SitesBLAST
Comparing NP_661063.1 NCBI__GCF_000006985.1:NP_661063.1 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)
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
59% identity, 98% coverage: 3:441/447 of query aligns to 1:442/448 of 2vpqB
- active site: V116 (≠ T118), K156 (= K158), H206 (= H208), R232 (= R234), T271 (= T273), E273 (= E275), E287 (= E288), N289 (= N290), R291 (= R292), E295 (= E296), R337 (= R336)
- binding phosphoaminophosphonic acid-adenylate ester: K114 (= K116), I154 (= I156), K156 (= K158), G161 (= G163), G163 (= G165), I166 (≠ M168), F200 (= F202), I201 (≠ L203), E273 (= E275), I275 (≠ L277), M286 (= M287), E287 (= E288)
- binding magnesium ion: E273 (= E275), E287 (= E288)
2vqdA Crystal structure of biotin carboxylase from pseudomonas aeruginosa complexed with ampcp (see paper)
57% identity, 98% coverage: 1:440/447 of query aligns to 1:441/447 of 2vqdA
- active site: K116 (= K116), K159 (= K158), P196 (≠ S195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R336)
- binding phosphomethylphosphonic acid adenosyl ester: K116 (= K116), I157 (= I156), K159 (= K158), G164 (= G163), G166 (= G165), F203 (= F202), L204 (= L203), H209 (= H208), Q233 (= Q232), H236 (= H235), L278 (= L277), E288 (= E288), I437 (≠ T436)
- binding magnesium ion: E276 (= E275), E288 (= E288)
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
56% identity, 98% coverage: 1:440/447 of query aligns to 1:438/442 of 4mv4A
- active site: K116 (= K116), K159 (= K158), D193 (≠ S195), H206 (= H208), R232 (= R234), T271 (= T273), E273 (= E275), E285 (= E288), N287 (= N290), R289 (= R292), E293 (= E296), R335 (= R336)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K158), G164 (= G163), M166 (= M168), E198 (= E200), Y200 (≠ F202), L201 (= L203), H233 (= H235), L275 (= L277), E285 (= E288)
- binding magnesium ion: E273 (= E275), E285 (= E288)
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)
56% identity, 98% coverage: 1:440/447 of query aligns to 1:436/440 of 6oi8A
- active site: K116 (= K116), K159 (= K158), D191 (≠ S195), H204 (= H208), R230 (= R234), T269 (= T273), E271 (= E275), E283 (= E288), N285 (= N290), R287 (= R292), E291 (= E296), R333 (= R336)
- 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 (= I156), K159 (= K158), M164 (= M168), E196 (= E200), Y198 (≠ F202), L199 (= L203), H204 (= H208), Q228 (= Q232), E271 (= E275), L273 (= L277), E283 (= E288), I432 (≠ T436)
4mv3A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and bicarbonate (see paper)
56% identity, 98% coverage: 1:440/447 of query aligns to 1:435/439 of 4mv3A
- active site: K116 (= K116), K159 (= K158), D190 (≠ S195), H203 (= H208), R229 (= R234), T268 (= T273), E270 (= E275), E282 (= E288), N284 (= N290), R286 (= R292), E290 (= E296), R332 (= R336)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K158), M163 (= M168), E195 (= E200), Y197 (≠ F202), L198 (= L203), E270 (= E275), L272 (= L277), E282 (= E288)
- binding bicarbonate ion: R286 (= R292), Q288 (= Q294), V289 (= V295)
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
56% identity, 98% coverage: 1:440/447 of query aligns to 1:439/444 of 2vr1A
- active site: K116 (= K116), K159 (= K158), D194 (≠ S195), H207 (= H208), R233 (= R234), T272 (= T273), E274 (= E275), E286 (= E288), N288 (= N290), R290 (= R292), E294 (= E296), R336 (= R336)
- binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (= K158), R165 (≠ K166), M167 (= M168), Y201 (≠ F202), L202 (= L203), E274 (= E275), L276 (= L277), E286 (= E288), N288 (= N290), I435 (≠ T436)
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)
57% identity, 98% coverage: 1:440/447 of query aligns to 1:441/448 of P43873
- K116 (= K116) binding ATP
- K159 (= K158) binding ATP
- EKYL 201:204 (≠ EKFL 200:203) binding ATP
- E276 (= E275) 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
57% identity, 98% coverage: 1:440/447 of query aligns to 1:441/445 of 6ojhA
- active site: K116 (= K116), K159 (= K158), D196 (≠ S195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R336)
- binding calcium ion: E276 (= E275), E288 (= E288), N290 (= N290)
- 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 (≠ F202), L204 (= L203), H236 (= H235), L278 (= L277), E288 (= E288), I437 (≠ T436)
3ouuA Crystal structure of biotin carboxylase-beta-gamma-atp complex from campylobacter jejuni
57% identity, 98% coverage: 2:439/447 of query aligns to 6:443/446 of 3ouuA
- active site: K162 (= K158), G168 (= G164), G169 (= G165), H212 (= H208), K241 (= K237), T277 (= T273), E279 (= E275), E292 (= E288), N294 (= N290), V299 (= V295), E300 (= E296), R341 (= R336)
- binding phosphoaminophosphonic acid-adenylate ester: K120 (= K116), I160 (= I156), K162 (= K158), G167 (= G163), G168 (= G164), G169 (= G165), M172 (= M168), E204 (= E200), Y206 (≠ F202), I207 (≠ L203), H212 (= H208), Q236 (= Q232), H239 (= H235), L281 (= L277), E292 (= E288), T440 (= T436)
- binding calcium ion: E279 (= E275), E292 (= E288)
3ouzA Crystal structure of biotin carboxylase-adp complex from campylobacter jejuni
57% identity, 98% coverage: 3:439/447 of query aligns to 6:442/445 of 3ouzA
- active site: K161 (= K158), G167 (= G164), G168 (= G165), H211 (= H208), K240 (= K237), T276 (= T273), E278 (= E275), E291 (= E288), N293 (= N290), V298 (= V295), E299 (= E296), R340 (= R336)
- binding adenosine-5'-diphosphate: K119 (= K116), I159 (= I156), K161 (= K158), G166 (= G163), G168 (= G165), M171 (= M168), E203 (= E200), Y205 (≠ F202), I206 (≠ L203), H211 (= H208), Q235 (= Q232), L280 (= L277), E291 (= E288), T439 (= T436)
- binding magnesium ion: E278 (= E275), E291 (= E288)
4mv1A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with adp and phosphate (see paper)
56% identity, 98% coverage: 1:440/447 of query aligns to 1:427/430 of 4mv1A
- active site: K116 (= K116), K159 (= K158), D182 (≠ G189), H195 (= H208), R221 (= R234), T260 (= T273), E262 (= E275), E274 (= E288), N276 (= N290), R278 (= R292), E282 (= E296), R324 (= R336)
- binding adenosine-5'-diphosphate: K159 (= K158), E187 (= E200), K188 (= K201), Y189 (≠ F202), L190 (= L203), L264 (= L277)
- binding phosphate ion: K224 (= K237), 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)
56% identity, 98% coverage: 1:440/447 of query aligns to 1:441/449 of P24182
- R19 (≠ H19) 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 (= K158) binding ATP
- GG 165:166 (= GG 164:165) binding ATP
- EKYL 201:204 (≠ EKFL 200:203) binding ATP
- H209 (= H208) binding ATP
- H236 (= H235) binding ATP
- K238 (= K237) binding hydrogencarbonate
- E276 (= E275) 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 (= R336) binding biotin; binding hydrogencarbonate; mutation to A: Severe reduction in catalytic activity.
- F363 (≠ P362) mutation to A: Loss of homodimerization. No effect on ATP binding.
- R366 (= R365) mutation to E: Loss of homodimerization. No effect on ATP binding.
3rupA Crystal structure of e.Coli biotin carboxylase in complex with two adp and two ca ions (see paper)
56% identity, 98% coverage: 1:440/447 of query aligns to 1:441/444 of 3rupA
- active site: K116 (= K116), K159 (= K158), D196 (≠ S195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R336)
- 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 (≠ F202), L204 (= L203), H209 (= H208), Q233 (= Q232), H236 (= H235), K238 (= K237), L278 (= L277), E288 (= E288), R292 (= R292), V295 (= V295), E296 (= E296), R338 (= R336), D382 (= D381), I437 (≠ T436)
- 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)
56% identity, 98% coverage: 1:440/447 of query aligns to 1:441/444 of 3g8cA
- active site: K116 (= K116), K159 (= K158), D196 (≠ S195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R336)
- binding adenosine-5'-diphosphate: I157 (= I156), K159 (= K158), G164 (= G163), M169 (= M168), E201 (= E200), K202 (= K201), Y203 (≠ F202), L204 (= L203), Q233 (= Q232), H236 (= H235), L278 (= L277), E288 (= E288), I437 (≠ T436)
- binding bicarbonate ion: K238 (= K237), R292 (= R292), Q294 (= Q294), V295 (= V295), E296 (= E296)
- binding biotin: Y82 (= Y82), F84 (= F84), R292 (= R292), V295 (= V295), R338 (= R336), D382 (= D381)
- binding magnesium ion: E276 (= E275), E288 (= E288)
3jziA Crystal structure of biotin carboxylase from e. Coli in complex with benzimidazole series (see paper)
56% identity, 98% coverage: 1:440/447 of query aligns to 1:441/445 of 3jziA
- active site: K116 (= K116), K159 (= K158), D196 (≠ S195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R336)
- binding 7-amino-2-[(2-chlorobenzyl)amino]-1-{[(1S,2S)-2-hydroxycycloheptyl]methyl}-1H-benzimidazole-5-carboxamide: K116 (= K116), K159 (= K158), A160 (≠ P159), G164 (= G163), G165 (= G164), M169 (= M168), Y199 (= Y198), E201 (= E200), K202 (= K201), Y203 (≠ F202), H209 (= H208), Q233 (= Q232), H236 (= H235), L278 (= L277), I287 (≠ M287), E288 (= E288)
2w6oA Crystal structure of biotin carboxylase from e. Coli in complex with 4-amino-7,7-dimethyl-7,8-dihydro-quinazolinone fragment (see paper)
56% identity, 98% coverage: 1:440/447 of query aligns to 1:441/445 of 2w6oA
- active site: K116 (= K116), K159 (= K158), D196 (≠ S195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R336)
- binding 4-amino-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-one: K159 (= K158), K202 (= K201), Y203 (≠ F202), L204 (= L203), L278 (= L277), I437 (≠ T436)
2w6nA Crystal structure of biotin carboxylase from e. Coli in complex with amino-oxazole fragment series (see paper)
56% identity, 98% coverage: 1:440/447 of query aligns to 1:441/445 of 2w6nA
- active site: K116 (= K116), K159 (= K158), D196 (≠ S195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R336)
- binding 2-amino-n,n-bis(phenylmethyl)-1,3-oxazole-5-carboxamide: I157 (= I156), K159 (= K158), M169 (= M168), E201 (= E200), K202 (= K201), Y203 (≠ F202), L278 (= L277)
2v59A Crystal structure of biotin carboxylase from e.Coli in complex with potent inhibitor 2 (see paper)
56% identity, 98% coverage: 1:440/447 of query aligns to 1:441/445 of 2v59A
- active site: K116 (= K116), K159 (= K158), D196 (≠ S195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R336)
- binding 6-(2,6-dimethoxyphenyl)pyrido[2,3-d]pyrimidine-2,7-diamine: K159 (= K158), Y203 (≠ F202), L204 (= L203), H209 (= H208), Q233 (= Q232), H236 (= H235), L278 (= L277), I437 (≠ T436)
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)
56% identity, 98% coverage: 1:440/447 of query aligns to 1:441/446 of 6oi9A
- active site: E276 (= E275), E288 (= E288), N290 (= N290), E296 (= E296), R338 (= R336)
- 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 (≠ F202), L204 (= L203), H209 (= H208), Q233 (= Q232), H236 (= H235), E276 (= E275), L278 (= L277), E288 (= E288), I437 (≠ T436)
2w71A Crystal structure of biotin carboxylase from e. Coli in complex with the imidazole-pyrimidine inhibitor (see paper)
56% identity, 98% coverage: 1:440/447 of query aligns to 1:441/446 of 2w71A
- active site: K116 (= K116), K159 (= K158), D196 (≠ S195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R336)
- binding 4-[1-(2,6-dichlorobenzyl)-2-methyl-1H-imidazol-4-yl]pyrimidin-2-amine: K159 (= K158), Y203 (≠ F202), L204 (= L203), H209 (= H208), Q233 (= Q232), H236 (= H235), L278 (= L277), I437 (≠ T436)
Query Sequence
>NP_661063.1 NCBI__GCF_000006985.1:NP_661063.1
MFKKILIANRGEIALRVMHTCREMGICTVAVYSTADADSLHVRYADEAVCIGPPLSRESY
LNIPRIIAAAEVTNADAIHPGYGFLAENADFAEVCSSSNIKFIGPSAEMINKMGDKNTAK
STMIAAGVPVVPGSEGLVEDVAHAIETAKKIGYPVIIKPTAGGGGKGMRVVHEESQLEKN
LKTAQSEAGMAFGNSGVYIEKFLENPRHIEIQILADQHGNVVHLGERDCTVQRRHQKLIE
ETPSPVVDEALRTKMGEAAVAAAKAINYEGAGTIEFLLDKHKNFYFMEMNTRIQVEHPIT
EQRYDVDIVREQISIAAGGSLEGKTFIPRGHSIECRINAEDPEHMFRPSPGEIQVFHTPG
GPGVRIDSHCYASYVVPSNYDSMIGKLIVTAHNRDEAIARMSRALDEFIIMGIKTTIPFH
KQVMHDPVFRSGEFDTSFLDSFRFEKP
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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