SitesBLAST
Comparing GFF4012 FitnessBrowser__psRCH2:GFF4012 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)
54% identity, 95% coverage: 1:449/471 of query aligns to 3:452/453 of 7kctA
- active site: E276 (= E274), E289 (= E286), N291 (= N288), E297 (= E294), R339 (= R336)
- 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 (= E286), R293 (= R290), Q295 (= Q292), V296 (= V293), E297 (= E294), R339 (= R336)
- binding bicarbonate ion: D116 (= D114), R119 (≠ E117)
- binding magnesium ion: E276 (= E274), E289 (= E286)
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
53% identity, 93% coverage: 3:442/471 of query aligns to 1:443/448 of 2vpqB
- active site: V116 (≠ E117), K156 (= K157), H206 (= H207), R232 (= R233), T271 (= T272), E273 (= E274), E287 (= E286), N289 (= N288), R291 (= R290), E295 (= E294), R337 (= R336)
- 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 (= M285), E287 (= E286)
- binding magnesium ion: E273 (= E274), E287 (= E286)
A0A0H3JRU9 Pyruvate carboxylase; EC 6.4.1.1 from Staphylococcus aureus (strain Mu50 / ATCC 700699) (see 2 papers)
48% identity, 95% coverage: 2:447/471 of query aligns to 4:458/1150 of A0A0H3JRU9
- R21 (= R19) mutation to A: Complete loss of catalytic activity.
- K119 (= K115) binding
- K161 (= K157) binding
- H211 (= H207) binding
- E278 (= E274) binding
- K411 (≠ R400) mutation to A: Complete loss of catalytic activity.
Sites not aligning to the query:
- 541:545 binding
- 542 binding
- 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
- 741 binding
- 743 binding
- 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)
50% identity, 93% coverage: 1:440/471 of query aligns to 1:439/444 of 2vr1A
- active site: K116 (= K115), K159 (= K157), D194 (≠ A194), H207 (= H207), R233 (= R233), T272 (= T272), E274 (= E274), E286 (= E286), N288 (= N288), R290 (= R290), E294 (= E294), R336 (= R336)
- binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (= K157), R165 (= R165), M167 (≠ I167), Y201 (≠ C201), L202 (≠ I202), E274 (= E274), L276 (= L276), E286 (= E286), N288 (= N288), I435 (≠ T436)
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
50% identity, 93% coverage: 1:440/471 of query aligns to 1:438/442 of 4mv4A
- active site: K116 (= K115), K159 (= K157), D193 (≠ A194), H206 (= H207), R232 (= R233), T271 (= T272), E273 (= E274), E285 (= E286), N287 (= N288), R289 (= R290), E293 (= E294), R335 (= R336)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K157), G164 (= G162), M166 (≠ G164), E198 (= E199), Y200 (≠ C201), L201 (≠ I202), H233 (≠ N234), L275 (= L276), E285 (= E286)
- binding magnesium ion: E273 (= E274), E285 (= E286)
8hz4A The tetrameric structure of biotin carboxylase from chloroflexus aurantiacus in complex with bicarbonate
50% identity, 96% coverage: 1:454/471 of query aligns to 1:452/456 of 8hz4A
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, 93% coverage: 1:440/471 of query aligns to 1:441/449 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
- K159 (= K157) binding
- GG 165:166 (= GG 163:164) binding
- EKYL 201:204 (≠ EKCI 199:202) binding
- H209 (= H207) binding
- H236 (≠ N234) binding
- K238 (= K236) binding
- E276 (= E274) binding ; binding
- E288 (= E286) binding ; binding
- R292 (= R290) active site; binding
- V295 (= V293) binding
- E296 (= E294) mutation to A: Severe reduction in catalytic activity.
- R338 (= R336) binding ; binding ; 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.
3bg5A Crystal structure of staphylococcus aureus pyruvate carboxylase (see paper)
47% identity, 95% coverage: 2:447/471 of query aligns to 2:449/1137 of 3bg5A
- active site: K117 (= K115), K159 (= K157), S189 (≠ A194), H202 (= H207), R228 (= R233), T267 (= T272), E269 (= E274), E281 (= E286), N283 (= N288), R285 (= R290), E289 (= E294), R337 (= R336)
- binding adenosine-5'-triphosphate: K117 (= K115), M157 (= M155), K159 (= K157), Y196 (≠ C201), I197 (= I202), H202 (= H207), Q226 (= Q231), H229 (≠ N234), E269 (= E274), L271 (= L276), E281 (= E286), N283 (= N288)
Sites not aligning to the query:
- active site: 533, 639, 703, 732, 734, 755, 761, 762, 801, 867, 869, 881, 883, 888
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: 463, 471, 472, 473, 579
- binding manganese (ii) ion: 533, 732, 734
- binding pyruvic acid: 603, 703
3rupA Crystal structure of e.Coli biotin carboxylase in complex with two adp and two ca ions (see paper)
51% identity, 93% coverage: 1:440/471 of query aligns to 1:441/444 of 3rupA
- active site: K116 (= K115), K159 (= K157), D196 (≠ A194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E286), N290 (= N288), R292 (= R290), E296 (= E294), R338 (= R336)
- 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 (= E286), R292 (= R290), V295 (= V293), E296 (= E294), R338 (= R336), D382 (= D381), I437 (≠ T436)
- binding calcium ion: E87 (= E86), E276 (= E274), E288 (= E286), E288 (= E286), N290 (= N288)
3g8cA Crystal structure of biotin carboxylase in complex with biotin, bicarbonate, adp and mg ion (see paper)
51% identity, 93% coverage: 1:440/471 of query aligns to 1:441/444 of 3g8cA
- active site: K116 (= K115), K159 (= K157), D196 (≠ A194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E286), N290 (= N288), R292 (= R290), E296 (= E294), R338 (= R336)
- 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 (= E286), I437 (≠ T436)
- binding bicarbonate ion: K238 (= K236), R292 (= R290), Q294 (= Q292), V295 (= V293), E296 (= E294)
- binding biotin: Y82 (= Y81), F84 (= F83), R292 (= R290), V295 (= V293), R338 (= R336), D382 (= D381)
- binding magnesium ion: E276 (= E274), E288 (= E286)
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, 93% coverage: 1:440/471 of query aligns to 1:441/446 of 6oi9A
- active site: E276 (= E274), E288 (= E286), N290 (= N288), E296 (= E294), R338 (= R336)
- 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 (= E286), I437 (≠ T436)
3jziA Crystal structure of biotin carboxylase from e. Coli in complex with benzimidazole series (see paper)
51% identity, 93% coverage: 1:440/471 of query aligns to 1:441/445 of 3jziA
- active site: K116 (= K115), K159 (= K157), D196 (≠ A194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E286), N290 (= N288), R292 (= R290), E296 (= E294), R338 (= R336)
- 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 (≠ M285), E288 (= E286)
2w71A Crystal structure of biotin carboxylase from e. Coli in complex with the imidazole-pyrimidine inhibitor (see paper)
51% identity, 93% coverage: 1:440/471 of query aligns to 1:441/446 of 2w71A
- active site: K116 (= K115), K159 (= K157), D196 (≠ A194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E286), N290 (= N288), R292 (= R290), E296 (= E294), R338 (= R336)
- 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 (≠ T436)
2w70A Crystal structure of biotin carboxylase from e. Coli in complex with the amino-thiazole-pyrimidine fragment (see paper)
51% identity, 93% coverage: 1:440/471 of query aligns to 1:441/446 of 2w70A
- active site: K116 (= K115), K159 (= K157), D196 (≠ A194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E286), N290 (= N288), R292 (= R290), E296 (= E294), R338 (= R336)
- 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)
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)
51% identity, 93% coverage: 1:440/471 of query aligns to 1:441/446 of 2w6zA
- active site: K116 (= K115), K159 (= K157), D196 (≠ A194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E286), N290 (= N288), R292 (= R290), E296 (= E294), R338 (= R336)
- binding 3-(3-methylbut-2-en-1-yl)-3H-purin-6-amine: K159 (= K157), Y203 (≠ C201), L204 (≠ I202), L278 (= L276)
2w6qA Crystal structure of biotin carboxylase from e. Coli in complex with the triazine-2,4-diamine fragment (see paper)
51% identity, 93% coverage: 1:440/471 of query aligns to 1:441/446 of 2w6qA
- active site: K116 (= K115), K159 (= K157), D196 (≠ A194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E286), N290 (= N288), R292 (= R290), E296 (= E294), R338 (= R336)
- binding 6-(2-phenoxyethoxy)-1,3,5-triazine-2,4-diamine: I157 (≠ M155), K159 (= K157), E201 (= E199), K202 (= K200), Y203 (≠ C201), L204 (≠ I202), H236 (≠ N234), L278 (= L276)
2w6pA Crystal structure of biotin carboxylase from e. Coli in complex with 5-methyl-6-phenyl-quinazoline-2,4-diamine (see paper)
51% identity, 93% coverage: 1:440/471 of query aligns to 1:441/446 of 2w6pA
- active site: K116 (= K115), K159 (= K157), D196 (≠ A194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E286), N290 (= N288), R292 (= R290), E296 (= E294), R338 (= R336)
- binding 5-methyl-6-phenylquinazoline-2,4-diamine: K159 (= K157), Y203 (≠ C201), L204 (≠ I202), Q233 (= Q231), H236 (≠ N234), L278 (= L276), I437 (≠ T436)
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, 93% coverage: 1:440/471 of query aligns to 1:441/445 of 2w6oA
- active site: K116 (= K115), K159 (= K157), D196 (≠ A194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E286), N290 (= N288), R292 (= R290), E296 (= E294), R338 (= R336)
- binding 4-amino-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-one: K159 (= K157), K202 (= K200), Y203 (≠ C201), L204 (≠ I202), L278 (= L276), I437 (≠ T436)
2w6nA Crystal structure of biotin carboxylase from e. Coli in complex with amino-oxazole fragment series (see paper)
51% identity, 93% coverage: 1:440/471 of query aligns to 1:441/445 of 2w6nA
- active site: K116 (= K115), K159 (= K157), D196 (≠ A194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E286), N290 (= N288), R292 (= R290), E296 (= E294), R338 (= R336)
- 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)
2w6mA Crystal structure of biotin carboxylase from e. Coli in complex with amino-oxazole fragment series (see paper)
51% identity, 93% coverage: 1:440/471 of query aligns to 1:441/446 of 2w6mA
- active site: K116 (= K115), K159 (= K157), D196 (≠ A194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E286), N290 (= N288), R292 (= R290), E296 (= E294), R338 (= R336)
- binding (2-amino-1,3-oxazol-5-yl)-(3-bromophenyl)methanone: I157 (≠ M155), K159 (= K157), M169 (≠ I167), E201 (= E199), K202 (= K200), Y203 (≠ C201), H236 (≠ N234), L278 (= L276), I437 (≠ T436)
Query Sequence
>GFF4012 FitnessBrowser__psRCH2:GFF4012
MIKKLLIANRGEIAVRIVRACAEMGVRSVAVFSEADRHALHVKRADEAHFIGEDPLAGYL
NPRKLVNLAVETGCDALHPGYGFLSENAELADICAERGIKFVGPSAEVIRRMGDKTEARR
SMIKAGVPVTPGTEGNVRDLAEALREAERIGYPVMLKATSGGGGRGIRRCNSQAELESAY
PRVISEATKAFGSAEVFLEKCIVEPKHIEAQILADSFGNTVHLFERDCSIQRRNQKLIEI
APSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLADGEVYFMEMNTRVQVEHTITEE
ITGIDIVREQIRIASGQPLSVKQEDIQHRGFSLQFRINAEDPRNNFLPCFGKITRYYAPG
GPGVRTDTAIYTGYTIPPYYDSMCLKLVVWALTWEEALARGSRALDDMRVQGVKTTATYY
QQILANPDFRSGQFNTSFVDNHPELLNYSIKRKPGELALAIAAAIAAHAGL
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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