SitesBLAST
Comparing WP_015927622.1 NCBI__GCF_000022085.1:WP_015927622.1 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)
61% identity, 98% coverage: 1:443/450 of query aligns to 1:441/442 of 4mv4A
- active site: K116 (= K116), K159 (= K158), D193 (≠ P195), H206 (= H208), R232 (= R234), T271 (= T273), E273 (= E275), E285 (= E287), N287 (= N289), R289 (= R291), E293 (= E295), R335 (= R337)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K158), G164 (= G163), M166 (= M168), E198 (= E200), Y200 (≠ F202), L201 (= L203), H233 (= H235), L275 (= L277), E285 (= E287)
- binding magnesium ion: E273 (= E275), E285 (= E287)
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)
60% identity, 98% coverage: 1:443/450 of query aligns to 1:439/440 of 6oi8A
- active site: K116 (= K116), K159 (= K158), D191 (≠ P195), H204 (= H208), R230 (= R234), T269 (= T273), E271 (= E275), E283 (= E287), N285 (= N289), R287 (= R291), E291 (= E295), R333 (= R337)
- 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 (= E287), I432 (= I436)
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
61% identity, 98% coverage: 1:443/450 of query aligns to 1:442/444 of 2vr1A
- active site: K116 (= K116), K159 (= K158), D194 (≠ P195), H207 (= H208), R233 (= R234), T272 (= T273), E274 (= E275), E286 (= E287), N288 (= N289), R290 (= R291), E294 (= E295), R336 (= R337)
- binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (= K158), R165 (= R166), M167 (= M168), Y201 (≠ F202), L202 (= L203), E274 (= E275), L276 (= L277), E286 (= E287), N288 (= N289), I435 (= I436)
4mv3A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and bicarbonate (see paper)
60% identity, 98% coverage: 1:443/450 of query aligns to 1:438/439 of 4mv3A
- active site: K116 (= K116), K159 (= K158), D190 (≠ P195), H203 (= H208), R229 (= R234), T268 (= T273), E270 (= E275), E282 (= E287), N284 (= N289), R286 (= R291), E290 (= E295), R332 (= R337)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K158), M163 (= M168), E195 (= E200), Y197 (≠ F202), L198 (= L203), E270 (= E275), L272 (= L277), E282 (= E287)
- binding bicarbonate ion: R286 (= R291), Q288 (= Q293), V289 (= V294)
2vqdA Crystal structure of biotin carboxylase from pseudomonas aeruginosa complexed with ampcp (see paper)
62% identity, 98% coverage: 1:443/450 of query aligns to 1:444/447 of 2vqdA
- active site: K116 (= K116), K159 (= K158), P196 (= P195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E287), N290 (= N289), R292 (= R291), E296 (= E295), R338 (= R337)
- 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 (= E287), I437 (= I436)
- binding magnesium ion: E276 (= E275), E288 (= E287)
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)
61% identity, 98% coverage: 1:443/450 of query aligns to 1:444/448 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 (= E287) binding ATP; binding Mg(2+)
- N290 (= N289) 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
61% identity, 98% coverage: 1:443/450 of query aligns to 1:444/445 of 6ojhA
- active site: K116 (= K116), K159 (= K158), D196 (≠ P195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E287), N290 (= N289), R292 (= R291), E296 (= E295), R338 (= R337)
- binding calcium ion: E276 (= E275), E288 (= E287), N290 (= N289)
- 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 (= E287), I437 (= I436)
4mv1A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with adp and phosphate (see paper)
59% identity, 98% coverage: 1:443/450 of query aligns to 1:430/430 of 4mv1A
- active site: K116 (= K116), K159 (= K158), D182 (≠ E187), H195 (= H208), R221 (= R234), T260 (= T273), E262 (= E275), E274 (= E287), N276 (= N289), R278 (= R291), E282 (= E295), R324 (= R337)
- binding adenosine-5'-diphosphate: K159 (= K158), E187 (= E200), K188 (= K201), Y189 (≠ F202), L190 (= L203), L264 (= L277)
- binding phosphate ion: K224 (= K237), R278 (= R291), Q280 (= Q293), V281 (= V294), E282 (= E295)
P24182 Biotin carboxylase; Acetyl-coenzyme A carboxylase biotin carboxylase subunit A; EC 6.3.4.14 from Escherichia coli (strain K12) (see 3 papers)
62% identity, 98% coverage: 1:443/450 of query aligns to 1:444/449 of P24182
- R19 (= R19) mutation to E: Loss of homodimerization. No effect on ATP binding.
- E23 (≠ L23) 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 (= E287) binding ATP; binding Mg(2+)
- R292 (= R291) active site; binding hydrogencarbonate
- V295 (= V294) binding hydrogencarbonate
- E296 (= E295) mutation to A: Severe reduction in catalytic activity.
- R338 (= R337) 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.
3jzfB Crystal structure of biotin carboxylase from e. Coli in complex with benzimidazoles series (see paper)
62% identity, 98% coverage: 1:443/450 of query aligns to 3:446/447 of 3jzfB
- active site: K118 (= K116), K161 (= K158), D198 (≠ P195), H211 (= H208), R237 (= R234), T276 (= T273), E278 (= E275), E290 (= E287), N292 (= N289), R294 (= R291), E298 (= E295), R340 (= R337)
- binding 2-[(2-chlorobenzyl)amino]-1-(cyclohexylmethyl)-1H-benzimidazole-5-carboxamide: K118 (= K116), K161 (= K158), A162 (= A159), G166 (= G163), G168 (= G165), R169 (= R166), G170 (= G167), M171 (= M168), Y201 (= Y198), E203 (= E200), K204 (= K201), Y205 (≠ F202), H211 (= H208), H238 (= H235), L280 (= L277), I289 (= I286), E290 (= E287)
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)
62% identity, 98% coverage: 1:443/450 of query aligns to 1:444/446 of 6oi9A
- active site: E276 (= E275), E288 (= E287), N290 (= N289), E296 (= E295), R338 (= R337)
- 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 (= E287), I437 (= I436)
2w71A Crystal structure of biotin carboxylase from e. Coli in complex with the imidazole-pyrimidine inhibitor (see paper)
62% identity, 98% coverage: 1:443/450 of query aligns to 1:444/446 of 2w71A
- active site: K116 (= K116), K159 (= K158), D196 (≠ P195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E287), N290 (= N289), R292 (= R291), E296 (= E295), R338 (= R337)
- 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 (= I436)
2w70A Crystal structure of biotin carboxylase from e. Coli in complex with the amino-thiazole-pyrimidine fragment (see paper)
62% identity, 98% coverage: 1:443/450 of query aligns to 1:444/446 of 2w70A
- active site: K116 (= K116), K159 (= K158), D196 (≠ P195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E287), N290 (= N289), R292 (= R291), E296 (= E295), R338 (= R337)
- binding 4-(2-amino-1,3-thiazol-4-yl)pyrimidin-2-amine: I157 (= I156), K159 (= K158), G166 (= G165), M169 (= M168), E201 (= E200), Y203 (≠ F202), L204 (= L203), L278 (= L277)
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)
62% identity, 98% coverage: 1:443/450 of query aligns to 1:444/446 of 2w6zA
- active site: K116 (= K116), K159 (= K158), D196 (≠ P195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E287), N290 (= N289), R292 (= R291), E296 (= E295), R338 (= R337)
- binding 3-(3-methylbut-2-en-1-yl)-3H-purin-6-amine: K159 (= K158), Y203 (≠ F202), L204 (= L203), L278 (= L277)
2w6qA Crystal structure of biotin carboxylase from e. Coli in complex with the triazine-2,4-diamine fragment (see paper)
62% identity, 98% coverage: 1:443/450 of query aligns to 1:444/446 of 2w6qA
- active site: K116 (= K116), K159 (= K158), D196 (≠ P195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E287), N290 (= N289), R292 (= R291), E296 (= E295), R338 (= R337)
- binding 6-(2-phenoxyethoxy)-1,3,5-triazine-2,4-diamine: I157 (= I156), K159 (= K158), E201 (= E200), K202 (= K201), Y203 (≠ F202), L204 (= L203), H236 (= H235), L278 (= L277)
2w6pA Crystal structure of biotin carboxylase from e. Coli in complex with 5-methyl-6-phenyl-quinazoline-2,4-diamine (see paper)
62% identity, 98% coverage: 1:443/450 of query aligns to 1:444/446 of 2w6pA
- active site: K116 (= K116), K159 (= K158), D196 (≠ P195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E287), N290 (= N289), R292 (= R291), E296 (= E295), R338 (= R337)
- binding 5-methyl-6-phenylquinazoline-2,4-diamine: K159 (= K158), Y203 (≠ F202), L204 (= L203), Q233 (= Q232), H236 (= H235), L278 (= L277), I437 (= I436)
2w6mA Crystal structure of biotin carboxylase from e. Coli in complex with amino-oxazole fragment series (see paper)
62% identity, 98% coverage: 1:443/450 of query aligns to 1:444/446 of 2w6mA
- active site: K116 (= K116), K159 (= K158), D196 (≠ P195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E287), N290 (= N289), R292 (= R291), E296 (= E295), R338 (= R337)
- binding (2-amino-1,3-oxazol-5-yl)-(3-bromophenyl)methanone: I157 (= I156), K159 (= K158), M169 (= M168), E201 (= E200), K202 (= K201), Y203 (≠ F202), H236 (= H235), L278 (= L277), I437 (= I436)
2v5aA Crystal structure of biotin carboxylase from e.Coli in complex with potent inhibitor 3 (see paper)
62% identity, 98% coverage: 1:443/450 of query aligns to 1:444/446 of 2v5aA
- active site: K116 (= K116), K159 (= K158), D196 (≠ P195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E287), N290 (= N289), R292 (= R291), E296 (= E295), R338 (= R337)
- binding 7-(2,5-dihydropyrrol-1-yl)-6-phenyl-pyrido[6,5-d]pyrimidin-2-amine: I157 (= I156), K159 (= K158), M169 (= M168), E201 (= E200), Y203 (≠ F202), L204 (= L203), Q233 (= Q232), H236 (= H235), L278 (= L277), I437 (= I436)
2v58A Crystal structure of biotin carboxylase from e.Coli in complex with potent inhibitor 1 (see paper)
62% identity, 98% coverage: 1:443/450 of query aligns to 1:444/446 of 2v58A
- active site: K116 (= K116), K159 (= K158), D196 (≠ P195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E287), N290 (= N289), R292 (= R291), E296 (= E295), R338 (= R337)
- binding 6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine: I157 (= I156), K159 (= K158), E201 (= E200), Y203 (≠ F202), L204 (= L203), H209 (= H208), Q233 (= Q232), H236 (= H235), L278 (= L277), I437 (= I436)
3rupA Crystal structure of e.Coli biotin carboxylase in complex with two adp and two ca ions (see paper)
62% identity, 98% coverage: 1:443/450 of query aligns to 1:444/444 of 3rupA
- active site: K116 (= K116), K159 (= K158), D196 (≠ P195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E287), N290 (= N289), R292 (= R291), E296 (= E295), R338 (= R337)
- binding adenosine-5'-diphosphate: Y82 (= Y82), G83 (= G83), K116 (= K116), K159 (= K158), G164 (= G163), G164 (= G163), G165 (= G164), G166 (= G165), R167 (= R166), M169 (= M168), F193 (= F192), E201 (= E200), K202 (= K201), Y203 (≠ F202), L204 (= L203), H209 (= H208), Q233 (= Q232), H236 (= H235), K238 (= K237), L278 (= L277), E288 (= E287), R292 (= R291), V295 (= V294), E296 (= E295), R338 (= R337), D382 (= D381), I437 (= I436)
- binding calcium ion: E87 (= E87), E276 (= E275), E288 (= E287), E288 (= E287), N290 (= N289)
Query Sequence
>WP_015927622.1 NCBI__GCF_000022085.1:WP_015927622.1
MFETLLIANRGEIALRIQRACRLLGVRSVQVYSEGDRGAPYLDTADEAVCIGPAASRDSY
LSIPRLLLAAEATGAEAIHPGYGFLSESAAFAEAVAAAGLIFVGPPASAIRLMGDKVAAK
RAMREAGVPCVPGGDGPLPDDAACRALAEDIGYPVIVKAAGGGGGRGMRVVRAAQDLAEA
VATTREEAGRAFGNPTVYMEKFLQAPRHVEIQVLADAHGDAVWLGERDCSLQRRHQKVVE
EAPAPGVPRDLIAAVGARCAEACRRIGYRGAGTFEFLYEAGELFFIEMNTRVQVEHPVTE
LVTGIDIVEAQLRIAAGEPLAFRQENIACRGHALECRINAETPFDFRPSPGRILRWRAPG
GPGIRVETHVESGYTVPAHYDSMIAKVLAHGADRAEALHRMRGALRQVVAEGIATNLPLH
RAIMDDPGFTAGGVGIHYLEDWLDRHSDDG
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