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Comparing WP_013136572.1 NCBI__GCF_000092245.1:WP_013136572.1 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)
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)
53% identity, 92% coverage: 7:451/483 of query aligns to 6:450/453 of 7kctA
- active site: E276 (= E277), E289 (= E290), N291 (= N292), E297 (= E298), R339 (= R340)
- binding adenosine-5'-diphosphate: K117 (= K118), L157 (≠ I158), K159 (= K160), G164 (= G165), G165 (= G166), G166 (= G167), I169 (≠ M170), E201 (= E202), Y203 (= Y204), I204 (≠ V205), H209 (= H210), Q233 (= Q234), Q237 (= Q238), K238 (= K239), I278 (≠ L279), E289 (= E290), R293 (= R294), Q295 (= Q296), V296 (= V297), E297 (= E298), R339 (= R340)
- binding bicarbonate ion: D116 (= D117), R119 (≠ A120)
- binding magnesium ion: E276 (= E277), E289 (= E290)
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
50% identity, 91% coverage: 7:446/483 of query aligns to 2:443/448 of 2vpqB
- active site: V116 (≠ A120), K156 (= K160), H206 (= H210), R232 (= R236), T271 (= T275), E273 (= E277), E287 (= E290), N289 (= N292), R291 (= R294), E295 (= E298), R337 (= R340)
- binding phosphoaminophosphonic acid-adenylate ester: K114 (= K118), I154 (= I158), K156 (= K160), G161 (= G165), G163 (= G167), I166 (≠ M170), F200 (≠ Y204), I201 (≠ V205), E273 (= E277), I275 (≠ L279), M286 (≠ I289), E287 (= E290)
- binding magnesium ion: E273 (= E277), E287 (= E290)
2vqdA Crystal structure of biotin carboxylase from pseudomonas aeruginosa complexed with ampcp (see paper)
51% identity, 92% coverage: 5:447/483 of query aligns to 2:444/447 of 2vqdA
- active site: K116 (= K118), K159 (= K160), P196 (≠ G197), H209 (= H210), R235 (= R236), T274 (= T275), E276 (= E277), E288 (= E290), N290 (= N292), R292 (= R294), E296 (= E298), R338 (= R340)
- binding phosphomethylphosphonic acid adenosyl ester: K116 (= K118), I157 (= I158), K159 (= K160), G164 (= G165), G166 (= G167), F203 (≠ Y204), L204 (≠ V205), H209 (= H210), Q233 (= Q234), H236 (= H237), L278 (= L279), E288 (= E290), I437 (≠ T440)
- binding magnesium ion: E276 (= E277), E288 (= E290)
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
50% identity, 92% coverage: 5:447/483 of query aligns to 2:441/442 of 4mv4A
- active site: K116 (= K118), K159 (= K160), D193 (≠ G197), H206 (= H210), R232 (= R236), T271 (= T275), E273 (= E277), E285 (= E290), N287 (= N292), R289 (= R294), E293 (= E298), R335 (= R340)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K160), G164 (≠ R168), M166 (= M170), E198 (= E202), Y200 (= Y204), L201 (≠ V205), H233 (= H237), L275 (= L279), E285 (= E290)
- binding magnesium ion: E273 (= E277), E285 (= E290)
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
50% identity, 92% coverage: 5:447/483 of query aligns to 2:442/444 of 2vr1A
- active site: K116 (= K118), K159 (= K160), D194 (≠ G197), H207 (= H210), R233 (= R236), T272 (= T275), E274 (= E277), E286 (= E290), N288 (= N292), R290 (= R294), E294 (= E298), R336 (= R340)
- binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (= K160), R165 (= R168), M167 (= M170), Y201 (= Y204), L202 (≠ V205), E274 (= E277), L276 (= L279), E286 (= E290), N288 (= N292), I435 (≠ T440)
4mv3A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and bicarbonate (see paper)
50% identity, 92% coverage: 5:447/483 of query aligns to 2:438/439 of 4mv3A
- active site: K116 (= K118), K159 (= K160), D190 (≠ G197), H203 (= H210), R229 (= R236), T268 (= T275), E270 (= E277), E282 (= E290), N284 (= N292), R286 (= R294), E290 (= E298), R332 (= R340)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K160), M163 (= M170), E195 (= E202), Y197 (= Y204), L198 (≠ V205), E270 (= E277), L272 (= L279), E282 (= E290)
- binding bicarbonate ion: R286 (= R294), Q288 (= Q296), V289 (= V297)
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)
50% identity, 92% coverage: 5:447/483 of query aligns to 2:439/440 of 6oi8A
- active site: K116 (= K118), K159 (= K160), D191 (≠ G197), H204 (= H210), R230 (= R236), T269 (= T275), E271 (= E277), E283 (= E290), N285 (= N292), R287 (= R294), E291 (= E298), R333 (= R340)
- 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 (= I158), K159 (= K160), M164 (= M170), E196 (= E202), Y198 (= Y204), L199 (≠ V205), H204 (= H210), Q228 (= Q234), E271 (= E277), L273 (= L279), E283 (= E290), I432 (≠ T440)
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)
51% identity, 92% coverage: 5:447/483 of query aligns to 2:444/448 of P43873
- K116 (= K118) binding ATP
- K159 (= K160) binding ATP
- EKYL 201:204 (≠ EKYV 202:205) binding ATP
- E276 (= E277) binding ATP; binding Mg(2+)
- E288 (= E290) binding ATP; binding Mg(2+)
- N290 (= N292) 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
51% identity, 92% coverage: 5:447/483 of query aligns to 2:444/445 of 6ojhA
- active site: K116 (= K118), K159 (= K160), D196 (≠ G197), H209 (= H210), R235 (= R236), T274 (= T275), E276 (= E277), E288 (= E290), N290 (= N292), R292 (= R294), E296 (= E298), R338 (= R340)
- binding calcium ion: E276 (= E277), E288 (= E290), N290 (= N292)
- binding 7-[(3R)-3-aminopyrrolidin-1-yl]-6-(naphthalen-1-yl)pyrido[2,3-d]pyrimidin-2-amine: K159 (= K160), M169 (= M170), E201 (= E202), Y203 (= Y204), L204 (≠ V205), H236 (= H237), L278 (= L279), E288 (= E290), I437 (≠ T440)
4mv1A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with adp and phosphate (see paper)
49% identity, 92% coverage: 5:447/483 of query aligns to 2:430/430 of 4mv1A
- active site: K116 (= K118), K159 (= K160), D182 (≠ E189), H195 (= H210), R221 (= R236), T260 (= T275), E262 (= E277), E274 (= E290), N276 (= N292), R278 (= R294), E282 (= E298), R324 (= R340)
- binding adenosine-5'-diphosphate: K159 (= K160), E187 (= E202), K188 (= K203), Y189 (= Y204), L190 (≠ V205), L264 (= L279)
- binding phosphate ion: K224 (= K239), R278 (= R294), Q280 (= Q296), V281 (= V297), E282 (= E298)
P24182 Biotin carboxylase; Acetyl-coenzyme A carboxylase biotin carboxylase subunit A; EC 6.3.4.14 from Escherichia coli (strain K12) (see 3 papers)
50% identity, 92% coverage: 5:447/483 of query aligns to 2:444/449 of P24182
- R19 (= R22) mutation to E: Loss of homodimerization. No effect on ATP binding.
- E23 (= E26) mutation to R: Loss of homodimerization. No effect on ATP binding.
- K116 (= K118) binding ATP
- K159 (= K160) binding ATP
- GG 165:166 (= GG 166:167) binding ATP
- EKYL 201:204 (≠ EKYV 202:205) binding ATP
- H209 (= H210) binding ATP
- H236 (= H237) binding ATP
- K238 (= K239) binding hydrogencarbonate
- E276 (= E277) binding ATP; binding Mg(2+)
- E288 (= E290) binding ATP; binding Mg(2+)
- R292 (= R294) active site; binding hydrogencarbonate
- V295 (= V297) binding hydrogencarbonate
- E296 (= E298) mutation to A: Severe reduction in catalytic activity.
- R338 (= R340) binding biotin; binding hydrogencarbonate; mutation to A: Severe reduction in catalytic activity.
- F363 (≠ P366) mutation to A: Loss of homodimerization. No effect on ATP binding.
- R366 (= R369) 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)
50% identity, 92% coverage: 5:447/483 of query aligns to 4:446/447 of 3jzfB
- active site: K118 (= K118), K161 (= K160), D198 (≠ G197), H211 (= H210), R237 (= R236), T276 (= T275), E278 (= E277), E290 (= E290), N292 (= N292), R294 (= R294), E298 (= E298), R340 (= R340)
- binding 2-[(2-chlorobenzyl)amino]-1-(cyclohexylmethyl)-1H-benzimidazole-5-carboxamide: K118 (= K118), K161 (= K160), A162 (= A161), G166 (= G165), G168 (= G167), R169 (= R168), G170 (= G169), M171 (= M170), Y201 (≠ F200), E203 (= E202), K204 (= K203), Y205 (= Y204), H211 (= H210), H238 (= H237), L280 (= L279), I289 (= I289), E290 (= E290)
3jziA Crystal structure of biotin carboxylase from e. Coli in complex with benzimidazole series (see paper)
50% identity, 92% coverage: 5:447/483 of query aligns to 2:444/445 of 3jziA
- active site: K116 (= K118), K159 (= K160), D196 (≠ G197), H209 (= H210), R235 (= R236), T274 (= T275), E276 (= E277), E288 (= E290), N290 (= N292), R292 (= R294), E296 (= E298), R338 (= R340)
- binding 7-amino-2-[(2-chlorobenzyl)amino]-1-{[(1S,2S)-2-hydroxycycloheptyl]methyl}-1H-benzimidazole-5-carboxamide: K116 (= K118), K159 (= K160), A160 (= A161), G164 (= G165), G165 (= G166), M169 (= M170), Y199 (≠ F200), E201 (= E202), K202 (= K203), Y203 (= Y204), H209 (= H210), Q233 (= Q234), H236 (= H237), L278 (= L279), I287 (= I289), E288 (= E290)
2w6oA Crystal structure of biotin carboxylase from e. Coli in complex with 4-amino-7,7-dimethyl-7,8-dihydro-quinazolinone fragment (see paper)
50% identity, 92% coverage: 5:447/483 of query aligns to 2:444/445 of 2w6oA
- active site: K116 (= K118), K159 (= K160), D196 (≠ G197), H209 (= H210), R235 (= R236), T274 (= T275), E276 (= E277), E288 (= E290), N290 (= N292), R292 (= R294), E296 (= E298), R338 (= R340)
- binding 4-amino-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-one: K159 (= K160), K202 (= K203), Y203 (= Y204), L204 (≠ V205), L278 (= L279), I437 (≠ T440)
2w6nA Crystal structure of biotin carboxylase from e. Coli in complex with amino-oxazole fragment series (see paper)
50% identity, 92% coverage: 5:447/483 of query aligns to 2:444/445 of 2w6nA
- active site: K116 (= K118), K159 (= K160), D196 (≠ G197), H209 (= H210), R235 (= R236), T274 (= T275), E276 (= E277), E288 (= E290), N290 (= N292), R292 (= R294), E296 (= E298), R338 (= R340)
- binding 2-amino-n,n-bis(phenylmethyl)-1,3-oxazole-5-carboxamide: I157 (= I158), K159 (= K160), M169 (= M170), E201 (= E202), K202 (= K203), Y203 (= Y204), L278 (= L279)
2v59A Crystal structure of biotin carboxylase from e.Coli in complex with potent inhibitor 2 (see paper)
50% identity, 92% coverage: 5:447/483 of query aligns to 2:444/445 of 2v59A
- active site: K116 (= K118), K159 (= K160), D196 (≠ G197), H209 (= H210), R235 (= R236), T274 (= T275), E276 (= E277), E288 (= E290), N290 (= N292), R292 (= R294), E296 (= E298), R338 (= R340)
- binding 6-(2,6-dimethoxyphenyl)pyrido[2,3-d]pyrimidine-2,7-diamine: K159 (= K160), Y203 (= Y204), L204 (≠ V205), H209 (= H210), Q233 (= Q234), H236 (= H237), L278 (= L279), I437 (≠ T440)
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)
50% identity, 92% coverage: 5:447/483 of query aligns to 2:444/446 of 6oi9A
- active site: E276 (= E277), E288 (= E290), N290 (= N292), E296 (= E298), R338 (= R340)
- binding 7-[(3S)-3-(aminomethyl)pyrrolidin-1-yl]-6-(2,6-dichlorophenyl)pyrido[2,3-d]pyrimidin-2-amine: K159 (= K160), M169 (= M170), E201 (= E202), Y203 (= Y204), L204 (≠ V205), H209 (= H210), Q233 (= Q234), H236 (= H237), E276 (= E277), L278 (= L279), E288 (= E290), I437 (≠ T440)
2w71A Crystal structure of biotin carboxylase from e. Coli in complex with the imidazole-pyrimidine inhibitor (see paper)
50% identity, 92% coverage: 5:447/483 of query aligns to 2:444/446 of 2w71A
- active site: K116 (= K118), K159 (= K160), D196 (≠ G197), H209 (= H210), R235 (= R236), T274 (= T275), E276 (= E277), E288 (= E290), N290 (= N292), R292 (= R294), E296 (= E298), R338 (= R340)
- binding 4-[1-(2,6-dichlorobenzyl)-2-methyl-1H-imidazol-4-yl]pyrimidin-2-amine: K159 (= K160), Y203 (= Y204), L204 (≠ V205), H209 (= H210), Q233 (= Q234), H236 (= H237), L278 (= L279), I437 (≠ T440)
2w70A Crystal structure of biotin carboxylase from e. Coli in complex with the amino-thiazole-pyrimidine fragment (see paper)
50% identity, 92% coverage: 5:447/483 of query aligns to 2:444/446 of 2w70A
- active site: K116 (= K118), K159 (= K160), D196 (≠ G197), H209 (= H210), R235 (= R236), T274 (= T275), E276 (= E277), E288 (= E290), N290 (= N292), R292 (= R294), E296 (= E298), R338 (= R340)
- binding 4-(2-amino-1,3-thiazol-4-yl)pyrimidin-2-amine: I157 (= I158), K159 (= K160), G166 (= G167), M169 (= M170), E201 (= E202), Y203 (= Y204), L204 (≠ V205), L278 (= L279)
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)
50% identity, 92% coverage: 5:447/483 of query aligns to 2:444/446 of 2w6zA
- active site: K116 (= K118), K159 (= K160), D196 (≠ G197), H209 (= H210), R235 (= R236), T274 (= T275), E276 (= E277), E288 (= E290), N290 (= N292), R292 (= R294), E296 (= E298), R338 (= R340)
- binding 3-(3-methylbut-2-en-1-yl)-3H-purin-6-amine: K159 (= K160), Y203 (= Y204), L204 (≠ V205), L278 (= L279)
Query Sequence
>WP_013136572.1 NCBI__GCF_000092245.1:WP_013136572.1
MSKKISKVLVANRGEIALRIIRACKELDIKSVAIFSEVDIEGIWVKKADECYPLLGDPLD
AYLNIDKIISLALKAQCDAIHPGYGFLSESAEFAEACDKAGIIFVGPKAEHIALFGDKMA
SKVAMKKIGVPVLEGTSTPIVDIKEGEKISREIGFPIIIKAAFGGGGRGMRIVKEEKDFK
AMFEAATAEAKKFFGKGDAFIEKYVENPRHIEVQVIADKYGNVLHLGERDCSIQRRHQKV
IEIAPSPRLNENVRRELYRVSTKAMFKLGYESVGTIEFLVDAQDNIYFIEMNTRVQVEHP
VTELITGVDIIQRMIEIAEGDKLQFLQEEINFRGYAIEFRINAEDPKKKFMPASGTITKY
LTPGGPGVRIDTSVYTGYKIPPNYDSMVGKLIVWALDWDGAVRKARRALDEFYIEGLPTN
IPLHREIVRDEDFIEGKLDTSYLDKKLEKFNMDAIDHIEEEETKMKNITKLIEQIKKNKL
NVR
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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