SitesBLAST
Comparing 16996 FitnessBrowser__Keio:16996 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)
8dyjB Crystal structure of human methylmalonyl-coa mutase in complex with adp and cob(ii)alamin (see paper)
59% identity, 99% coverage: 6:711/714 of query aligns to 6:705/708 of 8dyjB
- binding adenosine-5'-diphosphate: Y74 (= Y78), T151 (= T155), R192 (= R196), Y228 (= Y232), H229 (= H233), F272 (= F276), Q316 (= Q319), N352 (= N355), E356 (= E359), L360 (= L363), P361 (= P364)
- binding cobalamin: F102 (= F106), L104 (= L108), H107 (= H111), A124 (= A128), V191 (≠ C195), R192 (= R196), H229 (= H233), E232 (= E236), G319 (= G322), W320 (= W323), E356 (= E359), G359 (= G362), L360 (= L363), G590 (= G596), H591 (= H597), D592 (= D598), R593 (= R599), G594 (= G600), I598 (= I604), S636 (= S642), L638 (= L644), A640 (= A646), G666 (= G672), G667 (= G673), V668 (= V674), F686 (≠ Y692), G687 (= G693), T690 (= T696)
P22033 Methylmalonyl-CoA mutase, mitochondrial; MCM; Methylmalonyl-CoA isomerase; EC 5.4.99.2 from Homo sapiens (Human) (see 28 papers)
59% identity, 99% coverage: 6:711/714 of query aligns to 42:741/750 of P22033
- Q50 (≠ E14) binding
- I69 (= I35) to V: in MMAM; likely benign; dbSNP:rs115923556
- P86 (= P54) 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 (= G55) to E: in MMAM; mut0; dbSNP:rs1554160986
- R93 (= R61) to H: in MMAM; mut0; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918251
- G94 (= G62) to R: in MMAM; mut0; dbSNP:rs727504022; to V: in MMAM; mut- and mut0; dbSNP:rs535411418
- P95 (= P63) to R: in MMAM; mut0; dbSNP:rs190834116
- YPTM 96:99 (≠ RATM 64:67) binding
- Y100 (= Y68) 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 (= W73) to R: in MMAM; mut0; dbSNP:rs121918249
- TIRQY 106:110 (= TIRQY 74:78) binding
- R108 (= R76) to C: in MMAM; mut0; dbSNP:rs121918257; to G: in MMAM; mut-; to H: in MMAM; mut0; dbSNP:rs483352778
- Q109 (= Q77) to R: in MMAM; mut0; dbSNP:rs1461110052
- G133 (= G101) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253828
- A137 (= A105) to V: in MMAM; mut0; dbSNP:rs941483851
- D139 (= D107) to N: in MMAM; uncertain significance; dbSNP:rs879253829
- L140 (= L108) to P: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- A141 (= A109) to T: in MMAM; decreased protein expression; dbSNP:rs1554160730
- H143 (= H111) to Y: in MMAM; mut0
- G145 (= G113) to S: in MMAM; mut0
- S148 (= S116) to L: in MMAM; mut0; dbSNP:rs1300547552
- D156 (= D124) to N: in MMAM; mut-
- G158 (= G126) to V: in MMAM; mut0
- G161 (= G129) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; to V: in MMAM; decreased protein expression
- F174 (= F142) to S: in MMAM; mut0; dbSNP:rs864309733
- M186 (= M154) to V: in MMAM; mut-; dbSNP:rs148331800
- T187 (= T155) to S: in MMAM; mut0; dbSNP:rs879253830
- N189 (= N157) to I: in MMAM; mut-; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs200908035; to K: in MMAM; mut-; dbSNP:rs1561959114
- A191 (= A159) to E: in MMAM; mut- and mut0; affects proper folding; reduced protein level; decreased methylmalonyl-CoA mutase activity; dbSNP:rs760782399
- A197 (= A165) to E: in MMAM; mut0
- G203 (≠ A171) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs778702777
- E205 (= E173) natural variant: Missing (in MMAM; mut0; dbSNP:rs879253831)
- G215 (= G183) to C: in MMAM; mut- and mut0; dbSNP:rs121918258; to S: in MMAM; mut0; dbSNP:rs121918258
- TIQ 216:218 (= TIQ 184:186) binding
- Q218 (= Q186) to H: in MMAM; mut0 and mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability; dbSNP:rs1446389693
- N219 (= N187) to Y: in MMAM; mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; dbSNP:rs121918256
- R228 (= R196) binding ; to Q: in MMAM; mut0; dbSNP:rs770810987
- T230 (= T198) to I: in MMAM; mut-; to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253833
- Y231 (= Y199) 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 (≠ R223) binding
- S262 (= S230) to N: in MMAM; mut0
- H265 (= H233) binding ; to Y: in MMAM; mut-
- E276 (≠ Q244) to D: in MMAM; uncertain significance; mut-; dbSNP:rs12175488
- L281 (= L249) to S: in MMAM; mut0; dbSNP:rs796052007
- G284 (= G252) to E: in MMAM; mut0; dbSNP:rs879253835; to R: in MMAM; mut0; dbSNP:rs761477436
- S288 (≠ I256) to P: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1179778233
- G291 (≠ A259) to E: in MMAM; mut0
- Q293 (≠ S261) to P: in MMAM; mut0
- RLS 304:306 (= RLS 272:274) binding
- L305 (= L273) to S: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554160246
- S306 (= S274) to F: in MMAM; mut0; dbSNP:rs1085307929
- W309 (≠ F277) to G: in MMAM; decreased protein expression
- G312 (= G280) to V: in MMAM; mut0; dbSNP:rs864309734
- Y316 (≠ F284) 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 (= A292) to T: in MMAM; mut-; dbSNP:rs780387525
- R326 (= R294) to K: in MMAM; uncertain significance; dbSNP:rs758577372
- L328 (= L296) 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 (= S311) 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 (≠ A313) natural variant: Missing (in MMAM; mut0)
- L347 (= L314) to R: in MMAM; mut0; dbSNP:rs1026703654
- H350 (= H317) to Y: in MMAM; mut0; dbSNP:rs1407914109
- L358 (= L325) to P: in MMAM; mut0
- N366 (= N333) 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 (= R336) 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 (= T337) to P: in MMAM; mut0; dbSNP:rs368790885
- A377 (= A344) to E: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918250
- Q383 (= Q350) to H: in MMAM; mut0; to P: in MMAM; mut0
- H386 (= H353) to N: in MMAM; mut0; dbSNP:rs1554159937; to R: in MMAM; mut0; dbSNP:rs866933356
- T387 (= T354) 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 (= N355) to H: in MMAM; mut0; dbSNP:rs766010704; to K: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253840
- S389 (≠ A356) natural variant: Missing (in MMAM; mut0)
- I412 (= I379) natural variant: Missing (in MMAM; mut0)
- P424 (= P391) to L: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253842
- G426 (≠ A393) 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 (= G394) to D: in MMAM; mut0; dbSNP:rs753288303
- G454 (= G421) to E: in MMAM; mut0
- A499 (≠ E466) to T: in dbSNP:rs2229385
- I505 (= I472) to T: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- Q514 (= Q481) to E: in MMAM; uncertain significance; to K: in MMAM; decreased protein expression
- L518 (= L485) to P: in MMAM; mut0; dbSNP:rs864309738
- R532 (≠ A499) to H: in dbSNP:rs1141321
- A535 (≠ N502) to P: in MMAM; mut0; dbSNP:rs760183775
- A552 (= A518) to V: in MMAM; uncertain significance; dbSNP:rs879253845
- C560 (≠ A526) to Y: in MMAM; mut0; dbSNP:rs1238333040
- T566 (≠ S532) to R: in MMAM; mut0
- F573 (= F539) 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
- Y587 (≠ I553) to C: in MMAM; mut-
- I597 (≠ F567) to R: in MMAM; no changed in protein expression; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554158951
- P615 (= P585) to L: in MMAM; mut0; affects proper folding; reduced strongly protein level; to R: in MMAM; mut0; dbSNP:rs1554158777; to T: in MMAM; mut0; affects proper folding; reduced strongly protein level; loss of methylmalonyl-CoA mutase activity; dbSNP:rs1302409621
- R616 (= R586) to C: in MMAM; mut0; dbSNP:rs765284825
- L617 (≠ I587) to R: in MMAM; mut0; dbSNP:rs1554158775
- K621 (= K591) to N: in MMAM; mut0
- G623 (= G593) to R: in MMAM; mut0; dbSNP:rs121918254
- Q624 (= Q594) to R: in MMAM; no effect on protein abundance; dbSNP:rs768521956
- D625 (= D595) to G: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253847; to V: in MMAM; mut0; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity
- G626 (= G596) to C: in MMAM; mut-; dbSNP:rs982110849
- H627 (= H597) binding axial binding residue; to R: in MMAM; mut0; dbSNP:rs372486357
- G630 (= G600) to E: in MMAM; mut0; dbSNP:rs143023066
- V633 (= V603) to 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
- G637 (≠ A607) to E: in MMAM; mut-; to R: in MMAM; mut0; dbSNP:rs781501004
- F638 (≠ Y608) to I: in MMAM; mut0
- D640 (= D610) to Y: in MMAM; mut0; dbSNP:rs865815395
- G642 (= G612) to R: in MMAM; mut-; dbSNP:rs747897332
- G648 (≠ S618) to 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
- V669 (= V639) to E: in MMAM; mut0; dbSNP:rs1360470463
- I671 (≠ A641) to V: in dbSNP:rs8589
- L674 (= L644) to F: in MMAM; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1164271240
- H678 (= H648) to R: in MMAM; mut-; dbSNP:rs147094927
- E684 (= E654) natural variant: E -> EL (in MMAM; mut-)
- L685 (= L655) to R: in MMAM; mut-; dbSNP:rs864309739
- R694 (= R664) to L: in MMAM; mut-; decreased protein abundance; loss of methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability; to 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
- M700 (≠ V670) to 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
- G703 (= G673) to R: in MMAM; mut0; dbSNP:rs121918255
- G717 (= G687) to 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
- G723 (= G693) to D: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity; dbSNP:rs755077681
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
- 7:750 natural variant: Missing (in MMAM; mut-)
- 152:750 natural variant: Missing (in MMAM; mut0)
- 228:750 natural variant: Missing (in MMAM; mut0)
2xiqA Crystal structure of human methylmalonyl-coa mutase in complex with adenosylcobalamin and malonyl-coa (see paper)
59% identity, 99% coverage: 6:711/714 of query aligns to 7:706/714 of 2xiqA
- active site: Y75 (= Y78), Y229 (= Y232), H230 (= H233), K586 (= K591), D590 (= D595), H592 (= H597)
- binding cobalamin: Y75 (= Y78), L105 (= L108), H108 (= H111), A125 (= A128), R193 (= R196), E233 (= E236), G320 (= G322), W321 (= W323), E357 (= E359), G360 (= G362), L361 (= L363), G591 (= G596), H592 (= H597), D593 (= D598), R594 (= R599), G595 (= G600), I599 (= I604), G635 (= G640), S637 (= S642), L639 (= L644), A641 (= A646), G667 (= G672), G668 (= G673), F687 (≠ Y692), G688 (= G693), T691 (= T696)
- binding malonyl-coenzyme a: Y61 (≠ R64), T63 (= T66), M64 (= M67), R68 (≠ Q71), T71 (= T74), R73 (= R76), Y75 (= Y78), S150 (= S153), T152 (= T155), T181 (= T184), R193 (= R196), K220 (≠ R223), H230 (= H233), R269 (= R272), S271 (= S274), F273 (= F276), R313 (= R315), A314 (≠ T316), H315 (= H317), Q317 (= Q319), Q348 (= Q350)
6oxdA Structure of mycobacterium tuberculosis methylmalonyl-coa mutase with adenosyl cobalamin (see paper)
61% identity, 97% coverage: 21:711/714 of query aligns to 39:730/736 of 6oxdA
- active site: Y100 (= Y78), Y254 (= Y232), H255 (= H233), K610 (= K591), D614 (= D595), H616 (= H597)
- binding cobalamin: Y100 (= Y78), L130 (= L108), H133 (= H111), A150 (= A128), R218 (= R196), E258 (= E236), G344 (= G322), W345 (= W323), E381 (= E359), A382 (= A360), A384 (≠ G362), L385 (= L363), G615 (= G596), H616 (= H597), D617 (= D598), R618 (= R599), S661 (= S642), L663 (= L644), A665 (= A646), G691 (= G672), G692 (= G673), F711 (≠ Y692), P712 (≠ G693), T715 (= T696)
- binding Itaconyl coenzyme A: Y86 (≠ R64), T88 (= T66), M89 (= M67), Q93 (= Q71), T96 (= T74), R98 (= R76), Y100 (= Y78), S175 (= S153), T177 (= T155), T206 (= T184), R218 (= R196), H255 (= H233), R294 (= R272), S296 (= S274), F298 (= F276), R337 (= R315), T338 (= T316), H339 (= H317), Q341 (= Q319), Q372 (= Q350)
4reqA Methylmalonyl-coa mutase substrate complex (see paper)
61% identity, 94% coverage: 28:701/714 of query aligns to 37:712/726 of 4reqA
- active site: Y87 (= Y78), Y241 (= Y232), H242 (= H233), K602 (= K591), D606 (= D595), H608 (= H597)
- binding cobalamin: Y87 (= Y78), L117 (= L108), A137 (= A128), V204 (≠ C195), R205 (= R196), H242 (= H233), E245 (= E236), G331 (= G322), W332 (= W323), E368 (= E359), A369 (= A360), A371 (≠ G362), L372 (= L363), G607 (= G596), H608 (= H597), D609 (= D598), R610 (= R599), G611 (= G600), I615 (= I604), S653 (= S642), L655 (= L644), G683 (= G672), G684 (= G673), V685 (= V674), Y703 (= Y692), T704 (≠ G693), T707 (= T696)
- binding methylmalonyl-coenzyme a: Y73 (≠ R64), M76 (= M67), F79 (≠ A70), R80 (≠ Q71), T83 (= T74), R85 (= R76), Y87 (= Y78), S112 (= S103), S162 (= S153), T164 (= T155), T193 (= T184), R205 (= R196), N234 (= N225), Y241 (= Y232), H242 (= H233), R281 (= R272), S283 (= S274), F285 (= F276), H326 (= H317), Q328 (= Q319), Q359 (= Q350), S360 (= S351)
- binding succinyl-coenzyme a: Y73 (≠ R64), M76 (= M67), F79 (≠ A70), R80 (≠ Q71), T83 (= T74), R85 (= R76), Y87 (= Y78), S162 (= S153), T164 (= T155), T193 (= T184), Q195 (= Q186), R205 (= R196), N234 (= N225), Y241 (= Y232), H242 (= H233), R281 (= R272), S283 (= S274), F285 (= F276), R324 (= R315), H326 (= H317), Q359 (= Q350)
P11653 Methylmalonyl-CoA mutase large subunit; MCM-alpha; EC 5.4.99.2 from Propionibacterium freudenreichii subsp. shermanii (see 4 papers)
61% identity, 94% coverage: 28:701/714 of query aligns to 39:714/728 of P11653
- Y75 (≠ R64) binding
- M78 (= M67) binding
- R82 (≠ Q71) binding
- T85 (= T74) binding
- R87 (= R76) binding
- Y89 (= Y78) binding ; mutation to F: Does not significantly affect affinity for succiny-CoA, but kcat is lowered about 580-fold.
- S114 (= S103) binding
- F117 (= F106) binding
- A139 (= A128) binding
- T195 (= T184) binding
- Q197 (= Q186) binding
- V206 (≠ C195) binding
- R207 (= R196) binding ; binding
- H244 (= H233) binding
- R283 (= R272) binding
- S285 (= S274) binding
- G333 (= G322) binding
- E370 (= E359) binding
- A373 (≠ G362) binding
- G609 (= G596) binding
- H610 (= H597) binding axial binding residue
- D611 (= D598) binding
- R612 (= R599) binding
- S655 (= S642) binding
- L657 (= L644) binding
- G686 (= G673) binding
- T709 (= T696) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
7reqA Methylmalonyl-coa mutase, 2-carboxypropyl-coa inhibitor complex (see paper)
61% identity, 94% coverage: 28:701/714 of query aligns to 36:711/725 of 7reqA
- active site: Y86 (= Y78), Y240 (= Y232), H241 (= H233), K601 (= K591), D605 (= D595), H607 (= H597)
- binding 2-carboxypropyl-coenzyme a: Y72 (≠ R64), T74 (= T66), M75 (= M67), F78 (≠ A70), R79 (≠ Q71), T82 (= T74), R84 (= R76), Y86 (= Y78), S161 (= S153), T163 (= T155), T192 (= T184), R204 (= R196), H241 (= H233), R280 (= R272), S282 (= S274), F284 (= F276), H325 (= H317), Q358 (= Q350)
- binding cobalamin: Y86 (= Y78), L116 (= L108), A136 (= A128), R204 (= R196), E244 (= E236), G330 (= G322), W331 (= W323), E367 (= E359), A368 (= A360), A370 (≠ G362), G606 (= G596), H607 (= H597), D608 (= D598), R609 (= R599), G610 (= G600), I614 (= I604), S652 (= S642), L654 (= L644), G682 (= G672), G683 (= G673), Y702 (= Y692), T703 (≠ G693), T706 (= T696)
3reqA Methylmalonyl-coa mutase, substrate-free state (poor quality structure) (see paper)
61% identity, 94% coverage: 28:701/714 of query aligns to 36:711/725 of 3reqA
- active site: Y86 (= Y78), Y240 (= Y232), H241 (= H233), K601 (= K591), D605 (= D595), H607 (= H597)
- binding adenosine: Y86 (= Y78), Y240 (= Y232), E244 (= E236), G330 (= G322)
- binding cobalamin: L116 (= L108), V203 (≠ C195), R204 (= R196), E244 (= E236), G330 (= G322), W331 (= W323), A368 (= A360), G606 (= G596), H607 (= H597), D608 (= D598), R609 (= R599), G610 (= G600), I614 (= I604), G650 (= G640), S652 (= S642), L654 (= L644), G682 (= G672), G683 (= G673), Y702 (= Y692), T703 (≠ G693), P704 (= P694), T706 (= T696)
2reqA Methylmalonyl-coa mutase, non-productive coa complex, in open conformation representing substrate-free state (see paper)
61% identity, 94% coverage: 28:701/714 of query aligns to 36:711/725 of 2reqA
- active site: Y86 (= Y78), Y240 (= Y232), H241 (= H233), K601 (= K591), D605 (= D595), H607 (= H597)
- binding cobalamin: V203 (≠ C195), R204 (= R196), E244 (= E236), A245 (= A237), W331 (= W323), A368 (= A360), G606 (= G596), H607 (= H597), D608 (= D598), R609 (= R599), G610 (= G600), I614 (= I604), G650 (= G640), S652 (= S642), L654 (= L644), A655 (= A645), G682 (= G672), G683 (= G673), Y702 (= Y692), T703 (≠ G693), T706 (= T696)
- binding coenzyme a: Y72 (≠ R64), R79 (≠ Q71), K318 (= K310)
6reqA Methylmalonyl-coa mutase, 3-carboxypropyl-coa inhibitor complex (see paper)
61% identity, 94% coverage: 28:701/714 of query aligns to 38:713/727 of 6reqA
- active site: Y88 (= Y78), Y242 (= Y232), H243 (= H233), K603 (= K591), D607 (= D595), H609 (= H597)
- binding 3-carboxypropyl-coenzyme a: Y74 (≠ R64), T76 (= T66), M77 (= M67), F80 (≠ A70), R81 (≠ Q71), T84 (= T74), R86 (= R76), Y88 (= Y78), S113 (= S103), S163 (= S153), T165 (= T155), T194 (= T184), R206 (= R196), H243 (= H233), R282 (= R272), S284 (= S274), F286 (= F276), H327 (= H317), Q329 (= Q319), Q360 (= Q350)
- binding cobalamin: Y88 (= Y78), F116 (= F106), L118 (= L108), H121 (= H111), A138 (= A128), R206 (= R196), E246 (= E236), G332 (= G322), W333 (= W323), E369 (= E359), A370 (= A360), A372 (≠ G362), G608 (= G596), H609 (= H597), D610 (= D598), R611 (= R599), G612 (= G600), I616 (= I604), Y620 (= Y608), S654 (= S642), L656 (= L644), G658 (≠ A646), G684 (= G672), G685 (= G673), Y704 (= Y692), T705 (≠ G693), T708 (= T696)
5reqA Methylmalonyl-coa mutase, y89f mutant, substrate complex (see paper)
61% identity, 94% coverage: 28:701/714 of query aligns to 36:711/725 of 5reqA
- active site: F86 (≠ Y78), Y240 (= Y232), H241 (= H233), K601 (= K591), D605 (= D595), H607 (= H597)
- binding cobalamin: L116 (= L108), A136 (= A128), R204 (= R196), H241 (= H233), E244 (= E236), G330 (= G322), W331 (= W323), E367 (= E359), A368 (= A360), A370 (≠ G362), G606 (= G596), H607 (= H597), D608 (= D598), R609 (= R599), G610 (= G600), I614 (= I604), S652 (= S642), L654 (= L644), G682 (= G672), G683 (= G673), V684 (= V674), Y702 (= Y692), T703 (≠ G693), T706 (= T696)
- binding methylmalonyl(carbadethia)-coenzyme a: Y72 (≠ R64), T74 (= T66), M75 (= M67), R79 (≠ Q71), T82 (= T74), R84 (= R76), F86 (≠ Y78), S111 (= S103), S161 (= S153), T163 (= T155), T192 (= T184), Q194 (= Q186), R204 (= R196), N233 (= N225), H241 (= H233), R280 (= R272), S282 (= S274), F284 (= F276), T324 (= T316), H325 (= H317), Q358 (= Q350), S359 (= S351)
- binding succinyl(carbadethia)-coenzyme a: Y72 (≠ R64), T74 (= T66), M75 (= M67), R79 (≠ Q71), T82 (= T74), R84 (= R76), F86 (≠ Y78), S161 (= S153), T163 (= T155), T192 (= T184), R204 (= R196), N233 (= N225), H241 (= H233), R280 (= R272), S282 (= S274), F284 (= F276), H325 (= H317), Q358 (= Q350)
1e1cA Methylmalonyl-coa mutase h244a mutant (see paper)
61% identity, 94% coverage: 28:701/714 of query aligns to 38:713/727 of 1e1cA
- active site: Y88 (= Y78), Y242 (= Y232), A243 (≠ H233), K603 (= K591), D607 (= D595), H609 (= H597)
- binding cobalamin: Y88 (= Y78), L118 (= L108), H121 (= H111), A138 (= A128), V205 (≠ C195), R206 (= R196), E246 (= E236), G332 (= G322), W333 (= W323), E369 (= E359), A370 (= A360), A372 (≠ G362), L373 (= L363), G608 (= G596), H609 (= H597), D610 (= D598), R611 (= R599), G612 (= G600), I616 (= I604), Y620 (= Y608), S654 (= S642), L656 (= L644), G684 (= G672), G685 (= G673), V686 (= V674), Y704 (= Y692), T705 (≠ G693), T708 (= T696), S713 (= S701)
- binding desulfo-coenzyme a: Y74 (≠ R64), M77 (= M67), F80 (≠ A70), R81 (≠ Q71), T84 (= T74), R86 (= R76), S113 (= S103), S163 (= S153), T165 (= T155), T194 (= T184), R282 (= R272), S284 (= S274), H327 (= H317), Q360 (= Q350)
8gjuJ Crystal structure of human methylmalonyl-coa mutase (mmut) in complex with methylmalonic acidemia type a protein (mmaa), coenzyme a, and gdp (see paper)
58% identity, 99% coverage: 6:711/714 of query aligns to 7:683/689 of 8gjuJ
- binding coenzyme a: Y61 (≠ R64), T63 (= T66), R68 (≠ Q71), T71 (= T74), R73 (= R76), S150 (= S153), T152 (= T155), T181 (= T184), Q183 (= Q186), N222 (= N225), R269 (= R272), S271 (= S274), R313 (= R315), A314 (≠ T316), H315 (= H317), Q348 (= Q350)
4r3uA Crystal structure of 2-hydroxyisobutyryl-coa mutase (see paper)
42% identity, 71% coverage: 35:542/714 of query aligns to 45:555/557 of 4r3uA
- active site: I89 (≠ Y78), Y243 (= Y232), H244 (= H233)
- binding 3-hydroxybutanoyl-coenzyme a: Y75 (≠ R64), T77 (= T66), M78 (= M67), R82 (≠ Q71), T85 (= T74), R87 (= R76), I89 (≠ Y78), D116 (≠ A105), S164 (= S153), T166 (= T155), T195 (= T184), Q197 (= Q186), R234 (= R223), N236 (= N225), N239 (≠ S228), Y243 (= Y232), H244 (= H233), R283 (= R272), F287 (= F276), R327 (= R315), F328 (≠ T316), H329 (= H317), Q331 (= Q319), Q362 (= Q350)
- 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 (≠ R64), T77 (= T66), M78 (= M67), R82 (≠ Q71), T85 (= T74), R87 (= R76), I89 (≠ Y78), D116 (≠ A105), S164 (= S153), T166 (= T155), T195 (= T184), Q197 (= Q186), R234 (= R223), N236 (= N225), N239 (≠ S228), H244 (= H233), R283 (= R272), F287 (= F276), R327 (= R315), F328 (≠ T316), H329 (= H317), Q331 (= Q319), Q362 (= Q350)
- binding cobalamin: D116 (≠ A105), M119 (≠ L108), E139 (≠ A128), Q207 (≠ R196), E209 (≠ T198), E247 (= E236), A334 (≠ G322), E371 (= E359), A372 (= A360), A374 (≠ G362)
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)
42% identity, 71% coverage: 35:542/714 of query aligns to 46:556/562 of I3VE77
- YPTM 76:79 (≠ RATM 64:67) binding
- TMR 86:88 (≠ TIR 74:76) binding
- I90 (≠ Y78) 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 (≠ A105) 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 (≠ TIQ 184:186) binding
- R235 (= R223) binding
- N240 (≠ S228) binding
- H245 (= H233) binding
- R284 (= R272) binding
5cjvA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isovaleryl-coenzyme a (see paper)
37% identity, 68% coverage: 52:535/714 of query aligns to 544:1050/1061 of 5cjvA
- active site: F569 (≠ Y78), Y750 (= Y232), H751 (= H233)
- binding cobalamin: F598 (= F106), L603 (≠ H111), S621 (≠ A128), Q713 (≠ R196), E754 (= E236), A755 (= A237), G839 (= G322), R840 (≠ W323), E876 (= E359), A877 (= A360), T879 (≠ G362), H964 (≠ D447)
- binding guanosine-5'-diphosphate: E944 (= E427)
- binding Isovaleryl-coenzyme A: F556 (≠ R64), F558 (≠ T66), R560 (≠ Y68), R567 (= R76), F569 (≠ Y78), R593 (≠ G101), S648 (= S153), T650 (= T155), R699 (≠ T182), T701 (= T184), Q703 (= Q186), Q713 (≠ R196), Y743 (≠ N225), H751 (= H233), S792 (= S274), F794 (= F276), K832 (≠ R315), H834 (= H317)
Sites not aligning to the query:
- active site: 6
- binding cobalamin: 18, 19, 20, 21, 22, 26, 66, 67, 94, 96, 98, 116, 117, 129
- binding guanosine-5'-diphosphate: 199, 201, 202, 203, 204, 245, 336, 338, 373, 375
- binding magnesium ion: 203, 229, 242, 242, 288, 288
5cjwA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate pivalyl-coenzyme a (see paper)
37% identity, 68% coverage: 52:535/714 of query aligns to 546:1052/1063 of 5cjwA
- active site: F571 (≠ Y78), Y752 (= Y232), H753 (= H233)
- binding pivalyl-coenzyme A: F558 (≠ R64), F560 (≠ T66), R562 (≠ Y68), R569 (= R76), F571 (≠ Y78), R595 (≠ G101), S650 (= S153), T652 (= T155), R701 (≠ T182), T703 (= T184), Q705 (= Q186), Y745 (≠ N225), Y752 (= Y232), H753 (= H233), S794 (= S274), F796 (= F276), R829 (≠ K310), K834 (≠ R315), H836 (= H317)
- binding cobalamin: F600 (= F106), L605 (≠ H111), S623 (≠ A128), Q715 (≠ R196), H753 (= H233), E756 (= E236), A757 (= A237), G841 (= G322), R842 (≠ W323), E878 (= E359), A879 (= A360), T881 (≠ G362), H966 (≠ D447)
Sites not aligning to the query:
- active site: 6
- binding cobalamin: 18, 19, 20, 21, 22, 26, 66, 67, 94, 96, 98, 116, 117, 118
- binding guanosine-5'-diphosphate: 199, 201, 202, 203, 204, 245, 337, 338, 340, 375, 377, 1062
- binding magnesium ion: 203, 229, 242, 242, 290, 290
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)
36% identity, 73% coverage: 18:535/714 of query aligns to 533:1082/1093 of Q1LRY0
- F587 (≠ T66) binding
- F598 (≠ Y78) 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 (≠ G101) binding
- R728 (≠ T182) binding
- Y772 (≠ N225) binding
- S821 (= S274) binding
- R856 (≠ K310) binding
- K861 (≠ R315) binding
- E973 (= E427) binding
Sites not aligning to the query:
- 39 binding axial binding residue
- 169:417 GTPase chaperone MeaI
- 219:224 binding
- 223 binding
- 248 binding
- 249 binding
- 262 binding ; binding
- 265 binding
- 310 binding ; binding
- 311 binding
- 357:360 binding
- 418:579 Linker
- 1092 binding
4xc6A Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, and mg (holo-icmf/gdp) (see paper)
37% identity, 68% coverage: 52:535/714 of query aligns to 547:1056/1067 of 4xc6A
- active site: F572 (≠ Y78), Y753 (= Y232), H754 (= H233)
- binding cobalamin: F601 (= F106), L606 (≠ H111), S624 (≠ A128), Q716 (≠ R196), H754 (= H233), E757 (= E236), A758 (= A237), G842 (= G322), R843 (≠ W323), E879 (= E359), A880 (= A360), T882 (≠ G362), H967 (≠ D447)
- binding guanosine-5'-diphosphate: E947 (= E427)
Sites not aligning to the query:
- active site: 6
- binding cobalamin: 18, 19, 20, 21, 22, 26, 66, 67, 94, 96, 98, 116, 117, 118, 129
- binding guanosine-5'-diphosphate: 199, 201, 202, 203, 204, 245, 337, 338, 340, 375, 377
- binding magnesium ion: 203, 229, 242, 242, 290, 290
5cjtA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isobutyryl-coenzyme a (see paper)
36% identity, 74% coverage: 7:535/714 of query aligns to 495:1051/1062 of 5cjtA
- active site: F569 (≠ Y78), Y750 (= Y232), H751 (= H233)
- binding cobalamin: F598 (= F106), L603 (≠ H111), S621 (≠ A128), Q713 (≠ R196), H751 (= H233), E754 (= E236), A755 (= A237), G839 (= G322), R840 (≠ W323), E876 (= E359), A877 (= A360), T879 (≠ G362), H964 (≠ D447)
- binding isobutyryl-coenzyme a: F556 (≠ R64), F558 (≠ T66), R560 (≠ Y68), R567 (= R76), F569 (≠ Y78), R593 (≠ G101), S648 (= S153), T650 (= T155), R699 (≠ T182), T701 (= T184), Q703 (= Q186), Y743 (≠ N225), Y750 (= Y232), H751 (= H233), S792 (= S274), F794 (= F276), R827 (≠ K310), K832 (≠ R315), H834 (= H317)
- binding guanosine-5'-diphosphate: E944 (= E427)
Sites not aligning to the query:
- active site: 6
- binding cobalamin: 18, 19, 20, 21, 22, 26, 66, 67, 94, 96, 98, 116, 117
- binding guanosine-5'-diphosphate: 199, 201, 202, 203, 204, 245, 336, 337, 339, 374, 376
- binding magnesium ion: 203, 229, 242, 242, 289, 289
Query Sequence
>16996 FitnessBrowser__Keio:16996
MSNVQEWQQLANKELSRREKTVDSLVHQTAEGIAIKPLYTEADLDNLEVTGTLPGLPPYV
RGPRATMYTAQPWTIRQYAGFSTAKESNAFYRRNLAAGQKGLSVAFDLATHRGYDSDNPR
VAGDVGKAGVAIDTVEDMKVLFDQIPLDKMSVSMTMNGAVLPVLAFYIVAAEEQGVTPDK
LTGTIQNDILKEYLCRNTYIYPPKPSMRIIADIIAWCSGNMPRFNTISISGYHMGEAGAN
CVQQVAFTLADGIEYIKAAISAGLKIDDFAPRLSFFFGIGMDLFMNVAMLRAARYLWSEA
VSGFGAQDPKSLALRTHCQTSGWSLTEQDPYNNVIRTTIEALAATLGGTQSLHTNAFDEA
LGLPTDFSARIARNTQIIIQEESELCRTVDPLAGSYYIESLTDQIVKQARAIIQQIDEAG
GMAKAIEAGLPKRMIEEASAREQSLIDQGKRVIVGVNKYKLDHEDETDVLEIDNVMVRNE
QIASLERIRATRDDAAVTAALNALTHAAQHNENLLAAAVNAARVRATLGEISDALEVAFD
RYLVPSQCVTGVIAQSYHQSEKSASEFDAIVAQTEQFLADNGRRPRILIAKMGQDGHDRG
AKVIASAYSDLGFDVDLSPMFSTPEEIARLAVENDVHVVGASSLAAGHKTLIPELVEALK
KWGREDICVVAGGVIPPQDYAFLQERGVAAIYGPGTPMLDSVRDVLNLISQHHD
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