SitesBLAST
Comparing GFF3994 FitnessBrowser__Marino:GFF3994 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)
55% identity, 95% coverage: 3:451/473 of query aligns to 4:452/453 of 7kctA
- active site: E276 (= E275), E289 (= E288), N291 (= N290), E297 (= E296), R339 (= R338)
- binding adenosine-5'-diphosphate: K117 (= K116), L157 (≠ M156), K159 (= K158), G164 (= G163), G165 (= G164), G166 (= G165), I169 (= I168), E201 (= E200), Y203 (≠ C202), I204 (= I203), H209 (= H208), Q233 (= Q232), Q237 (= Q236), K238 (= K237), I278 (≠ L277), E289 (= E288), R293 (= R292), Q295 (= Q294), V296 (= V295), E297 (= E296), R339 (= R338)
- binding bicarbonate ion: D116 (= D115), R119 (≠ Q118)
- binding magnesium ion: E276 (= E275), E289 (= E288)
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
52% identity, 93% coverage: 4:444/473 of query aligns to 1:443/448 of 2vpqB
- active site: V116 (≠ Q118), K156 (= K158), H206 (= H208), R232 (= R234), T271 (= T273), E273 (= E275), E287 (= E288), N289 (= N290), R291 (= R292), E295 (= E296), R337 (= R338)
- binding phosphoaminophosphonic acid-adenylate ester: K114 (= K116), I154 (≠ M156), K156 (= K158), G161 (= G163), G163 (= G165), I166 (= I168), F200 (≠ C202), I201 (= I203), E273 (= E275), I275 (≠ L277), M286 (= M287), E287 (= E288)
- binding magnesium ion: E273 (= E275), E287 (= E288)
A0A0H3JRU9 Pyruvate carboxylase; EC 6.4.1.1 from Staphylococcus aureus (strain Mu50 / ATCC 700699) (see 2 papers)
48% identity, 95% coverage: 3:449/473 of query aligns to 4:458/1150 of A0A0H3JRU9
- R21 (= R20) mutation to A: Complete loss of catalytic activity.
- K119 (= K116) binding
- K161 (= K158) binding
- H211 (= H208) binding
- E278 (= E275) binding
- K411 (≠ R402) 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.
5vyzA Crystal structure of lactococcus lactis pyruvate carboxylase in complex with cyclic-di-amp (see paper)
49% identity, 95% coverage: 3:450/473 of query aligns to 8:461/1144 of 5vyzA
- binding adenosine-5'-diphosphate: K123 (= K116), M162 (= M156), K164 (= K158), G168 (= G162), G170 (= G164), G171 (= G165), M174 (≠ I168), Y208 (≠ C202), I209 (= I203), H214 (= H208), Q238 (= Q232), N241 (= N235), L283 (= L277), E293 (= E288), T449 (= T438)
- binding magnesium ion: E281 (= E275), E293 (= E288)
Sites not aligning to the query:
- binding (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide: 719, 722, 752, 753, 756
- binding manganese (ii) ion: 541, 710, 739, 741
7zz3A Cryo-em structure of "bc react" conformation of lactococcus lactis pyruvate carboxylase with acetyl-coa (see paper)
49% identity, 95% coverage: 3:450/473 of query aligns to 2:455/1138 of 7zz3A
- binding acetyl coenzyme *a: N22 (≠ S23), F43 (≠ K44), K44 (= K45), A45 (= A46), D46 (= D47), S48 (≠ A49), R363 (≠ Y359), H413 (≠ G408), E414 (≠ D409), R416 (≠ G411), R418 (≠ Y413)
- binding adenosine-5'-triphosphate: K117 (= K116), M156 (= M156), K158 (= K158), G163 (= G163), G164 (= G164), G165 (= G165), M168 (≠ I168), E200 (= E200), Y202 (≠ C202), I203 (= I203), H208 (= H208), Q232 (= Q232), N235 (= N235), L277 (= L277), E287 (= E288), N289 (= N290), T443 (= T438)
- binding bicarbonate ion: K237 (= K237), R291 (= R292), Q293 (= Q294), E295 (= E296)
- binding biotin: G84 (= G83), V294 (= V295), R342 (= R338)
- binding magnesium ion: E275 (= E275), E287 (= E288)
Sites not aligning to the query:
- binding acetyl coenzyme *a: 459, 461, 1016, 1017, 1018, 1045
- binding biotin: 1104
- binding magnesium ion: 520, 523, 754
- binding manganese (ii) ion: 535, 704, 733, 735
- binding pyruvic acid: 534, 538, 605, 704, 868
7zyyA Cryo-em structure of lactococcus lactis pyruvate carboxylase with acetyl-coa (see paper)
49% identity, 95% coverage: 3:450/473 of query aligns to 2:455/1056 of 7zyyA
- binding acetyl coenzyme *a: R19 (= R20), N22 (≠ S23), F43 (≠ K44), K44 (= K45), A45 (= A46), R363 (≠ Y359), E414 (≠ D409), R416 (≠ G411), R418 (≠ Y413)
- binding adenosine-5'-diphosphate: K158 (= K158), G163 (= G163), G164 (= G164), M168 (≠ I168), E200 (= E200), K201 (= K201), Y202 (≠ C202), I203 (= I203), H208 (= H208), Q232 (= Q232), N235 (= N235), E275 (= E275), L277 (= L277), E287 (= E288), T443 (= T438)
- binding bicarbonate ion: R291 (= R292), Q293 (= Q294), V294 (= V295), E295 (= E296)
- binding magnesium ion: E275 (= E275), E287 (= E288)
Sites not aligning to the query:
- binding acetyl coenzyme *a: 459, 460, 461, 1016, 1017, 1018, 1041, 1045
- binding magnesium ion: 520, 523, 754
- binding manganese (ii) ion: 535, 704, 733, 735
- binding pyruvic acid: 538, 572, 605, 607, 704, 868
Q05920 Pyruvate carboxylase, mitochondrial; Pyruvic carboxylase; PCB; EC 6.4.1.1 from Mus musculus (Mouse) (see paper)
47% identity, 95% coverage: 3:449/473 of query aligns to 37:489/1178 of Q05920
- K39 (= K5) modified: N6-acetyllysine
- K79 (= K45) modified: N6-acetyllysine; alternate; mutation K->Q,R: Reduced pyruvate carboxylase activity.
- K148 (≠ S112) modified: N6-acetyllysine
- K152 (= K116) modified: N6-acetyllysine; mutation K->Q,R: Reduced pyruvate carboxylase activity.
- K241 (≠ E205) modified: N6-acetyllysine
- K434 (≠ M394) modified: N6-acetyllysine
Sites not aligning to the query:
- 35 modified: N6-acetyllysine
- 589 modified: N6-acetyllysine
- 717 modified: N6-acetyllysine
- 748 modified: N6-acetyllysine; K→Q: Reduced pyruvate carboxylase activity.
- 892 modified: N6-acetyllysine
- 969 modified: N6-acetyllysine
3tw6B Structure of rhizobium etli pyruvate carboxylase t882a with the allosteric activator, acetyl coenzyme-a (see paper)
46% identity, 95% coverage: 3:449/473 of query aligns to 3:461/1129 of 3tw6B
- active site: K124 (= K116), K162 (= K158), H212 (= H208), R238 (= R234), T277 (= T273), E279 (= E275), E293 (= E288), N295 (= N290), R297 (= R292), E301 (= E296), R349 (= R338)
- binding adenosine-5'-diphosphate: K124 (= K116), K162 (= K158), G167 (= G163), G169 (= G165), M172 (≠ I168), E204 (= E200), L206 (≠ C202), V207 (≠ I203), H212 (= H208), Q236 (= Q232), N239 (= N235), L281 (= L277), E293 (= E288), T450 (= T438)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: R349 (= R338), D395 (= D383)
- binding magnesium ion: E279 (= E275), E293 (= E288)
Sites not aligning to the query:
- active site: 544, 650, 713, 742, 744, 877
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: 1102
- binding magnesium ion: 529, 530, 532, 763
- binding zinc ion: 544, 713, 742, 744
3bg5A Crystal structure of staphylococcus aureus pyruvate carboxylase (see paper)
47% identity, 95% coverage: 3:449/473 of query aligns to 2:449/1137 of 3bg5A
- active site: K117 (= K116), K159 (= K158), S189 (≠ A195), H202 (= H208), R228 (= R234), T267 (= T273), E269 (= E275), E281 (= E288), N283 (= N290), R285 (= R292), E289 (= E296), R337 (= R338)
- binding adenosine-5'-triphosphate: K117 (= K116), M157 (= M156), K159 (= K158), Y196 (≠ C202), I197 (= I203), H202 (= H208), Q226 (= Q232), H229 (≠ N235), E269 (= E275), L271 (= L277), E281 (= E288), N283 (= N290)
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
P11498 Pyruvate carboxylase, mitochondrial; Pyruvic carboxylase; PCB; EC 6.4.1.1 from Homo sapiens (Human) (see 6 papers)
47% identity, 95% coverage: 3:449/473 of query aligns to 37:489/1178 of P11498
- V145 (≠ A109) to A: in PC deficiency; mild; strongly reduced pyruvate carboxylase activity; dbSNP:rs28940591
- R156 (= R120) to Q: in PC deficiency; dbSNP:rs119103241
- R270 (= R234) to W: in PC deficiency; dbSNP:rs1258494752
- Y304 (= Y268) to C: in PC deficiency
- R451 (≠ G411) to C: in PC deficiency; mild; strongly reduced pyruvate carboxylase activity; dbSNP:rs113994143
Sites not aligning to the query:
- 572 binding
- 583 R → L: in PC deficiency; dbSNP:rs119103242
- 610 A → T: in PC deficiency; mild; dbSNP:rs28940589
- 631 R → Q: in PC deficiency; dbSNP:rs113994145
- 741 binding via carbamate group; modified: N6-carboxylysine
- 743 M → I: in PC deficiency; mild; dbSNP:rs28940590
- 771 binding
- 773 binding
- 1077 mutation F->A,E: Loss of tetramerization and enzyme activity, resulting in an inactive homodimer.
- 1131:1133 natural variant: Missing (in PC deficiency)
- 1144 modified: N6-biotinyllysine
7wtbB Cryo-em structure of human pyruvate carboxylase with acetyl-coa (see paper)
47% identity, 95% coverage: 3:449/473 of query aligns to 6:458/1147 of 7wtbB
- binding acetyl coenzyme *a: F22 (≠ A19), T26 (≠ S23), R46 (≠ V43), Q47 (≠ K44), K48 (= K45), A49 (= A46), D50 (= D47), R367 (≠ Y359), R414 (= R405), E418 (≠ D409), R420 (≠ G411), R422 (≠ Y413)
- binding phosphoaminophosphonic acid-adenylate ester: K163 (= K158), G168 (= G163), G169 (= G164), M173 (≠ I168), F207 (≠ C202), I208 (= I203), P211 (= P206), H240 (≠ N235)
Sites not aligning to the query:
7wtdC Cryo-em structure of human pyruvate carboxylase with acetyl-coa in the intermediate state 1 (see paper)
47% identity, 95% coverage: 3:449/473 of query aligns to 5:457/1146 of 7wtdC
- binding adenosine-5'-triphosphate: K162 (= K158), G167 (= G163), G168 (= G164), F206 (≠ C202), Q236 (= Q232), H239 (≠ N235), E292 (= E288)
- binding coenzyme a: F21 (≠ A19), R22 (= R20), T25 (≠ S23), R45 (≠ V43), Q46 (≠ K44), K47 (= K45), A48 (= A46), D49 (= D47), E50 (= E48), R366 (≠ Y359), R413 (= R405), A416 (≠ G408), R419 (≠ G411)
Sites not aligning to the query:
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
49% identity, 93% coverage: 3:443/473 of query aligns to 2:439/442 of 4mv4A
- active site: K116 (= K116), K159 (= K158), D193 (≠ A195), H206 (= H208), R232 (= R234), T271 (= T273), E273 (= E275), E285 (= E288), N287 (= N290), R289 (= R292), E293 (= E296), R335 (= R338)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K158), G164 (= G163), M166 (≠ G165), E198 (= E200), Y200 (≠ C202), L201 (≠ I203), H233 (≠ N235), L275 (= L277), E285 (= E288)
- binding magnesium ion: E273 (= E275), E285 (= E288)
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
49% identity, 93% coverage: 5:444/473 of query aligns to 4:441/444 of 2vr1A
- active site: K116 (= K116), K159 (= K158), D194 (≠ A195), H207 (= H208), R233 (= R234), T272 (= T273), E274 (= E275), E286 (= E288), N288 (= N290), R290 (= R292), E294 (= E296), R336 (= R338)
- binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (= K158), R165 (= R166), M167 (≠ I168), Y201 (≠ C202), L202 (≠ I203), E274 (= E275), L276 (= L277), E286 (= E288), N288 (= N290), I435 (≠ T438)
8hz4A The tetrameric structure of biotin carboxylase from chloroflexus aurantiacus in complex with bicarbonate
48% identity, 97% coverage: 3:460/473 of query aligns to 2:456/456 of 8hz4A
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)
49% identity, 93% coverage: 3:443/473 of query aligns to 2:437/440 of 6oi8A
- active site: K116 (= K116), K159 (= K158), D191 (≠ A195), H204 (= H208), R230 (= R234), T269 (= T273), E271 (= E275), 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 (≠ M156), K159 (= K158), M164 (≠ G165), E196 (= E200), Y198 (≠ C202), L199 (≠ I203), H204 (= H208), Q228 (= Q232), E271 (= E275), L273 (= L277), E283 (= E288), I432 (≠ T438)
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
50% identity, 93% coverage: 3:443/473 of query aligns to 2:442/445 of 6ojhA
- active site: K116 (= K116), K159 (= K158), D196 (≠ A195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R338)
- binding calcium ion: E276 (= E275), E288 (= E288), N290 (= N290)
- binding 7-[(3R)-3-aminopyrrolidin-1-yl]-6-(naphthalen-1-yl)pyrido[2,3-d]pyrimidin-2-amine: K159 (= K158), M169 (≠ I168), E201 (= E200), Y203 (≠ C202), L204 (≠ I203), H236 (≠ N235), L278 (= L277), E288 (= E288), I437 (≠ T438)
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)
50% identity, 93% coverage: 3:443/473 of query aligns to 2:442/448 of P43873
- K116 (= K116) binding
- K159 (= K158) binding
- EKYL 201:204 (≠ EKCI 200:203) binding
- E276 (= E275) binding ; binding
- E288 (= E288) binding ; binding
- N290 (= N290) binding
2vqdA Crystal structure of biotin carboxylase from pseudomonas aeruginosa complexed with ampcp (see paper)
48% identity, 93% coverage: 3:444/473 of query aligns to 2:443/447 of 2vqdA
- active site: K116 (= K116), K159 (= K158), P196 (≠ A195), H209 (= H208), R235 (= R234), T274 (= T273), E276 (= E275), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R338)
- binding phosphomethylphosphonic acid adenosyl ester: K116 (= K116), I157 (≠ M156), K159 (= K158), G164 (= G163), G166 (= G165), F203 (≠ C202), L204 (≠ I203), H209 (= H208), Q233 (= Q232), H236 (≠ N235), L278 (= L277), E288 (= E288), I437 (≠ T438)
- binding magnesium ion: E276 (= E275), 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)
49% identity, 94% coverage: 5:449/473 of query aligns to 4:448/449 of P24182
- R19 (= R20) mutation to E: Loss of homodimerization. No effect on ATP binding.
- E23 (= E24) mutation to R: Loss of homodimerization. No effect on ATP binding.
- K116 (= K116) binding
- K159 (= K158) binding
- GG 165:166 (= GG 164:165) binding
- EKYL 201:204 (≠ EKCI 200:203) binding
- H209 (= H208) binding
- H236 (≠ N235) binding
- K238 (= K237) binding
- E276 (= E275) binding ; binding
- E288 (= E288) binding ; binding
- R292 (= R292) active site; binding
- V295 (= V295) binding
- E296 (= E296) mutation to A: Severe reduction in catalytic activity.
- R338 (= R338) binding ; binding ; mutation to A: Severe reduction in catalytic activity.
- F363 (≠ P364) mutation to A: Loss of homodimerization. No effect on ATP binding.
- R366 (= R367) mutation to E: Loss of homodimerization. No effect on ATP binding.
Query Sequence
>GFF3994 FitnessBrowser__Marino:GFF3994
MAIRKLLIANRGEIAVRIARACSELGIRSVAIHSEADEYSLHVKKADEAYQISKDPLSGY
LNPHHIVNMAVETGCDALHPGYGFLSENAELAAICEQRGITFVGPSANAISSMGDKTQAR
QTALAAGVPVTPGSEGNLADVEDAVVQAADIGYPVMLKATSGGGGRGIRRCDNEKELRQN
FERVISEATKAFGSAEVFLEKCIIEPRHIEVQILADTHGNVVHLYERDCSIQRRNQKLIE
LAPSPQLEESQREYIGDLAKRVAKQCGYVNAGTVEFLLDHDGSFYFMEMNTRVQVEHTIT
EEITGVDIIKAQIRIAAGEPLGLKQEDISYRGFAAQFRINAEDPKNGFLPSFGRISRYYS
AGGPGVRTDANMYTGYEIPPYYDSMCAKLIVWAMDWDELIARSRRALGDMGIYGVQTTIP
YYKQILEHPDFQAADFNTGFVERNPQLLEYSSKTRPESIATAIAAAIAAQAGL
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