SitesBLAST
Comparing WP_101589656.1 NCBI__GCF_900169175.1:WP_101589656.1 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)
A0A0H3JRU9 Pyruvate carboxylase; EC 6.4.1.1 from Staphylococcus aureus (strain Mu50 / ATCC 700699) (see 2 papers)
40% identity, 41% coverage: 1:450/1090 of query aligns to 1:452/1150 of A0A0H3JRU9
- R21 (≠ S21) mutation to A: Complete loss of catalytic activity.
- K119 (= K117) binding ATP
- K161 (= K160) binding ATP
- H211 (= H210) binding ATP
- E278 (= E277) binding ATP
- K411 (≠ A409) 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.
5vyzA Crystal structure of lactococcus lactis pyruvate carboxylase in complex with cyclic-di-amp (see paper)
41% identity, 41% coverage: 5:450/1090 of query aligns to 9:454/1144 of 5vyzA
- binding adenosine-5'-diphosphate: K123 (= K117), M162 (= M158), K164 (= K160), G168 (= G164), G170 (= G166), G171 (= G167), M174 (≠ I170), Y208 (≠ L204), I209 (= I205), H214 (= H210), Q238 (= Q234), N241 (≠ R237), L283 (= L279), E293 (= E289), T449 (= T445)
- binding magnesium ion: E281 (= E277), E293 (= E289)
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)
41% identity, 41% coverage: 5:450/1090 of query aligns to 3:448/1138 of 7zz3A
- binding acetyl coenzyme *a: N22 (≠ A24), F43 (≠ T45), K44 (≠ A46), A45 (= A47), D46 (= D48), S48 (= S50), R363 (≠ E364), H413 (≠ A415), E414 (≠ D416), R416 (≠ Y418), R418 (= R420)
- binding adenosine-5'-triphosphate: K117 (= K117), M156 (= M158), K158 (= K160), G163 (= G165), G164 (= G166), G165 (= G167), M168 (≠ I170), E200 (= E202), Y202 (≠ L204), I203 (= I205), H208 (= H210), Q232 (= Q234), N235 (≠ R237), L277 (= L279), E287 (= E289), N289 (= N291), T443 (= T445)
- binding bicarbonate ion: K237 (= K239), R291 (= R293), Q293 (= Q295), E295 (= E297)
- binding biotin: G84 (= G84), V294 (= V296), R342 (= R341)
- binding magnesium ion: E275 (= E277), E287 (= E289)
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)
41% identity, 41% coverage: 5:450/1090 of query aligns to 3:448/1056 of 7zyyA
- binding acetyl coenzyme *a: R19 (≠ S21), N22 (≠ A24), F43 (≠ T45), K44 (≠ A46), A45 (= A47), R363 (≠ E364), E414 (≠ D416), R416 (≠ Y418), R418 (= R420)
- binding adenosine-5'-diphosphate: K158 (= K160), G163 (= G165), G164 (= G166), M168 (≠ I170), E200 (= E202), K201 (≠ E203), Y202 (≠ L204), I203 (= I205), H208 (= H210), Q232 (= Q234), N235 (≠ R237), E275 (= E277), L277 (= L279), E287 (= E289), T443 (= T445)
- binding bicarbonate ion: R291 (= R293), Q293 (= Q295), V294 (= V296), E295 (= E297)
- binding magnesium ion: E275 (= E277), E287 (= E289)
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)
41% identity, 41% coverage: 5:450/1090 of query aligns to 38:483/1178 of Q05920
- K39 (≠ R6) modified: N6-acetyllysine
- K79 (≠ A46) modified: N6-acetyllysine; alternate; mutation K->Q,R: Reduced pyruvate carboxylase activity.
- K148 (≠ Q113) modified: N6-acetyllysine
- K152 (= K117) modified: N6-acetyllysine; mutation K->Q,R: Reduced pyruvate carboxylase activity.
- K241 (≠ N207) modified: N6-acetyllysine
- K434 (≠ P399) 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
7wtbB Cryo-em structure of human pyruvate carboxylase with acetyl-coa (see paper)
41% identity, 41% coverage: 5:450/1090 of query aligns to 7:452/1147 of 7wtbB
- binding acetyl coenzyme *a: F22 (≠ A20), T26 (≠ A24), R46 (≠ V44), Q47 (≠ T45), K48 (≠ A46), A49 (= A47), D50 (= D48), R367 (≠ E364), R414 (= R412), E418 (≠ D416), R420 (≠ Y418), R422 (= R420)
- binding phosphoaminophosphonic acid-adenylate ester: K163 (= K160), G168 (= G165), G169 (= G166), M173 (≠ I170), F207 (≠ L204), I208 (= I205), P211 (≠ A208), H240 (≠ R237)
Sites not aligning to the query:
7wtdC Cryo-em structure of human pyruvate carboxylase with acetyl-coa in the intermediate state 1 (see paper)
41% identity, 41% coverage: 5:450/1090 of query aligns to 6:451/1146 of 7wtdC
- binding adenosine-5'-triphosphate: K162 (= K160), G167 (= G165), G168 (= G166), F206 (≠ L204), Q236 (= Q234), H239 (≠ R237), E292 (= E289)
- binding coenzyme a: F21 (≠ A20), R22 (≠ S21), T25 (≠ A24), R45 (≠ V44), Q46 (≠ T45), K47 (≠ A46), A48 (= A47), D49 (= D48), E50 (≠ H49), R366 (≠ E364), R413 (= R412), A416 (= A415), R419 (≠ Y418)
Sites not aligning to the query:
P11498 Pyruvate carboxylase, mitochondrial; Pyruvic carboxylase; PCB; EC 6.4.1.1 from Homo sapiens (Human) (see 6 papers)
41% identity, 41% coverage: 5:451/1090 of query aligns to 38:484/1178 of P11498
- V145 (= V110) to A: in PC deficiency; mild; strongly reduced pyruvate carboxylase activity; dbSNP:rs28940591
- R156 (= R121) to Q: in PC deficiency; dbSNP:rs119103241
- R270 (≠ N236) to W: in PC deficiency; dbSNP:rs1258494752
- Y304 (= Y270) to C: in PC deficiency
- R451 (≠ Y418) to C: in PC deficiency; mild; strongly reduced pyruvate carboxylase activity; dbSNP:rs113994143
Sites not aligning to the query:
- 572 binding Mn(2+)
- 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 Mn(2+)
- 773 binding Mn(2+)
- 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
2vqdA Crystal structure of biotin carboxylase from pseudomonas aeruginosa complexed with ampcp (see paper)
40% identity, 41% coverage: 5:452/1090 of query aligns to 3:444/447 of 2vqdA
- active site: K116 (= K117), K159 (= K160), P196 (≠ G197), H209 (= H210), R235 (≠ N236), T274 (= T275), E276 (= E277), E288 (= E289), N290 (= N291), R292 (= R293), E296 (= E297), R338 (= R341)
- binding phosphomethylphosphonic acid adenosyl ester: K116 (= K117), I157 (≠ M158), K159 (= K160), G164 (= G165), G166 (= G167), F203 (≠ L204), L204 (≠ I205), H209 (= H210), Q233 (= Q234), H236 (≠ R237), L278 (= L279), E288 (= E289), I437 (≠ T445)
- binding magnesium ion: E276 (= E277), E288 (= E289)
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
40% identity, 41% coverage: 5:449/1090 of query aligns to 1:441/448 of 2vpqB