SitesBLAST
Comparing RR42_RS01600 FitnessBrowser__Cup4G11:RR42_RS01600 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)
87% identity, 100% coverage: 1:1102/1102 of query aligns to 1:1093/1093 of Q1LRY0
- H39 (= H45) binding axial binding residue
- 169:417 (vs. 175:423, 87% identical) GTPase chaperone MeaI
- GAGKSS 219:224 (= GAGKSS 225:230) binding
- S223 (= S229) binding
- I248 (= I254) binding
- D249 (= D255) binding
- D262 (= D268) binding ; binding
- R265 (= R271) binding
- E310 (= E316) binding ; binding
- T311 (= T317) binding
- NKFD 357:360 (= NKFD 363:366) binding
- 418:579 (vs. 424:588, 75% identical) Linker
- F587 (= F596) binding
- F598 (= F607) 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 (= R631) binding
- R728 (= R737) binding
- Y772 (= Y781) binding
- S821 (= S830) binding
- R856 (= R865) binding
- K861 (= K870) binding
- E973 (= E982) binding
- N1092 (= N1101) binding
4xc6A Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, and mg (holo-icmf/gdp) (see paper)
87% identity, 98% coverage: 27:1102/1102 of query aligns to 1:1067/1067 of 4xc6A
- active site: K6 (= K32), F572 (= F607), Y753 (= Y788), H754 (= H789)
- binding cobalamin: G18 (= G44), H19 (= H45), D20 (= D46), A21 (= A47), S22 (= S48), M26 (= M52), Y66 (= Y92), Q67 (= Q93), G94 (= G120), G96 (= G122), V98 (= V124), Y116 (≠ F142), S117 (= S143), P118 (= P144), M129 (= M155), F601 (= F636), L606 (= L641), S624 (= S659), Q716 (= Q751), H754 (= H789), E757 (= E792), A758 (= A793), G842 (= G877), R843 (= R878), E879 (= E914), A880 (= A915), T882 (= T917), H967 (= H1002)
- binding guanosine-5'-diphosphate: G199 (= G225), G201 (= G227), K202 (= K228), S203 (= S229), S204 (= S230), R245 (= R271), N337 (= N363), K338 (= K364), D340 (= D366), Q375 (= Q401), S377 (= S403), E947 (= E982)
- binding magnesium ion: S203 (= S229), D229 (= D255), D242 (= D268), D242 (= D268), E290 (= E316), E290 (= E316)
5cjwA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate pivalyl-coenzyme a (see paper)
87% identity, 98% coverage: 27:1102/1102 of query aligns to 1:1063/1063 of 5cjwA
- active site: K6 (= K32), F571 (= F607), Y752 (= Y788), H753 (= H789)
- binding pivalyl-coenzyme A: F558 (= F594), F560 (= F596), R562 (= R598), R569 (= R605), F571 (= F607), R595 (= R631), S650 (= S686), T652 (= T688), R701 (= R737), T703 (= T739), Q705 (= Q741), Y745 (= Y781), Y752 (= Y788), H753 (= H789), S794 (= S830), F796 (= F832), R829 (= R865), K834 (= K870), H836 (= H872)
- binding cobalamin: G18 (= G44), H19 (= H45), D20 (= D46), A21 (= A47), S22 (= S48), M26 (= M52), Y66 (= Y92), Q67 (= Q93), G94 (= G120), G96 (= G122), V98 (= V124), Y116 (≠ F142), S117 (= S143), P118 (= P144), F600 (= F636), L605 (= L641), S623 (= S659), Q715 (= Q751), H753 (= H789), E756 (= E792), A757 (= A793), G841 (= G877), R842 (= R878), E878 (= E914), A879 (= A915), T881 (= T917), H966 (= H1002)
- binding guanosine-5'-diphosphate: G199 (= G225), G201 (= G227), K202 (= K228), S203 (= S229), S204 (= S230), R245 (= R271), N337 (= N363), K338 (= K364), D340 (= D366), Q375 (= Q401), S377 (= S403), N1062 (= N1101)
- binding magnesium ion: S203 (= S229), D229 (= D255), D242 (= D268), D242 (= D268), E290 (= E316), E290 (= E316)
5cjtA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isobutyryl-coenzyme a (see paper)
87% identity, 98% coverage: 27:1102/1102 of query aligns to 1:1062/1062 of 5cjtA
- active site: K6 (= K32), F569 (= F607), Y750 (= Y788), H751 (= H789)
- binding cobalamin: G18 (= G44), H19 (= H45), D20 (= D46), A21 (= A47), S22 (= S48), M26 (= M52), Y66 (= Y92), Q67 (= Q93), G94 (= G120), G96 (= G122), V98 (= V124), Y116 (≠ F142), S117 (= S143), F598 (= F636), L603 (= L641), S621 (= S659), Q713 (= Q751), H751 (= H789), E754 (= E792), A755 (= A793), G839 (= G877), R840 (= R878), E876 (= E914), A877 (= A915), T879 (= T917), H964 (= H1002)
- binding isobutyryl-coenzyme a: F556 (= F594), F558 (= F596), R560 (= R598), R567 (= R605), F569 (= F607), R593 (= R631), S648 (= S686), T650 (= T688), R699 (= R737), T701 (= T739), Q703 (= Q741), Y743 (= Y781), Y750 (= Y788), H751 (= H789), S792 (= S830), F794 (= F832), R827 (= R865), K832 (= K870), H834 (= H872)
- binding guanosine-5'-diphosphate: G199 (= G225), G201 (= G227), K202 (= K228), S203 (= S229), S204 (= S230), R245 (= R271), N336 (= N363), K337 (= K364), D339 (= D366), Q374 (= Q401), S376 (= S403), E944 (= E982)
- binding magnesium ion: S203 (= S229), D229 (= D255), D242 (= D268), D242 (= D268), E289 (= E316), E289 (= E316)
5cjvA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isovaleryl-coenzyme a (see paper)
87% identity, 98% coverage: 27:1102/1102 of query aligns to 1:1061/1061 of 5cjvA
- active site: K6 (= K32), F569 (= F607), Y750 (= Y788), H751 (= H789)
- binding cobalamin: G18 (= G44), H19 (= H45), D20 (= D46), A21 (= A47), S22 (= S48), M26 (= M52), Y66 (= Y92), Q67 (= Q93), G94 (= G120), G96 (= G122), V98 (= V124), Y116 (≠ F142), S117 (= S143), M129 (= M155), F598 (= F636), L603 (= L641), S621 (= S659), Q713 (= Q751), E754 (= E792), A755 (= A793), G839 (= G877), R840 (= R878), E876 (= E914), A877 (= A915), T879 (= T917), H964 (= H1002)
- binding guanosine-5'-diphosphate: G199 (= G225), G201 (= G227), K202 (= K228), S203 (= S229), S204 (= S230), R245 (= R271), K336 (= K364), D338 (= D366), Q373 (= Q401), S375 (= S403), E944 (= E982)
- binding Isovaleryl-coenzyme A: F556 (= F594), F558 (= F596), R560 (= R598), R567 (= R605), F569 (= F607), R593 (= R631), S648 (= S686), T650 (= T688), R699 (= R737), T701 (= T739), Q703 (= Q741), Q713 (= Q751), Y743 (= Y781), H751 (= H789), S792 (= S830), F794 (= F832), K832 (= K870), H834 (= H872)
- binding magnesium ion: S203 (= S229), D229 (= D255), D242 (= D268), D242 (= D268), E288 (= E316), E288 (= E316)
4xc7A Isobutyryl-coa mutase fused with bound butyryl-coa and without cobalamin or gdp (apo-icmf) (see paper)
86% identity, 98% coverage: 28:1102/1102 of query aligns to 1:1053/1053 of 4xc7A
- active site: K5 (= K32), F566 (= F607), Y747 (= Y788), H748 (= H789)
- binding Butyryl Coenzyme A: F553 (= F594), R557 (= R598), R564 (= R605), F566 (= F607), R590 (= R631), S645 (= S686), T647 (= T688), R696 (= R737), T698 (= T739), Y740 (= Y781), S789 (= S830), F791 (= F832), R824 (= R865), K829 (= K870), H831 (= H872)
Q5KUG0 Fused isobutyryl-CoA mutase; EC 5.4.99.13; EC 3.6.5.- from Geobacillus kaustophilus (strain HTA426) (see paper)
63% identity, 97% coverage: 29:1102/1102 of query aligns to 7:1086/1086 of Q5KUG0
- K213 (= K228) mutation to A: Loss of GTPase and ATPase activities. No effect on the mutase activity.
4r3uA Crystal structure of 2-hydroxyisobutyryl-coa mutase (see paper)
35% identity, 47% coverage: 583:1099/1102 of query aligns to 64:556/557 of 4r3uA
- active site: I89 (≠ F607), Y243 (= Y788), H244 (= H789)
- binding 3-hydroxybutanoyl-coenzyme a: Y75 (≠ F594), T77 (≠ A595), M78 (≠ F596), R82 (≠ N600), T85 (≠ P603), R87 (= R605), I89 (≠ F607), D116 (≠ A635), S164 (= S686), T166 (= T688), T195 (= T739), Q197 (= Q741), R234 (≠ N779), N236 (≠ Y781), N239 (≠ S784), Y243 (= Y788), H244 (= H789), R283 (≠ N828), F287 (= F832), R327 (≠ K870), F328 (≠ Y871), H329 (= H872), Q331 (= Q874), Q362 (≠ N905)
- 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 (≠ F594), T77 (≠ A595), M78 (≠ F596), R82 (≠ N600), T85 (≠ P603), R87 (= R605), I89 (≠ F607), D116 (≠ A635), S164 (= S686), T166 (= T688), T195 (= T739), Q197 (= Q741), R234 (≠ N779), N236 (≠ Y781), N239 (≠ S784), H244 (= H789), R283 (≠ N828), F287 (= F832), R327 (≠ K870), F328 (≠ Y871), H329 (= H872), Q331 (= Q874), Q362 (≠ N905)
- binding cobalamin: D116 (≠ A635), M119 (≠ S638), E139 (≠ S659), Q207 (= Q751), E209 (≠ T753), E247 (= E792), A334 (≠ G877), E371 (= E914), A372 (= A915), A374 (≠ T917)
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: 583:1101/1102 of query aligns to 65:559/562 of I3VE77
- YPTM 76:79 (≠ F-AF 594:596) binding
- TMR 86:88 (≠ PTR 603:605) binding
- I90 (≠ F607) 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 (≠ A635) 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 739:741) binding
- R235 (≠ N779) binding
- N240 (≠ S784) binding
- H245 (= H789) binding
- R284 (≠ N828) binding
P22033 Methylmalonyl-CoA mutase, mitochondrial; MCM; Methylmalonyl-CoA isomerase; EC 5.4.99.2 from Homo sapiens (Human) (see 28 papers)
35% identity, 47% coverage: 579:1101/1102 of query aligns to 81:579/750 of P22033
- P86 (= P584) 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 (= G585) to E: in MMAM; mut0; dbSNP:rs1554160986
- R93 (≠ A591) to H: in MMAM; mut0; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918251
- G94 (= G592) 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 593) binding
- Y100 (≠ F594) 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 (≠ E599) to R: in MMAM; mut0; dbSNP:rs121918249
- T---IRQY 106:110 (≠ NEDPTRMF 600:607) binding
- R108 (= R605) to C: in MMAM; mut0; dbSNP:rs121918257; to G: in MMAM; mut-; to H: in MMAM; mut0; dbSNP:rs483352778
- Q109 (≠ M606) to R: in MMAM; mut0; dbSNP:rs1461110052
- G133 (≠ A629) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253828
- A137 (= A635) to V: in MMAM; mut0; dbSNP:rs941483851
- D139 (= D637) to N: in MMAM; uncertain significance; dbSNP:rs879253829
- L140 (≠ S638) to P: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- A141 (≠ V639) to T: in MMAM; decreased protein expression; dbSNP:rs1554160730
- H143 (≠ L641) to Y: in MMAM; mut0
- G145 (= G643) to S: in MMAM; mut0
- S148 (≠ H647) to L: in MMAM; mut0; dbSNP:rs1300547552
- D156 (≠ K655) to N: in MMAM; mut-
- G158 (= G657) to V: in MMAM; mut0
- G161 (= G660) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; to V: in MMAM; decreased protein expression
- F174 (≠ Y673) to S: in MMAM; mut0; dbSNP:rs864309733
- M186 (= M687) to V: in MMAM; mut-; dbSNP:rs148331800
- T187 (= T688) to S: in MMAM; mut0; dbSNP:rs879253830
- N189 (= N690) to I: in MMAM; mut-; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs200908035; to K: in MMAM; mut-; dbSNP:rs1561959114
- A191 (≠ P692) to E: in MMAM; mut- and mut0; affects proper folding; reduced protein level; decreased methylmalonyl-CoA mutase activity; dbSNP:rs760782399
- A197 (= A698) to E: in MMAM; mut0
- G203 (≠ A704) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs778702777
- E205 (≠ D706) natural variant: Missing (in MMAM; mut0; dbSNP:rs879253831)
- G215 (= G738) to C: in MMAM; mut- and mut0; dbSNP:rs121918258; to S: in MMAM; mut0; dbSNP:rs121918258
- TIQ 216:218 (≠ TVQ 739:741) binding
- Q218 (= Q741) to H: in MMAM; mut0 and mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability; dbSNP:rs1446389693
- N219 (≠ A742) to Y: in MMAM; mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; dbSNP:rs121918256
- R228 (≠ Q751) binding ; to Q: in MMAM; mut0; dbSNP:rs770810987
- T230 (= T753) to I: in MMAM; mut-; to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253833
- Y231 (≠ C754) 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 (≠ R778) binding
- S262 (= S786) to N: in MMAM; mut0
- H265 (= H789) binding ; to Y: in MMAM; mut-
- E276 (≠ Q800) to D: in MMAM; uncertain significance; mut-; dbSNP:rs12175488
- L281 (= L805) to S: in MMAM; mut0; dbSNP:rs796052007
- G284 (= G808) to E: in MMAM; mut0; dbSNP:rs879253835; to R: in MMAM; mut0; dbSNP:rs761477436
- S288 (≠ V812) to P: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1179778233
- G291 (≠ Y815) to E: in MMAM; mut0
- Q293 (≠ A817) to P: in MMAM; mut0
- RLS 304:306 (≠ NLS 828:830) binding
- L305 (= L829) to S: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554160246
- S306 (= S830) to F: in MMAM; mut0; dbSNP:rs1085307929
- W309 (≠ F833) to G: in MMAM; decreased protein expression
- G312 (= G836) to V: in MMAM; mut0; dbSNP:rs864309734
- Y316 (≠ E840) 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 (≠ V847) to T: in MMAM; mut-; dbSNP:rs780387525
- R326 (= R849) to K: in MMAM; uncertain significance; dbSNP:rs758577372
- L328 (≠ I851) 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 (= S866) 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 (≠ K868) natural variant: Missing (in MMAM; mut0)
- L347 (= L869) to R: in MMAM; mut0; dbSNP:rs1026703654
- H350 (= H872) to Y: in MMAM; mut0; dbSNP:rs1407914109
- L358 (= L880) to P: in MMAM; mut0
- N366 (= N888) 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 (= R891) 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 (= T892) to P: in MMAM; mut0; dbSNP:rs368790885
- A377 (= A899) to E: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918250
- Q383 (≠ N905) to H: in MMAM; mut0; to P: in MMAM; mut0
- H386 (= H908) to N: in MMAM; mut0; dbSNP:rs1554159937; to R: in MMAM; mut0; dbSNP:rs866933356
- T387 (= T909) 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 (= N910) to H: in MMAM; mut0; dbSNP:rs766010704; to K: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253840
- S389 (≠ A911) natural variant: Missing (in MMAM; mut0)
- I412 (= I934) natural variant: Missing (in MMAM; mut0)
- P424 (= P946) to L: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253842
- G426 (≠ Q948) 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 (= G949) to D: in MMAM; mut0; dbSNP:rs753288303
- G454 (= G976) to E: in MMAM; mut0
- A499 (= A1021) to T: in dbSNP:rs2229385
- I505 (≠ R1030) to T: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- Q514 (= Q1039) to E: in MMAM; uncertain significance; to K: in MMAM; decreased protein expression
- L518 (= L1043) to P: in MMAM; mut0; dbSNP:rs864309738
- R532 (≠ A1056) to H: in dbSNP:rs1141321
- A535 (≠ Q1059) to P: in MMAM; mut0; dbSNP:rs760183775
- A552 (≠ L1075) to V: in MMAM; uncertain significance; dbSNP:rs879253845
- C560 (= C1082) to Y: in MMAM; mut0; dbSNP:rs1238333040
- T566 (= T1088) to R: in MMAM; mut0
- F573 (≠ G1095) 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
- 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
2xiqA Crystal structure of human methylmalonyl-coa mutase in complex with adenosylcobalamin and malonyl-coa (see paper)
35% identity, 47% coverage: 579:1101/1102 of query aligns to 46:544/714 of 2xiqA
- active site: Y75 (≠ F607), Y229 (= Y788), H230 (= H789)
- binding cobalamin: Y75 (≠ F607), L105 (≠ S638), H108 (≠ L641), A125 (≠ S659), R193 (≠ Q751), E233 (= E792), G320 (= G877), W321 (≠ R878), E357 (= E914), G360 (≠ T917), L361 (≠ T918)
- binding malonyl-coenzyme a: Y61 (vs. gap), T63 (vs. gap), M64 (≠ V593), R68 (≠ K597), T71 (≠ N600), R73 (= R605), Y75 (≠ F607), S150 (= S686), T152 (= T688), T181 (= T739), R193 (≠ Q751), K220 (≠ R778), H230 (= H789), R269 (≠ N828), S271 (= S830), F273 (= F832), R313 (≠ K870), A314 (≠ Y871), H315 (= H872), Q317 (= Q874), Q348 (≠ N905)
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)
34% identity, 47% coverage: 579:1101/1102 of query aligns to 45:543/708 of 8dyjB
- binding adenosine-5'-diphosphate: Y74 (≠ F607), T151 (= T688), R192 (≠ Q751), Y228 (= Y788), H229 (= H789), F272 (= F832), Q316 (= Q874), N352 (= N910), E356 (= E914), L360 (≠ T918), P361 (= P919)
- binding cobalamin: F102 (= F636), L104 (≠ S638), H107 (≠ L641), A124 (≠ S659), V191 (≠ G750), R192 (≠ Q751), H229 (= H789), E232 (= E792), G319 (= G877), W320 (≠ R878), E356 (= E914), G359 (≠ T917), L360 (≠ T918)
Sites not aligning to the query:
- binding cobalamin: 590, 591, 592, 593, 594, 598, 636, 638, 640, 666, 667, 668, 686, 687, 690
8gjuJ Crystal structure of human methylmalonyl-coa mutase (mmut) in complex with methylmalonic acidemia type a protein (mmaa), coenzyme a, and gdp (see paper)
34% identity, 47% coverage: 579:1099/1102 of query aligns to 46:542/689 of 8gjuJ
- binding coenzyme a: Y61 (vs. gap), T63 (vs. gap), R68 (≠ K597), T71 (≠ N600), R73 (= R605), S150 (= S686), T152 (= T688), T181 (= T739), Q183 (= Q741), N222 (≠ Y781), R269 (≠ N828), S271 (= S830), R313 (≠ K870), A314 (≠ Y871), H315 (= H872), Q348 (≠ N905)
6oxdA Structure of mycobacterium tuberculosis methylmalonyl-coa mutase with adenosyl cobalamin (see paper)
35% identity, 47% coverage: 581:1099/1102 of query aligns to 73:566/736 of 6oxdA
- active site: Y100 (≠ F607), Y254 (= Y788), H255 (= H789)
- binding cobalamin: Y100 (≠ F607), L130 (≠ S638), H133 (≠ L641), A150 (≠ S659), R218 (≠ Q751), E258 (= E792), G344 (= G877), W345 (≠ R878), E381 (= E914), A382 (= A915), A384 (≠ T917), L385 (≠ T918)
- binding Itaconyl coenzyme A: Y86 (≠ F594), T88 (≠ F596), M89 (≠ K597), Q93 (≠ E601), T96 (= T604), R98 (= R605), Y100 (≠ F607), S175 (= S686), T177 (= T688), T206 (= T739), R218 (≠ Q751), H255 (= H789), R294 (≠ N828), S296 (= S830), F298 (= F832), R337 (≠ K870), T338 (≠ Y871), H339 (= H872), Q341 (= Q874), Q372 (≠ N905)
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)
34% identity, 46% coverage: 588:1098/1102 of query aligns to 71:556/725 of 5reqA
- active site: F86 (= F607), Y240 (= Y788), H241 (= H789)
- binding cobalamin: L116 (≠ S638), A136 (≠ S659), R204 (≠ Q751), H241 (= H789), E244 (= E792), G330 (= G877), W331 (≠ R878), E367 (= E914), A368 (= A915), A370 (≠ T917)
- binding methylmalonyl(carbadethia)-coenzyme a: Y72 (= Y589), T74 (≠ G592), M75 (≠ V593), R79 (≠ K597), T82 (≠ N600), R84 (= R605), F86 (= F607), S111 (= S633), S161 (= S686), T163 (= T688), T192 (= T739), Q194 (= Q741), R204 (≠ Q751), N233 (≠ Y781), H241 (= H789), R280 (≠ N828), S282 (= S830), F284 (= F832), T324 (≠ Y871), H325 (= H872), Q358 (≠ N905), S359 (= S906)
- binding succinyl(carbadethia)-coenzyme a: Y72 (= Y589), T74 (≠ G592), M75 (≠ V593), R79 (≠ K597), T82 (≠ N600), R84 (= R605), F86 (= F607), S161 (= S686), T163 (= T688), T192 (= T739), R204 (≠ Q751), N233 (≠ Y781), H241 (= H789), R280 (≠ N828), S282 (= S830), F284 (= F832), H325 (= H872), Q358 (≠ N905)
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
6reqA Methylmalonyl-coa mutase, 3-carboxypropyl-coa inhibitor complex (see paper)
34% identity, 46% coverage: 588:1098/1102 of query aligns to 73:558/727 of 6reqA
- active site: Y88 (≠ F607), Y242 (= Y788), H243 (= H789)
- binding 3-carboxypropyl-coenzyme a: Y74 (= Y589), T76 (≠ G592), M77 (≠ V593), F80 (= F596), R81 (≠ K597), T84 (≠ N600), R86 (= R605), Y88 (≠ F607), S113 (= S633), S163 (= S686), T165 (= T688), T194 (= T739), R206 (≠ Q751), H243 (= H789), R282 (≠ N828), S284 (= S830), F286 (= F832), H327 (= H872), Q329 (= Q874), Q360 (≠ N905)
- binding cobalamin: Y88 (≠ F607), F116 (= F636), L118 (≠ S638), H121 (≠ L641), A138 (≠ S659), R206 (≠ Q751), E246 (= E792), G332 (= G877), W333 (≠ R878), E369 (= E914), A370 (= A915), A372 (≠ T917)
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)
34% identity, 46% coverage: 588:1098/1102 of query aligns to 72:557/726 of 4reqA
- active site: Y87 (≠ F607), Y241 (= Y788), H242 (= H789)
- binding cobalamin: Y87 (≠ F607), L117 (≠ S638), A137 (≠ S659), V204 (≠ G750), R205 (≠ Q751), H242 (= H789), E245 (= E792), G331 (= G877), W332 (≠ R878), E368 (= E914), A369 (= A915), A371 (≠ T917), L372 (≠ T918)
- binding methylmalonyl-coenzyme a: Y73 (= Y589), M76 (≠ V593), F79 (= F596), R80 (≠ K597), T83 (≠ N600), R85 (= R605), Y87 (≠ F607), S112 (= S633), S162 (= S686), T164 (= T688), T193 (= T739), R205 (≠ Q751), N234 (≠ Y781), Y241 (= Y788), H242 (= H789), R281 (≠ N828), S283 (= S830), F285 (= F832), H326 (= H872), Q328 (= Q874), Q359 (≠ N905), S360 (= S906)
- binding succinyl-coenzyme a: Y73 (= Y589), M76 (≠ V593), F79 (= F596), R80 (≠ K597), T83 (≠ N600), R85 (= R605), Y87 (≠ F607), S162 (= S686), T164 (= T688), T193 (= T739), Q195 (= Q741), R205 (≠ Q751), N234 (≠ Y781), Y241 (= Y788), H242 (= H789), R281 (≠ N828), S283 (= S830), F285 (= F832), R324 (≠ K870), H326 (= H872), Q359 (≠ N905)
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
P11653 Methylmalonyl-CoA mutase large subunit; MCM-alpha; EC 5.4.99.2 from Propionibacterium freudenreichii subsp. shermanii (see 4 papers)
34% identity, 46% coverage: 588:1098/1102 of query aligns to 74:559/728 of P11653
- Y75 (= Y589) binding
- M78 (≠ V593) binding
- R82 (≠ K597) binding
- T85 (≠ N600) binding
- R87 (= R605) binding
- Y89 (≠ F607) binding ; mutation to F: Does not significantly affect affinity for succiny-CoA, but kcat is lowered about 580-fold.
- S114 (= S633) binding
- F117 (= F636) binding
- A139 (≠ S659) binding
- T195 (= T739) binding
- Q197 (= Q741) binding
- V206 (≠ G750) binding
- R207 (≠ Q751) binding ; binding
- H244 (= H789) binding
- R283 (≠ N828) binding
- S285 (= S830) binding
- G333 (= G877) binding
- E370 (= E914) binding
- A373 (≠ T917) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 609 binding
- 610 binding axial binding residue
- 611 binding
- 612 binding
- 655 binding
- 657 binding
- 686 binding
- 709 binding
7reqA Methylmalonyl-coa mutase, 2-carboxypropyl-coa inhibitor complex (see paper)
34% identity, 46% coverage: 588:1098/1102 of query aligns to 71:556/725 of 7reqA
- active site: Y86 (≠ F607), Y240 (= Y788), H241 (= H789)
- binding 2-carboxypropyl-coenzyme a: Y72 (= Y589), T74 (≠ G592), M75 (≠ V593), F78 (= F596), R79 (≠ K597), T82 (≠ N600), R84 (= R605), Y86 (≠ F607), S161 (= S686), T163 (= T688), T192 (= T739), R204 (≠ Q751), H241 (= H789), R280 (≠ N828), S282 (= S830), F284 (= F832), H325 (= H872), Q358 (≠ N905)
- binding cobalamin: Y86 (≠ F607), L116 (≠ S638), A136 (≠ S659), R204 (≠ Q751), E244 (= E792), G330 (= G877), W331 (≠ R878), E367 (= E914), A368 (= A915), A370 (≠ T917)
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)
34% identity, 46% coverage: 588:1098/1102 of query aligns to 71:556/725 of 3reqA
- active site: Y86 (≠ F607), Y240 (= Y788), H241 (= H789)
- binding adenosine: Y86 (≠ F607), Y240 (= Y788), E244 (= E792), G330 (= G877)
- binding cobalamin: L116 (≠ S638), V203 (≠ G750), R204 (≠ Q751), E244 (= E792), G330 (= G877), W331 (≠ R878), A368 (= A915)
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
>RR42_RS01600 FitnessBrowser__Cup4G11:RR42_RS01600
MTDLSDVQKGAQPGAQPGAPHQAQGPKGPVNKVRFVTAASLFDGHDASINIMRRILQSSG
CEVIHLGHNRSVEEVVSAALQEDVQGIAISSYQGGHVEYFKYMVDLLRRRGGEHIQLFGG
GGGVIVADEIRELQAYGVARIFSPEDGQRLGLAGMIADMVQRCDIDLARYAPATLDAMKG
GDRRALAQLITALENGKADPALADTLRAEAATVKTPVLGITGTGGAGKSSLTDELIRRIR
LDQRDALSIAVISIDPSRRKSGGALLGDRIRMNAINHPHIFMRSMATREAGSEISRALPD
VLAACKVAGFDLIIVETSGIGQGDAAIVAHVDLSLYVMTPEFGAASQLEKIDMLDFADFV
AINKFDRKGAQDAWRDVAKQVQRNREQWHAKPEEMPVYGTQASRFNDDGVTMLYQGLREA
LCARGMRAPAGVLPQLSGRVSTGQNVIVPPARNRYLAEIADTVRAYHRRVDAQSRLARER
QQLREARRMLLAASGQEDQGEALQALATERDAALGAQERKLLAMWPQMRKAYSGDEYVVK
IRDKEIRTTLTTTTLSGTTVRKVVLPRFEDDGEVLKWLLRENVPGSFPYTAGVFAFKREN
EDPTRMFAGEGDAFRTNRRFKLVSEGMDAKRLSTAFDSVTLYGEDPHTRPDIYGKVGNSG
VSIATLDDMKVLYDGFDLTSPSTSVSMTINGPAPTILAMFMNTAIDQQFDKFRADNDREP
TVDEQGKIRAWVLQNVRGTVQADILKEDQGQNTCIFSTEFSLKVMGDIQAYFVHHQVRNF
YSVSISGYHIAEAGANPISQLAFTLSNGFTYVEAYLARGMHIDDFAPNLSFFFSNGMDPE
YSVLGRVARRIWAVTLRDKYGANERSQKLKYHIQTSGRSLHAQEIDFNDIRTTLQALIAI
YDNCNSLHTNAYDEAITTPTGESVRRALAIQLIINREWGVARCENPNQGSFLIDELTDLV
EDAVMQEFERIAERGGVLGAMETGYQRGKIQDESLYYEQRKHDGTLPIIGVNTFRNPDGD
AAPPSLELARSSEEEKQGQLARLADFHARHADAAPAMLQRLRQAVIDNGNVFAVLMDAVR
VCSLGQVTHALFEVGGQYRRNM
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