-amino-1,3-thiazol-4-yl)pyrimidin-2-amine: I157 (= I157), K159 (= K159), G166 (= G166), M169 (= M169), E201 (= E201), Y203 (≠ F203), L204 (= L204), L278 (= L278)
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)
68% identity, 99% coverage: 1:444/447 of query aligns to 1:444/446 of 2w6zA
- active site: K116 (= K116), K159 (= K159), D196 (= D196), H209 (= H209), R235 (= R235), T274 (= T274), E276 (= E276), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R338)
- binding 3-(3-methylbut-2-en-1-yl)-3H-purin-6-amine: K159 (= K159), Y203 (≠ F203), L204 (= L204), L278 (= L278)
2w6qA Crystal structure of biotin carboxylase from e. Coli in complex with the triazine-2,4-diamine fragment (see paper)
68% identity, 99% coverage: 1:444/447 of query aligns to 1:444/446 of 2w6qA
- active site: K116 (= K116), K159 (= K159), D196 (= D196), H209 (= H209), R235 (= R235), T274 (= T274), E276 (= E276), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R338)
- binding 6-(2-phenoxyethoxy)-1,3,5-triazine-2,4-diamine: I157 (= I157), K159 (= K159), E201 (= E201), K202 (= K202), Y203 (≠ F203), L204 (= L204), H236 (= H236), L278 (= L278)
2w6pA Crystal structure of biotin carboxylase from e. Coli in complex with 5-methyl-6-phenyl-quinazoline-2,4-diamine (see paper)
68% identity, 99% coverage: 1:444/447 of query aligns to 1:444/446 of 2w6pA
- active site: K116 (= K116), K159 (= K159), D196 (= D196), H209 (= H209), R235 (= R235), T274 (= T274), E276 (= E276), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R338)
- binding 5-methyl-6-phenylquinazoline-2,4-diamine: K159 (= K159), Y203 (≠ F203), L204 (= L204), Q233 (= Q233), H236 (= H236), L278 (= L278), I437 (= I437)
2w6mA Crystal structure of biotin carboxylase from e. Coli in complex with amino-oxazole fragment series (see paper)
68% identity, 99% coverage: 1:444/447 of query aligns to 1:444/446 of 2w6mA
- active site: K116 (= K116), K159 (= K159), D196 (= D196), H209 (= H209), R235 (= R235), T274 (= T274), E276 (= E276), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R338)
- binding (2-amino-1,3-oxazol-5-yl)-(3-bromophenyl)methanone: I157 (= I157), K159 (= K159), M169 (= M169), E201 (= E201), K202 (= K202), Y203 (≠ F203), H236 (= H236), L278 (= L278), I437 (= I437)
2v5aA Crystal structure of biotin carboxylase from e.Coli in complex with potent inhibitor 3 (see paper)
68% identity, 99% coverage: 1:444/447 of query aligns to 1:444/446 of 2v5aA
- active site: K116 (= K116), K159 (= K159), D196 (= D196), H209 (= H209), R235 (= R235), T274 (= T274), E276 (= E276), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R338)
- binding 7-(2,5-dihydropyrrol-1-yl)-6-phenyl-pyrido[6,5-d]pyrimidin-2-amine: I157 (= I157), K159 (= K159), M169 (= M169), E201 (= E201), Y203 (≠ F203), L204 (= L204), Q233 (= Q233), H236 (= H236), L278 (= L278), I437 (= I437)
2v58A Crystal structure of biotin carboxylase from e.Coli in complex with potent inhibitor 1 (see paper)
68% identity, 99% coverage: 1:444/447 of query aligns to 1:444/446 of 2v58A
- active site: K116 (= K116), K159 (= K159), D196 (= D196), H209 (= H209), R235 (= R235), T274 (= T274), E276 (= E276), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R338)
- binding 6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine: I157 (= I157), K159 (= K159), E201 (= E201), Y203 (≠ F203), L204 (= L204), H209 (= H209), Q233 (= Q233), H236 (= H236), L278 (= L278), I437 (= I437)
3rupA Crystal structure of e.Coli biotin carboxylase in complex with two adp and two ca ions (see paper)
68% identity, 99% coverage: 1:444/447 of query aligns to 1:444/444 of 3rupA
- active site: K116 (= K116), K159 (= K159), D196 (= D196), H209 (= H209), R235 (= R235), T274 (= T274), E276 (= E276), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R338)
- binding adenosine-5'-diphosphate: Y82 (= Y82), G83 (= G83), K116 (= K116), K159 (= K159), G164 (= G164), G164 (= G164), G165 (= G165), G166 (= G166), R167 (= R167), M169 (= M169), F193 (= F193), E201 (= E201), K202 (= K202), Y203 (≠ F203), L204 (= L204), H209 (= H209), Q233 (= Q233), H236 (= H236), K238 (= K238), L278 (= L278), E288 (= E288), R292 (= R292), V295 (= V295), E296 (= E296), R338 (= R338), D382 (= D382), I437 (= I437)
- binding calcium ion: E87 (= E87), E276 (= E276), E288 (= E288), E288 (= E288), N290 (= N290)
3g8cA Crystal structure of biotin carboxylase in complex with biotin, bicarbonate, adp and mg ion (see paper)
68% identity, 99% coverage: 1:444/447 of query aligns to 1:444/444 of 3g8cA
- active site: K116 (= K116), K159 (= K159), D196 (= D196), H209 (= H209), R235 (= R235), T274 (= T274), E276 (= E276), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R338)
- binding adenosine-5'-diphosphate: I157 (= I157), K159 (= K159), G164 (= G164), M169 (= M169), E201 (= E201), K202 (= K202), Y203 (≠ F203), L204 (= L204), Q233 (= Q233), H236 (= H236), L278 (= L278), E288 (= E288), I437 (= I437)
- binding bicarbonate ion: K238 (= K238), R292 (= R292), Q294 (= Q294), V295 (= V295), E296 (= E296)
- binding biotin: Y82 (= Y82), F84 (= F84), R292 (= R292), V295 (= V295), R338 (= R338), D382 (= D382)
- binding magnesium ion: E276 (= E276), E288 (= E288)
3jziA Crystal structure of biotin carboxylase from e. Coli in complex with benzimidazole series (see paper)
68% identity, 99% coverage: 1:444/447 of query aligns to 1:444/445 of 3jziA
- active site: K116 (= K116), K159 (= K159), D196 (= D196), H209 (= H209), R235 (= R235), T274 (= T274), E276 (= E276), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R338)
- binding 7-amino-2-[(2-chlorobenzyl)amino]-1-{[(1S,2S)-2-hydroxycycloheptyl]methyl}-1H-benzimidazole-5-carboxamide: K116 (= K116), K159 (= K159), A160 (= A160), G164 (= G164), G165 (= G165), M169 (= M169), Y199 (= Y199), E201 (= E201), K202 (= K202), Y203 (≠ F203), H209 (= H209), Q233 (= Q233), H236 (= H236), L278 (= L278), I287 (= I287), E288 (= E288)
Query Sequence
>WP_024328274.1 NCBI__GCF_001995255.1:WP_024328274.1
MFEKILIANRGEIALRVLRACREMGIATVAVHSDADRDLKHVRLADESVCIGPAPSNESY
LNIPALIAAAEVTDAGALHPGYGFLSENADFAERVESSGFAFIGPRAETIRLMGDKVSAK
QSMLSAGVPCVPGSGGALSEEPEANLQLAREIGYPVIVKAAAGGGGRGMRVVHTEGALLN
AISLTRNEARQGFGDDTLYMEKFLERPRHVEFQILADTHGNAVCLGERDCSMQRRHQKVI
EEAPAPEITDTQRRDMSERLIRACQEIGYRGAGTFEFLYEDGQFFFIEMNTRLQVEHTVT
EEVTGIDLVREQIRIAAGEPLGITQDDVTIHGHAIECRINAEDPATFVPSPGTIQQYHAP
GGPGIRMDTHIYNGYAVPPHYDSMVGKLIAHGTTRDIAIARMRGALGEIIVDGIRTNISL
HSDLMNDANFQRGATDIHYLEKKLKTH
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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