SitesBLAST
Comparing Echvi_2441 FitnessBrowser__Cola:Echvi_2441 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
Q5KUG0 Fused isobutyryl-CoA mutase; EC 5.4.99.13; EC 3.6.5.- from Geobacillus kaustophilus (strain HTA426) (see paper)
61% identity, 99% coverage: 8:1125/1125 of query aligns to 5:1086/1086 of Q5KUG0
- K213 (= K209) mutation to A: Loss of GTPase and ATPase activities. No effect on the mutase activity.
Q1LRY0 Fused isobutyryl-CoA mutase; EC 5.4.99.13; EC 3.6.5.- from Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34) (Ralstonia metallidurans) (see 2 papers)
60% identity, 99% coverage: 10:1125/1125 of query aligns to 23:1093/1093 of Q1LRY0
- H39 (= H26) binding axial binding residue
- 169:417 (vs. 152:403, 57% identical) GTPase chaperone MeaI
- GAGKSS 219:224 (= GAGKSS 206:211) binding
- S223 (= S210) binding
- I248 (≠ V234) binding
- D249 (= D235) binding
- D262 (= D248) binding ; binding
- R265 (= R251) binding
- E310 (= E296) binding ; binding
- T311 (= T297) binding
- NKFD 357:360 (= NKFD 343:346) binding
- 418:579 (vs. 404:567, 33% identical) Linker
- F587 (= F575) binding
- F598 (= F586) 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 (= R610) binding
- R728 (= R760) binding
- Y772 (= Y804) binding
- S821 (= S853) binding
- R856 (= R888) binding
- K861 (= K893) binding
- E973 (= E1005) binding
- N1092 (= N1124) binding
4xc6A Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, and mg (holo-icmf/gdp) (see paper)
60% identity, 99% coverage: 10:1125/1125 of query aligns to 3:1067/1067 of 4xc6A
- active site: K6 (≠ H13), F572 (= F586), Y753 (= Y811), H754 (= H812)
- binding cobalamin: G18 (= G25), H19 (= H26), D20 (= D27), A21 (= A28), S22 (≠ A29), M26 (= M33), Y66 (= Y73), Q67 (= Q74), G94 (= G101), G96 (= G103), V98 (≠ T105), Y116 (= Y123), S117 (≠ A124), P118 (= P125), M129 (= M136), F601 (= F615), L606 (= L620), S624 (= S638), Q716 (= Q774), H754 (= H812), E757 (= E815), A758 (= A816), G842 (= G900), R843 (= R901), E879 (= E937), A880 (= A938), T882 (= T940), H967 (= H1025)
- binding guanosine-5'-diphosphate: G199 (= G206), G201 (= G208), K202 (= K209), S203 (= S210), S204 (= S211), R245 (= R251), N337 (= N343), K338 (= K344), D340 (= D346), Q375 (≠ I381), S377 (= S383), E947 (= E1005)
- binding magnesium ion: S203 (= S210), D229 (= D235), D242 (= D248), D242 (= D248), E290 (= E296), E290 (= E296)
5cjwA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate pivalyl-coenzyme a (see paper)
60% identity, 99% coverage: 10:1125/1125 of query aligns to 3:1063/1063 of 5cjwA
- active site: K6 (≠ H13), F571 (= F586), Y752 (= Y811), H753 (= H812)
- binding pivalyl-coenzyme A: F558 (= F573), F560 (= F575), R562 (= R577), R569 (= R584), F571 (= F586), R595 (= R610), S650 (= S665), T652 (= T667), R701 (= R760), T703 (= T762), Q705 (= Q764), Y745 (= Y804), Y752 (= Y811), H753 (= H812), S794 (= S853), F796 (= F855), R829 (= R888), K834 (= K893), H836 (= H895)
- binding cobalamin: G18 (= G25), H19 (= H26), D20 (= D27), A21 (= A28), S22 (≠ A29), M26 (= M33), Y66 (= Y73), Q67 (= Q74), G94 (= G101), G96 (= G103), V98 (≠ T105), Y116 (= Y123), S117 (≠ A124), P118 (= P125), F600 (= F615), L605 (= L620), S623 (= S638), Q715 (= Q774), H753 (= H812), E756 (= E815), A757 (= A816), G841 (= G900), R842 (= R901), E878 (= E937), A879 (= A938), T881 (= T940), H966 (= H1025)
- binding guanosine-5'-diphosphate: G199 (= G206), G201 (= G208), K202 (= K209), S203 (= S210), S204 (= S211), R245 (= R251), N337 (= N343), K338 (= K344), D340 (= D346), Q375 (≠ I381), S377 (= S383), N1062 (= N1124)
- binding magnesium ion: S203 (= S210), D229 (= D235), D242 (= D248), D242 (= D248), E290 (= E296), E290 (= E296)
5cjtA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isobutyryl-coenzyme a (see paper)
59% identity, 99% coverage: 10:1125/1125 of query aligns to 3:1062/1062 of 5cjtA
- active site: K6 (≠ H13), F569 (= F586), Y750 (= Y811), H751 (= H812)
- binding cobalamin: G18 (= G25), H19 (= H26), D20 (= D27), A21 (= A28), S22 (≠ A29), M26 (= M33), Y66 (= Y73), Q67 (= Q74), G94 (= G101), G96 (= G103), V98 (≠ T105), Y116 (= Y123), S117 (≠ A124), F598 (= F615), L603 (= L620), S621 (= S638), Q713 (= Q774), H751 (= H812), E754 (= E815), A755 (= A816), G839 (= G900), R840 (= R901), E876 (= E937), A877 (= A938), T879 (= T940), H964 (= H1025)
- binding isobutyryl-coenzyme a: F556 (= F573), F558 (= F575), R560 (= R577), R567 (= R584), F569 (= F586), R593 (= R610), S648 (= S665), T650 (= T667), R699 (= R760), T701 (= T762), Q703 (= Q764), Y743 (= Y804), Y750 (= Y811), H751 (= H812), S792 (= S853), F794 (= F855), R827 (= R888), K832 (= K893), H834 (= H895)
- binding guanosine-5'-diphosphate: G199 (= G206), G201 (= G208), K202 (= K209), S203 (= S210), S204 (= S211), R245 (= R251), N336 (= N343), K337 (= K344), D339 (= D346), Q374 (≠ I381), S376 (= S383), E944 (= E1005)
- binding magnesium ion: S203 (= S210), D229 (= D235), D242 (= D248), D242 (= D248), E289 (= E296), E289 (= E296)
5cjvA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isovaleryl-coenzyme a (see paper)
59% identity, 99% coverage: 10:1125/1125 of query aligns to 3:1061/1061 of 5cjvA
- active site: K6 (≠ H13), F569 (= F586), Y750 (= Y811), H751 (= H812)
- binding cobalamin: G18 (= G25), H19 (= H26), D20 (= D27), A21 (= A28), S22 (≠ A29), M26 (= M33), Y66 (= Y73), Q67 (= Q74), G94 (= G101), G96 (= G103), V98 (≠ T105), Y116 (= Y123), S117 (≠ A124), M129 (= M136), F598 (= F615), L603 (= L620), S621 (= S638), Q713 (= Q774), E754 (= E815), A755 (= A816), G839 (= G900), R840 (= R901), E876 (= E937), A877 (= A938), T879 (= T940), H964 (= H1025)
- binding guanosine-5'-diphosphate: G199 (= G206), G201 (= G208), K202 (= K209), S203 (= S210), S204 (= S211), R245 (= R251), K336 (= K344), D338 (= D346), Q373 (≠ I381), S375 (= S383), E944 (= E1005)
- binding Isovaleryl-coenzyme A: F556 (= F573), F558 (= F575), R560 (= R577), R567 (= R584), F569 (= F586), R593 (= R610), S648 (= S665), T650 (= T667), R699 (= R760), T701 (= T762), Q703 (= Q764), Q713 (= Q774), Y743 (= Y804), H751 (= H812), S792 (= S853), F794 (= F855), K832 (= K893), H834 (= H895)
- binding magnesium ion: S203 (= S210), D229 (= D235), D242 (= D248), D242 (= D248), E288 (= E296), E288 (= E296)
4xc7A Isobutyryl-coa mutase fused with bound butyryl-coa and without cobalamin or gdp (apo-icmf) (see paper)
59% identity, 99% coverage: 10:1125/1125 of query aligns to 2:1053/1053 of 4xc7A
- active site: K5 (≠ H13), F566 (= F586), Y747 (= Y811), H748 (= H812)
- binding Butyryl Coenzyme A: F553 (= F573), R557 (= R577), R564 (= R584), F566 (= F586), R590 (= R610), S645 (= S665), T647 (= T667), R696 (= R760), T698 (= T762), Y740 (= Y804), S789 (= S853), F791 (= F855), R824 (= R888), K829 (= K893), H831 (= H895)
P22033 Methylmalonyl-CoA mutase, mitochondrial; MCM; Methylmalonyl-CoA isomerase; EC 5.4.99.2 from Homo sapiens (Human) (see 28 papers)
31% identity, 50% coverage: 558:1124/1125 of query aligns to 81:579/750 of P22033
- P86 (= P563) 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 (= G564) to E: in MMAM; mut0; dbSNP:rs1554160986
- R93 (≠ A570) to H: in MMAM; mut0; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918251
- G94 (= G571) to R: in MMAM; mut0; dbSNP:rs727504022; to V: in MMAM; mut- and mut0; dbSNP:rs535411418
- P95 (≠ V572) to R: in MMAM; mut0; dbSNP:rs190834116
- YPTM 96:99 (≠ FPFK 573:576) binding
- Y100 (≠ R577) 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 (≠ P582) to R: in MMAM; mut0; dbSNP:rs121918249
- TIRQY 106:110 (≠ T-RMF 583:586) binding
- R108 (= R584) to C: in MMAM; mut0; dbSNP:rs121918257; to G: in MMAM; mut-; to H: in MMAM; mut0; dbSNP:rs483352778
- Q109 (≠ M585) to R: in MMAM; mut0; dbSNP:rs1461110052
- G133 (≠ R610) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253828
- A137 (= A614) to V: in MMAM; mut0; dbSNP:rs941483851
- D139 (= D616) to N: in MMAM; uncertain significance; dbSNP:rs879253829
- L140 (≠ S617) to P: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- A141 (≠ V618) to T: in MMAM; decreased protein expression; dbSNP:rs1554160730
- H143 (≠ L620) to Y: in MMAM; mut0
- G145 (= G622) to S: in MMAM; mut0
- S148 (≠ P625) to L: in MMAM; mut0; dbSNP:rs1300547552
- D156 (≠ K634) to N: in MMAM; mut-
- G158 (= G636) to V: in MMAM; mut0
- G161 (= G639) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; to V: in MMAM; decreased protein expression
- F174 (≠ Y652) to S: in MMAM; mut0; dbSNP:rs864309733
- M186 (= M666) to V: in MMAM; mut-; dbSNP:rs148331800
- T187 (= T667) to S: in MMAM; mut0; dbSNP:rs879253830
- N189 (= N681) to I: in MMAM; mut-; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs200908035; to K: in MMAM; mut-; dbSNP:rs1561959114
- A191 (= A683) to E: in MMAM; mut- and mut0; affects proper folding; reduced protein level; decreased methylmalonyl-CoA mutase activity; dbSNP:rs760782399
- A197 (≠ E689) to E: in MMAM; mut0
- G203 (= G739) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs778702777
- E205 (vs. gap) natural variant: Missing (in MMAM; mut0; dbSNP:rs879253831)
- G215 (= G761) to C: in MMAM; mut- and mut0; dbSNP:rs121918258; to S: in MMAM; mut0; dbSNP:rs121918258
- TIQ 216:218 (≠ TVQ 762:764) binding
- Q218 (= Q764) to H: in MMAM; mut0 and mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability; dbSNP:rs1446389693
- N219 (≠ A765) to Y: in MMAM; mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; dbSNP:rs121918256
- R228 (≠ Q774) binding ; to Q: in MMAM; mut0; dbSNP:rs770810987
- T230 (= T776) to I: in MMAM; mut-; to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253833
- Y231 (≠ C777) 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 (≠ N802) binding
- S262 (= S809) to N: in MMAM; mut0
- H265 (= H812) binding ; to Y: in MMAM; mut-
- E276 (≠ Q823) to D: in MMAM; uncertain significance; mut-; dbSNP:rs12175488
- L281 (= L828) to S: in MMAM; mut0; dbSNP:rs796052007
- G284 (= G831) to E: in MMAM; mut0; dbSNP:rs879253835; to R: in MMAM; mut0; dbSNP:rs761477436
- S288 (≠ V835) to P: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1179778233
- G291 (≠ Y838) to E: in MMAM; mut0
- Q293 (≠ S840) to P: in MMAM; mut0
- RLS 304:306 (≠ NLS 851:853) binding
- L305 (= L852) to S: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554160246
- S306 (= S853) to F: in MMAM; mut0; dbSNP:rs1085307929
- W309 (≠ F856) to G: in MMAM; decreased protein expression
- G312 (= G859) to V: in MMAM; mut0; dbSNP:rs864309734
- Y316 (= Y864) 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 (≠ V870) to T: in MMAM; mut-; dbSNP:rs780387525
- R326 (= R872) to K: in MMAM; uncertain significance; dbSNP:rs758577372
- L328 (≠ I874) 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 (= S889) 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 (≠ M891) natural variant: Missing (in MMAM; mut0)
- L347 (= L892) to R: in MMAM; mut0; dbSNP:rs1026703654
- H350 (= H895) to Y: in MMAM; mut0; dbSNP:rs1407914109
- L358 (= L903) to P: in MMAM; mut0
- N366 (= N911) 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 (= R914) 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 (= T915) to P: in MMAM; mut0; dbSNP:rs368790885
- A377 (= A922) to E: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918250
- Q383 (≠ N928) to H: in MMAM; mut0; to P: in MMAM; mut0
- H386 (= H931) to N: in MMAM; mut0; dbSNP:rs1554159937; to R: in MMAM; mut0; dbSNP:rs866933356
- T387 (= T932) 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 (= N933) to H: in MMAM; mut0; dbSNP:rs766010704; to K: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253840
- S389 (≠ A934) natural variant: Missing (in MMAM; mut0)
- I412 (= I957) natural variant: Missing (in MMAM; mut0)
- P424 (= P969) to L: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253842
- G426 (≠ Q971) 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 (= G972) to D: in MMAM; mut0; dbSNP:rs753288303
- G454 (= G999) to E: in MMAM; mut0
- A499 (= A1041) to T: in dbSNP:rs2229385
- I505 (≠ T1047) to T: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- Q514 (= Q1056) to E: in MMAM; uncertain significance; to K: in MMAM; decreased protein expression
- L518 (≠ E1060) to P: in MMAM; mut0; dbSNP:rs864309738
- R532 (≠ E1079) to H: in dbSNP:rs1141321
- A535 (≠ N1082) to P: in MMAM; mut0; dbSNP:rs760183775
- A552 (≠ L1098) to V: in MMAM; uncertain significance; dbSNP:rs879253845
- C560 (= C1105) to Y: in MMAM; mut0; dbSNP:rs1238333040
- T566 (= T1111) to R: in MMAM; mut0
- F573 (≠ G1118) 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
8dyjB Crystal structure of human methylmalonyl-coa mutase in complex with adp and cob(ii)alamin (see paper)
31% identity, 50% coverage: 558:1124/1125 of query aligns to 45:543/708 of 8dyjB
- binding adenosine-5'-diphosphate: Y74 (≠ F586), T151 (= T667), R192 (≠ Q774), Y228 (= Y811), H229 (= H812), F272 (= F855), Q316 (= Q897), N352 (= N933), E356 (= E937), L360 (≠ T941), P361 (= P942)
- binding cobalamin: F102 (= F615), L104 (≠ S617), H107 (≠ L620), A124 (≠ S638), V191 (≠ A773), R192 (≠ Q774), H229 (= H812), E232 (= E815), G319 (= G900), W320 (≠ R901), E356 (= E937), G359 (≠ T940), L360 (≠ T941)
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)
31% identity, 50% coverage: 558:1124/1125 of query aligns to 46:544/714 of 2xiqA
- active site: Y75 (≠ F586), Y229 (= Y811), H230 (= H812)
- binding cobalamin: Y75 (≠ F586), L105 (≠ S617), H108 (≠ L620), A125 (≠ S638), R193 (≠ Q774), E233 (= E815), G320 (= G900), W321 (≠ R901), E357 (= E937), G360 (≠ T940), L361 (≠ T941)
- binding malonyl-coenzyme a: Y61 (≠ F573), T63 (≠ F575), M64 (≠ K576), R68 (≠ E580), T71 (= T583), R73 (= R584), Y75 (≠ F586), S150 (= S665), T152 (= T667), T181 (= T762), R193 (≠ Q774), K220 (≠ N802), H230 (= H812), R269 (≠ N851), S271 (= S853), F273 (= F855), R313 (≠ K893), A314 (≠ Y894), H315 (= H895), Q317 (= Q897), Q348 (≠ N928)
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
8gjuJ Crystal structure of human methylmalonyl-coa mutase (mmut) in complex with methylmalonic acidemia type a protein (mmaa), coenzyme a, and gdp (see paper)
31% identity, 50% coverage: 558:1122/1125 of query aligns to 46:542/689 of 8gjuJ
- binding coenzyme a: Y61 (≠ F573), T63 (≠ F575), R68 (≠ E580), T71 (= T583), R73 (= R584), S150 (= S665), T152 (= T667), T181 (= T762), Q183 (= Q764), N222 (≠ Y804), R269 (≠ N851), S271 (= S853), R313 (≠ K893), A314 (≠ Y894), H315 (= H895), Q348 (≠ N928)
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, 33% coverage: 756:1122/1125 of query aligns to 190:557/562 of I3VE77
Sites not aligning to the query:
- 76:79 binding
- 86:88 binding
- 90 I→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.; I→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.; I→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.
- 117 binding ; D→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.; D→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.
4r3uA Crystal structure of 2-hydroxyisobutyryl-coa mutase (see paper)
35% identity, 33% coverage: 756:1122/1125 of query aligns to 189:556/557 of 4r3uA
- active site: Y243 (= Y811), H244 (= H812)
- binding 3-hydroxybutanoyl-coenzyme a: T195 (= T762), Q197 (= Q764), R234 (≠ N802), N236 (≠ Y804), N239 (≠ S807), Y243 (= Y811), H244 (= H812), R283 (≠ N851), F287 (= F855), R327 (≠ K893), F328 (≠ Y894), H329 (= H895), Q331 (= Q897), Q362 (≠ N928)
- 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: T195 (= T762), Q197 (= Q764), R234 (≠ N802), N236 (≠ Y804), N239 (≠ S807), H244 (= H812), R283 (≠ N851), F287 (= F855), R327 (≠ K893), F328 (≠ Y894), H329 (= H895), Q331 (= Q897), Q362 (≠ N928)
- binding cobalamin: Q207 (= Q774), E209 (≠ T776), E247 (= E815), A334 (≠ G900), E371 (= E937), A372 (= A938), A374 (≠ T940)
Sites not aligning to the query:
- active site: 89
- binding 3-hydroxybutanoyl-coenzyme a: 75, 77, 78, 82, 85, 87, 89, 116, 164, 166
- 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: 75, 77, 78, 82, 85, 87, 89, 116, 164, 166
- binding cobalamin: 116, 119, 139
6oxdA Structure of mycobacterium tuberculosis methylmalonyl-coa mutase with adenosyl cobalamin (see paper)
30% identity, 50% coverage: 561:1122/1125 of query aligns to 74:566/736 of 6oxdA
- active site: Y100 (≠ F586), Y254 (= Y811), H255 (= H812)
- binding cobalamin: Y100 (≠ F586), L130 (≠ S617), H133 (≠ L620), A150 (≠ S638), R218 (≠ Q774), E258 (= E815), G344 (= G900), W345 (≠ R901), E381 (= E937), A382 (= A938), A384 (≠ T940), L385 (≠ T941)
- binding Itaconyl coenzyme A: Y86 (≠ F573), T88 (≠ F575), M89 (≠ K576), Q93 (≠ E580), T96 (= T583), R98 (= R584), Y100 (≠ F586), S175 (= S665), T177 (= T667), T206 (= T762), R218 (≠ Q774), H255 (= H812), R294 (≠ N851), S296 (= S853), F298 (= F855), R337 (≠ K893), T338 (≠ Y894), H339 (= H895), Q341 (= Q897), Q372 (≠ N928)
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)
28% identity, 42% coverage: 651:1121/1125 of query aligns to 51:556/725 of 5reqA
- active site: F86 (vs. gap), Y240 (= Y811), H241 (= H812)
- binding cobalamin: L116 (≠ D706), A136 (≠ N728), R204 (≠ Q774), H241 (= H812), E244 (= E815), G330 (= G900), W331 (≠ R901), E367 (= E937), A368 (= A938), A370 (≠ T940)
- binding methylmalonyl(carbadethia)-coenzyme a: Y72 (≠ A672), T74 (= T674), M75 (= M675), R79 (vs. gap), T82 (vs. gap), R84 (vs. gap), F86 (vs. gap), S111 (≠ V701), S161 (vs. gap), T163 (vs. gap), T192 (= T762), Q194 (= Q764), R204 (≠ Q774), N233 (≠ Y804), H241 (= H812), R280 (≠ N851), S282 (= S853), F284 (= F855), T324 (≠ Y894), H325 (= H895), Q358 (≠ N928), S359 (= S929)
- binding succinyl(carbadethia)-coenzyme a: Y72 (≠ A672), T74 (= T674), M75 (= M675), R79 (vs. gap), T82 (vs. gap), R84 (vs. gap), F86 (vs. gap), S161 (vs. gap), T163 (vs. gap), T192 (= T762), R204 (≠ Q774), N233 (≠ Y804), H241 (= H812), R280 (≠ N851), S282 (= S853), F284 (= F855), H325 (= H895), Q358 (≠ N928)
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)
28% identity, 42% coverage: 651:1121/1125 of query aligns to 52:557/726 of 4reqA
- active site: Y87 (vs. gap), Y241 (= Y811), H242 (= H812)
- binding cobalamin: Y87 (vs. gap), L117 (≠ D706), A137 (≠ N728), V204 (≠ A773), R205 (≠ Q774), H242 (= H812), E245 (= E815), G331 (= G900), W332 (≠ R901), E368 (= E937), A369 (= A938), A371 (≠ T940), L372 (≠ T941)
- binding methylmalonyl-coenzyme a: Y73 (≠ A672), M76 (= M675), F79 (= F678), R80 (vs. gap), T83 (vs. gap), R85 (vs. gap), Y87 (vs. gap), S112 (≠ V701), S162 (vs. gap), T164 (vs. gap), T193 (= T762), R205 (≠ Q774), N234 (≠ Y804), Y241 (= Y811), H242 (= H812), R281 (≠ N851), S283 (= S853), F285 (= F855), H326 (= H895), Q328 (= Q897), Q359 (≠ N928), S360 (= S929)
- binding succinyl-coenzyme a: Y73 (≠ A672), M76 (= M675), F79 (= F678), R80 (vs. gap), T83 (vs. gap), R85 (vs. gap), Y87 (vs. gap), S162 (vs. gap), T164 (vs. gap), T193 (= T762), Q195 (= Q764), R205 (≠ Q774), N234 (≠ Y804), Y241 (= Y811), H242 (= H812), R281 (≠ N851), S283 (= S853), F285 (= F855), R324 (≠ K893), H326 (= H895), Q359 (≠ N928)
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)
28% identity, 42% coverage: 651:1121/1125 of query aligns to 54:559/728 of P11653
- Y75 (≠ A672) binding
- M78 (= M675) binding
- R82 (vs. gap) binding
- T85 (vs. gap) binding
- R87 (vs. gap) binding
- Y89 (vs. gap) binding ; mutation to F: Does not significantly affect affinity for succiny-CoA, but kcat is lowered about 580-fold.
- S114 (≠ V701) binding
- F117 (≠ K704) binding
- A139 (≠ N728) binding
- T195 (= T762) binding
- Q197 (= Q764) binding
- V206 (≠ A773) binding
- R207 (≠ Q774) binding ; binding
- H244 (= H812) binding
- R283 (≠ N851) binding
- S285 (= S853) binding
- G333 (= G900) binding
- E370 (= E937) binding
- A373 (≠ T940) 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)
28% identity, 42% coverage: 651:1121/1125 of query aligns to 51:556/725 of 7reqA
- active site: Y86 (vs. gap), Y240 (= Y811), H241 (= H812)
- binding 2-carboxypropyl-coenzyme a: Y72 (≠ A672), T74 (= T674), M75 (= M675), F78 (= F678), R79 (vs. gap), T82 (vs. gap), R84 (vs. gap), Y86 (vs. gap), S161 (vs. gap), T163 (vs. gap), T192 (= T762), R204 (≠ Q774), H241 (= H812), R280 (≠ N851), S282 (= S853), F284 (= F855), H325 (= H895), Q358 (≠ N928)
- binding cobalamin: Y86 (vs. gap), L116 (≠ D706), A136 (≠ N728), R204 (≠ Q774), E244 (= E815), G330 (= G900), W331 (≠ R901), E367 (= E937), A368 (= A938), A370 (≠ T940)
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)
28% identity, 42% coverage: 651:1121/1125 of query aligns to 51:556/725 of 3reqA
- active site: Y86 (vs. gap), Y240 (= Y811), H241 (= H812)
- binding adenosine: Y86 (vs. gap), Y240 (= Y811), E244 (= E815), G330 (= G900)
- binding cobalamin: L116 (≠ D706), V203 (≠ A773), R204 (≠ Q774), E244 (= E815), G330 (= G900), W331 (≠ R901), A368 (= A938)
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)
28% identity, 42% coverage: 651:1121/1125 of query aligns to 51:556/725 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
>Echvi_2441 FitnessBrowser__Cola:Echvi_2441
MTQKVTAYKPKSHVRIVTAASLFDGHDAAINIMRRIIQSVGCEVIHLGHNRSVQEIVSCA
IQEDVQAIAITSYQGGHIEFFKYMYDLLQEKGAGHIKIFGGGGGTILPAEIKELHAYGVA
RIYAPDDGRSMGLQGMINDLVGQADFPLGDKLDGGALPDVRHPERIARWISAAENFPDAY
QSMREKQGHGGEDKTVPVLGITGTGGAGKSSLVDELARRFLVDFPDKHLAIISVDPSKRK
TGGALLGDRIRMNAIHHPRVYMRSLATRQANLSLSKHVKDAVDIVKMAGFDLVILETSGI
GQSDTEVADHADLSLYVMTPEYGAASQLEKIDMLDFADLIALNKFDKKGAFDALRDVKKQ
FVRNHGLWDAKDEELPVIGTIASQFNDPGMNRLYRELMLRLTALKIADFTPSDGASLEEL
EKLFIIPPSRTRYLAEIVEENQRYEQWAATQKELANRLYGVKKAIETFEEEAEGESAVME
SLEAAYTALTNKLDAENLQWLENWKELVGSYANDQFTFMVRGKEIAIQTFSTSLSGTRIP
KVALPKYEAWGDLLQWKFKENVPGKFPFTAGVFPFKREGEDPTRMFAGEGGPERTNRRFH
YVSKDMPAKRLSTAFDSVTLYGEDPGYRPDIYGKIGNSGVNICCLDDMKKLYAGFDLADP
RTSVSMTINGPAATMTAFFMNTAIDQQCERYIYDKGSEGEVEAKLDEMYRENGLERPRYQ
GTVPEGNNGLGLLLLGVTGDQVLPKEVYESIKADTLTKVRGTVQADILKEDQAQNTCIFS
TEFSLRLMGDVQEYFIDQGVRNFYSVSISGYHIAEAGANPITQLALTLSNGFTYVEYYVS
RGMDVNAFAPNLSFFFSNGIDPEYAVIGRVARRIWAKAMKLKYGANERSQMLKYHIQTSG
RSLHAQEIDFNDIRTTLQALYAIYDNCNSLHTNAYDEAITTPTEASVRRAMAIQLIINKE
LGLAKNENPLQGAFIIEELTDLVEEAVYAEFERITERGGVLGAMETMYQRGKIQEESLHY
ETLKHAGTYPIIGVNTFLSSAGSPTITPGEVIRATQEEKEMQIKGLENLHRKYEFQSVEL
LNDLKEAAVTNENLFSQLMEAVKCCSLGQITHALYEVGGQFRRNM
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