SitesBLAST
Comparing WP_020563409.1 NCBI__GCF_000372865.1:WP_020563409.1 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)
57% identity, 95% coverage: 1:450/472 of query aligns to 3:452/453 of 7kctA
- active site: E276 (= E274), E289 (= E287), N291 (= N289), E297 (= E295), R339 (= R337)
- binding adenosine-5'-diphosphate: K117 (= K115), L157 (≠ M155), K159 (= K157), G164 (= G162), G165 (= G163), G166 (= G164), I169 (= I167), E201 (= E199), Y203 (≠ C201), I204 (= I202), H209 (= H207), Q233 (= Q231), Q237 (= Q235), K238 (= K236), I278 (≠ L276), E289 (= E287), R293 (= R291), Q295 (= Q293), V296 (= V294), E297 (= E295), R339 (= R337)
- binding bicarbonate ion: D116 (= D114), R119 (≠ E117)
- binding magnesium ion: E276 (= E274), E289 (= E287)
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
53% identity, 93% coverage: 3:443/472 of query aligns to 1:443/448 of 2vpqB
- active site: V116 (≠ E117), K156 (= K157), H206 (= H207), R232 (= R233), T271 (= T272), E273 (= E274), E287 (= E287), N289 (= N289), R291 (= R291), E295 (= E295), R337 (= R337)
- binding phosphoaminophosphonic acid-adenylate ester: K114 (= K115), I154 (≠ M155), K156 (= K157), G161 (= G162), G163 (= G164), I166 (= I167), F200 (≠ C201), I201 (= I202), E273 (= E274), I275 (≠ L276), M286 (= M286), E287 (= E287)
- binding magnesium ion: E273 (= E274), E287 (= E287)
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
51% identity, 94% coverage: 1:442/472 of query aligns to 1:439/442 of 4mv4A
- active site: K116 (= K115), K159 (= K157), D193 (≠ A194), H206 (= H207), R232 (= R233), T271 (= T272), E273 (= E274), E285 (= E287), N287 (= N289), R289 (= R291), E293 (= E295), R335 (= R337)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K157), G164 (= G162), M166 (≠ G164), E198 (= E199), Y200 (≠ C201), L201 (≠ I202), H233 (≠ N234), L275 (= L276), E285 (= E287)
- binding magnesium ion: E273 (= E274), E285 (= E287)
A0A0H3JRU9 Pyruvate carboxylase; EC 6.4.1.1 from Staphylococcus aureus (strain Mu50 / ATCC 700699) (see 2 papers)
48% identity, 94% coverage: 2:446/472 of query aligns to 4:456/1150 of A0A0H3JRU9
- R21 (= R19) mutation to A: Complete loss of catalytic activity.
- K119 (= K115) binding ATP
- K161 (= K157) binding ATP
- H211 (= H207) binding ATP
- E278 (= E274) binding ATP
- K411 (≠ R401) mutation to A: Complete loss of catalytic activity.
Sites not aligning to the query:
- 541:545 binding substrate
- 542 binding Mn(2+)
- 580 A→T: Complete loss of catalytic activity.
- 614 R→A: Complete loss of catalytic activity.
- 621 Y→A: Complete loss of catalytic activity.
- 712 binding Mn(2+)
- 741 binding Mn(2+)
- 743 binding Mn(2+)
- 838 Q→A: About 2.5-fold loss of catalytic activity.
- 876 T→A: Complete loss of catalytic activity.
- 879 S→A: About 2-fold loss of catalytic activity.
- 880 K→T: Complete loss of catalytic activity.
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
51% identity, 94% coverage: 1:442/472 of query aligns to 1:440/444 of 2vr1A
- active site: K116 (= K115), K159 (= K157), D194 (≠ A194), H207 (= H207), R233 (= R233), T272 (= T272), E274 (= E274), E286 (= E287), N288 (= N289), R290 (= R291), E294 (= E295), R336 (= R337)
- binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (= K157), R165 (= R165), M167 (≠ I167), Y201 (≠ C201), L202 (≠ I202), E274 (= E274), L276 (= L276), E286 (= E287), N288 (= N289), I435 (≠ T437)
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, 94% coverage: 1:442/472 of query aligns to 1:437/440 of 6oi8A
- active site: K116 (= K115), K159 (= K157), D191 (≠ A194), H204 (= H207), R230 (= R233), T269 (= T272), E271 (= E274), 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 (≠ M155), K159 (= K157), M164 (≠ G164), E196 (= E199), Y198 (≠ C201), L199 (≠ I202), H204 (= H207), Q228 (= Q231), E271 (= E274), L273 (= L276), E283 (= E287), I432 (≠ T437)
4mv3A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and bicarbonate (see paper)
50% identity, 94% coverage: 1:442/472 of query aligns to 1:436/439 of 4mv3A
- active site: K116 (= K115), K159 (= K157), D190 (≠ A194), H203 (= H207), R229 (= R233), T268 (= T272), E270 (= E274), E282 (= E287), N284 (= N289), R286 (= R291), E290 (= E295), R332 (= R337)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K157), M163 (≠ I167), E195 (= E199), Y197 (≠ C201), L198 (≠ I202), E270 (= E274), L272 (= L276), E282 (= E287)
- binding bicarbonate ion: R286 (= R291), Q288 (= Q293), V289 (= V294)
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, 94% coverage: 1:442/472 of query aligns to 1:442/445 of 6ojhA
- active site: K116 (= K115), K159 (= K157), D196 (≠ A194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E287), N290 (= N289), R292 (= R291), E296 (= E295), R338 (= R337)
- binding calcium ion: E276 (= E274), E288 (= E287), N290 (= N289)
- binding 7-[(3R)-3-aminopyrrolidin-1-yl]-6-(naphthalen-1-yl)pyrido[2,3-d]pyrimidin-2-amine: K159 (= K157), M169 (≠ I167), E201 (= E199), Y203 (≠ C201), L204 (≠ I202), H236 (≠ N234), L278 (= L276), E288 (= E287), I437 (≠ T437)
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, 94% coverage: 1:442/472 of query aligns to 1:442/448 of P43873
- K116 (= K115) binding ATP
- K159 (= K157) binding ATP
- EKYL 201:204 (≠ EKCI 199:202) binding ATP
- E276 (= E274) binding ATP; binding Mg(2+)
- E288 (= E287) binding ATP; binding Mg(2+)
- N290 (= N289) binding Mg(2+)
3rupA Crystal structure of e.Coli biotin carboxylase in complex with two adp and two ca ions (see paper)
51% identity, 94% coverage: 1:442/472 of query aligns to 1:442/444 of 3rupA
- active site: K116 (= K115), K159 (= K157), D196 (≠ A194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E287), N290 (= N289), R292 (= R291), E296 (= E295), R338 (= R337)
- binding adenosine-5'-diphosphate: Y82 (= Y81), G83 (= G82), K116 (= K115), K159 (= K157), G164 (= G162), G164 (= G162), G165 (= G163), G166 (= G164), R167 (= R165), M169 (≠ I167), F193 (= F191), E201 (= E199), K202 (= K200), Y203 (≠ C201), L204 (≠ I202), H209 (= H207), Q233 (= Q231), H236 (≠ N234), K238 (= K236), L278 (= L276), E288 (= E287), R292 (= R291), V295 (= V294), E296 (= E295), R338 (= R337), D382 (= D382), I437 (≠ T437)
- binding calcium ion: E87 (= E86), E276 (= E274), E288 (= E287), E288 (= E287), N290 (= N289)
3g8cA Crystal structure of biotin carboxylase in complex with biotin, bicarbonate, adp and mg ion (see paper)
51% identity, 94% coverage: 1:442/472 of query aligns to 1:442/444 of 3g8cA
- active site: K116 (= K115), K159 (= K157), D196 (≠ A194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E287), N290 (= N289), R292 (= R291), E296 (= E295), R338 (= R337)
- binding adenosine-5'-diphosphate: I157 (≠ M155), K159 (= K157), G164 (= G162), M169 (≠ I167), E201 (= E199), K202 (= K200), Y203 (≠ C201), L204 (≠ I202), Q233 (= Q231), H236 (≠ N234), L278 (= L276), E288 (= E287), I437 (≠ T437)
- binding bicarbonate ion: K238 (= K236), R292 (= R291), Q294 (= Q293), V295 (= V294), E296 (= E295)
- binding biotin: Y82 (= Y81), F84 (= F83), R292 (= R291), V295 (= V294), R338 (= R337), D382 (= D382)
- binding magnesium ion: E276 (= E274), E288 (= E287)
P24182 Biotin carboxylase; Acetyl-coenzyme A carboxylase biotin carboxylase subunit A; EC 6.3.4.14 from Escherichia coli (strain K12) (see 3 papers)
51% identity, 94% coverage: 1:442/472 of query aligns to 1:442/449 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 (= K115) binding ATP
- K159 (= K157) binding ATP
- GG 165:166 (= GG 163:164) binding ATP
- EKYL 201:204 (≠ EKCI 199:202) binding ATP
- H209 (= H207) binding ATP
- H236 (≠ N234) binding ATP
- K238 (= K236) binding hydrogencarbonate
- E276 (= E274) 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 (≠ 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.
3jzfB Crystal structure of biotin carboxylase from e. Coli in complex with benzimidazoles series (see paper)
51% identity, 94% coverage: 1:442/472 of query aligns to 3:444/447 of 3jzfB
- active site: K118 (= K115), K161 (= K157), D198 (≠ A194), H211 (= H207), R237 (= R233), T276 (= T272), E278 (= E274), E290 (= E287), N292 (= N289), R294 (= R291), E298 (= E295), R340 (= R337)
- binding 2-[(2-chlorobenzyl)amino]-1-(cyclohexylmethyl)-1H-benzimidazole-5-carboxamide: K118 (= K115), K161 (= K157), A162 (= A158), G166 (= G162), G168 (= G164), R169 (= R165), G170 (= G166), M171 (≠ I167), Y201 (≠ F197), E203 (= E199), K204 (= K200), Y205 (≠ C201), H211 (= H207), H238 (≠ N234), L280 (= L276), I289 (≠ M286), E290 (= E287)
3jziA Crystal structure of biotin carboxylase from e. Coli in complex with benzimidazole series (see paper)
51% identity, 94% coverage: 1:442/472 of query aligns to 1:442/445 of 3jziA
- active site: K116 (= K115), K159 (= K157), D196 (≠ A194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E287), N290 (= N289), R292 (= R291), E296 (= E295), R338 (= R337)
- binding 7-amino-2-[(2-chlorobenzyl)amino]-1-{[(1S,2S)-2-hydroxycycloheptyl]methyl}-1H-benzimidazole-5-carboxamide: K116 (= K115), K159 (= K157), A160 (= A158), G164 (= G162), G165 (= G163), M169 (≠ I167), Y199 (≠ F197), E201 (= E199), K202 (= K200), Y203 (≠ C201), H209 (= H207), Q233 (= Q231), H236 (≠ N234), L278 (= L276), I287 (≠ M286), E288 (= E287)
2w6oA Crystal structure of biotin carboxylase from e. Coli in complex with 4-amino-7,7-dimethyl-7,8-dihydro-quinazolinone fragment (see paper)
51% identity, 94% coverage: 1:442/472 of query aligns to 1:442/445 of 2w6oA
- active site: K116 (= K115), K159 (= K157), D196 (≠ A194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E287), N290 (= N289), R292 (= R291), E296 (= E295), R338 (= R337)
- binding 4-amino-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-one: K159 (= K157), K202 (= K200), Y203 (≠ C201), L204 (≠ I202), L278 (= L276), I437 (≠ T437)
2w6nA Crystal structure of biotin carboxylase from e. Coli in complex with amino-oxazole fragment series (see paper)
51% identity, 94% coverage: 1:442/472 of query aligns to 1:442/445 of 2w6nA
- active site: K116 (= K115), K159 (= K157), D196 (≠ A194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E287), N290 (= N289), R292 (= R291), E296 (= E295), R338 (= R337)
- binding 2-amino-n,n-bis(phenylmethyl)-1,3-oxazole-5-carboxamide: I157 (≠ M155), K159 (= K157), M169 (≠ I167), E201 (= E199), K202 (= K200), Y203 (≠ C201), L278 (= L276)
2v59A Crystal structure of biotin carboxylase from e.Coli in complex with potent inhibitor 2 (see paper)
51% identity, 94% coverage: 1:442/472 of query aligns to 1:442/445 of 2v59A
- active site: K116 (= K115), K159 (= K157), D196 (≠ A194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E287), N290 (= N289), R292 (= R291), E296 (= E295), R338 (= R337)
- binding 6-(2,6-dimethoxyphenyl)pyrido[2,3-d]pyrimidine-2,7-diamine: K159 (= K157), Y203 (≠ C201), L204 (≠ I202), H209 (= H207), Q233 (= Q231), H236 (≠ N234), L278 (= L276), I437 (≠ T437)
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)
51% identity, 94% coverage: 1:442/472 of query aligns to 1:442/446 of 6oi9A
- active site: E276 (= E274), 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 (= K157), M169 (≠ I167), E201 (= E199), Y203 (≠ C201), L204 (≠ I202), H209 (= H207), Q233 (= Q231), H236 (≠ N234), E276 (= E274), L278 (= L276), E288 (= E287), I437 (≠ T437)
2w71A Crystal structure of biotin carboxylase from e. Coli in complex with the imidazole-pyrimidine inhibitor (see paper)
51% identity, 94% coverage: 1:442/472 of query aligns to 1:442/446 of 2w71A
- active site: K116 (= K115), K159 (= K157), D196 (≠ A194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), 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 (= K157), Y203 (≠ C201), L204 (≠ I202), H209 (= H207), Q233 (= Q231), H236 (≠ N234), L278 (= L276), I437 (≠ T437)
2w70A Crystal structure of biotin carboxylase from e. Coli in complex with the amino-thiazole-pyrimidine fragment (see paper)
51% identity, 94% coverage: 1:442/472 of query aligns to 1:442/446 of 2w70A
- active site: K116 (= K115), K159 (= K157), D196 (≠ A194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E287), N290 (= N289), R292 (= R291), E296 (= E295), R338 (= R337)
- binding 4-(2-amino-1,3-thiazol-4-yl)pyrimidin-2-amine: I157 (≠ M155), K159 (= K157), G166 (= G164), M169 (≠ I167), E201 (= E199), Y203 (≠ C201), L204 (≠ I202), L278 (= L276)
Query Sequence
>WP_020563409.1 NCBI__GCF_000372865.1:WP_020563409.1
MLRKILIANRGEIAVRIIRACAEMGIRSVAIYTEADRFALHVKKADESYCIGSEPVAGYL
NVYALVDLAAATGCDAVHPGYGFLSENPQFARACKERGLIFIGPDADIIRRMGDKTEARK
AMVAAGIPVTPGSDGNLGTVEEALDVAERIGYPVMLKATSGGGGRGIRRCDSTQDLRRNY
QRVISEATKAFGSAEVFLEKCIVNPRHIEVQILADHDGNTIHLFERDCSIQRRNQKLIEI
APSPQLDEAQRQYLGGLAVLAAKAVGYTNAGTVEFLLDDQGRFYFMEMNTRVQVEHTITE
TITGVDIVEEQIRVAAGLPLRFKQEEIVRRGYAIQFRINAEDPKNGFLPSFGRISRYYAP
GGPGVRTDTAIYTGYEIPPYFDSMLAKVIVNALTWEDAVKRGERALRDMGLFGIKTTIPY
YLEILKHPEFREADFNTGFVEKHPELVHYSNKPRPEVLASVIAAAMAAHTGL
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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