SitesBLAST
Comparing WP_068167311.1 NCBI__GCF_001592305.1:WP_068167311.1 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)
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
68% identity, 99% coverage: 1:444/449 of query aligns to 1:441/442 of 4mv4A
- active site: K116 (= K116), K159 (= K159), D193 (≠ P196), 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)
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)
68% identity, 99% coverage: 1:444/449 of query aligns to 1:439/440 of 6oi8A
- active site: K116 (= K116), K159 (= K159), D191 (≠ P196), 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)
4mv3A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and bicarbonate (see paper)
68% identity, 99% coverage: 1:444/449 of query aligns to 1:438/439 of 4mv3A
- active site: K116 (= K116), K159 (= K159), D190 (≠ P196), 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)
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)
69% identity, 100% coverage: 1:448/449 of query aligns to 1:448/448 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
69% identity, 99% coverage: 1:444/449 of query aligns to 1:444/445 of 6ojhA
- active site: K116 (= K116), K159 (= K159), D196 (≠ P196), 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)
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
67% identity, 99% coverage: 1:444/449 of query aligns to 1:442/444 of 2vr1A
- active site: K116 (= K116), K159 (= K159), D194 (≠ P196), 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)
4mv1A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with adp and phosphate (see paper)
66% identity, 99% coverage: 1:444/449 of query aligns to 1:430/430 of 4mv1A
- active site: K116 (= K116), K159 (= K159), D182 (≠ E188), 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)
2vqdA Crystal structure of biotin carboxylase from pseudomonas aeruginosa complexed with ampcp (see paper)
66% identity, 99% coverage: 1:444/449 of query aligns to 1:444/447 of 2vqdA
- active site: K116 (= K116), K159 (= K159), P196 (= P196), H209 (= H209), R235 (= R235), T274 (= T274), E276 (= E276), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R338)
- binding phosphomethylphosphonic acid adenosyl ester: K116 (= K116), I157 (= I157), K159 (= K159), G164 (= G164), G166 (= G166), F203 (= F203), L204 (= L204), H209 (= H209), Q233 (= Q233), H236 (= H236), L278 (= L278), E288 (= E288), I437 (= I437)
- binding magnesium ion: E276 (= E276), E288 (= E288)
P24182 Biotin carboxylase; Acetyl-coenzyme A carboxylase biotin carboxylase subunit A; EC 6.3.4.14 from Escherichia coli (strain K12) (see 3 papers)
67% identity, 100% coverage: 1:449/449 of query aligns to 1:449/449 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.
4rzqA Structural analysis of substrate, reaction intermediate and product binding in haemophilus influenzae biotin carboxylase (see paper)
66% identity, 99% coverage: 1:444/449 of query aligns to 2:420/422 of 4rzqA
- active site: K117 (= K116), K155 (= K159), H185 (= H209), R211 (= R235), T250 (= T274), E252 (= E276), E264 (= E288), N266 (= N290), R268 (= R292), E272 (= E296), R314 (= R338)
- binding adenosine-5'-diphosphate: Y179 (≠ F203), L180 (= L204), L254 (= L278)
- binding methyl (3aS,4S,6aR)-4-(5-methoxy-5-oxopentyl)-2-oxohexahydro-1H-thieno[3,4-d]imidazole-1-carboxylate: N10 (= N9), R11 (= R10), Y83 (= Y82), F85 (= F84), K214 (= K238), R268 (= R292), Q270 (= Q294), V271 (= V295), E272 (= E296), R314 (= R338), D358 (= D382)
3rupA Crystal structure of e.Coli biotin carboxylase in complex with two adp and two ca ions (see paper)
68% identity, 99% coverage: 1:444/449 of query aligns to 1:444/444 of 3rupA
- active site: K116 (= K116), K159 (= K159), D196 (≠ P196), 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: 1:444/449 of query aligns to 1:444/444 of 3g8cA
- active site: K116 (= K116), K159 (= K159), D196 (≠ P196), 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: 1:444/449 of query aligns to 1:444/445 of 3jziA
- active site: K116 (= K116), K159 (= K159), D196 (≠ P196), 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)
2w6oA Crystal structure of biotin carboxylase from e. Coli in complex with 4-amino-7,7-dimethyl-7,8-dihydro-quinazolinone fragment (see paper)
68% identity, 99% coverage: 1:444/449 of query aligns to 1:444/445 of 2w6oA
- active site: K116 (= K116), K159 (= K159), D196 (≠ P196), H209 (= H209), R235 (= R235), T274 (= T274), E276 (= E276), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R338)
- binding 4-amino-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-one: K159 (= K159), K202 (= K202), Y203 (≠ F203), L204 (= L204), L278 (= L278), I437 (= I437)
2w6nA Crystal structure of biotin carboxylase from e. Coli in complex with amino-oxazole fragment series (see paper)
68% identity, 99% coverage: 1:444/449 of query aligns to 1:444/445 of 2w6nA
- active site: K116 (= K116), K159 (= K159), D196 (≠ P196), H209 (= H209), R235 (= R235), T274 (= T274), E276 (= E276), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R338)
- binding 2-amino-n,n-bis(phenylmethyl)-1,3-oxazole-5-carboxamide: I157 (= I157), K159 (= K159), M169 (= M169), E201 (= E201), K202 (= K202), Y203 (≠ F203), L278 (= L278)
2v59A Crystal structure of biotin carboxylase from e.Coli in complex with potent inhibitor 2 (see paper)
68% identity, 99% coverage: 1:444/449 of query aligns to 1:444/445 of 2v59A
- active site: K116 (= K116), K159 (= K159), D196 (≠ P196), H209 (= H209), R235 (= R235), T274 (= T274), E276 (= E276), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R338)
- binding 6-(2,6-dimethoxyphenyl)pyrido[2,3-d]pyrimidine-2,7-diamine: K159 (= K159), Y203 (≠ F203), L204 (= L204), H209 (= H209), Q233 (= Q233), H236 (= H236), L278 (= L278), I437 (= I437)
3jzfB Crystal structure of biotin carboxylase from e. Coli in complex with benzimidazoles series (see paper)
68% identity, 99% coverage: 1:444/449 of query aligns to 3:446/447 of 3jzfB
- active site: K118 (= K116), K161 (= K159), D198 (≠ P196), H211 (= H209), R237 (= R235), T276 (= T274), E278 (= E276), E290 (= E288), N292 (= N290), R294 (= R292), E298 (= E296), R340 (= R338)
- binding 2-[(2-chlorobenzyl)amino]-1-(cyclohexylmethyl)-1H-benzimidazole-5-carboxamide: K118 (= K116), K161 (= K159), A162 (= A160), G166 (= G164), G168 (= G166), R169 (= R167), G170 (= G168), M171 (= M169), Y201 (= Y199), E203 (= E201), K204 (= K202), Y205 (≠ F203), H211 (= H209), H238 (= H236), L280 (= L278), I289 (= I287), E290 (= 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)
68% identity, 99% coverage: 1:444/449 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: 1:444/449 of query aligns to 1:444/446 of 2w71A
- active site: K116 (= K116), K159 (= K159), D196 (≠ P196), 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: 1:444/449 of query aligns to 1:444/446 of 2w70A
- active site: K116 (= K116), K159 (= K159), D196 (≠ P196), 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)
Query Sequence
>WP_068167311.1 NCBI__GCF_001592305.1:WP_068167311.1
MFKKILIANRGEIALRVQRACREMGIKAVMVYSEADRDAKYVRLADESVCIGPAQSSLSY
LNMPAIISAAEVTDAEAIHPGYGFLSENADFAERVEKSGFTFIGPTPESIRLMGDKVSAK
QAMIRAGVPCVPGSEGALPDDPAVIKRTAKAVGYPVIIKAAGGGGGRGMRVVHTEAALLH
AVQTTKAEAGAAFGNPEVYMEKFLQNPRHIEIQILADTHRNAVYLGERDCSMQRRHQKVI
EEAPAPGIPRRLIEKIGERCATACKKIGYRGAGTFEFLYENGEFYFIEMNTRVQVEHPVT
EWISGVDIVRTQIAVAAGEKLPFTQRQIQLRGHAIECRINAEDAYKFTPSPGRITTWHAP
GGPGVRVDSHAYTNYFVPPHYDSMIGKIIVHGDTREQALARMRTALAETVIEGIKTNIPL
HRELMVDASFVAGGTNIHYLEEWLSQRER
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