SitesBLAST
Comparing N515DRAFT_0973 FitnessBrowser__Dyella79:N515DRAFT_0973 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)
Q5KUG0 Fused isobutyryl-CoA mutase; EC 5.4.99.13; EC 3.6.5.- from Geobacillus kaustophilus (strain HTA426) (see paper)
56% identity, 99% coverage: 15:1155/1155 of query aligns to 3:1086/1086 of Q5KUG0
- K213 (= K222) mutation to A: Loss of GTPase and ATPase activities. No effect on the mutase activity.
Q1LRY0 Fused isobutyryl-CoA mutase; EC 5.4.99.13; EC 3.6.5.- from Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34) (Ralstonia metallidurans) (see 2 papers)
57% identity, 98% coverage: 20:1155/1155 of query aligns to 27:1093/1093 of Q1LRY0
- H39 (= H32) binding axial binding residue
- 169:417 (vs. 162:416, 49% identical) GTPase chaperone MeaI
- GAGKSS 219:224 (= GAGKSS 219:224) binding
- S223 (= S223) binding
- I248 (≠ V247) binding
- D249 (= D248) binding
- D262 (= D261) binding ; binding
- R265 (= R264) binding
- E310 (= E309) binding ; binding
- T311 (= T310) binding
- NKFD 357:360 (= NKFD 356:359) binding
- 418:579 (vs. 417:598, 29% identical) Linker
- F587 (≠ Y606) binding
- F598 (= F617) mutation to A: Switches the substrate specificity and enhances the catalytic efficiency of the isovaleryl-CoA mutase over the native isobutyryl-CoA mutase activity about 4000-fold. Is even more susceptible to inactivation than wild-type during turnover.
- R622 (= R641) binding
- R728 (= R789) binding
- Y772 (= Y833) binding
- S821 (= S882) binding
- R856 (= R917) binding
- K861 (= K922) binding
- E973 (≠ D1034) binding
- N1092 (= N1154) binding
4xc6A Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, and mg (holo-icmf/gdp) (see paper)
57% identity, 98% coverage: 20:1155/1155 of query aligns to 7:1067/1067 of 4xc6A
- active site: F572 (= F617), Y753 (= Y840), H754 (= H841)
- binding cobalamin: G18 (= G31), H19 (= H32), D20 (= D33), A21 (= A34), S22 (≠ A35), M26 (= M39), Y66 (= Y79), Q67 (= Q80), G94 (= G107), G96 (= G109), V98 (≠ T111), Y116 (= Y129), S117 (≠ H130), P118 (= P131), M129 (= M142), F601 (= F646), L606 (= L651), S624 (= S669), Q716 (= Q803), H754 (= H841), E757 (= E844), A758 (= A845), G842 (= G929), R843 (= R930), E879 (= E966), A880 (= A967), T882 (= T969), H967 (= H1054)
- binding guanosine-5'-diphosphate: G199 (= G219), G201 (= G221), K202 (= K222), S203 (= S223), S204 (= S224), R245 (= R264), N337 (= N356), K338 (= K357), D340 (= D359), Q375 (≠ I394), S377 (= S396), E947 (≠ D1034)
- binding magnesium ion: S203 (= S223), D229 (= D248), D242 (= D261), D242 (= D261), E290 (= E309), E290 (= E309)
Sites not aligning to the query:
5cjwA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate pivalyl-coenzyme a (see paper)
57% identity, 98% coverage: 20:1155/1155 of query aligns to 7:1063/1063 of 5cjwA
- active site: F571 (= F617), Y752 (= Y840), H753 (= H841)
- binding pivalyl-coenzyme A: F558 (≠ Y604), F560 (≠ Y606), R562 (= R608), R569 (= R615), F571 (= F617), R595 (= R641), S650 (= S696), T652 (= T698), R701 (= R789), T703 (= T791), Q705 (= Q793), Y745 (= Y833), Y752 (= Y840), H753 (= H841), S794 (= S882), F796 (= F884), R829 (= R917), K834 (= K922), H836 (= H924)
- binding cobalamin: G18 (= G31), H19 (= H32), D20 (= D33), A21 (= A34), S22 (≠ A35), M26 (= M39), Y66 (= Y79), Q67 (= Q80), G94 (= G107), G96 (= G109), V98 (≠ T111), Y116 (= Y129), S117 (≠ H130), P118 (= P131), F600 (= F646), L605 (= L651), S623 (= S669), Q715 (= Q803), H753 (= H841), E756 (= E844), A757 (= A845), G841 (= G929), R842 (= R930), E878 (= E966), A879 (= A967), T881 (= T969), H966 (= H1054)
- binding guanosine-5'-diphosphate: G199 (= G219), G201 (= G221), K202 (= K222), S203 (= S223), S204 (= S224), R245 (= R264), N337 (= N356), K338 (= K357), D340 (= D359), Q375 (≠ I394), S377 (= S396), N1062 (= N1154)
- binding magnesium ion: S203 (= S223), D229 (= D248), D242 (= D261), D242 (= D261), E290 (= E309), E290 (= E309)
Sites not aligning to the query:
5cjvA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isovaleryl-coenzyme a (see paper)
57% identity, 98% coverage: 20:1155/1155 of query aligns to 7:1061/1061 of 5cjvA
- active site: F569 (= F617), Y750 (= Y840), H751 (= H841)
- binding cobalamin: G18 (= G31), H19 (= H32), D20 (= D33), A21 (= A34), S22 (≠ A35), M26 (= M39), Y66 (= Y79), Q67 (= Q80), G94 (= G107), G96 (= G109), V98 (≠ T111), Y116 (= Y129), S117 (≠ H130), M129 (= M142), F598 (= F646), L603 (= L651), S621 (= S669), Q713 (= Q803), E754 (= E844), A755 (= A845), G839 (= G929), R840 (= R930), E876 (= E966), A877 (= A967), T879 (= T969), H964 (= H1054)
- binding guanosine-5'-diphosphate: G199 (= G219), G201 (= G221), K202 (= K222), S203 (= S223), S204 (= S224), R245 (= R264), K336 (= K357), D338 (= D359), Q373 (≠ I394), S375 (= S396), E944 (≠ D1034)
- binding Isovaleryl-coenzyme A: F556 (≠ Y604), F558 (≠ Y606), R560 (= R608), R567 (= R615), F569 (= F617), R593 (= R641), S648 (= S696), T650 (= T698), R699 (= R789), T701 (= T791), Q703 (= Q793), Q713 (= Q803), Y743 (= Y833), H751 (= H841), S792 (= S882), F794 (= F884), K832 (= K922), H834 (= H924)
- binding magnesium ion: S203 (= S223), D229 (= D248), D242 (= D261), D242 (= D261), E288 (= E309), E288 (= E309)
Sites not aligning to the query:
5cjtA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isobutyryl-coenzyme a (see paper)
57% identity, 98% coverage: 20:1155/1155 of query aligns to 7:1062/1062 of 5cjtA
- active site: F569 (= F617), Y750 (= Y840), H751 (= H841)
- binding cobalamin: G18 (= G31), H19 (= H32), D20 (= D33), A21 (= A34), S22 (≠ A35), M26 (= M39), Y66 (= Y79), Q67 (= Q80), G94 (= G107), G96 (= G109), V98 (≠ T111), Y116 (= Y129), S117 (≠ H130), F598 (= F646), L603 (= L651), S621 (= S669), Q713 (= Q803), H751 (= H841), E754 (= E844), A755 (= A845), G839 (= G929), R840 (= R930), E876 (= E966), A877 (= A967), T879 (= T969), H964 (= H1054)
- binding isobutyryl-coenzyme a: F556 (≠ Y604), F558 (≠ Y606), R560 (= R608), R567 (= R615), F569 (= F617), R593 (= R641), S648 (= S696), T650 (= T698), R699 (= R789), T701 (= T791), Q703 (= Q793), Y743 (= Y833), Y750 (= Y840), H751 (= H841), S792 (= S882), F794 (= F884), R827 (= R917), K832 (= K922), H834 (= H924)
- binding guanosine-5'-diphosphate: G199 (= G219), G201 (= G221), K202 (= K222), S203 (= S223), S204 (= S224), R245 (= R264), N336 (= N356), K337 (= K357), D339 (= D359), Q374 (≠ I394), S376 (= S396), E944 (≠ D1034)
- binding magnesium ion: S203 (= S223), D229 (= D248), D242 (= D261), D242 (= D261), E289 (= E309), E289 (= E309)
Sites not aligning to the query:
4xc7A Isobutyryl-coa mutase fused with bound butyryl-coa and without cobalamin or gdp (apo-icmf) (see paper)
57% identity, 98% coverage: 20:1155/1155 of query aligns to 6:1053/1053 of 4xc7A
- active site: F566 (= F617), Y747 (= Y840), H748 (= H841)
- binding Butyryl Coenzyme A: F553 (≠ Y604), R557 (= R608), R564 (= R615), F566 (= F617), R590 (= R641), S645 (= S696), T647 (= T698), R696 (= R789), T698 (= T791), Y740 (= Y833), S789 (= S882), F791 (= F884), R824 (= R917), K829 (= K922), H831 (= H924)
Sites not aligning to the query:
4r3uA Crystal structure of 2-hydroxyisobutyryl-coa mutase (see paper)
30% identity, 48% coverage: 593:1152/1155 of query aligns to 64:556/557 of 4r3uA
- active site: I89 (≠ F617), Y243 (= Y840), H244 (= H841)
- binding 3-hydroxybutanoyl-coenzyme a: Y75 (= Y604), T77 (vs. gap), M78 (≠ Y606), R82 (≠ G610), T85 (≠ P613), R87 (= R615), I89 (≠ F617), D116 (≠ L676), S164 (≠ H722), T166 (≠ K724), T195 (= T791), Q197 (= Q793), R234 (≠ N831), N236 (≠ Y833), N239 (≠ S836), Y243 (= Y840), H244 (= H841), R283 (≠ N880), F287 (= F884), R327 (≠ K922), F328 (≠ Y923), H329 (= H924), Q331 (= Q926), Q362 (≠ N957)
- binding S-{(3R,5R,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5-dioxido-10,14-dioxo-2,4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl} 2-hydroxy-2-methylpropanethioate: Y75 (= Y604), T77 (vs. gap), M78 (≠ Y606), R82 (≠ G610), T85 (≠ P613), R87 (= R615), I89 (≠ F617), D116 (≠ L676), S164 (≠ H722), T166 (≠ K724), T195 (= T791), Q197 (= Q793), R234 (≠ N831), N236 (≠ Y833), N239 (≠ S836), H244 (= H841), R283 (≠ N880), F287 (= F884), R327 (≠ K922), F328 (≠ Y923), H329 (= H924), Q331 (= Q926), Q362 (≠ N957)
- binding cobalamin: D116 (≠ L676), M119 (= M679), E139 (≠ N700), Q207 (= Q803), E209 (≠ T805), E247 (= E844), A334 (≠ G929), E371 (= E966), A372 (= A967), A374 (≠ T969)
I3VE77 2-hydroxyisobutanoyl-CoA mutase large subunit; 2-hydroxyisobutyryl-CoA mutase large subunit; HCM large subunit; EC 5.4.99.64 from Aquincola tertiaricarbonis (see 2 papers)
30% identity, 48% coverage: 593:1152/1155 of query aligns to 65:557/562 of I3VE77
- YPTM 76:79 (≠ YP-Y 604:606) binding
- TMR 86:88 (≠ PTR 613:615) binding
- I90 (≠ F617) mutation to A: 6-fold decrease in catalytic efficiency with 2-hydroxyisobutyryl-CoA as substrate. 320-fold decrease in catalytic efficiency with (S)-3-hydroxybuytryl-CoA as substrate. 6-fold increase in catalytic efficiency with (R)-3-hydroxybutyryl-CoA as substrate. No change in catalytic efficiencies with pivalyl-CoA and isovaleryl-CoA as substrates.; mutation I->F,Y: Loss of activity.; mutation to L: 37-fold decrease in catalytic efficiency with 2-hydroxyisobutyryl-CoA as substrate. 290-fold decrease in catalytic efficiency with (S)-3-hydroxybuytryl-CoA as substrate. Does not show any significant activities with pivalyl-CoA and isovaleryl-CoA.; mutation to V: 100-fold decrease in catalytic efficiency with (S)-3-hydroxybuytryl-CoA as substrate. No change in catalytic efficiencies with pivalyl-CoA and isovaleryl-CoA as substrates.
- D117 (≠ L676) binding ; mutation to A: 2-fold increase in catalytic efficiency with 2-hydroxyisobutyryl-CoA as substrate. Small increase in catalytic efficiency with (S)-3-hydroxybuytryl-CoA as substrate. 1800-fold increase in catalytic efficiency with (R)-3-hydroxybutyryl-CoA as substrate.; mutation to V: 1.5-fold increase in catalytic efficiency with 2-hydroxyisobutyryl-CoA as substrate. 3-fold decrease in catalytic efficiency with (S)-3-hydroxybuytryl-CoA as substrate. 1300-fold increase in catalytic efficiency with (R)-3-hydroxybutyryl-CoA as substrate. 74-fold increase in catalytic efficiency with pivalyl-CoA as substrate.
- TVQ 196:198 (= TVQ 791:793) binding
- R235 (≠ N831) binding
- N240 (≠ S836) binding
- H245 (= H841) binding
- R284 (≠ N880) binding
6oxdA Structure of mycobacterium tuberculosis methylmalonyl-coa mutase with adenosyl cobalamin (see paper)
31% identity, 49% coverage: 592:1152/1155 of query aligns to 74:566/736 of 6oxdA
- active site: Y100 (≠ F617), Y254 (= Y840), H255 (= H841)
- binding cobalamin: Y100 (≠ F617), L130 (≠ S648), H133 (≠ L651), A150 (≠ S669), R218 (≠ Q803), E258 (= E844), G344 (= G929), W345 (≠ R930), E381 (= E966), A382 (= A967), A384 (≠ T969), L385 (≠ T970)
- binding Itaconyl coenzyme A: Y86 (= Y604), T88 (≠ Y606), M89 (≠ R607), Q93 (≠ E611), T96 (= T614), R98 (= R615), Y100 (≠ F617), S175 (= S696), T177 (= T698), T206 (= T791), R218 (≠ Q803), H255 (= H841), R294 (≠ N880), S296 (= S882), F298 (= F884), R337 (≠ K922), T338 (≠ Y923), H339 (= H924), Q341 (= Q926), Q372 (≠ N957)
Sites not aligning to the query:
- active site: 610, 614, 616
- binding cobalamin: 615, 616, 617, 618, 661, 663, 665, 691, 692, 711, 712, 715
P22033 Methylmalonyl-CoA mutase, mitochondrial; MCM; Methylmalonyl-CoA isomerase; EC 5.4.99.2 from Homo sapiens (Human) (see 28 papers)
36% identity, 32% coverage: 790:1154/1155 of query aligns to 215:579/750 of P22033
- G215 (= G790) to C: in MMAM; mut- and mut0; dbSNP:rs121918258; to S: in MMAM; mut0; dbSNP:rs121918258
- TIQ 216:218 (≠ TVQ 791:793) binding
- Q218 (= Q793) to H: in MMAM; mut0 and mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability; dbSNP:rs1446389693
- N219 (≠ A794) to Y: in MMAM; mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; dbSNP:rs121918256
- R228 (≠ Q803) binding ; to Q: in MMAM; mut0; dbSNP:rs770810987
- T230 (= T805) to I: in MMAM; mut-; to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253833
- Y231 (≠ C806) to N: in MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; strong decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability; dbSNP:rs864309736
- K255 (≠ N831) binding
- S262 (= S838) to N: in MMAM; mut0
- H265 (= H841) binding ; to Y: in MMAM; mut-
- E276 (≠ Q852) to D: in MMAM; uncertain significance; mut-; dbSNP:rs12175488
- L281 (= L857) to S: in MMAM; mut0; dbSNP:rs796052007
- G284 (= G860) to E: in MMAM; mut0; dbSNP:rs879253835; to R: in MMAM; mut0; dbSNP:rs761477436
- S288 (≠ V864) to P: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1179778233
- G291 (≠ Y867) to E: in MMAM; mut0
- Q293 (≠ A869) to P: in MMAM; mut0
- RLS 304:306 (≠ NLS 880:882) binding
- L305 (= L881) to S: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554160246
- S306 (= S882) to F: in MMAM; mut0; dbSNP:rs1085307929
- W309 (≠ F885) to G: in MMAM; decreased protein expression
- G312 (= G888) to V: in MMAM; mut0; dbSNP:rs864309734
- Y316 (= Y893) to C: in MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; no decreased affinity for adenosylcob(III)alamin; dbSNP:rs781474200
- A324 (≠ V899) to T: in MMAM; mut-; dbSNP:rs780387525
- R326 (= R901) to K: in MMAM; uncertain significance; dbSNP:rs758577372
- L328 (≠ I903) to F: in MMAM; mut0; affects proper folding; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; dbSNP:rs796052002; to P: in MMAM; mut0; dbSNP:rs965316043
- S344 (= S918) to F: in MMAM; mut-; affects proper folding; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin
- L346 (≠ M920) natural variant: Missing (in MMAM; mut0)
- L347 (= L921) to R: in MMAM; mut0; dbSNP:rs1026703654
- H350 (= H924) to Y: in MMAM; mut0; dbSNP:rs1407914109
- L358 (= L932) to P: in MMAM; mut0
- N366 (= N940) to S: in MMAM; mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability; dbSNP:rs864309737
- R369 (= R943) to C: in MMAM; mut0; dbSNP:rs772552898; to H: in MMAM; mut- and mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability; dbSNP:rs564069299
- T370 (= T944) to P: in MMAM; mut0; dbSNP:rs368790885
- A377 (= A951) to E: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918250
- Q383 (≠ N957) to H: in MMAM; mut0; to P: in MMAM; mut0
- H386 (= H960) to N: in MMAM; mut0; dbSNP:rs1554159937; to R: in MMAM; mut0; dbSNP:rs866933356
- T387 (= T961) to I: in MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability
- N388 (= N962) to H: in MMAM; mut0; dbSNP:rs766010704; to K: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253840
- S389 (≠ A963) natural variant: Missing (in MMAM; mut0)
- I412 (= I986) natural variant: Missing (in MMAM; mut0)
- P424 (= P998) to L: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253842
- G426 (≠ Q1000) to E: in MMAM; mut-; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs533755473; to R: in MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; strong decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability; dbSNP:rs769922244
- G427 (= G1001) to D: in MMAM; mut0; dbSNP:rs753288303
- G454 (= G1028) to E: in MMAM; mut0
- A499 (≠ G1072) to T: in dbSNP:rs2229385
- I505 (≠ T1077) to T: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- Q514 (≠ E1086) to E: in MMAM; uncertain significance; to K: in MMAM; decreased protein expression
- L518 (≠ G1090) to P: in MMAM; mut0; dbSNP:rs864309738
- R532 (≠ N1104) to H: in dbSNP:rs1141321
- A535 (= A1107) to P: in MMAM; mut0; dbSNP:rs760183775
- A552 (≠ L1128) to V: in MMAM; uncertain significance; dbSNP:rs879253845
- C560 (vs. gap) to Y: in MMAM; mut0; dbSNP:rs1238333040
- T566 (≠ S1141) to R: in MMAM; mut0
- F573 (≠ G1148) to S: in MMAM; mut-; affects proper folding; no effect on protein abundance; no effect on methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; does not alter thermodynamic stability; dbSNP:rs775593146
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
- 7:750 natural variant: Missing (in MMAM; mut-)
- 50 binding
- 69 I → V: in MMAM; likely benign; dbSNP:rs115923556
- 86 P → L: in MMAM; mut0 and mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability; dbSNP:rs769348060
- 87 G → E: in MMAM; mut0; dbSNP:rs1554160986
- 93 R → H: in MMAM; mut0; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918251
- 94 G → R: in MMAM; mut0; dbSNP:rs727504022; G → V: in MMAM; mut- and mut0; dbSNP:rs535411418
- 95 P → R: in MMAM; mut0; dbSNP:rs190834116
- 96:99 binding
- 100 Y → C: in MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability; dbSNP:rs864309735
- 105 W → R: in MMAM; mut0; dbSNP:rs121918249
- 106:110 binding
- 108 R → C: in MMAM; mut0; dbSNP:rs121918257; R → G: in MMAM; mut-; R → H: in MMAM; mut0; dbSNP:rs483352778
- 109 Q → R: in MMAM; mut0; dbSNP:rs1461110052
- 133 G → R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253828
- 137 A → V: in MMAM; mut0; dbSNP:rs941483851
- 139 D → N: in MMAM; uncertain significance; dbSNP:rs879253829
- 140 L → P: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- 141 A → T: in MMAM; decreased protein expression; dbSNP:rs1554160730
- 143 H → Y: in MMAM; mut0
- 145 G → S: in MMAM; mut0
- 148 S → L: in MMAM; mut0; dbSNP:rs1300547552
- 152:750 natural variant: Missing (in MMAM; mut0)
- 156 D → N: in MMAM; mut-
- 158 G → V: in MMAM; mut0
- 161 G → R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; G → V: in MMAM; decreased protein expression
- 174 F → S: in MMAM; mut0; dbSNP:rs864309733
- 186 M → V: in MMAM; mut-; dbSNP:rs148331800
- 187 T → S: in MMAM; mut0; dbSNP:rs879253830
- 189 N → I: in MMAM; mut-; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs200908035; N → K: in MMAM; mut-; dbSNP:rs1561959114
- 191 A → E: in MMAM; mut- and mut0; affects proper folding; reduced protein level; decreased methylmalonyl-CoA mutase activity; dbSNP:rs760782399
- 197 A → E: in MMAM; mut0
- 203 G → R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs778702777
- 205 natural variant: Missing (in MMAM; mut0; dbSNP:rs879253831)
- 228:750 natural variant: Missing (in MMAM; mut0)
- 587 Y → C: in MMAM; mut-
- 597 I → R: in MMAM; no changed in protein expression; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554158951
- 615 P → L: in MMAM; mut0; affects proper folding; reduced strongly protein level; P → R: in MMAM; mut0; dbSNP:rs1554158777; P → T: in MMAM; mut0; affects proper folding; reduced strongly protein level; loss of methylmalonyl-CoA mutase activity; dbSNP:rs1302409621
- 616 R → C: in MMAM; mut0; dbSNP:rs765284825
- 617 L → R: in MMAM; mut0; dbSNP:rs1554158775
- 621 K → N: in MMAM; mut0
- 623 G → R: in MMAM; mut0; dbSNP:rs121918254
- 624 Q → R: in MMAM; no effect on protein abundance; dbSNP:rs768521956
- 625 D → G: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253847; D → V: in MMAM; mut0; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity
- 626 G → C: in MMAM; mut-; dbSNP:rs982110849
- 627 binding axial binding residue; H → R: in MMAM; mut0; dbSNP:rs372486357
- 630 G → E: in MMAM; mut0; dbSNP:rs143023066
- 633 V → G: in MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; does not alter thermodynamic stability; dbSNP:rs200055428
- 637 G → E: in MMAM; mut-; G → R: in MMAM; mut0; dbSNP:rs781501004
- 638 F → I: in MMAM; mut0
- 640 D → Y: in MMAM; mut0; dbSNP:rs865815395
- 642 G → R: in MMAM; mut-; dbSNP:rs747897332
- 648 G → D: in MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; strong decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability; dbSNP:rs766721811
- 669 V → E: in MMAM; mut0; dbSNP:rs1360470463
- 671 I → V: in dbSNP:rs8589
- 674 L → F: in MMAM; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1164271240
- 678 H → R: in MMAM; mut-; dbSNP:rs147094927
- 684 natural variant: E -> EL (in MMAM; mut-)
- 685 L → R: in MMAM; mut-; dbSNP:rs864309739
- 694 R → L: in MMAM; mut-; decreased protein abundance; loss of methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability; R → W: in MMAM; mut- and mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability; dbSNP:rs777758903
- 700 M → K: in MMAM; mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability; dbSNP:rs140600746
- 703 G → R: in MMAM; mut0; dbSNP:rs121918255
- 717 G → V: in MMAM; mut-; no effect on protein abundance; interferes with the binding of the cofactor to the apoenzyme; decreased methylmalonyl-CoA mutase activity; strong decreased affinity for adenosylcob(III)alamin; decreased thermodynamic stability; dbSNP:rs121918252
- 723 G → D: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity; dbSNP:rs755077681
8dyjB Crystal structure of human methylmalonyl-coa mutase in complex with adp and cob(ii)alamin (see paper)
36% identity, 32% coverage: 790:1154/1155 of query aligns to 179:543/708 of 8dyjB
- binding adenosine-5'-diphosphate: R192 (≠ Q803), Y228 (= Y840), H229 (= H841), F272 (= F884), Q316 (= Q926), N352 (= N962), E356 (= E966), L360 (≠ T970), P361 (= P971)
- binding cobalamin: V191 (≠ A802), R192 (≠ Q803), H229 (= H841), E232 (= E844), G319 (= G929), W320 (≠ R930), E356 (= E966), G359 (≠ T969), L360 (≠ T970)
Sites not aligning to the query:
- binding adenosine-5'-diphosphate: 74, 151
- binding cobalamin: 102, 104, 107, 124, 590, 591, 592, 593, 594, 598, 636, 638, 640, 666, 667, 668, 686, 687, 690
2xiqA Crystal structure of human methylmalonyl-coa mutase in complex with adenosylcobalamin and malonyl-coa (see paper)
36% identity, 32% coverage: 790:1154/1155 of query aligns to 180:544/714 of 2xiqA
- active site: Y229 (= Y840), H230 (= H841)
- binding cobalamin: R193 (≠ Q803), E233 (= E844), G320 (= G929), W321 (≠ R930), E357 (= E966), G360 (≠ T969), L361 (≠ T970)
- binding malonyl-coenzyme a: T181 (= T791), R193 (≠ Q803), K220 (≠ N831), H230 (= H841), R269 (≠ N880), S271 (= S882), F273 (= F884), R313 (≠ K922), A314 (≠ Y923), H315 (= H924), Q317 (= Q926), Q348 (≠ N957)
Sites not aligning to the query:
- active site: 75, 586, 590, 592
- binding cobalamin: 75, 105, 108, 125, 591, 592, 593, 594, 595, 599, 635, 637, 639, 641, 667, 668, 687, 688, 691
- binding malonyl-coenzyme a: 61, 63, 64, 68, 71, 73, 75, 150, 152
8gjuJ Crystal structure of human methylmalonyl-coa mutase (mmut) in complex with methylmalonic acidemia type a protein (mmaa), coenzyme a, and gdp (see paper)
36% identity, 31% coverage: 790:1152/1155 of query aligns to 180:542/689 of 8gjuJ
Sites not aligning to the query:
5reqA Methylmalonyl-coa mutase, y89f mutant, substrate complex (see paper)
30% identity, 39% coverage: 615:1066/1155 of query aligns to 84:467/725 of 5reqA
- active site: F86 (= F617), Y240 (= Y840), H241 (= H841)
- binding cobalamin: L116 (≠ S648), A136 (≠ S669), R204 (≠ Q803), H241 (= H841), E244 (= E844), G330 (= G929), W331 (≠ R930), E367 (= E966), A368 (= A967), A370 (≠ T969)
- binding methylmalonyl(carbadethia)-coenzyme a: R84 (= R615), F86 (= F617), S111 (= S643), S161 (= S694), T163 (≠ F710), T192 (= T791), Q194 (= Q793), R204 (≠ Q803), N233 (≠ Y833), H241 (= H841), R280 (≠ N880), S282 (= S882), F284 (= F884), T324 (≠ Y923), H325 (= H924), Q358 (≠ N957), S359 (= S958)
- binding succinyl(carbadethia)-coenzyme a: R84 (= R615), F86 (= F617), S161 (= S694), T163 (≠ F710), T192 (= T791), R204 (≠ Q803), N233 (≠ Y833), H241 (= H841), R280 (≠ N880), S282 (= S882), F284 (= F884), H325 (= H924), Q358 (≠ N957)
Sites not aligning to the query:
- active site: 601, 605, 607
- binding cobalamin: 606, 607, 608, 609, 610, 614, 652, 654, 682, 683, 684, 702, 703, 706
- binding methylmalonyl(carbadethia)-coenzyme a: 72, 74, 75, 79, 82
- binding succinyl(carbadethia)-coenzyme a: 72, 74, 75, 79, 82
P11653 Methylmalonyl-CoA mutase large subunit; MCM-alpha; EC 5.4.99.2 from Propionibacterium freudenreichii subsp. shermanii (see 4 papers)
30% identity, 39% coverage: 615:1066/1155 of query aligns to 87:470/728 of P11653
- R87 (= R615) binding
- Y89 (≠ F617) binding ; mutation to F: Does not significantly affect affinity for succiny-CoA, but kcat is lowered about 580-fold.
- S114 (= S643) binding
- F117 (= F646) binding
- A139 (≠ S669) binding
- T195 (= T791) binding
- Q197 (= Q793) binding
- V206 (≠ A802) binding
- R207 (≠ Q803) binding ; binding
- H244 (= H841) binding
- R283 (≠ N880) binding
- S285 (= S882) binding
- G333 (= G929) binding
- E370 (= E966) binding
- A373 (≠ T969) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 75 binding
- 78 binding
- 82 binding
- 85 binding
- 609 binding
- 610 binding axial binding residue
- 611 binding
- 612 binding
- 655 binding
- 657 binding
- 686 binding
- 709 binding
4reqA Methylmalonyl-coa mutase substrate complex (see paper)
30% identity, 39% coverage: 615:1066/1155 of query aligns to 85:468/726 of 4reqA
- active site: Y87 (≠ F617), Y241 (= Y840), H242 (= H841)
- binding cobalamin: Y87 (≠ F617), L117 (≠ S648), A137 (≠ S669), V204 (≠ A802), R205 (≠ Q803), H242 (= H841), E245 (= E844), G331 (= G929), W332 (≠ R930), E368 (= E966), A369 (= A967), A371 (≠ T969), L372 (≠ T970)
- binding methylmalonyl-coenzyme a: R85 (= R615), Y87 (≠ F617), S112 (= S643), S162 (= S694), T164 (≠ F710), T193 (= T791), R205 (≠ Q803), N234 (≠ Y833), Y241 (= Y840), H242 (= H841), R281 (≠ N880), S283 (= S882), F285 (= F884), H326 (= H924), Q328 (= Q926), Q359 (≠ N957), S360 (= S958)
- binding succinyl-coenzyme a: R85 (= R615), Y87 (≠ F617), S162 (= S694), T164 (≠ F710), T193 (= T791), Q195 (= Q793), R205 (≠ Q803), N234 (≠ Y833), Y241 (= Y840), H242 (= H841), R281 (≠ N880), S283 (= S882), F285 (= F884), R324 (≠ K922), H326 (= H924), Q359 (≠ N957)
Sites not aligning to the query:
- active site: 602, 606, 608
- binding cobalamin: 607, 608, 609, 610, 611, 615, 653, 655, 683, 684, 685, 703, 704, 707
- binding methylmalonyl-coenzyme a: 73, 76, 79, 80, 83
- binding succinyl-coenzyme a: 73, 76, 79, 80, 83
6reqA Methylmalonyl-coa mutase, 3-carboxypropyl-coa inhibitor complex (see paper)
30% identity, 39% coverage: 615:1066/1155 of query aligns to 86:469/727 of 6reqA
- active site: Y88 (≠ F617), Y242 (= Y840), H243 (= H841)
- binding 3-carboxypropyl-coenzyme a: R86 (= R615), Y88 (≠ F617), S113 (= S643), S163 (= S694), T165 (≠ F710), T194 (= T791), R206 (≠ Q803), H243 (= H841), R282 (≠ N880), S284 (= S882), F286 (= F884), H327 (= H924), Q329 (= Q926), Q360 (≠ N957)
- binding cobalamin: Y88 (≠ F617), F116 (= F646), L118 (≠ S648), H121 (≠ L651), A138 (≠ S669), R206 (≠ Q803), E246 (= E844), G332 (= G929), W333 (≠ R930), E369 (= E966), A370 (= A967), A372 (≠ T969)
Sites not aligning to the query:
- active site: 603, 607, 609
- binding 3-carboxypropyl-coenzyme a: 74, 76, 77, 80, 81, 84
- binding cobalamin: 608, 609, 610, 611, 612, 616, 620, 654, 656, 658, 684, 685, 704, 705, 708
7reqA Methylmalonyl-coa mutase, 2-carboxypropyl-coa inhibitor complex (see paper)
30% identity, 39% coverage: 615:1066/1155 of query aligns to 84:467/725 of 7reqA
- active site: Y86 (≠ F617), Y240 (= Y840), H241 (= H841)
- binding 2-carboxypropyl-coenzyme a: R84 (= R615), Y86 (≠ F617), S161 (= S694), T163 (≠ F710), T192 (= T791), R204 (≠ Q803), H241 (= H841), R280 (≠ N880), S282 (= S882), F284 (= F884), H325 (= H924), Q358 (≠ N957)
- binding cobalamin: Y86 (≠ F617), L116 (≠ S648), A136 (≠ S669), R204 (≠ Q803), E244 (= E844), G330 (= G929), W331 (≠ R930), E367 (= E966), A368 (= A967), A370 (≠ T969)
Sites not aligning to the query:
- active site: 601, 605, 607
- binding 2-carboxypropyl-coenzyme a: 72, 74, 75, 78, 79, 82
- binding cobalamin: 606, 607, 608, 609, 610, 614, 652, 654, 682, 683, 702, 703, 706
3reqA Methylmalonyl-coa mutase, substrate-free state (poor quality structure) (see paper)
30% identity, 39% coverage: 615:1066/1155 of query aligns to 84:467/725 of 3reqA
- active site: Y86 (≠ F617), Y240 (= Y840), H241 (= H841)
- binding adenosine: Y86 (≠ F617), Y240 (= Y840), E244 (= E844), G330 (= G929)
- binding cobalamin: L116 (≠ S648), V203 (≠ A802), R204 (≠ Q803), E244 (= E844), G330 (= G929), W331 (≠ R930), A368 (= A967)
Sites not aligning to the query:
- active site: 601, 605, 607
- binding cobalamin: 606, 607, 608, 609, 610, 614, 650, 652, 654, 682, 683, 702, 703, 704, 706
Query Sequence
>N515DRAFT_0973 FitnessBrowser__Dyella79:N515DRAFT_0973
MSSPAQHVSASAAVHEGRPLRFVTAASLFDGHDAAINIMRRIIQSQGAEVIHLGHNRSVE
DVVRAALQEDADAIALSSYQGGHVEYFKYMVDMLKEHGAAHIRVFGGGGGTITPEEIREL
QAYGVERIYHPNDGMKLGLTEMIEDVMRRTREAADQRAGAEQATAVAPRVDIDDEISIGH
MLSSIEEGQLPEAELDHLRKQWKMAGKQTPVLGVTGTGGAGKSSVVDELLLRFLHAFPDM
RIAVLAVDPTRRRSGGALLGDRIRMNSLRSHRVYMRSMATRRQHAATSVVLHDCIDFLKA
QPYDLVIVETAGIGQSDSEIVDLVDFPMYVMTSDYGAASQLEKIDMLDFAELVVLNKFDK
RGAEDALRDVRKQWKRNRTAFALKDDEVPVYPTIASQFNDPGVTWMFANLCRLLRDKLTL
PAPKWTPELDTSLKEPRATVLIPGSRVRYLAEIAEQGRGINAGIEREAEFASKAQHYYES
LKDLGDARLPRELARYDSQSLHEEGADRTLLTLRQRYNQAVKELSHEAVHLLHDWPARYK
SVTDEYNEYKVRDKTIRVENYRESLSHQKIPKVSPPRTKDWGDLVRFLMRENLPGYYPYT
GGVYPYRRTGEDPTRMFAGEGTPERTNRRFHYLSQGGAATRLSTAFDSVTLYGEDPAPRP
DIYGKIGNSGVNVATLDDMKKLYSGFDLSAPSSSVSMTINGPAPIILAMFMNTAIDQNIE
KHLKADPARWAEAQQKIAALQSHGGPRYSGELPKGNEGLGLGLLGITGDQLVDAQTYARI
KEETLQIVRGTVQADILKEDQAQNTCIFSTEFALRMMGDIQQYFVDHKVRNFYSVSISGY
HIAEAGANPISQLAFTLSNGFTIVEYYLARGMHIDDFAPNLSFFFSNGMDPEYTVIGRVA
RRIWARAMRERYGASARSQMLKYHIQTSGRSLHAQEIQFNDIRTTLQALYALFDNCNSLH
TNAYDEAITTPTEESVRRAVAIQLIINRELGLNFNENPWQGSFVVDALTDLVEEAVYREF
EAISERGGVLGAMDTMYQRGKIQEESMYYEQKKHDGSLPLIGVNTFLPKDHGGEIATEIE
LIRSTEEEKGQQIDNVQAYAKARNGLAPESLKILQNTARERRNVFEQLMEAVKYNSLGQI
SHALYDVGGEYRRNM
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