SitesBLAST
Comparing 207299 MicrobesOnline__882:207299 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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)
32% identity, 94% coverage: 16:1177/1234 of query aligns to 5:1128/1150 of A0A0H3JRU9
- R21 (= R32) mutation to A: Complete loss of catalytic activity.
- K119 (= K128) binding
- K161 (= K169) binding
- H211 (= H219) binding
- E278 (= E288) binding
- K411 (≠ I415) mutation to A: Complete loss of catalytic activity.
- RDAHQ 541:545 (≠ RDITQ 549:553) binding
- D542 (= D550) binding
- A580 (= A586) mutation to T: Complete loss of catalytic activity.
- R614 (= R620) mutation to A: Complete loss of catalytic activity.
- Y621 (= Y627) mutation to A: Complete loss of catalytic activity.
- K712 (= K724) binding
- H741 (= H754) binding
- H743 (= H756) binding
- Q838 (≠ A853) mutation to A: About 2.5-fold loss of catalytic activity.
- T876 (= T890) mutation to A: Complete loss of catalytic activity.
- S879 (= S893) mutation to A: About 2-fold loss of catalytic activity.
- K880 (≠ Q894) mutation to T: Complete loss of catalytic activity.
3bg5A Crystal structure of staphylococcus aureus pyruvate carboxylase (see paper)
31% identity, 94% coverage: 16:1177/1234 of query aligns to 3:1119/1137 of 3bg5A
- active site: K117 (= K128), K159 (= K169), S189 (≠ P206), H202 (= H219), R228 (≠ N245), T267 (= T286), E269 (= E288), E281 (= E301), N283 (= N303), R285 (= R305), E289 (= E309), R337 (= R351), D533 (= D550), D639 (= D653), K703 (= K724), H732 (= H754), H734 (= H756), I755 (≠ V777), S761 (≠ A783), M762 (≠ S784), T801 (≠ Q824), T867 (= T890), S869 (≠ G892), V881 (= V904), N883 (≠ G906), Q888 (≠ G911)
- binding adenosine-5'-triphosphate: K117 (= K128), I132 (≠ V143), M157 (= M167), K159 (= K169), E194 (= E211), Y196 (= Y213), I197 (≠ L214), H202 (= H219), Q226 (= Q243), H229 (= H246), K231 (= K248), E269 (= E288), L271 (= L290), E281 (= E301), N283 (= N303)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: Y463 (≠ L476), N466 (≠ E479), G471 (= G484), F472 (= F485), P473 (= P487), F579 (≠ A594), K581 (≠ M596)
- binding manganese (ii) ion: D533 (= D550), H732 (= H754), H734 (= H756)
- binding pyruvic acid: R532 (= R549), Q536 (= Q553), L603 (= L618), F638 (= F652), K703 (= K724), T867 (= T890)
7wtbB Cryo-em structure of human pyruvate carboxylase with acetyl-coa (see paper)
32% identity, 95% coverage: 16:1182/1234 of query aligns to 7:1134/1147 of 7wtbB
- binding acetyl coenzyme *a: F22 (≠ C31), R23 (= R32), T26 (≠ R35), R46 (≠ P54), Q47 (≠ A55), K48 (≠ A56), A49 (≠ S57), D50 (≠ A58), E51 (≠ A59), A52 (≠ Q60), R367 (≠ V372), R414 (= R418), A417 (≠ S421), E418 (= E422), R420 (≠ I424), R422 (≠ G426), A462 (≠ E469), Q463 (≠ G470), N464 (≠ E471), R465 (= R472), K1025 (= K1072), T1026 (≠ P1073), R1054 (≠ M1101)
- binding phosphoaminophosphonic acid-adenylate ester: I161 (≠ M167), K163 (= K169), G168 (= G174), G169 (= G175), G170 (= G176), M173 (≠ I179), K206 (= K212), F207 (≠ Y213), I208 (≠ L214), P211 (≠ V217), H213 (= H219), Q237 (= Q243), H240 (= H246), E280 (= E288), L282 (= L290), I292 (= I300), E293 (= E301)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: D582 (≠ H589), R613 (= R620), Y620 (= Y627), Q839 (≠ A853), N842 (≠ S856), T877 (= T890), S880 (= S893), K881 (≠ Q894)
7wtdC Cryo-em structure of human pyruvate carboxylase with acetyl-coa in the intermediate state 1 (see paper)
32% identity, 95% coverage: 16:1182/1234 of query aligns to 6:1133/1146 of 7wtdC