SitesBLAST
Comparing WP_092057248.1 NCBI__GCF_900111775.1:WP_092057248.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
P22033 Methylmalonyl-CoA mutase, mitochondrial; MCM; Methylmalonyl-CoA isomerase; EC 5.4.99.2 from Homo sapiens (Human) (see 28 papers)
65% identity, 98% coverage: 11:711/714 of query aligns to 42:741/750 of P22033
- Q50 (≠ E19) binding malonyl-CoA
- I69 (≠ V38) to V: in MMAM; likely benign; dbSNP:rs115923556
- P86 (= P57) 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 (= G58) to E: in MMAM; mut0; dbSNP:rs1554160986
- R93 (= R64) to H: in MMAM; mut0; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918251
- G94 (= G65) to R: in MMAM; mut0; dbSNP:rs727504022; to V: in MMAM; mut- and mut0; dbSNP:rs535411418
- P95 (= P66) to R: in MMAM; mut0; dbSNP:rs190834116
- YPTM 96:99 (≠ MASM 67:70) binding malonyl-CoA
- Y100 (= Y71) 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 (= W76) to R: in MMAM; mut0; dbSNP:rs121918249
- TIRQY 106:110 (≠ TVRQY 77:81) binding malonyl-CoA
- R108 (= R79) to C: in MMAM; mut0; dbSNP:rs121918257; to G: in MMAM; mut-; to H: in MMAM; mut0; dbSNP:rs483352778
- Q109 (= Q80) to R: in MMAM; mut0; dbSNP:rs1461110052
- G133 (= G104) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253828
- A137 (= A108) to V: in MMAM; mut0; dbSNP:rs941483851
- D139 (= D110) to N: in MMAM; uncertain significance; dbSNP:rs879253829
- L140 (= L111) to P: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- A141 (= A112) to T: in MMAM; decreased protein expression; dbSNP:rs1554160730
- H143 (= H114) to Y: in MMAM; mut0
- G145 (= G116) to S: in MMAM; mut0
- S148 (= S119) to L: in MMAM; mut0; dbSNP:rs1300547552
- D156 (= D127) to N: in MMAM; mut-
- G158 (= G129) to V: in MMAM; mut0
- G161 (= G132) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; to V: in MMAM; decreased protein expression
- F174 (= F145) to S: in MMAM; mut0; dbSNP:rs864309733
- M186 (= M157) to V: in MMAM; mut-; dbSNP:rs148331800
- T187 (= T158) to S: in MMAM; mut0; dbSNP:rs879253830
- N189 (= N160) to I: in MMAM; mut-; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs200908035; to K: in MMAM; mut-; dbSNP:rs1561959114
- A191 (= A162) to E: in MMAM; mut- and mut0; affects proper folding; reduced protein level; decreased methylmalonyl-CoA mutase activity; dbSNP:rs760782399
- A197 (= A168) to E: in MMAM; mut0
- G203 (≠ A174) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs778702777
- E205 (= E176) natural variant: Missing (in MMAM; mut0; dbSNP:rs879253831)
- G215 (= G186) to C: in MMAM; mut- and mut0; dbSNP:rs121918258; to S: in MMAM; mut0; dbSNP:rs121918258
- TIQ 216:218 (= TIQ 187:189) binding malonyl-CoA
- Q218 (= Q189) to H: in MMAM; mut0 and mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability; dbSNP:rs1446389693
- N219 (= N190) to Y: in MMAM; mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; dbSNP:rs121918256
- R228 (= R199) binding malonyl-CoA; to Q: in MMAM; mut0; dbSNP:rs770810987
- T230 (= T201) to I: in MMAM; mut-; to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253833
- Y231 (= Y202) 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 (= K226) binding malonyl-CoA
- S262 (= S233) to N: in MMAM; mut0
- H265 (= H236) binding malonyl-CoA; to Y: in MMAM; mut-
- E276 (= E247) to D: in MMAM; uncertain significance; mut-; dbSNP:rs12175488
- L281 (= L252) to S: in MMAM; mut0; dbSNP:rs796052007
- G284 (= G255) to E: in MMAM; mut0; dbSNP:rs879253835; to R: in MMAM; mut0; dbSNP:rs761477436
- S288 (≠ V259) to P: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1179778233
- G291 (≠ A262) to E: in MMAM; mut0
- Q293 (≠ A264) to P: in MMAM; mut0
- RLS 304:306 (= RLS 275:277) binding malonyl-CoA
- L305 (= L276) to S: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554160246
- S306 (= S277) to F: in MMAM; mut0; dbSNP:rs1085307929
- W309 (≠ F280) to G: in MMAM; decreased protein expression
- G312 (= G283) to V: in MMAM; mut0; dbSNP:rs864309734
- Y316 (≠ F287) 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 (= A295) to T: in MMAM; mut-; dbSNP:rs780387525
- R326 (= R297) to K: in MMAM; uncertain significance; dbSNP:rs758577372
- L328 (= L299) 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 (= S314) 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 (≠ M316) natural variant: Missing (in MMAM; mut0)
- L347 (= L317) to R: in MMAM; mut0; dbSNP:rs1026703654
- H350 (= H320) to Y: in MMAM; mut0; dbSNP:rs1407914109
- L358 (= L328) to P: in MMAM; mut0
- N366 (= N336) 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 (= R339) 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 (= T340) to P: in MMAM; mut0; dbSNP:rs368790885
- A377 (= A347) to E: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918250
- Q383 (= Q353) to H: in MMAM; mut0; to P: in MMAM; mut0
- H386 (= H356) to N: in MMAM; mut0; dbSNP:rs1554159937; to R: in MMAM; mut0; dbSNP:rs866933356
- T387 (= T357) 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 (= N358) to H: in MMAM; mut0; dbSNP:rs766010704; to K: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253840
- S389 (≠ A359) natural variant: Missing (in MMAM; mut0)
- I412 (= I382) natural variant: Missing (in MMAM; mut0)
- P424 (= P394) to L: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253842
- G426 (= G396) 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 (= G397) to D: in MMAM; mut0; dbSNP:rs753288303
- G454 (= G424) to E: in MMAM; mut0
- A499 (≠ P469) to T: in dbSNP:rs2229385
- I505 (= I475) to T: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- Q514 (= Q484) to E: in MMAM; uncertain significance; to K: in MMAM; decreased protein expression
- L518 (= L488) to P: in MMAM; mut0; dbSNP:rs864309738
- R532 (≠ K502) to H: in dbSNP:rs1141321
- A535 (= A505) to P: in MMAM; mut0; dbSNP:rs760183775
- A552 (≠ C522) to V: in MMAM; uncertain significance; dbSNP:rs879253845
- C560 (≠ A530) to Y: in MMAM; mut0; dbSNP:rs1238333040
- T566 (≠ S536) to R: in MMAM; mut0
- F573 (= F543) 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 (= Y557) 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 (= G618) 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 (≠ V641) 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 (≠ Q654) natural variant: E -> EL (in MMAM; mut-)
- L685 (= L655) to R: in MMAM; mut-; dbSNP:rs864309739
- R694 (≠ A664) 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)
65% identity, 98% coverage: 11:711/714 of query aligns to 7:706/714 of 2xiqA
- active site: Y75 (= Y81), Y229 (= Y235), H230 (= H236), K586 (= K591), D590 (= D595), H592 (= H597)
- binding cobalamin: Y75 (= Y81), L105 (= L111), H108 (= H114), A125 (= A131), R193 (= R199), E233 (= E239), G320 (= G325), W321 (= W326), E357 (= E362), G360 (≠ A365), L361 (= L366), G591 (= G596), H592 (= H597), D593 (= D598), R594 (= R599), G595 (= G600), I599 (≠ V604), G635 (= G640), S637 (= S642), L639 (= L644), A641 (= A646), G667 (= G672), G668 (= G673), F687 (= F692), G688 (= G693), T691 (= T696)
- binding malonyl-coenzyme a: Y61 (≠ M67), T63 (≠ S69), M64 (= M70), R68 (= R74), T71 (= T77), R73 (= R79), Y75 (= Y81), S150 (= S156), T152 (= T158), T181 (= T187), R193 (= R199), K220 (= K226), H230 (= H236), R269 (= R275), S271 (= S277), F273 (= F279), R313 (= R318), A314 (≠ T319), H315 (= H320), Q317 (= Q322), Q348 (= Q353)
8dyjB Crystal structure of human methylmalonyl-coa mutase in complex with adp and cob(ii)alamin (see paper)
65% identity, 98% coverage: 11:711/714 of query aligns to 6:705/708 of 8dyjB
- binding adenosine-5'-diphosphate: Y74 (= Y81), T151 (= T158), R192 (= R199), Y228 (= Y235), H229 (= H236), F272 (= F279), Q316 (= Q322), N352 (= N358), E356 (= E362), L360 (= L366), P361 (= P367)
- binding cobalamin: F102 (= F109), L104 (= L111), H107 (= H114), A124 (= A131), V191 (= V198), R192 (= R199), H229 (= H236), E232 (= E239), G319 (= G325), W320 (= W326), E356 (= E362), G359 (≠ A365), L360 (= L366), G590 (= G596), H591 (= H597), D592 (= D598), R593 (= R599), G594 (= G600), I598 (≠ V604), S636 (= S642), L638 (= L644), A640 (= A646), G666 (= G672), G667 (= G673), V668 (= V674), F686 (= F692), G687 (= G693), T690 (= T696)
8gjuJ Crystal structure of human methylmalonyl-coa mutase (mmut) in complex with methylmalonic acidemia type a protein (mmaa), coenzyme a, and gdp (see paper)
64% identity, 98% coverage: 11:711/714 of query aligns to 7:683/689 of 8gjuJ
- binding coenzyme a: Y61 (≠ M67), T63 (≠ S69), R68 (= R74), T71 (= T77), R73 (= R79), S150 (= S156), T152 (= T158), T181 (= T187), Q183 (= Q189), N222 (= N228), R269 (= R275), S271 (= S277), R313 (= R318), A314 (≠ T319), H315 (= H320), Q348 (= Q353)
6reqA Methylmalonyl-coa mutase, 3-carboxypropyl-coa inhibitor complex (see paper)
65% identity, 94% coverage: 30:702/714 of query aligns to 37:714/727 of 6reqA
- active site: Y88 (= Y81), Y242 (= Y235), H243 (= H236), K603 (= K591), D607 (= D595), H609 (= H597)
- binding 3-carboxypropyl-coenzyme a: Y74 (≠ M67), T76 (≠ S69), M77 (= M70), F80 (≠ G73), R81 (= R74), T84 (= T77), R86 (= R79), Y88 (= Y81), S113 (= S106), S163 (= S156), T165 (= T158), T194 (= T187), R206 (= R199), H243 (= H236), R282 (= R275), S284 (= S277), F286 (= F279), H327 (= H320), Q329 (= Q322), Q360 (= Q353)
- binding cobalamin: Y88 (= Y81), F116 (= F109), L118 (= L111), H121 (= H114), A138 (= A131), R206 (= R199), E246 (= E239), G332 (= G325), W333 (= W326), E369 (= E362), A370 (= A363), A372 (= A365), G608 (= G596), H609 (= H597), D610 (= D598), R611 (= R599), G612 (= G600), I616 (≠ V604), Y620 (= Y608), S654 (= S642), L656 (= L644), G658 (≠ A646), G684 (= G672), G685 (= G673), Y704 (≠ F692), T705 (≠ G693), T708 (= T696)
4reqA Methylmalonyl-coa mutase substrate complex (see paper)
65% identity, 94% coverage: 30:702/714 of query aligns to 36:713/726 of 4reqA
- active site: Y87 (= Y81), Y241 (= Y235), H242 (= H236), K602 (= K591), D606 (= D595), H608 (= H597)
- binding cobalamin: Y87 (= Y81), L117 (= L111), A137 (= A131), V204 (= V198), R205 (= R199), H242 (= H236), E245 (= E239), G331 (= G325), W332 (= W326), E368 (= E362), A369 (= A363), A371 (= A365), L372 (= L366), G607 (= G596), H608 (= H597), D609 (= D598), R610 (= R599), G611 (= G600), I615 (≠ V604), S653 (= S642), L655 (= L644), G683 (= G672), G684 (= G673), V685 (= V674), Y703 (≠ F692), T704 (≠ G693), T707 (= T696)
- binding methylmalonyl-coenzyme a: Y73 (≠ M67), M76 (= M70), F79 (≠ G73), R80 (= R74), T83 (= T77), R85 (= R79), Y87 (= Y81), S112 (= S106), S162 (= S156), T164 (= T158), T193 (= T187), R205 (= R199), N234 (= N228), Y241 (= Y235), H242 (= H236), R281 (= R275), S283 (= S277), F285 (= F279), H326 (= H320), Q328 (= Q322), Q359 (= Q353), S360 (= S354)
- binding succinyl-coenzyme a: Y73 (≠ M67), M76 (= M70), F79 (≠ G73), R80 (= R74), T83 (= T77), R85 (= R79), Y87 (= Y81), S162 (= S156), T164 (= T158), T193 (= T187), Q195 (= Q189), R205 (= R199), N234 (= N228), Y241 (= Y235), H242 (= H236), R281 (= R275), S283 (= S277), F285 (= F279), R324 (= R318), H326 (= H320), Q359 (= Q353)
7reqA Methylmalonyl-coa mutase, 2-carboxypropyl-coa inhibitor complex (see paper)
65% identity, 94% coverage: 30:702/714 of query aligns to 35:712/725 of 7reqA
- active site: Y86 (= Y81), Y240 (= Y235), H241 (= H236), K601 (= K591), D605 (= D595), H607 (= H597)
- binding 2-carboxypropyl-coenzyme a: Y72 (≠ M67), T74 (≠ S69), M75 (= M70), F78 (≠ G73), R79 (= R74), T82 (= T77), R84 (= R79), Y86 (= Y81), S161 (= S156), T163 (= T158), T192 (= T187), R204 (= R199), H241 (= H236), R280 (= R275), S282 (= S277), F284 (= F279), H325 (= H320), Q358 (= Q353)
- binding cobalamin: Y86 (= Y81), L116 (= L111), A136 (= A131), R204 (= R199), E244 (= E239), G330 (= G325), W331 (= W326), E367 (= E362), A368 (= A363), A370 (= A365), G606 (= G596), H607 (= H597), D608 (= D598), R609 (= R599), G610 (= G600), I614 (≠ V604), S652 (= S642), L654 (= L644), G682 (= G672), G683 (= G673), Y702 (≠ F692), T703 (≠ G693), T706 (= T696)
3reqA Methylmalonyl-coa mutase, substrate-free state (poor quality structure) (see paper)
65% identity, 94% coverage: 30:702/714 of query aligns to 35:712/725 of 3reqA
- active site: Y86 (= Y81), Y240 (= Y235), H241 (= H236), K601 (= K591), D605 (= D595), H607 (= H597)
- binding adenosine: Y86 (= Y81), Y240 (= Y235), E244 (= E239), G330 (= G325)
- binding cobalamin: L116 (= L111), V203 (= V198), R204 (= R199), E244 (= E239), G330 (= G325), W331 (= W326), A368 (= A363), G606 (= G596), H607 (= H597), D608 (= D598), R609 (= R599), G610 (= G600), I614 (≠ V604), G650 (= G640), S652 (= S642), L654 (= L644), G682 (= G672), G683 (= G673), Y702 (≠ F692), T703 (≠ G693), P704 (= P694), T706 (= T696)
2reqA Methylmalonyl-coa mutase, non-productive coa complex, in open conformation representing substrate-free state (see paper)
65% identity, 94% coverage: 30:702/714 of query aligns to 35:712/725 of 2reqA
- active site: Y86 (= Y81), Y240 (= Y235), H241 (= H236), K601 (= K591), D605 (= D595), H607 (= H597)
- binding cobalamin: V203 (= V198), R204 (= R199), E244 (= E239), A245 (= A240), W331 (= W326), A368 (= A363), G606 (= G596), H607 (= H597), D608 (= D598), R609 (= R599), G610 (= G600), I614 (≠ V604), G650 (= G640), S652 (= S642), L654 (= L644), A655 (= A645), G682 (= G672), G683 (= G673), Y702 (≠ F692), T703 (≠ G693), T706 (= T696)
- binding coenzyme a: Y72 (≠ M67), R79 (= R74), K318 (= K313)
P11653 Methylmalonyl-CoA mutase large subunit; MCM-alpha; EC 5.4.99.2 from Propionibacterium freudenreichii subsp. shermanii (see 4 papers)
65% identity, 94% coverage: 30:702/714 of query aligns to 38:715/728 of P11653
- Y75 (≠ M67) binding (R)-methylmalonyl-CoA
- M78 (= M70) binding (R)-methylmalonyl-CoA
- R82 (= R74) binding (R)-methylmalonyl-CoA
- T85 (= T77) binding (R)-methylmalonyl-CoA
- R87 (= R79) binding (R)-methylmalonyl-CoA
- Y89 (= Y81) binding (R)-methylmalonyl-CoA; mutation to F: Does not significantly affect affinity for succiny-CoA, but kcat is lowered about 580-fold.
- S114 (= S106) binding (R)-methylmalonyl-CoA
- F117 (= F109) binding cob(II)alamin
- A139 (= A131) binding cob(II)alamin
- T195 (= T187) binding (R)-methylmalonyl-CoA
- Q197 (= Q189) binding (R)-methylmalonyl-CoA
- V206 (= V198) binding cob(II)alamin
- R207 (= R199) binding (R)-methylmalonyl-CoA; binding cob(II)alamin
- H244 (= H236) binding (R)-methylmalonyl-CoA
- R283 (= R275) binding (R)-methylmalonyl-CoA
- S285 (= S277) binding (R)-methylmalonyl-CoA
- G333 (= G325) binding cob(II)alamin
- E370 (= E362) binding cob(II)alamin
- A373 (= A365) binding cob(II)alamin
- G609 (= G596) binding cob(II)alamin
- H610 (= H597) binding axial binding residue
- D611 (= D598) binding cob(II)alamin
- R612 (= R599) binding cob(II)alamin
- S655 (= S642) binding cob(II)alamin
- L657 (= L644) binding cob(II)alamin
- G686 (= G673) binding cob(II)alamin
- T709 (= T696) binding cob(II)alamin
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
5reqA Methylmalonyl-coa mutase, y89f mutant, substrate complex (see paper)
65% identity, 94% coverage: 30:702/714 of query aligns to 35:712/725 of 5reqA
- active site: F86 (≠ Y81), Y240 (= Y235), H241 (= H236), K601 (= K591), D605 (= D595), H607 (= H597)
- binding cobalamin: L116 (= L111), A136 (= A131), R204 (= R199), H241 (= H236), E244 (= E239), G330 (= G325), W331 (= W326), E367 (= E362), A368 (= A363), A370 (= A365), G606 (= G596), H607 (= H597), D608 (= D598), R609 (= R599), G610 (= G600), I614 (≠ V604), S652 (= S642), L654 (= L644), G682 (= G672), G683 (= G673), V684 (= V674), Y702 (≠ F692), T703 (≠ G693), T706 (= T696)
- binding methylmalonyl(carbadethia)-coenzyme a: Y72 (≠ M67), T74 (≠ S69), M75 (= M70), R79 (= R74), T82 (= T77), R84 (= R79), F86 (≠ Y81), S111 (= S106), S161 (= S156), T163 (= T158), T192 (= T187), Q194 (= Q189), R204 (= R199), N233 (= N228), H241 (= H236), R280 (= R275), S282 (= S277), F284 (= F279), T324 (= T319), H325 (= H320), Q358 (= Q353), S359 (= S354)
- binding succinyl(carbadethia)-coenzyme a: Y72 (≠ M67), T74 (≠ S69), M75 (= M70), R79 (= R74), T82 (= T77), R84 (= R79), F86 (≠ Y81), S161 (= S156), T163 (= T158), T192 (= T187), R204 (= R199), N233 (= N228), H241 (= H236), R280 (= R275), S282 (= S277), F284 (= F279), H325 (= H320), Q358 (= Q353)
6oxdA Structure of mycobacterium tuberculosis methylmalonyl-coa mutase with adenosyl cobalamin (see paper)
65% identity, 96% coverage: 26:712/714 of query aligns to 41:731/736 of 6oxdA
- active site: Y100 (= Y81), Y254 (= Y235), H255 (= H236), K610 (= K591), D614 (= D595), H616 (= H597)
- binding cobalamin: Y100 (= Y81), L130 (= L111), H133 (= H114), A150 (= A131), R218 (= R199), E258 (= E239), G344 (= G325), W345 (= W326), E381 (= E362), A382 (= A363), A384 (= A365), L385 (= L366), G615 (= G596), H616 (= H597), D617 (= D598), R618 (= R599), S661 (= S642), L663 (= L644), A665 (= A646), G691 (= G672), G692 (= G673), F711 (= F692), P712 (≠ G693), T715 (= T696)
- binding Itaconyl coenzyme A: Y86 (≠ M67), T88 (≠ S69), M89 (= M70), Q93 (≠ R74), T96 (= T77), R98 (= R79), Y100 (= Y81), S175 (= S156), T177 (= T158), T206 (= T187), R218 (= R199), H255 (= H236), R294 (= R275), S296 (= S277), F298 (= F279), R337 (= R318), T338 (= T319), H339 (= H320), Q341 (= Q322), Q372 (= Q353)
1e1cA Methylmalonyl-coa mutase h244a mutant (see paper)
65% identity, 94% coverage: 30:702/714 of query aligns to 37:714/727 of 1e1cA
- active site: Y88 (= Y81), Y242 (= Y235), A243 (≠ H236), K603 (= K591), D607 (= D595), H609 (= H597)
- binding cobalamin: Y88 (= Y81), L118 (= L111), H121 (= H114), A138 (= A131), V205 (= V198), R206 (= R199), E246 (= E239), G332 (= G325), W333 (= W326), E369 (= E362), A370 (= A363), A372 (= A365), L373 (= L366), G608 (= G596), H609 (= H597), D610 (= D598), R611 (= R599), G612 (= G600), I616 (≠ V604), Y620 (= Y608), S654 (= S642), L656 (= L644), G684 (= G672), G685 (= G673), V686 (= V674), Y704 (≠ F692), T705 (≠ G693), T708 (= T696), S713 (= S701)
- binding desulfo-coenzyme a: Y74 (≠ M67), M77 (= M70), F80 (≠ G73), R81 (= R74), T84 (= T77), R86 (= R79), S113 (= S106), S163 (= S156), T165 (= T158), T194 (= T187), R282 (= R275), S284 (= S277), H327 (= H320), Q360 (= Q353)
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)
46% identity, 75% coverage: 11:547/714 of query aligns to 18:557/562 of I3VE77
- YPTM 76:79 (≠ MASM 67:70) binding (3S)-3-hydroxybutanoyl-CoA
- TMR 86:88 (≠ TVR 77:79) binding (3S)-3-hydroxybutanoyl-CoA
- I90 (≠ Y81) 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 (≠ A108) binding (3S)-3-hydroxybutanoyl-CoA; mutation to A: 2-fold increase in catalytic efficiency with 2-hydroxyisobutyryl-CoA as substrate. Small increase in catalytic efficiency with (S)-3-hydroxybuytryl-CoA as substrate. 1800-fold increase in catalytic efficiency with (R)-3-hydroxybutyryl-CoA as substrate.; mutation to V: 1.5-fold increase in catalytic efficiency with 2-hydroxyisobutyryl-CoA as substrate. 3-fold decrease in catalytic efficiency with (S)-3-hydroxybuytryl-CoA as substrate. 1300-fold increase in catalytic efficiency with (R)-3-hydroxybutyryl-CoA as substrate. 74-fold increase in catalytic efficiency with pivalyl-CoA as substrate.
- TVQ 196:198 (≠ TIQ 187:189) binding (3S)-3-hydroxybutanoyl-CoA
- R235 (≠ K226) binding (3S)-3-hydroxybutanoyl-CoA
- N240 (≠ S231) binding (3S)-3-hydroxybutanoyl-CoA
- H245 (= H236) binding (3S)-3-hydroxybutanoyl-CoA
- R284 (= R275) binding (3S)-3-hydroxybutanoyl-CoA
4r3uA Crystal structure of 2-hydroxyisobutyryl-coa mutase (see paper)
46% identity, 75% coverage: 11:547/714 of query aligns to 17:556/557 of 4r3uA
- active site: I89 (≠ Y81), Y243 (= Y235), H244 (= H236)
- binding 3-hydroxybutanoyl-coenzyme a: Y75 (≠ M67), T77 (≠ S69), M78 (= M70), R82 (= R74), T85 (= T77), R87 (= R79), I89 (≠ Y81), D116 (≠ A108), S164 (= S156), T166 (= T158), T195 (= T187), Q197 (= Q189), R234 (≠ K226), N236 (= N228), N239 (≠ S231), Y243 (= Y235), H244 (= H236), R283 (= R275), F287 (= F279), R327 (= R318), F328 (≠ T319), H329 (= H320), Q331 (= Q322), Q362 (= Q353)
- 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 (≠ M67), T77 (≠ S69), M78 (= M70), R82 (= R74), T85 (= T77), R87 (= R79), I89 (≠ Y81), D116 (≠ A108), S164 (= S156), T166 (= T158), T195 (= T187), Q197 (= Q189), R234 (≠ K226), N236 (= N228), N239 (≠ S231), H244 (= H236), R283 (= R275), F287 (= F279), R327 (= R318), F328 (≠ T319), H329 (= H320), Q331 (= Q322), Q362 (= Q353)
- binding cobalamin: D116 (≠ A108), M119 (≠ L111), E139 (≠ A131), Q207 (≠ R199), E209 (≠ T201), E247 (= E239), A334 (≠ G325), E371 (= E362), A372 (= A363), A374 (= A365)
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, 77% coverage: 1:547/714 of query aligns to 515:1090/1093 of Q1LRY0
- F587 (≠ S69) binding substrate
- F598 (≠ Y81) 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 (vs. gap) binding substrate
- R728 (≠ A185) binding substrate
- Y772 (≠ N228) binding substrate
- S821 (= S277) binding substrate
- R856 (≠ K313) binding substrate
- K861 (≠ R318) binding substrate
- E973 (= E430) binding GTP
Sites not aligning to the query:
- 39 binding axial binding residue
- 169:417 GTPase chaperone MeaI
- 219:224 binding GTP
- 223 binding Mg(2+)
- 248 binding Mg(2+)
- 249 binding Mg(2+)
- 262 binding Mg(2+); binding Mg(2+)
- 265 binding GTP
- 310 binding Mg(2+); binding Mg(2+)
- 311 binding Mg(2+)
- 357:360 binding GTP
- 418:579 Linker
- 1092 binding GTP
8sslA Isobutyryl-coa mutase fused q341a in the presence of gtp (see paper)
35% identity, 77% coverage: 1:547/714 of query aligns to 494:1069/1072 of 8sslA
Sites not aligning to the query:
- binding guanosine-5'-diphosphate: 200, 201, 202, 241, 244, 337, 339, 374, 375, 376, 1071
- binding magnesium ion: 201, 241
4xc7A Isobutyryl-coa mutase fused with bound butyryl-coa and without cobalamin or gdp (apo-icmf) (see paper)
37% identity, 71% coverage: 44:547/714 of query aligns to 530:1050/1053 of 4xc7A
- active site: F566 (≠ Y81), Y747 (= Y235), H748 (= H236)
- binding Butyryl Coenzyme A: F553 (≠ M67), R557 (≠ Y71), R564 (= R79), F566 (≠ Y81), R590 (vs. gap), S645 (= S156), T647 (= T158), R696 (≠ A185), T698 (= T187), Y740 (≠ N228), S789 (= S277), F791 (= F279), R824 (≠ K313), K829 (≠ R318), H831 (= H320)
Sites not aligning to the query:
5cjtA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isobutyryl-coenzyme a (see paper)
37% identity, 71% coverage: 44:547/714 of query aligns to 533:1059/1062 of 5cjtA
- active site: F569 (≠ Y81), Y750 (= Y235), H751 (= H236)
- binding cobalamin: F598 (= F109), L603 (≠ H114), S621 (≠ A131), Q713 (≠ R199), H751 (= H236), E754 (= E239), A755 (= A240), G839 (= G325), R840 (≠ W326), E876 (= E362), A877 (= A363), T879 (≠ A365), H964 (≠ D450)
- binding isobutyryl-coenzyme a: F556 (≠ M67), F558 (≠ S69), R560 (≠ Y71), R567 (= R79), F569 (≠ Y81), R593 (vs. gap), S648 (= S156), T650 (= T158), R699 (≠ A185), T701 (= T187), Q703 (= Q189), Y743 (≠ N228), Y750 (= Y235), H751 (= H236), S792 (= S277), F794 (= F279), R827 (≠ K313), K832 (≠ R318), H834 (= H320)
- binding guanosine-5'-diphosphate: E944 (= E430)
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
4xc6A Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, and mg (holo-icmf/gdp) (see paper)
37% identity, 71% coverage: 44:547/714 of query aligns to 536:1064/1067 of 4xc6A
- active site: F572 (≠ Y81), Y753 (= Y235), H754 (= H236)
- binding cobalamin: F601 (= F109), L606 (≠ H114), S624 (≠ A131), Q716 (≠ R199), H754 (= H236), E757 (= E239), A758 (= A240), G842 (= G325), R843 (≠ W326), E879 (= E362), A880 (= A363), T882 (≠ A365), H967 (≠ D450)
- binding guanosine-5'-diphosphate: E947 (= E430)
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
Query Sequence
>WP_092057248.1 NCBI__GCF_900111775.1:WP_092057248.1
MSPFEKKSLSDWEALVKKELKTDNLDKLQWDTAEGIRVKPLYTKADVEKLETADTLPGVA
PFVRGPMASMYAGRPWTVRQYAGFSTAEESNAFYKRNLAAGQQGLSVAFDLATHRGYDSD
HPRVVGDVGKAGVAIDSVEDMKILFSDIPLDKVSVSMTMNGAVLPIMANYIVAAEEQGVS
QEKLAGTIQNDILKEFMVRNTYIYPPEPSMRIISDIIEYTSKHMPKFNSISISGYHIQEA
GANNALELAFTLADGLEYVKAAIAKGLDVDAFAPRLSFFFAIGMNFFMEAAKLRAARFLW
ADLMQQFQPKNPKSLMLRTHCQTSGWSLTEQDPYNNVIRTTLEALAAVLGGTQSLHTNAL
DEAIALPTEQSARIARNTQLIIQEESGVTNVVDPLGGSYYVESLTSALVEEARKILAEID
GLGGMTKAIESGMPKLRIEESAAKKQAAIDSGREVIVGVNKYKLAKEEPIDVLDIDNTAV
REGQIARLKKMRAERDEAACQKALAAITAACADTQQNLLGLCVEAARLRASVGEISDAME
KVFGRHRAEIKLVSGAYGSIVEKDQDFSALKARIDAFAATEGRRPRILVAKMGQDGHDRG
AKVVATAYADAGFDVDMGPLFQTPEEAAKMAVENDVHVVGVSSLAAGHKTLVPQLAAELK
KLGADDIVIVCGGVIPRQDYDELLAAGAARIFGPGTPITVSATETLDAIEEKRR
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