SitesBLAST
Comparing WP_041096999.1 NCBI__GCF_000828635.1:WP_041096999.1 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)
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: 1:1089/1089 of query aligns to 1:1093/1093 of Q1LRY0
- H39 (= H31) binding axial binding residue
- 169:417 (vs. 161:413, 72% identical) GTPase chaperone MeaI
- GAGKSS 219:224 (= GAGKSS 215:220) binding GTP
- S223 (= S219) binding Mg(2+)
- I248 (= I244) binding Mg(2+)
- D249 (= D245) binding Mg(2+)
- D262 (= D258) binding Mg(2+); binding Mg(2+)
- R265 (= R261) binding GTP
- E310 (= E306) binding Mg(2+); binding Mg(2+)
- T311 (= T307) binding Mg(2+)
- NKFD 357:360 (= NKFD 353:356) binding GTP
- 418:579 (vs. 414:575, 57% identical) Linker
- F587 (= F583) binding substrate
- F598 (= F594) 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 (= R618) binding substrate
- R728 (= R724) binding substrate
- Y772 (= Y768) binding substrate
- S821 (= S817) binding substrate
- R856 (= R852) binding substrate
- K861 (= K857) binding substrate
- E973 (= E969) binding GTP
- N1092 (≠ S1088) binding GTP
8sslA Isobutyryl-coa mutase fused q341a in the presence of gtp (see paper)
75% identity, 99% coverage: 15:1089/1089 of query aligns to 2:1072/1072 of 8sslA
- binding guanosine-5'-diphosphate: G200 (= G217), K201 (= K218), S202 (= S219), D241 (= D258), R244 (= R261), K337 (= K354), D339 (= D356), Q374 (≠ M391), A375 (= A392), S376 (≠ A393), N1071 (≠ S1088)
- binding magnesium ion: K201 (= K218), D241 (= D258)
4xc6A Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, and mg (holo-icmf/gdp) (see paper)
75% identity, 99% coverage: 15:1089/1089 of query aligns to 3:1067/1067 of 4xc6A
- active site: K6 (= K18), F572 (= F594), Y753 (= Y775), H754 (= H776)
- 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 (≠ V130), M129 (= M141), F601 (= F623), L606 (= L628), S624 (= S646), Q716 (= Q738), H754 (= H776), E757 (= E779), A758 (= A780), G842 (= G864), R843 (= R865), E879 (= E901), A880 (= A902), T882 (= T904), H967 (= H989)
- binding guanosine-5'-diphosphate: G199 (= G215), G201 (= G217), K202 (= K218), S203 (= S219), S204 (= S220), R245 (= R261), N337 (= N353), K338 (= K354), D340 (= D356), Q375 (≠ M391), S377 (≠ A393), E947 (= E969)
- binding magnesium ion: S203 (= S219), D229 (= D245), D242 (= D258), D242 (= D258), E290 (= E306), E290 (= E306)
5cjwA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate pivalyl-coenzyme a (see paper)
75% identity, 99% coverage: 15:1089/1089 of query aligns to 3:1063/1063 of 5cjwA
- active site: K6 (= K18), F571 (= F594), Y752 (= Y775), H753 (= H776)
- binding pivalyl-coenzyme A: F558 (= F581), F560 (= F583), R562 (= R585), R569 (= R592), F571 (= F594), R595 (= R618), S650 (= S673), T652 (= T675), R701 (= R724), T703 (= T726), Q705 (= Q728), Y745 (= Y768), Y752 (= Y775), H753 (= H776), S794 (= S817), F796 (= F819), R829 (= R852), K834 (= K857), H836 (= H859)
- 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 (≠ V130), F600 (= F623), L605 (= L628), S623 (= S646), Q715 (= Q738), H753 (= H776), E756 (= E779), A757 (= A780), G841 (= G864), R842 (= R865), E878 (= E901), A879 (= A902), T881 (= T904), H966 (= H989)
- binding guanosine-5'-diphosphate: G199 (= G215), G201 (= G217), K202 (= K218), S203 (= S219), S204 (= S220), R245 (= R261), N337 (= N353), K338 (= K354), D340 (= D356), Q375 (≠ M391), S377 (≠ A393), N1062 (≠ S1088)
- binding magnesium ion: S203 (= S219), D229 (= D245), D242 (= D258), D242 (= D258), E290 (= E306), E290 (= E306)
5cjvA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isovaleryl-coenzyme a (see paper)
75% identity, 99% coverage: 15:1089/1089 of query aligns to 3:1061/1061 of 5cjvA
- active site: K6 (= K18), F569 (= F594), Y750 (= Y775), H751 (= H776)
- 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 (= F623), L603 (= L628), S621 (= S646), Q713 (= Q738), E754 (= E779), A755 (= A780), G839 (= G864), R840 (= R865), E876 (= E901), A877 (= A902), T879 (= T904), H964 (= H989)
- binding guanosine-5'-diphosphate: G199 (= G215), G201 (= G217), K202 (= K218), S203 (= S219), S204 (= S220), R245 (= R261), K336 (= K354), D338 (= D356), Q373 (≠ M391), S375 (≠ A393), E944 (= E969)
- binding Isovaleryl-coenzyme A: F556 (= F581), F558 (= F583), R560 (= R585), R567 (= R592), F569 (= F594), R593 (= R618), S648 (= S673), T650 (= T675), R699 (= R724), T701 (= T726), Q703 (= Q728), Q713 (= Q738), Y743 (= Y768), H751 (= H776), S792 (= S817), F794 (= F819), K832 (= K857), H834 (= H859)
- binding magnesium ion: S203 (= S219), D229 (= D245), D242 (= D258), D242 (= D258), E288 (= E306), E288 (= E306)
5cjtA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isobutyryl-coenzyme a (see paper)
75% identity, 99% coverage: 15:1089/1089 of query aligns to 3:1062/1062 of 5cjtA
- active site: K6 (= K18), F569 (= F594), Y750 (= Y775), H751 (= H776)
- 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 (= F623), L603 (= L628), S621 (= S646), Q713 (= Q738), H751 (= H776), E754 (= E779), A755 (= A780), G839 (= G864), R840 (= R865), E876 (= E901), A877 (= A902), T879 (= T904), H964 (= H989)
- binding isobutyryl-coenzyme a: F556 (= F581), F558 (= F583), R560 (= R585), R567 (= R592), F569 (= F594), R593 (= R618), S648 (= S673), T650 (= T675), R699 (= R724), T701 (= T726), Q703 (= Q728), Y743 (= Y768), Y750 (= Y775), H751 (= H776), S792 (= S817), F794 (= F819), R827 (= R852), K832 (= K857), H834 (= H859)
- binding guanosine-5'-diphosphate: G199 (= G215), G201 (= G217), K202 (= K218), S203 (= S219), S204 (= S220), R245 (= R261), N336 (= N353), K337 (= K354), D339 (= D356), Q374 (≠ M391), S376 (≠ A393), E944 (= E969)
- binding magnesium ion: S203 (= S219), D229 (= D245), D242 (= D258), D242 (= D258), E289 (= E306), E289 (= E306)
4xc7A Isobutyryl-coa mutase fused with bound butyryl-coa and without cobalamin or gdp (apo-icmf) (see paper)
74% identity, 99% coverage: 15:1089/1089 of query aligns to 2:1053/1053 of 4xc7A
- active site: K5 (= K18), F566 (= F594), Y747 (= Y775), H748 (= H776)
- binding Butyryl Coenzyme A: F553 (= F581), R557 (= R585), R564 (= R592), F566 (= F594), R590 (= R618), S645 (= S673), T647 (= T675), R696 (= R724), T698 (= T726), Y740 (= Y768), S789 (= S817), F791 (= F819), R824 (= R852), K829 (= K857), H831 (= H859)
Q5KUG0 Fused isobutyryl-CoA mutase; EC 5.4.99.13; EC 3.6.5.- from Geobacillus kaustophilus (strain HTA426) (see paper)
63% identity, 99% coverage: 13:1089/1089 of query aligns to 5:1086/1086 of Q5KUG0
- K213 (= K218) 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)
36% identity, 48% coverage: 570:1088/1089 of query aligns to 65:559/562 of I3VE77
- YPTM 76:79 (≠ F-AF 581:583) binding (3S)-3-hydroxybutanoyl-CoA
- TMR 86:88 (≠ PTR 590:592) binding (3S)-3-hydroxybutanoyl-CoA
- I90 (≠ F594) 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 (≠ A622) binding (3S)-3-hydroxybutanoyl-CoA; 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 726:728) binding (3S)-3-hydroxybutanoyl-CoA
- R235 (≠ N766) binding (3S)-3-hydroxybutanoyl-CoA
- N240 (≠ S771) binding (3S)-3-hydroxybutanoyl-CoA
- H245 (= H776) binding (3S)-3-hydroxybutanoyl-CoA
- R284 (≠ N815) binding (3S)-3-hydroxybutanoyl-CoA
4r3uA Crystal structure of 2-hydroxyisobutyryl-coa mutase (see paper)
36% identity, 47% coverage: 570:1086/1089 of query aligns to 64:556/557 of 4r3uA
- active site: I89 (≠ F594), Y243 (= Y775), H244 (= H776)
- binding 3-hydroxybutanoyl-coenzyme a: Y75 (≠ F581), T77 (≠ A582), M78 (≠ F583), R82 (≠ N587), T85 (≠ P590), R87 (= R592), I89 (≠ F594), D116 (≠ A622), S164 (= S673), T166 (= T675), T195 (= T726), Q197 (= Q728), R234 (≠ N766), N236 (≠ Y768), N239 (≠ S771), Y243 (= Y775), H244 (= H776), R283 (≠ N815), F287 (= F819), R327 (≠ K857), F328 (≠ Y858), H329 (= H859), Q331 (= Q861), Q362 (≠ N892)
- 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 (≠ F581), T77 (≠ A582), M78 (≠ F583), R82 (≠ N587), T85 (≠ P590), R87 (= R592), I89 (≠ F594), D116 (≠ A622), S164 (= S673), T166 (= T675), T195 (= T726), Q197 (= Q728), R234 (≠ N766), N236 (≠ Y768), N239 (≠ S771), H244 (= H776), R283 (≠ N815), F287 (= F819), R327 (≠ K857), F328 (≠ Y858), H329 (= H859), Q331 (= Q861), Q362 (≠ N892)
- binding cobalamin: D116 (≠ A622), M119 (≠ S625), E139 (≠ S646), Q207 (= Q738), E209 (≠ T740), E247 (= E779), A334 (≠ G864), E371 (= E901), A372 (= A902), A374 (≠ T904)
P22033 Methylmalonyl-CoA mutase, mitochondrial; MCM; Methylmalonyl-CoA isomerase; EC 5.4.99.2 from Homo sapiens (Human) (see 28 papers)
35% identity, 51% coverage: 537:1086/1089 of query aligns to 59:577/750 of P22033
- I69 (= I547) to V: in MMAM; likely benign; dbSNP:rs115923556
- P86 (= P571) 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 (= G572) to E: in MMAM; mut0; dbSNP:rs1554160986
- R93 (≠ A578) to H: in MMAM; mut0; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918251
- G94 (= G579) to R: in MMAM; mut0; dbSNP:rs727504022; to V: in MMAM; mut- and mut0; dbSNP:rs535411418
- P95 (vs. gap) to R: in MMAM; mut0; dbSNP:rs190834116
- YPTM 96:99 (≠ ---V 580) binding malonyl-CoA
- Y100 (≠ F581) 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 (≠ E586) to R: in MMAM; mut0; dbSNP:rs121918249
- T---IRQY 106:110 (≠ NEDPTRMF 587:594) binding malonyl-CoA
- R108 (= R592) to C: in MMAM; mut0; dbSNP:rs121918257; to G: in MMAM; mut-; to H: in MMAM; mut0; dbSNP:rs483352778
- Q109 (≠ M593) to R: in MMAM; mut0; dbSNP:rs1461110052
- G133 (≠ R618) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253828
- A137 (= A622) to V: in MMAM; mut0; dbSNP:rs941483851
- D139 (= D624) to N: in MMAM; uncertain significance; dbSNP:rs879253829
- L140 (≠ S625) to P: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- A141 (≠ V626) to T: in MMAM; decreased protein expression; dbSNP:rs1554160730
- H143 (≠ L628) to Y: in MMAM; mut0
- G145 (= G630) to S: in MMAM; mut0
- S148 (≠ P633) to L: in MMAM; mut0; dbSNP:rs1300547552
- D156 (≠ K642) to N: in MMAM; mut-
- G158 (= G644) to V: in MMAM; mut0
- G161 (= G647) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; to V: in MMAM; decreased protein expression
- F174 (≠ Y660) to S: in MMAM; mut0; dbSNP:rs864309733
- M186 (= M674) to V: in MMAM; mut-; dbSNP:rs148331800
- T187 (= T675) to S: in MMAM; mut0; dbSNP:rs879253830
- N189 (= N677) to I: in MMAM; mut-; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs200908035; to K: in MMAM; mut-; dbSNP:rs1561959114
- A191 (≠ P679) to E: in MMAM; mut- and mut0; affects proper folding; reduced protein level; decreased methylmalonyl-CoA mutase activity; dbSNP:rs760782399
- A197 (= A685) to E: in MMAM; mut0
- G203 (≠ A691) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs778702777
- E205 (≠ D693) natural variant: Missing (in MMAM; mut0; dbSNP:rs879253831)
- G215 (= G725) to C: in MMAM; mut- and mut0; dbSNP:rs121918258; to S: in MMAM; mut0; dbSNP:rs121918258
- TIQ 216:218 (≠ TVQ 726:728) binding malonyl-CoA
- Q218 (= Q728) to H: in MMAM; mut0 and mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability; dbSNP:rs1446389693
- N219 (≠ A729) to Y: in MMAM; mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; dbSNP:rs121918256
- R228 (≠ Q738) binding malonyl-CoA; to Q: in MMAM; mut0; dbSNP:rs770810987
- T230 (= T740) to I: in MMAM; mut-; to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253833
- Y231 (≠ C741) 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 (≠ N766) binding malonyl-CoA
- S262 (= S773) to N: in MMAM; mut0
- H265 (= H776) binding malonyl-CoA; to Y: in MMAM; mut-
- E276 (≠ Q787) to D: in MMAM; uncertain significance; mut-; dbSNP:rs12175488
- L281 (= L792) to S: in MMAM; mut0; dbSNP:rs796052007
- G284 (= G795) to E: in MMAM; mut0; dbSNP:rs879253835; to R: in MMAM; mut0; dbSNP:rs761477436
- S288 (≠ V799) to P: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1179778233
- G291 (≠ Y802) to E: in MMAM; mut0
- Q293 (≠ A804) to P: in MMAM; mut0
- RLS 304:306 (≠ NLS 815:817) binding malonyl-CoA
- L305 (= L816) to S: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554160246
- S306 (= S817) to F: in MMAM; mut0; dbSNP:rs1085307929
- W309 (≠ F820) to G: in MMAM; decreased protein expression
- G312 (= G823) to V: in MMAM; mut0; dbSNP:rs864309734
- Y316 (≠ E827) 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 (≠ V834) to T: in MMAM; mut-; dbSNP:rs780387525
- R326 (= R836) to K: in MMAM; uncertain significance; dbSNP:rs758577372
- L328 (≠ I838) 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 (= S853) 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 (≠ K855) natural variant: Missing (in MMAM; mut0)
- L347 (= L856) to R: in MMAM; mut0; dbSNP:rs1026703654
- H350 (= H859) to Y: in MMAM; mut0; dbSNP:rs1407914109
- L358 (= L867) to P: in MMAM; mut0
- N366 (= N875) 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 (= R878) 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 (= T879) to P: in MMAM; mut0; dbSNP:rs368790885
- A377 (= A886) to E: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918250
- Q383 (≠ N892) to H: in MMAM; mut0; to P: in MMAM; mut0
- H386 (= H895) to N: in MMAM; mut0; dbSNP:rs1554159937; to R: in MMAM; mut0; dbSNP:rs866933356
- T387 (= T896) 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 (= N897) to H: in MMAM; mut0; dbSNP:rs766010704; to K: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253840
- S389 (≠ A898) natural variant: Missing (in MMAM; mut0)
- I412 (= I921) natural variant: Missing (in MMAM; mut0)
- P424 (= P933) to L: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253842
- G426 (≠ Q935) 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 (= G936) to D: in MMAM; mut0; dbSNP:rs753288303
- G454 (= G963) to E: in MMAM; mut0
- A499 (≠ G1008) to T: in dbSNP:rs2229385
- I505 (≠ R1017) to T: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- Q514 (= Q1026) to E: in MMAM; uncertain significance; to K: in MMAM; decreased protein expression
- L518 (= L1030) to P: in MMAM; mut0; dbSNP:rs864309738
- R532 (≠ A1043) to H: in dbSNP:rs1141321
- A535 (= A1046) to P: in MMAM; mut0; dbSNP:rs760183775
- A552 (≠ M1062) to V: in MMAM; uncertain significance; dbSNP:rs879253845
- C560 (= C1069) to Y: in MMAM; mut0; dbSNP:rs1238333040
- T566 (≠ S1075) to R: in MMAM; mut0
- F573 (≠ G1082) 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 malonyl-CoA
- 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, 51% coverage: 537:1086/1089 of query aligns to 24:542/689 of 8gjuJ
- binding coenzyme a: Y61 (vs. gap), T63 (vs. gap), R68 (≠ K584), T71 (≠ N587), R73 (= R592), S150 (= S673), T152 (= T675), T181 (= T726), Q183 (= Q728), N222 (≠ Y768), R269 (≠ N815), S271 (= S817), R313 (≠ K857), A314 (≠ Y858), H315 (= H859), Q348 (≠ N892)
8dyjB Crystal structure of human methylmalonyl-coa mutase in complex with adp and cob(ii)alamin (see paper)
35% identity, 51% coverage: 537:1086/1089 of query aligns to 23:541/708 of 8dyjB
- binding adenosine-5'-diphosphate: Y74 (≠ F594), T151 (= T675), R192 (≠ Q738), Y228 (= Y775), H229 (= H776), F272 (= F819), Q316 (= Q861), N352 (= N897), E356 (= E901), L360 (≠ T905), P361 (= P906)
- binding cobalamin: F102 (= F623), L104 (≠ S625), H107 (≠ L628), A124 (≠ S646), V191 (≠ G737), R192 (≠ Q738), H229 (= H776), E232 (= E779), G319 (= G864), W320 (≠ R865), E356 (= E901), G359 (≠ T904), L360 (≠ T905)
Sites not aligning to the query:
- binding cobalamin: 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)
35% identity, 51% coverage: 537:1086/1089 of query aligns to 24:542/714 of 2xiqA
- active site: Y75 (≠ F594), Y229 (= Y775), H230 (= H776)
- binding cobalamin: Y75 (≠ F594), L105 (≠ S625), H108 (≠ L628), A125 (≠ S646), R193 (≠ Q738), E233 (= E779), G320 (= G864), W321 (≠ R865), E357 (= E901), G360 (≠ T904), L361 (≠ T905)
- binding malonyl-coenzyme a: Y61 (vs. gap), T63 (vs. gap), M64 (≠ V580), R68 (≠ K584), T71 (≠ N587), R73 (= R592), Y75 (≠ F594), S150 (= S673), T152 (= T675), T181 (= T726), R193 (≠ Q738), K220 (≠ N766), H230 (= H776), R269 (≠ N815), S271 (= S817), F273 (= F819), R313 (≠ K857), A314 (≠ Y858), H315 (= H859), Q317 (= Q861), Q348 (≠ N892)
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
6oxdA Structure of mycobacterium tuberculosis methylmalonyl-coa mutase with adenosyl cobalamin (see paper)
34% identity, 48% coverage: 568:1086/1089 of query aligns to 73:566/736 of 6oxdA
- active site: Y100 (≠ F594), Y254 (= Y775), H255 (= H776)
- binding cobalamin: Y100 (≠ F594), L130 (≠ S625), H133 (≠ L628), A150 (≠ S646), R218 (≠ Q738), E258 (= E779), G344 (= G864), W345 (≠ R865), E381 (= E901), A382 (= A902), A384 (≠ T904), L385 (≠ T905)
- binding Itaconyl coenzyme A: Y86 (≠ F581), T88 (≠ F583), M89 (≠ K584), Q93 (≠ E588), T96 (= T591), R98 (= R592), Y100 (≠ F594), S175 (= S673), T177 (= T675), T206 (= T726), R218 (≠ Q738), H255 (= H776), R294 (≠ N815), S296 (= S817), F298 (= F819), R337 (≠ K857), T338 (≠ Y858), H339 (= H859), Q341 (= Q861), Q372 (≠ N892)
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: 575:1085/1089 of query aligns to 71:556/725 of 5reqA
- active site: F86 (= F594), Y240 (= Y775), H241 (= H776)
- binding cobalamin: L116 (≠ S625), A136 (≠ S646), R204 (≠ Q738), H241 (= H776), E244 (= E779), G330 (= G864), W331 (≠ R865), E367 (= E901), A368 (= A902), A370 (≠ T904)
- binding methylmalonyl(carbadethia)-coenzyme a: Y72 (= Y576), T74 (≠ G579), M75 (≠ V580), R79 (≠ K584), T82 (≠ N587), R84 (= R592), F86 (= F594), S111 (= S620), S161 (= S673), T163 (= T675), T192 (= T726), Q194 (= Q728), R204 (≠ Q738), N233 (≠ Y768), H241 (= H776), R280 (≠ N815), S282 (= S817), F284 (= F819), T324 (≠ Y858), H325 (= H859), Q358 (≠ N892), S359 (= S893)
- binding succinyl(carbadethia)-coenzyme a: Y72 (= Y576), T74 (≠ G579), M75 (≠ V580), R79 (≠ K584), T82 (≠ N587), R84 (= R592), F86 (= F594), S161 (= S673), T163 (= T675), T192 (= T726), R204 (≠ Q738), N233 (≠ Y768), H241 (= H776), R280 (≠ N815), S282 (= S817), F284 (= F819), H325 (= H859), Q358 (≠ N892)
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
P11653 Methylmalonyl-CoA mutase large subunit; MCM-alpha; EC 5.4.99.2 from Propionibacterium freudenreichii subsp. shermanii (see 4 papers)
33% identity, 47% coverage: 575:1085/1089 of query aligns to 74:559/728 of P11653
- Y75 (= Y576) binding (R)-methylmalonyl-CoA
- M78 (≠ V580) binding (R)-methylmalonyl-CoA
- R82 (≠ K584) binding (R)-methylmalonyl-CoA
- T85 (≠ N587) binding (R)-methylmalonyl-CoA
- R87 (= R592) binding (R)-methylmalonyl-CoA
- Y89 (≠ F594) binding (R)-methylmalonyl-CoA; mutation to F: Does not significantly affect affinity for succiny-CoA, but kcat is lowered about 580-fold.
- S114 (= S620) binding (R)-methylmalonyl-CoA
- F117 (= F623) binding cob(II)alamin
- A139 (≠ S646) binding cob(II)alamin
- T195 (= T726) binding (R)-methylmalonyl-CoA
- Q197 (= Q728) binding (R)-methylmalonyl-CoA
- V206 (≠ G737) binding cob(II)alamin
- R207 (≠ Q738) binding (R)-methylmalonyl-CoA; binding cob(II)alamin
- H244 (= H776) binding (R)-methylmalonyl-CoA
- R283 (≠ N815) binding (R)-methylmalonyl-CoA
- S285 (= S817) binding (R)-methylmalonyl-CoA
- G333 (= G864) binding cob(II)alamin
- E370 (= E901) binding cob(II)alamin
- A373 (≠ T904) binding cob(II)alamin
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 609 binding cob(II)alamin
- 610 binding axial binding residue
- 611 binding cob(II)alamin
- 612 binding cob(II)alamin
- 655 binding cob(II)alamin
- 657 binding cob(II)alamin
- 686 binding cob(II)alamin
- 709 binding cob(II)alamin
6reqA Methylmalonyl-coa mutase, 3-carboxypropyl-coa inhibitor complex (see paper)
33% identity, 47% coverage: 575:1085/1089 of query aligns to 73:558/727 of 6reqA
- active site: Y88 (≠ F594), Y242 (= Y775), H243 (= H776)
- binding 3-carboxypropyl-coenzyme a: Y74 (= Y576), T76 (≠ G579), M77 (≠ V580), F80 (= F583), R81 (≠ K584), T84 (≠ N587), R86 (= R592), Y88 (≠ F594), S113 (= S620), S163 (= S673), T165 (= T675), T194 (= T726), R206 (≠ Q738), H243 (= H776), R282 (≠ N815), S284 (= S817), F286 (= F819), H327 (= H859), Q329 (= Q861), Q360 (≠ N892)
- binding cobalamin: Y88 (≠ F594), F116 (= F623), L118 (≠ S625), H121 (≠ L628), A138 (≠ S646), R206 (≠ Q738), E246 (= E779), G332 (= G864), W333 (≠ R865), E369 (= E901), A370 (= A902), A372 (≠ T904)
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
4reqA Methylmalonyl-coa mutase substrate complex (see paper)
33% identity, 47% coverage: 575:1085/1089 of query aligns to 72:557/726 of 4reqA
- active site: Y87 (≠ F594), Y241 (= Y775), H242 (= H776)
- binding cobalamin: Y87 (≠ F594), L117 (≠ S625), A137 (≠ S646), V204 (≠ G737), R205 (≠ Q738), H242 (= H776), E245 (= E779), G331 (= G864), W332 (≠ R865), E368 (= E901), A369 (= A902), A371 (≠ T904), L372 (≠ T905)
- binding methylmalonyl-coenzyme a: Y73 (= Y576), M76 (≠ V580), F79 (= F583), R80 (≠ K584), T83 (≠ N587), R85 (= R592), Y87 (≠ F594), S112 (= S620), S162 (= S673), T164 (= T675), T193 (= T726), R205 (≠ Q738), N234 (≠ Y768), Y241 (= Y775), H242 (= H776), R281 (≠ N815), S283 (= S817), F285 (= F819), H326 (= H859), Q328 (= Q861), Q359 (≠ N892), S360 (= S893)
- binding succinyl-coenzyme a: Y73 (= Y576), M76 (≠ V580), F79 (= F583), R80 (≠ K584), T83 (≠ N587), R85 (= R592), Y87 (≠ F594), S162 (= S673), T164 (= T675), T193 (= T726), Q195 (= Q728), R205 (≠ Q738), N234 (≠ Y768), Y241 (= Y775), H242 (= H776), R281 (≠ N815), S283 (= S817), F285 (= F819), R324 (≠ K857), H326 (= H859), Q359 (≠ N892)
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
7reqA Methylmalonyl-coa mutase, 2-carboxypropyl-coa inhibitor complex (see paper)
33% identity, 47% coverage: 575:1085/1089 of query aligns to 71:556/725 of 7reqA
- active site: Y86 (≠ F594), Y240 (= Y775), H241 (= H776)
- binding 2-carboxypropyl-coenzyme a: Y72 (= Y576), T74 (≠ G579), M75 (≠ V580), F78 (= F583), R79 (≠ K584), T82 (≠ N587), R84 (= R592), Y86 (≠ F594), S161 (= S673), T163 (= T675), T192 (= T726), R204 (≠ Q738), H241 (= H776), R280 (≠ N815), S282 (= S817), F284 (= F819), H325 (= H859), Q358 (≠ N892)
- binding cobalamin: Y86 (≠ F594), L116 (≠ S625), A136 (≠ S646), R204 (≠ Q738), E244 (= E779), G330 (= G864), W331 (≠ R865), E367 (= E901), A368 (= A902), A370 (≠ T904)
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
Query Sequence
>WP_041096999.1 NCBI__GCF_000828635.1:WP_041096999.1
MTDLSIAAKLVPYKPKHKVRFVTATSLFDGHDASINIMRRILQSSGVEVIHLGHNRSVDE
IVNAALQEDAQGIAVSSYQGGHVEFFKYMIDLLKQRGGGNIQVFGGGGGVIVPAEAAELH
AYGVSHLYSVEDGQTMGLQGMINDMVARCDLDLSRRSPQDIKALEVDDRAERLRNLSQII
TALENGAWPEKAKKTLLEKAAVSPAPTLGITGTGGAGKSSLTDELIRRFRLDQADSQKIA
VISIDPSRKRTGGALLGDRIRMNAIGHPNIYMRSLATRDTGSEISKALPDVIAACKVAGF
DLIVVETSGIGQGDAAIVPLVDVSLYVMTPEFGAASQLEKIDMLDFADFVAINKFDRKGA
EDALRDVRKQYQRNRERFGEKPDDMPVFGTMAARFNDDGVTALYQALAPRLAERGLKFGK
SALPAVKVKSSSAGRAIVPADRVRYLADIADTLRGYHSHIAEQALLARERQSLKTAKAIF
EGCKKNAADFDELIVWKDGQLTPHARKLLAMWPDMKKAYAGDEYVVKIRDKEIRTGLIYE
TLSGTRIRKVALPRFDDEGELLKFLMRENVPGSFPYTAGVFAFKRENEDPTRMFAGEGDA
FRTNKRFLKVSEGMPAKRLSTAFDSVTLYGCDPDPRPDIYGKVGNSGVSIATLDDLKVLY
SGFDLCDPATSVSMTINGPAPMILAMFLNTAIDQQIEKFREQNGRDATEEEAEKIREWTL
SSVRGTVQADILKEDQGQNTCIFSTEFALKMMGDIQEYFVHNQIRNFYSVSISGYHIAEA
GANPISQLAFTLANGFTYVETYLARGMHIDDFAGNLSFFFSNGMDPEYSVIGRVARRIWA
VAMKNRYGANERSQKLKYHIQTSGRSLHAQEMDFNDIRTTLQALIAIYDNCNSLHTNAYD
EAITTPTEESVRRAMAIQLIINREWGVAKNENPNQGAFIIEELTDLVEEAVLKEFEAIAS
RGGVLGAMETGYQRGKIQEESMHYEHKKHDGSYPIIGVNTFLNPHGSGVASEIELARSTE
GEKQSQLARLKDFQTRNAGEAEACLARLKQAVIDNQNVFAVMMEAVRHCSLGQISNALYE
VGGQYRRSM
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