SitesBLAST
Comparing Ga0059261_3988 FitnessBrowser__Korea:Ga0059261_3988 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)
P22033 Methylmalonyl-CoA mutase, mitochondrial; MCM; Methylmalonyl-CoA isomerase; EC 5.4.99.2 from Homo sapiens (Human) (see 28 papers)
62% identity, 97% coverage: 4:697/712 of query aligns to 37:736/750 of P22033
- Q50 (≠ E17) binding
- I69 (≠ V33) to V: in MMAM; likely benign; dbSNP:rs115923556
- P86 (= P49) 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 (= G50) to E: in MMAM; mut0; dbSNP:rs1554160986
- R93 (= R56) to H: in MMAM; mut0; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918251
- G94 (= G57) to R: in MMAM; mut0; dbSNP:rs727504022; to V: in MMAM; mut- and mut0; dbSNP:rs535411418
- P95 (≠ V58) to R: in MMAM; mut0; dbSNP:rs190834116
- YPTM 96:99 (≠ RGSM 59:62) binding
- Y100 (= Y63) 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 (= W68) to R: in MMAM; mut0; dbSNP:rs121918249
- TIRQY 106:110 (= TIRQY 69:73) binding
- R108 (= R71) to C: in MMAM; mut0; dbSNP:rs121918257; to G: in MMAM; mut-; to H: in MMAM; mut0; dbSNP:rs483352778
- Q109 (= Q72) to R: in MMAM; mut0; dbSNP:rs1461110052
- G133 (= G96) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253828
- A137 (= A100) to V: in MMAM; mut0; dbSNP:rs941483851
- D139 (= D102) to N: in MMAM; uncertain significance; dbSNP:rs879253829
- L140 (= L103) to P: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- A141 (= A104) to T: in MMAM; decreased protein expression; dbSNP:rs1554160730
- H143 (= H106) to Y: in MMAM; mut0
- G145 (= G108) to S: in MMAM; mut0
- S148 (= S111) to L: in MMAM; mut0; dbSNP:rs1300547552
- D156 (= D119) to N: in MMAM; mut-
- G158 (= G121) to V: in MMAM; mut0
- G161 (= G124) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; to V: in MMAM; decreased protein expression
- F174 (= F137) to S: in MMAM; mut0; dbSNP:rs864309733
- M186 (= M149) to V: in MMAM; mut-; dbSNP:rs148331800
- T187 (= T150) to S: in MMAM; mut0; dbSNP:rs879253830
- N189 (= N152) to I: in MMAM; mut-; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs200908035; to K: in MMAM; mut-; dbSNP:rs1561959114
- A191 (= A154) to E: in MMAM; mut- and mut0; affects proper folding; reduced protein level; decreased methylmalonyl-CoA mutase activity; dbSNP:rs760782399
- A197 (= A160) to E: in MMAM; mut0
- G203 (= G166) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs778702777
- E205 (= E168) natural variant: Missing (in MMAM; mut0; dbSNP:rs879253831)
- G215 (= G178) to C: in MMAM; mut- and mut0; dbSNP:rs121918258; to S: in MMAM; mut0; dbSNP:rs121918258
- TIQ 216:218 (= TIQ 179:181) binding
- Q218 (= Q181) to H: in MMAM; mut0 and mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability; dbSNP:rs1446389693
- N219 (= N182) to Y: in MMAM; mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; dbSNP:rs121918256
- R228 (= R191) binding ; to Q: in MMAM; mut0; dbSNP:rs770810987
- T230 (= T193) to I: in MMAM; mut-; to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253833
- Y231 (= Y194) 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 (= K218) binding
- S262 (= S225) to N: in MMAM; mut0
- H265 (= H228) binding ; to Y: in MMAM; mut-
- E276 (= E239) to D: in MMAM; uncertain significance; mut-; dbSNP:rs12175488
- L281 (≠ I244) to S: in MMAM; mut0; dbSNP:rs796052007
- G284 (= G247) to E: in MMAM; mut0; dbSNP:rs879253835; to R: in MMAM; mut0; dbSNP:rs761477436
- S288 (≠ V251) to P: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1179778233
- G291 (= G254) to E: in MMAM; mut0
- Q293 (≠ A256) to P: in MMAM; mut0
- RLS 304:306 (= RLS 267:269) binding
- L305 (= L268) to S: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554160246
- S306 (= S269) to F: in MMAM; mut0; dbSNP:rs1085307929
- W309 (≠ F272) to G: in MMAM; decreased protein expression
- G312 (= G275) to V: in MMAM; mut0; dbSNP:rs864309734
- Y316 (≠ F279) 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 (= A287) to T: in MMAM; mut-; dbSNP:rs780387525
- R326 (= R289) to K: in MMAM; uncertain significance; dbSNP:rs758577372
- L328 (= L291) 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 (= S306) 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 (≠ M308) natural variant: Missing (in MMAM; mut0)
- L347 (= L309) to R: in MMAM; mut0; dbSNP:rs1026703654
- H350 (= H312) to Y: in MMAM; mut0; dbSNP:rs1407914109
- L358 (= L320) to P: in MMAM; mut0
- N366 (= N328) 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 (= R331) 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 (= T332) to P: in MMAM; mut0; dbSNP:rs368790885
- A377 (= A339) to E: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918250
- Q383 (= Q345) to H: in MMAM; mut0; to P: in MMAM; mut0
- H386 (= H348) to N: in MMAM; mut0; dbSNP:rs1554159937; to R: in MMAM; mut0; dbSNP:rs866933356
- T387 (= T349) 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 (= N350) to H: in MMAM; mut0; dbSNP:rs766010704; to K: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253840
- S389 (≠ A351) natural variant: Missing (in MMAM; mut0)
- I412 (= I374) natural variant: Missing (in MMAM; mut0)
- P424 (= P386) to L: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253842
- G426 (= G388) 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 (= G389) to D: in MMAM; mut0; dbSNP:rs753288303
- G454 (= G416) to E: in MMAM; mut0
- A499 (≠ P461) to T: in dbSNP:rs2229385
- I505 (≠ V467) to T: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- Q514 (= Q476) to E: in MMAM; uncertain significance; to K: in MMAM; decreased protein expression
- L518 (≠ I480) to P: in MMAM; mut0; dbSNP:rs864309738
- R532 (≠ A494) to H: in dbSNP:rs1141321
- A535 (≠ D497) to P: in MMAM; mut0; dbSNP:rs760183775
- A552 (= A513) to V: in MMAM; uncertain significance; dbSNP:rs879253845
- C560 (≠ A521) to Y: in MMAM; mut0; dbSNP:rs1238333040
- T566 (≠ S527) to R: in MMAM; mut0
- F573 (= F534) 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 (= Y548) to C: in MMAM; mut-
- I597 (≠ W558) to R: in MMAM; no changed in protein expression; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554158951
- P615 (= P576) 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 (= R577) to C: in MMAM; mut0; dbSNP:rs765284825
- L617 (≠ M578) to R: in MMAM; mut0; dbSNP:rs1554158775
- K621 (= K582) to N: in MMAM; mut0
- G623 (= G584) to R: in MMAM; mut0; dbSNP:rs121918254
- Q624 (= Q585) to R: in MMAM; no effect on protein abundance; dbSNP:rs768521956
- D625 (= D586) 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 (= G587) to C: in MMAM; mut-; dbSNP:rs982110849
- H627 (= H588) binding axial binding residue; to R: in MMAM; mut0; dbSNP:rs372486357
- G630 (= G591) to E: in MMAM; mut0; dbSNP:rs143023066
- V633 (≠ L594) 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 (≠ A598) to E: in MMAM; mut-; to R: in MMAM; mut0; dbSNP:rs781501004
- F638 (= F599) to I: in MMAM; mut0
- D640 (= D601) to Y: in MMAM; mut0; dbSNP:rs865815395
- G642 (= G603) to R: in MMAM; mut-; dbSNP:rs747897332
- G648 (= G609) 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 (= V630) to E: in MMAM; mut0; dbSNP:rs1360470463
- I671 (≠ A632) to V: in dbSNP:rs8589
- L674 (= L635) to F: in MMAM; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1164271240
- H678 (= H639) to R: in MMAM; mut-; dbSNP:rs147094927
- E684 (≠ Q645) natural variant: E -> EL (in MMAM; mut-)
- L685 (≠ M646) to R: in MMAM; mut-; dbSNP:rs864309739
- R694 (= R655) 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 (≠ I661) 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 (= G664) to R: in MMAM; mut0; dbSNP:rs121918255
- G717 (= G678) 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 (= G684) 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)
8dyjB Crystal structure of human methylmalonyl-coa mutase in complex with adp and cob(ii)alamin (see paper)
62% identity, 97% coverage: 4:697/712 of query aligns to 1:700/708 of 8dyjB
- binding adenosine-5'-diphosphate: Y74 (= Y73), T151 (= T150), R192 (= R191), Y228 (= Y227), H229 (= H228), F272 (= F271), Q316 (= Q314), N352 (= N350), E356 (= E354), L360 (= L358), P361 (= P359)
- binding cobalamin: F102 (= F101), L104 (= L103), H107 (= H106), A124 (= A123), V191 (= V190), R192 (= R191), H229 (= H228), E232 (= E231), G319 (= G317), W320 (≠ V318), E356 (= E354), G359 (≠ A357), L360 (= L358), G590 (= G587), H591 (= H588), D592 (= D589), R593 (= R590), G594 (= G591), I598 (≠ V595), S636 (= S633), L638 (= L635), A640 (= A637), G666 (= G663), G667 (= G664), V668 (= V665), F686 (= F683), G687 (= G684), T690 (= T687)
2xiqA Crystal structure of human methylmalonyl-coa mutase in complex with adenosylcobalamin and malonyl-coa (see paper)
62% identity, 97% coverage: 4:697/712 of query aligns to 2:701/714 of 2xiqA
- active site: Y75 (= Y73), Y229 (= Y227), H230 (= H228), K586 (= K582), D590 (= D586), H592 (= H588)
- binding cobalamin: Y75 (= Y73), L105 (= L103), H108 (= H106), A125 (= A123), R193 (= R191), E233 (= E231), G320 (= G317), W321 (≠ V318), E357 (= E354), G360 (≠ A357), L361 (= L358), G591 (= G587), H592 (= H588), D593 (= D589), R594 (= R590), G595 (= G591), I599 (≠ V595), G635 (= G631), S637 (= S633), L639 (= L635), A641 (= A637), G667 (= G663), G668 (= G664), F687 (= F683), G688 (= G684), T691 (= T687)
- binding malonyl-coenzyme a: Y61 (≠ R59), T63 (≠ S61), M64 (= M62), R68 (= R66), T71 (= T69), R73 (= R71), Y75 (= Y73), S150 (= S148), T152 (= T150), T181 (= T179), R193 (= R191), K220 (= K218), H230 (= H228), R269 (= R267), S271 (= S269), F273 (= F271), R313 (= R310), A314 (≠ T311), H315 (= H312), Q317 (= Q314), Q348 (= Q345)
8gjuJ Crystal structure of human methylmalonyl-coa mutase (mmut) in complex with methylmalonic acidemia type a protein (mmaa), coenzyme a, and gdp (see paper)
60% identity, 97% coverage: 4:697/712 of query aligns to 2:678/689 of 8gjuJ
- binding coenzyme a: Y61 (≠ R59), T63 (≠ S61), R68 (= R66), T71 (= T69), R73 (= R71), S150 (= S148), T152 (= T150), T181 (= T179), Q183 (= Q181), N222 (= N220), R269 (= R267), S271 (= S269), R313 (= R310), A314 (≠ T311), H315 (= H312), Q348 (= Q345)
6oxdA Structure of mycobacterium tuberculosis methylmalonyl-coa mutase with adenosyl cobalamin (see paper)
60% identity, 96% coverage: 23:704/712 of query aligns to 43:732/736 of 6oxdA
- active site: Y100 (= Y73), Y254 (= Y227), H255 (= H228), K610 (= K582), D614 (= D586), H616 (= H588)
- binding cobalamin: Y100 (= Y73), L130 (= L103), H133 (= H106), A150 (= A123), R218 (= R191), E258 (= E231), G344 (= G317), W345 (≠ V318), E381 (= E354), A382 (= A355), A384 (= A357), L385 (= L358), G615 (= G587), H616 (= H588), D617 (= D589), R618 (= R590), S661 (= S633), L663 (= L635), A665 (= A637), G691 (= G663), G692 (= G664), F711 (= F683), P712 (≠ G684), T715 (= T687)
- binding Itaconyl coenzyme A: Y86 (≠ R59), T88 (≠ S61), M89 (= M62), Q93 (≠ R66), T96 (= T69), R98 (= R71), Y100 (= Y73), S175 (= S148), T177 (= T150), T206 (= T179), R218 (= R191), H255 (= H228), R294 (= R267), S296 (= S269), F298 (= F271), R337 (= R310), T338 (= T311), H339 (= H312), Q341 (= Q314), Q372 (= Q345)
4reqA Methylmalonyl-coa mutase substrate complex (see paper)
59% identity, 96% coverage: 25:704/712 of query aligns to 36:724/726 of 4reqA
- active site: Y87 (= Y73), Y241 (= Y227), H242 (= H228), K602 (= K582), D606 (= D586), H608 (= H588)
- binding cobalamin: Y87 (= Y73), L117 (= L103), A137 (= A123), V204 (= V190), R205 (= R191), H242 (= H228), E245 (= E231), G331 (= G317), W332 (≠ V318), E368 (= E354), A369 (= A355), A371 (= A357), L372 (= L358), G607 (= G587), H608 (= H588), D609 (= D589), R610 (= R590), G611 (= G591), I615 (≠ V595), S653 (= S633), L655 (= L635), G683 (= G663), G684 (= G664), V685 (= V665), Y703 (≠ F683), T704 (≠ G684), T707 (= T687)
- binding methylmalonyl-coenzyme a: Y73 (≠ R59), M76 (= M62), F79 (≠ G65), R80 (= R66), T83 (= T69), R85 (= R71), Y87 (= Y73), S112 (= S98), S162 (= S148), T164 (= T150), T193 (= T179), R205 (= R191), N234 (= N220), Y241 (= Y227), H242 (= H228), R281 (= R267), S283 (= S269), F285 (= F271), H326 (= H312), Q328 (= Q314), Q359 (= Q345), S360 (= S346)
- binding succinyl-coenzyme a: Y73 (≠ R59), M76 (= M62), F79 (≠ G65), R80 (= R66), T83 (= T69), R85 (= R71), Y87 (= Y73), S162 (= S148), T164 (= T150), T193 (= T179), Q195 (= Q181), R205 (= R191), N234 (= N220), Y241 (= Y227), H242 (= H228), R281 (= R267), S283 (= S269), F285 (= F271), R324 (= R310), H326 (= H312), Q359 (= Q345)
6reqA Methylmalonyl-coa mutase, 3-carboxypropyl-coa inhibitor complex (see paper)
59% identity, 96% coverage: 25:704/712 of query aligns to 37:725/727 of 6reqA
- active site: Y88 (= Y73), Y242 (= Y227), H243 (= H228), K603 (= K582), D607 (= D586), H609 (= H588)
- binding 3-carboxypropyl-coenzyme a: Y74 (≠ R59), T76 (≠ S61), M77 (= M62), F80 (≠ G65), R81 (= R66), T84 (= T69), R86 (= R71), Y88 (= Y73), S113 (= S98), S163 (= S148), T165 (= T150), T194 (= T179), R206 (= R191), H243 (= H228), R282 (= R267), S284 (= S269), F286 (= F271), H327 (= H312), Q329 (= Q314), Q360 (= Q345)
- binding cobalamin: Y88 (= Y73), F116 (= F101), L118 (= L103), H121 (= H106), A138 (= A123), R206 (= R191), E246 (= E231), G332 (= G317), W333 (≠ V318), E369 (= E354), A370 (= A355), A372 (= A357), G608 (= G587), H609 (= H588), D610 (= D589), R611 (= R590), G612 (= G591), I616 (≠ V595), Y620 (≠ F599), S654 (= S633), L656 (= L635), G658 (≠ A637), G684 (= G663), G685 (= G664), Y704 (≠ F683), T705 (≠ G684), T708 (= T687)
7reqA Methylmalonyl-coa mutase, 2-carboxypropyl-coa inhibitor complex (see paper)
59% identity, 96% coverage: 25:704/712 of query aligns to 35:723/725 of 7reqA
- active site: Y86 (= Y73), Y240 (= Y227), H241 (= H228), K601 (= K582), D605 (= D586), H607 (= H588)
- binding 2-carboxypropyl-coenzyme a: Y72 (≠ R59), T74 (≠ S61), M75 (= M62), F78 (≠ G65), R79 (= R66), T82 (= T69), R84 (= R71), Y86 (= Y73), S161 (= S148), T163 (= T150), T192 (= T179), R204 (= R191), H241 (= H228), R280 (= R267), S282 (= S269), F284 (= F271), H325 (= H312), Q358 (= Q345)
- binding cobalamin: Y86 (= Y73), L116 (= L103), A136 (= A123), R204 (= R191), E244 (= E231), G330 (= G317), W331 (≠ V318), E367 (= E354), A368 (= A355), A370 (= A357), G606 (= G587), H607 (= H588), D608 (= D589), R609 (= R590), G610 (= G591), I614 (≠ V595), S652 (= S633), L654 (= L635), G682 (= G663), G683 (= G664), Y702 (≠ F683), T703 (≠ G684), T706 (= T687)
3reqA Methylmalonyl-coa mutase, substrate-free state (poor quality structure) (see paper)
59% identity, 96% coverage: 25:704/712 of query aligns to 35:723/725 of 3reqA
- active site: Y86 (= Y73), Y240 (= Y227), H241 (= H228), K601 (= K582), D605 (= D586), H607 (= H588)
- binding adenosine: Y86 (= Y73), Y240 (= Y227), E244 (= E231), G330 (= G317)
- binding cobalamin: L116 (= L103), V203 (= V190), R204 (= R191), E244 (= E231), G330 (= G317), W331 (≠ V318), A368 (= A355), G606 (= G587), H607 (= H588), D608 (= D589), R609 (= R590), G610 (= G591), I614 (≠ V595), G650 (= G631), S652 (= S633), L654 (= L635), G682 (= G663), G683 (= G664), Y702 (≠ F683), T703 (≠ G684), P704 (= P685), T706 (= T687)
2reqA Methylmalonyl-coa mutase, non-productive coa complex, in open conformation representing substrate-free state (see paper)
59% identity, 96% coverage: 25:704/712 of query aligns to 35:723/725 of 2reqA
- active site: Y86 (= Y73), Y240 (= Y227), H241 (= H228), K601 (= K582), D605 (= D586), H607 (= H588)
- binding cobalamin: V203 (= V190), R204 (= R191), E244 (= E231), A245 (= A232), W331 (≠ V318), A368 (= A355), G606 (= G587), H607 (= H588), D608 (= D589), R609 (= R590), G610 (= G591), I614 (≠ V595), G650 (= G631), S652 (= S633), L654 (= L635), A655 (= A636), G682 (= G663), G683 (= G664), Y702 (≠ F683), T703 (≠ G684), T706 (= T687)
- binding coenzyme a: Y72 (≠ R59), R79 (= R66), K318 (≠ R305)
P11653 Methylmalonyl-CoA mutase large subunit; MCM-alpha; EC 5.4.99.2 from Propionibacterium freudenreichii subsp. shermanii (see 4 papers)
59% identity, 96% coverage: 25:704/712 of query aligns to 38:726/728 of P11653
- Y75 (≠ R59) binding
- M78 (= M62) binding
- R82 (= R66) binding
- T85 (= T69) binding
- R87 (= R71) binding
- Y89 (= Y73) binding ; mutation to F: Does not significantly affect affinity for succiny-CoA, but kcat is lowered about 580-fold.
- S114 (= S98) binding
- F117 (= F101) binding
- A139 (= A123) binding
- T195 (= T179) binding
- Q197 (= Q181) binding
- V206 (= V190) binding
- R207 (= R191) binding ; binding
- H244 (= H228) binding
- R283 (= R267) binding
- S285 (= S269) binding
- G333 (= G317) binding
- E370 (= E354) binding
- A373 (= A357) binding
- G609 (= G587) binding
- H610 (= H588) binding axial binding residue
- D611 (= D589) binding
- R612 (= R590) binding
- S655 (= S633) binding
- L657 (= L635) binding
- G686 (= G664) binding
- T709 (= T687) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
5reqA Methylmalonyl-coa mutase, y89f mutant, substrate complex (see paper)
59% identity, 96% coverage: 25:704/712 of query aligns to 35:723/725 of 5reqA
- active site: F86 (≠ Y73), Y240 (= Y227), H241 (= H228), K601 (= K582), D605 (= D586), H607 (= H588)
- binding cobalamin: L116 (= L103), A136 (= A123), R204 (= R191), H241 (= H228), E244 (= E231), G330 (= G317), W331 (≠ V318), E367 (= E354), A368 (= A355), A370 (= A357), G606 (= G587), H607 (= H588), D608 (= D589), R609 (= R590), G610 (= G591), I614 (≠ V595), S652 (= S633), L654 (= L635), G682 (= G663), G683 (= G664), V684 (= V665), Y702 (≠ F683), T703 (≠ G684), T706 (= T687)
- binding methylmalonyl(carbadethia)-coenzyme a: Y72 (≠ R59), T74 (≠ S61), M75 (= M62), R79 (= R66), T82 (= T69), R84 (= R71), F86 (≠ Y73), S111 (= S98), S161 (= S148), T163 (= T150), T192 (= T179), Q194 (= Q181), R204 (= R191), N233 (= N220), H241 (= H228), R280 (= R267), S282 (= S269), F284 (= F271), T324 (= T311), H325 (= H312), Q358 (= Q345), S359 (= S346)
- binding succinyl(carbadethia)-coenzyme a: Y72 (≠ R59), T74 (≠ S61), M75 (= M62), R79 (= R66), T82 (= T69), R84 (= R71), F86 (≠ Y73), S161 (= S148), T163 (= T150), T192 (= T179), R204 (= R191), N233 (= N220), H241 (= H228), R280 (= R267), S282 (= S269), F284 (= F271), H325 (= H312), Q358 (= Q345)
1e1cA Methylmalonyl-coa mutase h244a mutant (see paper)
59% identity, 96% coverage: 25:704/712 of query aligns to 37:725/727 of 1e1cA
- active site: Y88 (= Y73), Y242 (= Y227), A243 (≠ H228), K603 (= K582), D607 (= D586), H609 (= H588)
- binding cobalamin: Y88 (= Y73), L118 (= L103), H121 (= H106), A138 (= A123), V205 (= V190), R206 (= R191), E246 (= E231), G332 (= G317), W333 (≠ V318), E369 (= E354), A370 (= A355), A372 (= A357), L373 (= L358), G608 (= G587), H609 (= H588), D610 (= D589), R611 (= R590), G612 (= G591), I616 (≠ V595), Y620 (≠ F599), S654 (= S633), L656 (= L635), G684 (= G663), G685 (= G664), V686 (= V665), Y704 (≠ F683), T705 (≠ G684), T708 (= T687), S713 (≠ A692)
- binding desulfo-coenzyme a: Y74 (≠ R59), M77 (= M62), F80 (≠ G65), R81 (= R66), T84 (= T69), R86 (= R71), S113 (= S98), S163 (= S148), T165 (= T150), T194 (= T179), R282 (= R267), S284 (= S269), H327 (= H312), Q360 (= Q345)
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)
45% identity, 71% coverage: 33:541/712 of query aligns to 46:560/562 of I3VE77
- YPTM 76:79 (≠ RGSM 59:62) binding
- TMR 86:88 (≠ TIR 69:71) binding
- I90 (≠ Y73) 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 (≠ A100) 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 179:181) binding
- R235 (≠ K218) binding
- N240 (≠ S223) binding
- H245 (= H228) binding
- R284 (= R267) binding
4r3uA Crystal structure of 2-hydroxyisobutyryl-coa mutase (see paper)
45% identity, 71% coverage: 33:537/712 of query aligns to 45:555/557 of 4r3uA
- active site: I89 (≠ Y73), Y243 (= Y227), H244 (= H228)
- binding 3-hydroxybutanoyl-coenzyme a: Y75 (≠ R59), T77 (≠ S61), M78 (= M62), R82 (= R66), T85 (= T69), R87 (= R71), I89 (≠ Y73), D116 (≠ A100), S164 (= S148), T166 (= T150), T195 (= T179), Q197 (= Q181), R234 (≠ K218), N236 (= N220), N239 (≠ S223), Y243 (= Y227), H244 (= H228), R283 (= R267), F287 (= F271), R327 (= R310), F328 (≠ T311), H329 (= H312), Q331 (= Q314), Q362 (= Q345)
- 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 (≠ R59), T77 (≠ S61), M78 (= M62), R82 (= R66), T85 (= T69), R87 (= R71), I89 (≠ Y73), D116 (≠ A100), S164 (= S148), T166 (= T150), T195 (= T179), Q197 (= Q181), R234 (≠ K218), N236 (= N220), N239 (≠ S223), H244 (= H228), R283 (= R267), F287 (= F271), R327 (= R310), F328 (≠ T311), H329 (= H312), Q331 (= Q314), Q362 (= Q345)
- binding cobalamin: D116 (≠ A100), M119 (≠ L103), E139 (≠ A123), Q207 (≠ R191), E209 (≠ T193), E247 (= E231), A334 (≠ G317), E371 (= E354), A372 (= A355), A374 (= A357)
5cjtA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isobutyryl-coenzyme a (see paper)
37% identity, 69% coverage: 47:537/712 of query aligns to 544:1058/1062 of 5cjtA
- active site: F569 (≠ Y73), Y750 (= Y227), H751 (= H228)
- binding cobalamin: F598 (= F101), L603 (≠ H106), S621 (≠ A123), Q713 (≠ R191), H751 (= H228), E754 (= E231), A755 (= A232), G839 (= G317), R840 (≠ V318), E876 (= E354), A877 (= A355), T879 (≠ A357), H964 (≠ D442)
- binding isobutyryl-coenzyme a: F556 (≠ R59), F558 (≠ S61), R560 (≠ Y63), R567 (= R71), F569 (≠ Y73), R593 (≠ G96), S648 (= S148), T650 (= T150), R699 (vs. gap), T701 (= T179), Q703 (= Q181), Y743 (≠ N220), Y750 (= Y227), H751 (= H228), S792 (= S269), F794 (= F271), R827 (= R305), K832 (≠ R310), H834 (= H312)
- binding guanosine-5'-diphosphate: E944 (≠ A422)
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
4xc7A Isobutyryl-coa mutase fused with bound butyryl-coa and without cobalamin or gdp (apo-icmf) (see paper)
37% identity, 69% coverage: 47:537/712 of query aligns to 541:1049/1053 of 4xc7A
- active site: F566 (≠ Y73), Y747 (= Y227), H748 (= H228)
- binding Butyryl Coenzyme A: F553 (≠ R59), R557 (≠ Y63), R564 (= R71), F566 (≠ Y73), R590 (≠ G96), S645 (= S148), T647 (= T150), R696 (vs. gap), T698 (= T179), Y740 (≠ N220), S789 (= S269), F791 (= F271), R824 (= R305), K829 (≠ R310), H831 (= H312)
Sites not aligning to the query:
5cjvA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isovaleryl-coenzyme a (see paper)
37% identity, 69% coverage: 47:537/712 of query aligns to 544:1057/1061 of 5cjvA
- active site: F569 (≠ Y73), Y750 (= Y227), H751 (= H228)
- binding cobalamin: F598 (= F101), L603 (≠ H106), S621 (≠ A123), Q713 (≠ R191), E754 (= E231), A755 (= A232), G839 (= G317), R840 (≠ V318), E876 (= E354), A877 (= A355), T879 (≠ A357), H964 (≠ D442)
- binding guanosine-5'-diphosphate: E944 (≠ A422)
- binding Isovaleryl-coenzyme A: F556 (≠ R59), F558 (≠ S61), R560 (≠ Y63), R567 (= R71), F569 (≠ Y73), R593 (≠ G96), S648 (= S148), T650 (= T150), R699 (vs. gap), T701 (= T179), Q703 (= Q181), Q713 (≠ R191), Y743 (≠ N220), H751 (= H228), S792 (= S269), F794 (= F271), K832 (≠ R310), H834 (= H312)
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, 69% coverage: 48:537/712 of query aligns to 547:1059/1063 of 5cjwA
- active site: F571 (≠ Y73), Y752 (= Y227), H753 (= H228)
- binding pivalyl-coenzyme A: F558 (≠ R59), F560 (≠ S61), R562 (≠ Y63), R569 (= R71), F571 (≠ Y73), R595 (≠ G96), S650 (= S148), T652 (= T150), R701 (vs. gap), T703 (= T179), Q705 (= Q181), Y745 (≠ N220), Y752 (= Y227), H753 (= H228), S794 (= S269), F796 (= F271), R829 (= R305), K834 (≠ R310), H836 (= H312)
- binding cobalamin: F600 (= F101), L605 (≠ H106), S623 (≠ A123), Q715 (≠ R191), H753 (= H228), E756 (= E231), A757 (= A232), G841 (= G317), R842 (≠ V318), E878 (= E354), A879 (= A355), T881 (≠ A357), H966 (≠ D442)
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)
37% identity, 69% coverage: 47:537/712 of query aligns to 573:1089/1093 of Q1LRY0
- F587 (≠ S61) binding
- F598 (≠ Y73) 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 (≠ G96) binding
- R728 (vs. gap) binding
- Y772 (≠ N220) binding
- S821 (= S269) binding
- R856 (= R305) binding
- K861 (≠ R310) binding
- E973 (≠ A422) 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
Query Sequence
>Ga0059261_3988 FitnessBrowser__Korea:Ga0059261_3988
MTDKPTLDAWKALSEKEVKGRDLTWRTPEGIDVKPLYTAEDVTADPGLPGFAPFTRGVRG
SMYAGRPWTIRQYAGFSTAEESNAFYRRNLAAGQKGLSVAFDLATHRGYDSDHPRVPGDV
GKAGVAIDSVEDMKILFDGIPLGEMSVSMTMNGAVIPILAFFIVAGEEQGVPRAQLDGTI
QNDILKEFMVRNTYIYPPEPSMRIISDIFGYTSREMPKFNSISISGYHMQEAGATQVQEL
AFTIADGMEYVKYGVASGLDIDKFAGRLSFFFAIGMNFFMEVAKLRAARVLWHRVMTKLG
AKDERSKMLRTHCQTSGVSLTEQDPYNNVIRTTIEAMAAMLGGTQSLHTNALDEAIALPT
DFSARIARNTQIVIQEETGMTKVVDPLGGSYYVEALTQELVDKAWEIIERVEAEGGMAKA
VAAGWPKAMIEEASAATAARIDRGEQVIVGVNKYRKAEEDPIDILDVDNHAVREAQIARI
KKVKSARDEAKCQAALDALREGARGTENLLALAVEAARHRATLGEISLAMEDVFGRHGTV
PTPVSGVYGGAYAEDRRWERLKDGVAATERRLGRKPRMLVAKMGQDGHDRGANLVSSAFG
DLGFEVVPGPLFQTPQEAAELAIAENVDVVGASSLAAGHKTLIPQMIGHLKDAGRGDIKV
IAGGVIPAQDYQFLRDAGVQAIFGPGTNLVNAAADVLTLLGHNLPPEEEAAE
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