SitesBLAST
Comparing Dsui_1105 FitnessBrowser__PS:Dsui_1105 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)
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)
75% identity, 100% coverage: 1:1093/1093 of query aligns to 1:1093/1093 of Q1LRY0
- H39 (= H31) binding axial binding residue
- 169:417 (vs. 161:414, 72% identical) GTPase chaperone MeaI
- GAGKSS 219:224 (= GAGKSS 216:221) binding
- S223 (= S220) binding
- I248 (= I245) binding
- D249 (= D246) binding
- D262 (= D259) binding ; binding
- R265 (= R262) binding
- E310 (= E307) binding ; binding
- T311 (= T308) binding
- NKFD 357:360 (= NKFD 354:357) binding
- 418:579 (vs. 415:580, 54% identical) Linker
- F587 (= F588) binding
- F598 (= F599) 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 (= R623) binding
- R728 (= R729) binding
- Y772 (= Y773) binding
- S821 (= S822) binding
- R856 (= R857) binding
- K861 (= K862) binding
- E973 (= E974) binding
- N1092 (≠ S1092) binding
4xc6A Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, and mg (holo-icmf/gdp) (see paper)
75% identity, 99% coverage: 15:1093/1093 of query aligns to 3:1067/1067 of 4xc6A
- active site: K6 (= K18), F572 (= F599), Y753 (= Y780), H754 (= H781)
- binding cobalamin: G18 (= G30), H19 (= H31), D20 (= D32), A21 (= A33), S22 (= S34), M26 (= M38), Y66 (= Y78), Q67 (= Q79), G94 (= G106), G96 (= G108), V98 (= V110), Y116 (= Y128), S117 (= S129), P118 (= P130), M129 (= M141), F601 (= F628), L606 (= L633), S624 (= S651), Q716 (= Q743), H754 (= H781), E757 (= E784), A758 (= A785), G842 (= G869), R843 (= R870), E879 (= E906), A880 (= A907), T882 (= T909), H967 (= H994)
- binding guanosine-5'-diphosphate: G199 (= G216), G201 (= G218), K202 (= K219), S203 (= S220), S204 (= S221), R245 (= R262), N337 (= N354), K338 (= K355), D340 (= D357), Q375 (≠ M392), S377 (≠ A394), E947 (= E974)
- binding magnesium ion: S203 (= S220), D229 (= D246), D242 (= D259), D242 (= D259), E290 (= E307), E290 (= E307)
5cjwA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate pivalyl-coenzyme a (see paper)
75% identity, 99% coverage: 15:1093/1093 of query aligns to 3:1063/1063 of 5cjwA
- active site: K6 (= K18), F571 (= F599), Y752 (= Y780), H753 (= H781)
- binding pivalyl-coenzyme A: F558 (= F586), F560 (= F588), R562 (= R590), R569 (= R597), F571 (= F599), R595 (= R623), S650 (= S678), T652 (= T680), R701 (= R729), T703 (= T731), Q705 (= Q733), Y745 (= Y773), Y752 (= Y780), H753 (= H781), S794 (= S822), F796 (= F824), R829 (= R857), K834 (= K862), H836 (= H864)
- binding cobalamin: G18 (= G30), H19 (= H31), D20 (= D32), A21 (= A33), S22 (= S34), M26 (= M38), Y66 (= Y78), Q67 (= Q79), G94 (= G106), G96 (= G108), V98 (= V110), Y116 (= Y128), S117 (= S129), P118 (= P130), F600 (= F628), L605 (= L633), S623 (= S651), Q715 (= Q743), H753 (= H781), E756 (= E784), A757 (= A785), G841 (= G869), R842 (= R870), E878 (= E906), A879 (= A907), T881 (= T909), H966 (= H994)
- binding guanosine-5'-diphosphate: G199 (= G216), G201 (= G218), K202 (= K219), S203 (= S220), S204 (= S221), R245 (= R262), N337 (= N354), K338 (= K355), D340 (= D357), Q375 (≠ M392), S377 (≠ A394), N1062 (≠ S1092)
- binding magnesium ion: S203 (= S220), D229 (= D246), D242 (= D259), D242 (= D259), E290 (= E307), E290 (= E307)
5cjtA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isobutyryl-coenzyme a (see paper)
75% identity, 99% coverage: 15:1093/1093 of query aligns to 3:1062/1062 of 5cjtA
- active site: K6 (= K18), F569 (= F599), Y750 (= Y780), H751 (= H781)
- binding cobalamin: G18 (= G30), H19 (= H31), D20 (= D32), A21 (= A33), S22 (= S34), M26 (= M38), Y66 (= Y78), Q67 (= Q79), G94 (= G106), G96 (= G108), V98 (= V110), Y116 (= Y128), S117 (= S129), F598 (= F628), L603 (= L633), S621 (= S651), Q713 (= Q743), H751 (= H781), E754 (= E784), A755 (= A785), G839 (= G869), R840 (= R870), E876 (= E906), A877 (= A907), T879 (= T909), H964 (= H994)
- binding isobutyryl-coenzyme a: F556 (= F586), F558 (= F588), R560 (= R590), R567 (= R597), F569 (= F599), R593 (= R623), S648 (= S678), T650 (= T680), R699 (= R729), T701 (= T731), Q703 (= Q733), Y743 (= Y773), Y750 (= Y780), H751 (= H781), S792 (= S822), F794 (= F824), R827 (= R857), K832 (= K862), H834 (= H864)
- binding guanosine-5'-diphosphate: G199 (= G216), G201 (= G218), K202 (= K219), S203 (= S220), S204 (= S221), R245 (= R262), N336 (= N354), K337 (= K355), D339 (= D357), Q374 (≠ M392), S376 (≠ A394), E944 (= E974)
- binding magnesium ion: S203 (= S220), D229 (= D246), D242 (= D259), D242 (= D259), E289 (= E307), E289 (= E307)
5cjvA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isovaleryl-coenzyme a (see paper)
75% identity, 99% coverage: 15:1093/1093 of query aligns to 3:1061/1061 of 5cjvA
- active site: K6 (= K18), F569 (= F599), Y750 (= Y780), H751 (= H781)
- binding cobalamin: G18 (= G30), H19 (= H31), D20 (= D32), A21 (= A33), S22 (= S34), M26 (= M38), Y66 (= Y78), Q67 (= Q79), G94 (= G106), G96 (= G108), V98 (= V110), Y116 (= Y128), S117 (= S129), M129 (= M141), F598 (= F628), L603 (= L633), S621 (= S651), Q713 (= Q743), E754 (= E784), A755 (= A785), G839 (= G869), R840 (= R870), E876 (= E906), A877 (= A907), T879 (= T909), H964 (= H994)
- binding guanosine-5'-diphosphate: G199 (= G216), G201 (= G218), K202 (= K219), S203 (= S220), S204 (= S221), R245 (= R262), K336 (= K355), D338 (= D357), Q373 (≠ M392), S375 (≠ A394), E944 (= E974)
- binding Isovaleryl-coenzyme A: F556 (= F586), F558 (= F588), R560 (= R590), R567 (= R597), F569 (= F599), R593 (= R623), S648 (= S678), T650 (= T680), R699 (= R729), T701 (= T731), Q703 (= Q733), Q713 (= Q743), Y743 (= Y773), H751 (= H781), S792 (= S822), F794 (= F824), K832 (= K862), H834 (= H864)
- binding magnesium ion: S203 (= S220), D229 (= D246), D242 (= D259), D242 (= D259), E288 (= E307), E288 (= E307)
4xc7A Isobutyryl-coa mutase fused with bound butyryl-coa and without cobalamin or gdp (apo-icmf) (see paper)
74% identity, 99% coverage: 15:1093/1093 of query aligns to 2:1053/1053 of 4xc7A
- active site: K5 (= K18), F566 (= F599), Y747 (= Y780), H748 (= H781)
- binding Butyryl Coenzyme A: F553 (= F586), R557 (= R590), R564 (= R597), F566 (= F599), R590 (= R623), S645 (= S678), T647 (= T680), R696 (= R729), T698 (= T731), Y740 (= Y773), S789 (= S822), F791 (= F824), R824 (= R857), K829 (= K862), H831 (= H864)
Q5KUG0 Fused isobutyryl-CoA mutase; EC 5.4.99.13; EC 3.6.5.- from Geobacillus kaustophilus (strain HTA426) (see paper)
64% identity, 99% coverage: 13:1093/1093 of query aligns to 5:1086/1086 of Q5KUG0
- K213 (= K219) mutation to A: Loss of GTPase and ATPase activities. No effect on the mutase activity.
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)
35% identity, 47% coverage: 575:1092/1093 of query aligns to 65:559/562 of I3VE77
- YPTM 76:79 (≠ F-AF 586:588) binding
- TMR 86:88 (≠ PTR 595:597) binding
- I90 (≠ F599) 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 (≠ A627) 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 731:733) binding
- R235 (≠ N771) binding
- N240 (≠ S776) binding
- H245 (= H781) binding
- R284 (≠ N820) binding
4r3uA Crystal structure of 2-hydroxyisobutyryl-coa mutase (see paper)
35% identity, 47% coverage: 575:1090/1093 of query aligns to 64:556/557 of 4r3uA
- active site: I89 (≠ F599), Y243 (= Y780), H244 (= H781)
- binding 3-hydroxybutanoyl-coenzyme a: Y75 (≠ F586), T77 (≠ A587), M78 (≠ F588), R82 (≠ G592), T85 (≠ P595), R87 (= R597), I89 (≠ F599), D116 (≠ A627), S164 (= S678), T166 (= T680), T195 (= T731), Q197 (= Q733), R234 (≠ N771), N236 (≠ Y773), N239 (≠ S776), Y243 (= Y780), H244 (= H781), R283 (≠ N820), F287 (= F824), R327 (≠ K862), F328 (≠ Y863), H329 (= H864), Q331 (= Q866), Q362 (≠ N897)
- 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 (≠ F586), T77 (≠ A587), M78 (≠ F588), R82 (≠ G592), T85 (≠ P595), R87 (= R597), I89 (≠ F599), D116 (≠ A627), S164 (= S678), T166 (= T680), T195 (= T731), Q197 (= Q733), R234 (≠ N771), N236 (≠ Y773), N239 (≠ S776), H244 (= H781), R283 (≠ N820), F287 (= F824), R327 (≠ K862), F328 (≠ Y863), H329 (= H864), Q331 (= Q866), Q362 (≠ N897)
- binding cobalamin: D116 (≠ A627), M119 (≠ S630), E139 (≠ S651), Q207 (= Q743), E209 (≠ T745), E247 (= E784), A334 (≠ G869), E371 (= E906), A372 (= A907), A374 (≠ T909)
P22033 Methylmalonyl-CoA mutase, mitochondrial; MCM; Methylmalonyl-CoA isomerase; EC 5.4.99.2 from Homo sapiens (Human) (see 28 papers)
35% identity, 50% coverage: 542:1090/1093 of query aligns to 59:577/750 of P22033
- I69 (= I552) to V: in MMAM; likely benign; dbSNP:rs115923556
- P86 (= P576) to 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
- G87 (= G577) to E: in MMAM; mut0; dbSNP:rs1554160986
- R93 (≠ A583) to H: in MMAM; mut0; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918251
- G94 (= G584) to R: in MMAM; mut0; dbSNP:rs727504022; to V: in MMAM; mut- and mut0; dbSNP:rs535411418
- P95 (≠ V585) to R: in MMAM; mut0; dbSNP:rs190834116
- YPTM 96:99 (≠ FAFK 586:589) binding
- Y100 (≠ R590) to 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
- W105 (≠ P595) to R: in MMAM; mut0; dbSNP:rs121918249
- TIRQY 106:110 (≠ T-RMF 596:599) binding
- R108 (= R597) to C: in MMAM; mut0; dbSNP:rs121918257; to G: in MMAM; mut-; to H: in MMAM; mut0; dbSNP:rs483352778
- Q109 (≠ M598) to R: in MMAM; mut0; dbSNP:rs1461110052
- G133 (≠ A621) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253828
- A137 (= A627) to V: in MMAM; mut0; dbSNP:rs941483851
- D139 (= D629) to N: in MMAM; uncertain significance; dbSNP:rs879253829
- L140 (≠ S630) to P: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- A141 (≠ V631) to T: in MMAM; decreased protein expression; dbSNP:rs1554160730
- H143 (≠ L633) to Y: in MMAM; mut0
- G145 (= G635) to S: in MMAM; mut0
- S148 (≠ P638) to L: in MMAM; mut0; dbSNP:rs1300547552
- D156 (≠ K647) to N: in MMAM; mut-
- G158 (= G649) to V: in MMAM; mut0
- G161 (= G652) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; to V: in MMAM; decreased protein expression
- F174 (≠ Y665) to S: in MMAM; mut0; dbSNP:rs864309733
- M186 (= M679) to V: in MMAM; mut-; dbSNP:rs148331800
- T187 (= T680) to S: in MMAM; mut0; dbSNP:rs879253830
- N189 (= N682) to I: in MMAM; mut-; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs200908035; to K: in MMAM; mut-; dbSNP:rs1561959114
- A191 (≠ P684) to E: in MMAM; mut- and mut0; affects proper folding; reduced protein level; decreased methylmalonyl-CoA mutase activity; dbSNP:rs760782399
- A197 (= A690) to E: in MMAM; mut0
- G203 (≠ A696) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs778702777
- E205 (≠ D698) natural variant: Missing (in MMAM; mut0; dbSNP:rs879253831)
- G215 (= G730) to C: in MMAM; mut- and mut0; dbSNP:rs121918258; to S: in MMAM; mut0; dbSNP:rs121918258
- TIQ 216:218 (≠ TVQ 731:733) binding
- Q218 (= Q733) to H: in MMAM; mut0 and mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability; dbSNP:rs1446389693
- N219 (≠ A734) to Y: in MMAM; mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; dbSNP:rs121918256
- R228 (≠ Q743) binding ; to Q: in MMAM; mut0; dbSNP:rs770810987
- T230 (= T745) to I: in MMAM; mut-; to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253833
- Y231 (≠ C746) 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 (≠ N771) binding
- S262 (= S778) to N: in MMAM; mut0
- H265 (= H781) binding ; to Y: in MMAM; mut-
- E276 (≠ Q792) to D: in MMAM; uncertain significance; mut-; dbSNP:rs12175488
- L281 (= L797) to S: in MMAM; mut0; dbSNP:rs796052007
- G284 (= G800) to E: in MMAM; mut0; dbSNP:rs879253835; to R: in MMAM; mut0; dbSNP:rs761477436
- S288 (≠ V804) to P: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1179778233
- G291 (≠ Y807) to E: in MMAM; mut0
- Q293 (≠ A809) to P: in MMAM; mut0
- RLS 304:306 (≠ NLS 820:822) binding
- L305 (= L821) to S: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554160246
- S306 (= S822) to F: in MMAM; mut0; dbSNP:rs1085307929
- W309 (≠ F825) to G: in MMAM; decreased protein expression
- G312 (= G828) to V: in MMAM; mut0; dbSNP:rs864309734
- Y316 (≠ E832) 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 (≠ V839) to T: in MMAM; mut-; dbSNP:rs780387525
- R326 (= R841) to K: in MMAM; uncertain significance; dbSNP:rs758577372
- L328 (≠ I843) 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 (= S858) 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 (≠ K860) natural variant: Missing (in MMAM; mut0)
- L347 (= L861) to R: in MMAM; mut0; dbSNP:rs1026703654
- H350 (= H864) to Y: in MMAM; mut0; dbSNP:rs1407914109
- L358 (= L872) to P: in MMAM; mut0
- N366 (= N880) 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 (= R883) 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 (= T884) to P: in MMAM; mut0; dbSNP:rs368790885
- A377 (= A891) to E: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918250
- Q383 (≠ N897) to H: in MMAM; mut0; to P: in MMAM; mut0
- H386 (= H900) to N: in MMAM; mut0; dbSNP:rs1554159937; to R: in MMAM; mut0; dbSNP:rs866933356
- T387 (= T901) 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 (= N902) to H: in MMAM; mut0; dbSNP:rs766010704; to K: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253840
- S389 (≠ A903) natural variant: Missing (in MMAM; mut0)
- I412 (= I926) natural variant: Missing (in MMAM; mut0)
- P424 (= P938) to L: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253842
- G426 (≠ Q940) 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 (= G941) to D: in MMAM; mut0; dbSNP:rs753288303
- G454 (= G968) to E: in MMAM; mut0
- A499 (= A1013) to T: in dbSNP:rs2229385
- I505 (≠ R1021) to T: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- Q514 (= Q1030) to E: in MMAM; uncertain significance; to K: in MMAM; decreased protein expression
- L518 (= L1034) to P: in MMAM; mut0; dbSNP:rs864309738
- R532 (≠ A1047) to H: in dbSNP:rs1141321
- A535 (= A1050) to P: in MMAM; mut0; dbSNP:rs760183775
- A552 (≠ L1066) to V: in MMAM; uncertain significance; dbSNP:rs879253845
- C560 (= C1073) to Y: in MMAM; mut0; dbSNP:rs1238333040
- T566 (= T1079) to R: in MMAM; mut0
- F573 (≠ G1086) 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
- 152:750 natural variant: Missing (in MMAM; mut0)
- 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
8gjuJ Crystal structure of human methylmalonyl-coa mutase (mmut) in complex with methylmalonic acidemia type a protein (mmaa), coenzyme a, and gdp (see paper)
35% identity, 50% coverage: 542:1090/1093 of query aligns to 24:542/689 of 8gjuJ
- binding coenzyme a: Y61 (≠ F586), T63 (≠ F588), R68 (≠ E593), T71 (= T596), R73 (= R597), S150 (= S678), T152 (= T680), T181 (= T731), Q183 (= Q733), N222 (≠ Y773), R269 (≠ N820), S271 (= S822), R313 (≠ K862), A314 (≠ Y863), H315 (= H864), Q348 (≠ N897)
2xiqA Crystal structure of human methylmalonyl-coa mutase in complex with adenosylcobalamin and malonyl-coa (see paper)
35% identity, 50% coverage: 542:1090/1093 of query aligns to 24:542/714 of 2xiqA
- active site: Y75 (≠ F599), Y229 (= Y780), H230 (= H781)
- binding cobalamin: Y75 (≠ F599), L105 (≠ S630), H108 (≠ L633), A125 (≠ S651), R193 (≠ Q743), E233 (= E784), G320 (= G869), W321 (≠ R870), E357 (= E906), G360 (≠ T909), L361 (≠ T910)
- binding malonyl-coenzyme a: Y61 (≠ F586), T63 (≠ F588), M64 (≠ K589), R68 (≠ E593), T71 (= T596), R73 (= R597), Y75 (≠ F599), S150 (= S678), T152 (= T680), T181 (= T731), R193 (≠ Q743), K220 (≠ N771), H230 (= H781), R269 (≠ N820), S271 (= S822), F273 (= F824), R313 (≠ K862), A314 (≠ Y863), H315 (= H864), Q317 (= Q866), Q348 (≠ N897)
Sites not aligning to the query:
- active site: 586, 590, 592
- binding cobalamin: 591, 592, 593, 594, 595, 599, 635, 637, 639, 641, 667, 668, 687, 688, 691
8dyjB Crystal structure of human methylmalonyl-coa mutase in complex with adp and cob(ii)alamin (see paper)
35% identity, 50% coverage: 542:1090/1093 of query aligns to 23:541/708 of 8dyjB
- binding adenosine-5'-diphosphate: Y74 (≠ F599), T151 (= T680), R192 (≠ Q743), Y228 (= Y780), H229 (= H781), F272 (= F824), Q316 (= Q866), N352 (= N902), E356 (= E906), L360 (≠ T910), P361 (= P911)
- binding cobalamin: F102 (= F628), L104 (≠ S630), H107 (≠ L633), A124 (≠ S651), V191 (≠ G742), R192 (≠ Q743), H229 (= H781), E232 (= E784), G319 (= G869), W320 (≠ R870), E356 (= E906), G359 (≠ T909), L360 (≠ T910)
Sites not aligning to the query:
- binding cobalamin: 590, 591, 592, 593, 594, 598, 636, 638, 640, 666, 667, 668, 686, 687, 690
6oxdA Structure of mycobacterium tuberculosis methylmalonyl-coa mutase with adenosyl cobalamin (see paper)
33% identity, 47% coverage: 573:1090/1093 of query aligns to 73:566/736 of 6oxdA
- active site: Y100 (≠ F599), Y254 (= Y780), H255 (= H781)
- binding cobalamin: Y100 (≠ F599), L130 (≠ S630), H133 (≠ L633), A150 (≠ S651), R218 (≠ Q743), E258 (= E784), G344 (= G869), W345 (≠ R870), E381 (= E906), A382 (= A907), A384 (≠ T909), L385 (≠ T910)
- binding Itaconyl coenzyme A: Y86 (≠ F586), T88 (≠ F588), M89 (≠ K589), Q93 (≠ E593), T96 (= T596), R98 (= R597), Y100 (≠ F599), S175 (= S678), T177 (= T680), T206 (= T731), R218 (≠ Q743), H255 (= H781), R294 (≠ N820), S296 (= S822), F298 (= F824), R337 (≠ K862), T338 (≠ Y863), H339 (= H864), Q341 (= Q866), Q372 (≠ N897)
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
5reqA Methylmalonyl-coa mutase, y89f mutant, substrate complex (see paper)
33% identity, 47% coverage: 580:1089/1093 of query aligns to 71:556/725 of 5reqA
- active site: F86 (= F599), Y240 (= Y780), H241 (= H781)
- binding cobalamin: L116 (≠ S630), A136 (≠ S651), R204 (≠ Q743), H241 (= H781), E244 (= E784), G330 (= G869), W331 (≠ R870), E367 (= E906), A368 (= A907), A370 (≠ T909)
- binding methylmalonyl(carbadethia)-coenzyme a: Y72 (= Y581), T74 (≠ G584), M75 (≠ V585), R79 (≠ K589), T82 (≠ G592), R84 (= R597), F86 (= F599), S111 (= S625), S161 (= S678), T163 (= T680), T192 (= T731), Q194 (= Q733), R204 (≠ Q743), N233 (≠ Y773), H241 (= H781), R280 (≠ N820), S282 (= S822), F284 (= F824), T324 (≠ Y863), H325 (= H864), Q358 (≠ N897), S359 (= S898)
- binding succinyl(carbadethia)-coenzyme a: Y72 (= Y581), T74 (≠ G584), M75 (≠ V585), R79 (≠ K589), T82 (≠ G592), R84 (= R597), F86 (= F599), S161 (= S678), T163 (= T680), T192 (= T731), R204 (≠ Q743), N233 (≠ Y773), H241 (= H781), R280 (≠ N820), S282 (= S822), F284 (= F824), H325 (= H864), Q358 (≠ N897)
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
4reqA Methylmalonyl-coa mutase substrate complex (see paper)
32% identity, 47% coverage: 580:1089/1093 of query aligns to 72:557/726 of 4reqA
- active site: Y87 (≠ F599), Y241 (= Y780), H242 (= H781)
- binding cobalamin: Y87 (≠ F599), L117 (≠ S630), A137 (≠ S651), V204 (≠ G742), R205 (≠ Q743), H242 (= H781), E245 (= E784), G331 (= G869), W332 (≠ R870), E368 (= E906), A369 (= A907), A371 (≠ T909), L372 (≠ T910)
- binding methylmalonyl-coenzyme a: Y73 (= Y581), M76 (≠ V585), F79 (= F588), R80 (≠ K589), T83 (≠ G592), R85 (= R597), Y87 (≠ F599), S112 (= S625), S162 (= S678), T164 (= T680), T193 (= T731), R205 (≠ Q743), N234 (≠ Y773), Y241 (= Y780), H242 (= H781), R281 (≠ N820), S283 (= S822), F285 (= F824), H326 (= H864), Q328 (= Q866), Q359 (≠ N897), S360 (= S898)
- binding succinyl-coenzyme a: Y73 (= Y581), M76 (≠ V585), F79 (= F588), R80 (≠ K589), T83 (≠ G592), R85 (= R597), Y87 (≠ F599), S162 (= S678), T164 (= T680), T193 (= T731), Q195 (= Q733), R205 (≠ Q743), N234 (≠ Y773), Y241 (= Y780), H242 (= H781), R281 (≠ N820), S283 (= S822), F285 (= F824), R324 (≠ K862), H326 (= H864), Q359 (≠ N897)
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
6reqA Methylmalonyl-coa mutase, 3-carboxypropyl-coa inhibitor complex (see paper)
32% identity, 47% coverage: 580:1089/1093 of query aligns to 73:558/727 of 6reqA
- active site: Y88 (≠ F599), Y242 (= Y780), H243 (= H781)
- binding 3-carboxypropyl-coenzyme a: Y74 (= Y581), T76 (≠ G584), M77 (≠ V585), F80 (= F588), R81 (≠ K589), T84 (≠ G592), R86 (= R597), Y88 (≠ F599), S113 (= S625), S163 (= S678), T165 (= T680), T194 (= T731), R206 (≠ Q743), H243 (= H781), R282 (≠ N820), S284 (= S822), F286 (= F824), H327 (= H864), Q329 (= Q866), Q360 (≠ N897)
- binding cobalamin: Y88 (≠ F599), F116 (= F628), L118 (≠ S630), H121 (≠ L633), A138 (≠ S651), R206 (≠ Q743), E246 (= E784), G332 (= G869), W333 (≠ R870), E369 (= E906), A370 (= A907), A372 (≠ T909)
Sites not aligning to the query:
- active site: 603, 607, 609
- 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)
32% identity, 47% coverage: 580:1089/1093 of query aligns to 71:556/725 of 7reqA
- active site: Y86 (≠ F599), Y240 (= Y780), H241 (= H781)
- binding 2-carboxypropyl-coenzyme a: Y72 (= Y581), T74 (≠ G584), M75 (≠ V585), F78 (= F588), R79 (≠ K589), T82 (≠ G592), R84 (= R597), Y86 (≠ F599), S161 (= S678), T163 (= T680), T192 (= T731), R204 (≠ Q743), H241 (= H781), R280 (≠ N820), S282 (= S822), F284 (= F824), H325 (= H864), Q358 (≠ N897)
- binding cobalamin: Y86 (≠ F599), L116 (≠ S630), A136 (≠ S651), R204 (≠ Q743), E244 (= E784), G330 (= G869), W331 (≠ R870), E367 (= E906), A368 (= A907), A370 (≠ T909)
Sites not aligning to the query:
- active site: 601, 605, 607
- 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)
32% identity, 47% coverage: 580:1089/1093 of query aligns to 71:556/725 of 3reqA
- active site: Y86 (≠ F599), Y240 (= Y780), H241 (= H781)
- binding adenosine: Y86 (≠ F599), Y240 (= Y780), E244 (= E784), G330 (= G869)
- binding cobalamin: L116 (≠ S630), V203 (≠ G742), R204 (≠ Q743), E244 (= E784), G330 (= G869), W331 (≠ R870), A368 (= A907)
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
2reqA Methylmalonyl-coa mutase, non-productive coa complex, in open conformation representing substrate-free state (see paper)
32% identity, 47% coverage: 580:1089/1093 of query aligns to 71:556/725 of 2reqA
Sites not aligning to the query:
- active site: 601, 605, 607
- binding cobalamin: 606, 607, 608, 609, 610, 614, 650, 652, 654, 655, 682, 683, 702, 703, 706
Query Sequence
>Dsui_1105 FitnessBrowser__PS:Dsui_1105
MTDLSIAKKIVPYKPKNKVRFITAASLFDGHDASINIMRRILQSTGSEVIHLGHNRSVGD
IVNAALQEDVQGIAITSYQGGHVEFFKYMIDLLKENGGENIKVFGGGGGVIVPSEIKELH
EYGVTRIYSPEDGQHLGLQGMINDVVEQSDYNLTTLAPQKPEEVMAALQSGNRRALARIV
SALENGAYPEGLRKQIVEAAALVATTPTLGITGTGGAGKSSLTDELVRRFRLDQEDGLKL
AIISIDPSRKRTGGALLGDRIRMNAIEHPNIFMRSLATRETGSEISAALPEVIAACKLSG
FDLIIVETSGIGQGDAAIVPLVDASLYVMTPEFGAASQLEKIDMLDFADFVAINKFDRKG
AEDALRDVRKQYQRNRELFTQSPDEMPVFGTMAARFNDDGVTALYQAILPKLVEFGLKAK
AGKLPVVTVKESSRGRAIVPVERTRYLAEIADTLRAYHKHTEEQVKIARERQSLRISKDL
FNSYDEAAKAALPKFDELIACKESELDAKAKKLLDMWPDTVKAYSGDEYVVKIRDKEIRT
KLVSESLSGTKIKKVVLPRFTDDGETLRFLMKENVPGSFPYTAGVFAFKREGEDPTRMFA
GEGDAFRTNRRFKKVSEGMPAHRLSTAFDSVTLYGCDPDVRPDIYGKIGNSGVSIATLDD
MKVLYSGFDLVCPTTSVSMTINGPAPIILACFFNTAIDQQLDKFRADNGREPTEDEAEKI
REWVLASVRGTVQADILKEDQGQNTCIFSTEFALKMMGDIQEFFVHNQVQNFYSVSISGY
HIAEAGANPISQLAFTLANGFTYVESYLARGMHIDDFAPNLSFFFSNGMDPEYSVIGRVA
RRIWAVAMKNKYGANERSQKLKYHIQTSGRSLHAQEMDFNDIRTTLQALIAIYDNCNSLH
TNAYDEAITTPTEESVRRAMAIQLIINREWGVAKNENPNQGAFIIDELTDLVEEAVLKEF
EAIASRGGVLGAMETGYQRGKIQEESLYYEHKKHDGSYPIIGVNTFLNPKGSAQVEIELA
RSTEEEKQSQIARLKDFHQRNADKAPAMLAKLKQTVIENGNVFAVLVEAVRVCSLGQITG
ALYEVGGQYRRSM
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