SitesBLAST
Comparing WP_011880186.1 NCBI__GCF_000016205.1:WP_011880186.1 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)
2xiqA Crystal structure of human methylmalonyl-coa mutase in complex with adenosylcobalamin and malonyl-coa (see paper)
49% identity, 95% coverage: 26:704/713 of query aligns to 32:712/714 of 2xiqA
- active site: Y75 (= Y71), Y229 (= Y225), H230 (= H226), K586 (= K583), D590 (= D587), H592 (= H589)
- binding cobalamin: Y75 (= Y71), L105 (= L101), H108 (≠ Q104), A125 (= A121), R193 (= R189), E233 (= E229), G320 (= G315), W321 (= W316), E357 (= E352), G360 (≠ A355), L361 (= L356), G591 (= G588), H592 (= H589), D593 (= D590), R594 (= R591), G595 (= G592), I599 (≠ V596), G635 (= G632), S637 (= S634), L639 (= L636), A641 (≠ G638), G667 (= G663), G668 (= G664), F687 (= F683), G688 (= G684), T691 (= T687)
- binding malonyl-coenzyme a: Y61 (= Y57), T63 (≠ S59), M64 (= M60), R68 (= R64), T71 (= T67), R73 (= R69), Y75 (= Y71), S150 (= S146), T152 (= T148), T181 (= T177), R193 (= R189), K220 (≠ R216), H230 (= H226), R269 (= R265), S271 (= S267), F273 (= F269), R313 (= R308), A314 (≠ M309), H315 (= H310), Q317 (= Q312), Q348 (= Q343)
P22033 Methylmalonyl-CoA mutase, mitochondrial; MCM; Methylmalonyl-CoA isomerase; EC 5.4.99.2 from Homo sapiens (Human) (see 28 papers)
49% identity, 95% coverage: 26:704/713 of query aligns to 67:747/750 of P22033
- I69 (≠ L28) to V: in MMAM; likely benign; dbSNP:rs115923556
- P86 (= P47) 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 (= G48) to E: in MMAM; mut0; dbSNP:rs1554160986
- R93 (= R54) to H: in MMAM; mut0; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918251
- G94 (= G55) to R: in MMAM; mut0; dbSNP:rs727504022; to V: in MMAM; mut- and mut0; dbSNP:rs535411418
- P95 (= P56) to R: in MMAM; mut0; dbSNP:rs190834116
- YPTM 96:99 (≠ YASM 57:60) binding malonyl-CoA
- Y100 (= Y61) 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 (= W66) to R: in MMAM; mut0; dbSNP:rs121918249
- TIRQY 106:110 (= TIRQY 67:71) binding malonyl-CoA
- R108 (= R69) to C: in MMAM; mut0; dbSNP:rs121918257; to G: in MMAM; mut-; to H: in MMAM; mut0; dbSNP:rs483352778
- Q109 (= Q70) to R: in MMAM; mut0; dbSNP:rs1461110052
- G133 (= G94) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253828
- A137 (= A98) to V: in MMAM; mut0; dbSNP:rs941483851
- D139 (= D100) to N: in MMAM; uncertain significance; dbSNP:rs879253829
- L140 (= L101) to P: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- A141 (= A102) to T: in MMAM; decreased protein expression; dbSNP:rs1554160730
- H143 (≠ Q104) to Y: in MMAM; mut0
- G145 (= G106) to S: in MMAM; mut0
- S148 (= S109) to L: in MMAM; mut0; dbSNP:rs1300547552
- D156 (= D117) to N: in MMAM; mut-
- G158 (= G119) to V: in MMAM; mut0
- G161 (= G122) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; to V: in MMAM; decreased protein expression
- F174 (= F135) to S: in MMAM; mut0; dbSNP:rs864309733
- M186 (= M147) to V: in MMAM; mut-; dbSNP:rs148331800
- T187 (= T148) to S: in MMAM; mut0; dbSNP:rs879253830
- N189 (= N150) to I: in MMAM; mut-; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs200908035; to K: in MMAM; mut-; dbSNP:rs1561959114
- A191 (= A152) to E: in MMAM; mut- and mut0; affects proper folding; reduced protein level; decreased methylmalonyl-CoA mutase activity; dbSNP:rs760782399
- A197 (= A158) to E: in MMAM; mut0
- G203 (≠ A164) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs778702777
- E205 (= E166) natural variant: Missing (in MMAM; mut0; dbSNP:rs879253831)
- G215 (= G176) to C: in MMAM; mut- and mut0; dbSNP:rs121918258; to S: in MMAM; mut0; dbSNP:rs121918258
- TIQ 216:218 (= TIQ 177:179) binding malonyl-CoA
- Q218 (= Q179) to H: in MMAM; mut0 and mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability; dbSNP:rs1446389693
- N219 (= N180) to Y: in MMAM; mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; dbSNP:rs121918256
- R228 (= R189) binding malonyl-CoA; to Q: in MMAM; mut0; dbSNP:rs770810987
- T230 (= T191) to I: in MMAM; mut-; to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253833
- Y231 (≠ W192) 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 (≠ R216) binding malonyl-CoA
- S262 (= S223) to N: in MMAM; mut0
- H265 (= H226) binding malonyl-CoA; to Y: in MMAM; mut-
- E276 (= E237) to D: in MMAM; uncertain significance; mut-; dbSNP:rs12175488
- L281 (= L242) to S: in MMAM; mut0; dbSNP:rs796052007
- G284 (≠ A245) to E: in MMAM; mut0; dbSNP:rs879253835; to R: in MMAM; mut0; dbSNP:rs761477436
- S288 (≠ V249) to P: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1179778233
- G291 (≠ L252) to E: in MMAM; mut0
- Q293 (≠ A254) to P: in MMAM; mut0
- RLS 304:306 (= RLS 265:267) binding malonyl-CoA
- L305 (= L266) to S: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554160246
- S306 (= S267) to F: in MMAM; mut0; dbSNP:rs1085307929
- W309 (≠ F270) to G: in MMAM; decreased protein expression
- G312 (= G273) to V: in MMAM; mut0; dbSNP:rs864309734
- Y316 (= Y277) 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 (= A285) to T: in MMAM; mut-; dbSNP:rs780387525
- R326 (= R287) to K: in MMAM; uncertain significance; dbSNP:rs758577372
- L328 (= L289) 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 (≠ A304) 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 (≠ A306) natural variant: Missing (in MMAM; mut0)
- L347 (= L307) to R: in MMAM; mut0; dbSNP:rs1026703654
- H350 (= H310) to Y: in MMAM; mut0; dbSNP:rs1407914109
- L358 (= L318) to P: in MMAM; mut0
- N366 (= N326) 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 (= R329) 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 (≠ V330) to P: in MMAM; mut0; dbSNP:rs368790885
- A377 (= A337) to E: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918250
- Q383 (= Q343) to H: in MMAM; mut0; to P: in MMAM; mut0
- H386 (= H346) to N: in MMAM; mut0; dbSNP:rs1554159937; to R: in MMAM; mut0; dbSNP:rs866933356
- T387 (= T347) 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 (= N348) to H: in MMAM; mut0; dbSNP:rs766010704; to K: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253840
- S389 (≠ A349) natural variant: Missing (in MMAM; mut0)
- I412 (≠ L372) natural variant: Missing (in MMAM; mut0)
- P424 (= P384) to L: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253842
- G426 (≠ A386) 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 (= G387) to D: in MMAM; mut0; dbSNP:rs753288303
- G454 (= G414) to E: in MMAM; mut0
- A499 (≠ E460) to T: in dbSNP:rs2229385
- I505 (≠ M466) to T: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- Q514 (= Q475) to E: in MMAM; uncertain significance; to K: in MMAM; decreased protein expression
- L518 (≠ I479) to P: in MMAM; mut0; dbSNP:rs864309738
- R532 (≠ A493) to H: in dbSNP:rs1141321
- A535 (≠ W496) 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 (= T527) to R: in MMAM; mut0
- F573 (≠ W534) 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 (= Y549) to C: in MMAM; mut-
- I597 (≠ W559) to R: in MMAM; no changed in protein expression; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554158951
- P615 (= P577) 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 (= R578) to C: in MMAM; mut0; dbSNP:rs765284825
- L617 (≠ I579) to R: in MMAM; mut0; dbSNP:rs1554158775
- K621 (= K583) to N: in MMAM; mut0
- G623 (= G585) to R: in MMAM; mut0; dbSNP:rs121918254
- Q624 (= Q586) to R: in MMAM; no effect on protein abundance; dbSNP:rs768521956
- D625 (= D587) 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 (= G588) to C: in MMAM; mut-; dbSNP:rs982110849
- H627 (= H589) binding axial binding residue; to R: in MMAM; mut0; dbSNP:rs372486357
- G630 (= G592) to E: in MMAM; mut0; dbSNP:rs143023066
- V633 (= V595) 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 (≠ A599) to E: in MMAM; mut-; to R: in MMAM; mut0; dbSNP:rs781501004
- F638 (≠ L600) to I: in MMAM; mut0
- D640 (= D602) to Y: in MMAM; mut0; dbSNP:rs865815395
- G642 (= G604) to R: in MMAM; mut-; dbSNP:rs747897332
- G648 (≠ L610) 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 (= V631) to E: in MMAM; mut0; dbSNP:rs1360470463
- I671 (≠ V633) to V: in dbSNP:rs8589
- L674 (= L636) to F: in MMAM; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1164271240
- H678 (= H640) to R: in MMAM; mut-; dbSNP:rs147094927
- E684 (≠ G646) natural variant: E -> EL (in MMAM; mut-)
- L685 (= L647) 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 (≠ V661) 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-)
- 50 binding malonyl-CoA
- 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)
49% identity, 95% coverage: 26:701/713 of query aligns to 31:708/708 of 8dyjB
- binding adenosine-5'-diphosphate: Y74 (= Y71), T151 (= T148), R192 (= R189), Y228 (= Y225), H229 (= H226), F272 (= F269), Q316 (= Q312), N352 (= N348), E356 (= E352), L360 (= L356), P361 (= P357)
- binding cobalamin: F102 (= F99), L104 (= L101), H107 (≠ Q104), A124 (= A121), V191 (= V188), R192 (= R189), H229 (= H226), E232 (= E229), G319 (= G315), W320 (= W316), E356 (= E352), G359 (≠ A355), L360 (= L356), G590 (= G588), H591 (= H589), D592 (= D590), R593 (= R591), G594 (= G592), I598 (≠ V596), S636 (= S634), L638 (= L636), A640 (≠ G638), G666 (= G663), G667 (= G664), V668 (≠ I665), F686 (= F683), G687 (= G684), T690 (= T687)
6oxdA Structure of mycobacterium tuberculosis methylmalonyl-coa mutase with adenosyl cobalamin (see paper)
52% identity, 93% coverage: 43:702/713 of query aligns to 72:731/736 of 6oxdA
- active site: Y100 (= Y71), Y254 (= Y225), H255 (= H226), K610 (= K583), D614 (= D587), H616 (= H589)
- binding cobalamin: Y100 (= Y71), L130 (= L101), H133 (≠ Q104), A150 (= A121), R218 (= R189), E258 (= E229), G344 (= G315), W345 (= W316), E381 (= E352), A382 (= A353), A384 (= A355), L385 (= L356), G615 (= G588), H616 (= H589), D617 (= D590), R618 (= R591), S661 (= S634), L663 (= L636), A665 (≠ G638), G691 (= G663), G692 (= G664), F711 (= F683), P712 (≠ G684), T715 (= T687)
- binding Itaconyl coenzyme A: Y86 (= Y57), T88 (≠ S59), M89 (= M60), Q93 (≠ R64), T96 (= T67), R98 (= R69), Y100 (= Y71), S175 (= S146), T177 (= T148), T206 (= T177), R218 (= R189), H255 (= H226), R294 (= R265), S296 (= S267), F298 (= F269), R337 (= R308), T338 (≠ M309), H339 (= H310), Q341 (= Q312), Q372 (= Q343)
8gjuJ Crystal structure of human methylmalonyl-coa mutase (mmut) in complex with methylmalonic acidemia type a protein (mmaa), coenzyme a, and gdp (see paper)
48% identity, 95% coverage: 26:704/713 of query aligns to 32:689/689 of 8gjuJ
- binding coenzyme a: Y61 (= Y57), T63 (≠ S59), R68 (= R64), T71 (= T67), R73 (= R69), S150 (= S146), T152 (= T148), T181 (= T177), Q183 (= Q179), N222 (= N218), R269 (= R265), S271 (= S267), R313 (= R308), A314 (≠ M309), H315 (= H310), Q348 (= Q343)
P11653 Methylmalonyl-CoA mutase large subunit; MCM-alpha; EC 5.4.99.2 from Propionibacterium freudenreichii subsp. shermanii (see 4 papers)
48% identity, 96% coverage: 23:705/713 of query aligns to 41:724/728 of P11653
- Y75 (= Y57) binding (R)-methylmalonyl-CoA
- M78 (= M60) binding (R)-methylmalonyl-CoA
- R82 (= R64) binding (R)-methylmalonyl-CoA
- T85 (= T67) binding (R)-methylmalonyl-CoA
- R87 (= R69) binding (R)-methylmalonyl-CoA
- Y89 (= Y71) binding (R)-methylmalonyl-CoA; mutation to F: Does not significantly affect affinity for succiny-CoA, but kcat is lowered about 580-fold.
- S114 (= S96) binding (R)-methylmalonyl-CoA
- F117 (= F99) binding cob(II)alamin
- A139 (= A121) binding cob(II)alamin
- T195 (= T177) binding (R)-methylmalonyl-CoA
- Q197 (= Q179) binding (R)-methylmalonyl-CoA
- V206 (= V188) binding cob(II)alamin
- R207 (= R189) binding (R)-methylmalonyl-CoA; binding cob(II)alamin
- H244 (= H226) binding (R)-methylmalonyl-CoA
- R283 (= R265) binding (R)-methylmalonyl-CoA
- S285 (= S267) binding (R)-methylmalonyl-CoA
- G333 (= G315) binding cob(II)alamin
- E370 (= E352) binding cob(II)alamin
- A373 (= A355) binding cob(II)alamin
- G609 (= G588) binding cob(II)alamin
- H610 (= H589) binding axial binding residue
- D611 (= D590) binding cob(II)alamin
- R612 (= R591) binding cob(II)alamin
- S655 (= S634) binding cob(II)alamin
- L657 (= L636) binding cob(II)alamin
- G686 (= G664) binding cob(II)alamin
- T709 (= T687) binding cob(II)alamin
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
7reqA Methylmalonyl-coa mutase, 2-carboxypropyl-coa inhibitor complex (see paper)
48% identity, 96% coverage: 23:705/713 of query aligns to 38:721/725 of 7reqA
- active site: Y86 (= Y71), Y240 (= Y225), H241 (= H226), K601 (= K583), D605 (= D587), H607 (= H589)
- binding 2-carboxypropyl-coenzyme a: Y72 (= Y57), T74 (≠ S59), M75 (= M60), F78 (≠ D63), R79 (= R64), T82 (= T67), R84 (= R69), Y86 (= Y71), S161 (= S146), T163 (= T148), T192 (= T177), R204 (= R189), H241 (= H226), R280 (= R265), S282 (= S267), F284 (= F269), H325 (= H310), Q358 (= Q343)
- binding cobalamin: Y86 (= Y71), L116 (= L101), A136 (= A121), R204 (= R189), E244 (= E229), G330 (= G315), W331 (= W316), E367 (= E352), A368 (= A353), A370 (= A355), G606 (= G588), H607 (= H589), D608 (= D590), R609 (= R591), G610 (= G592), I614 (≠ V596), S652 (= S634), L654 (= L636), G682 (= G663), G683 (= G664), Y702 (≠ F683), T703 (≠ G684), T706 (= T687)
3reqA Methylmalonyl-coa mutase, substrate-free state (poor quality structure) (see paper)
48% identity, 96% coverage: 23:705/713 of query aligns to 38:721/725 of 3reqA
- active site: Y86 (= Y71), Y240 (= Y225), H241 (= H226), K601 (= K583), D605 (= D587), H607 (= H589)
- binding adenosine: Y86 (= Y71), Y240 (= Y225), E244 (= E229), G330 (= G315)
- binding cobalamin: L116 (= L101), V203 (= V188), R204 (= R189), E244 (= E229), G330 (= G315), W331 (= W316), A368 (= A353), G606 (= G588), H607 (= H589), D608 (= D590), R609 (= R591), G610 (= G592), I614 (≠ V596), G650 (= G632), S652 (= S634), L654 (= L636), 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)
48% identity, 96% coverage: 23:705/713 of query aligns to 38:721/725 of 2reqA
- active site: Y86 (= Y71), Y240 (= Y225), H241 (= H226), K601 (= K583), D605 (= D587), H607 (= H589)
- binding cobalamin: V203 (= V188), R204 (= R189), E244 (= E229), A245 (= A230), W331 (= W316), A368 (= A353), G606 (= G588), H607 (= H589), D608 (= D590), R609 (= R591), G610 (= G592), I614 (≠ V596), G650 (= G632), S652 (= S634), L654 (= L636), A655 (≠ S637), G682 (= G663), G683 (= G664), Y702 (≠ F683), T703 (≠ G684), T706 (= T687)
- binding coenzyme a: Y72 (= Y57), R79 (= R64), K318 (≠ R303)
4reqA Methylmalonyl-coa mutase substrate complex (see paper)
48% identity, 96% coverage: 23:705/713 of query aligns to 39:722/726 of 4reqA
- active site: Y87 (= Y71), Y241 (= Y225), H242 (= H226), K602 (= K583), D606 (= D587), H608 (= H589)
- binding cobalamin: Y87 (= Y71), L117 (= L101), A137 (= A121), V204 (= V188), R205 (= R189), H242 (= H226), E245 (= E229), G331 (= G315), W332 (= W316), E368 (= E352), A369 (= A353), A371 (= A355), L372 (= L356), G607 (= G588), H608 (= H589), D609 (= D590), R610 (= R591), G611 (= G592), I615 (≠ V596), S653 (= S634), L655 (= L636), G683 (= G663), G684 (= G664), V685 (≠ I665), Y703 (≠ F683), T704 (≠ G684), T707 (= T687)
- binding methylmalonyl-coenzyme a: Y73 (= Y57), M76 (= M60), F79 (≠ D63), R80 (= R64), T83 (= T67), R85 (= R69), Y87 (= Y71), S112 (= S96), S162 (= S146), T164 (= T148), T193 (= T177), R205 (= R189), N234 (= N218), Y241 (= Y225), H242 (= H226), R281 (= R265), S283 (= S267), F285 (= F269), H326 (= H310), Q328 (= Q312), Q359 (= Q343), S360 (= S344)
- binding succinyl-coenzyme a: Y73 (= Y57), M76 (= M60), F79 (≠ D63), R80 (= R64), T83 (= T67), R85 (= R69), Y87 (= Y71), S162 (= S146), T164 (= T148), T193 (= T177), Q195 (= Q179), R205 (= R189), N234 (= N218), Y241 (= Y225), H242 (= H226), R281 (= R265), S283 (= S267), F285 (= F269), R324 (= R308), H326 (= H310), Q359 (= Q343)
6reqA Methylmalonyl-coa mutase, 3-carboxypropyl-coa inhibitor complex (see paper)
48% identity, 96% coverage: 23:705/713 of query aligns to 40:723/727 of 6reqA
- active site: Y88 (= Y71), Y242 (= Y225), H243 (= H226), K603 (= K583), D607 (= D587), H609 (= H589)
- binding 3-carboxypropyl-coenzyme a: Y74 (= Y57), T76 (≠ S59), M77 (= M60), F80 (≠ D63), R81 (= R64), T84 (= T67), R86 (= R69), Y88 (= Y71), S113 (= S96), S163 (= S146), T165 (= T148), T194 (= T177), R206 (= R189), H243 (= H226), R282 (= R265), S284 (= S267), F286 (= F269), H327 (= H310), Q329 (= Q312), Q360 (= Q343)
- binding cobalamin: Y88 (= Y71), F116 (= F99), L118 (= L101), H121 (≠ Q104), A138 (= A121), R206 (= R189), E246 (= E229), G332 (= G315), W333 (= W316), E369 (= E352), A370 (= A353), A372 (= A355), G608 (= G588), H609 (= H589), D610 (= D590), R611 (= R591), G612 (= G592), I616 (≠ V596), Y620 (≠ L600), S654 (= S634), L656 (= L636), G658 (= G638), G684 (= G663), G685 (= G664), Y704 (≠ F683), T705 (≠ G684), T708 (= T687)
5reqA Methylmalonyl-coa mutase, y89f mutant, substrate complex (see paper)
48% identity, 96% coverage: 23:705/713 of query aligns to 38:721/725 of 5reqA
- active site: F86 (≠ Y71), Y240 (= Y225), H241 (= H226), K601 (= K583), D605 (= D587), H607 (= H589)
- binding cobalamin: L116 (= L101), A136 (= A121), R204 (= R189), H241 (= H226), E244 (= E229), G330 (= G315), W331 (= W316), E367 (= E352), A368 (= A353), A370 (= A355), G606 (= G588), H607 (= H589), D608 (= D590), R609 (= R591), G610 (= G592), I614 (≠ V596), S652 (= S634), L654 (= L636), G682 (= G663), G683 (= G664), V684 (≠ I665), Y702 (≠ F683), T703 (≠ G684), T706 (= T687)
- binding methylmalonyl(carbadethia)-coenzyme a: Y72 (= Y57), T74 (≠ S59), M75 (= M60), R79 (= R64), T82 (= T67), R84 (= R69), F86 (≠ Y71), S111 (= S96), S161 (= S146), T163 (= T148), T192 (= T177), Q194 (= Q179), R204 (= R189), N233 (= N218), H241 (= H226), R280 (= R265), S282 (= S267), F284 (= F269), T324 (≠ M309), H325 (= H310), Q358 (= Q343), S359 (= S344)
- binding succinyl(carbadethia)-coenzyme a: Y72 (= Y57), T74 (≠ S59), M75 (= M60), R79 (= R64), T82 (= T67), R84 (= R69), F86 (≠ Y71), S161 (= S146), T163 (= T148), T192 (= T177), R204 (= R189), N233 (= N218), H241 (= H226), R280 (= R265), S282 (= S267), F284 (= F269), H325 (= H310), Q358 (= Q343)
1e1cA Methylmalonyl-coa mutase h244a mutant (see paper)
48% identity, 96% coverage: 23:705/713 of query aligns to 40:723/727 of 1e1cA
- active site: Y88 (= Y71), Y242 (= Y225), A243 (≠ H226), K603 (= K583), D607 (= D587), H609 (= H589)
- binding cobalamin: Y88 (= Y71), L118 (= L101), H121 (≠ Q104), A138 (= A121), V205 (= V188), R206 (= R189), E246 (= E229), G332 (= G315), W333 (= W316), E369 (= E352), A370 (= A353), A372 (= A355), L373 (= L356), G608 (= G588), H609 (= H589), D610 (= D590), R611 (= R591), G612 (= G592), I616 (≠ V596), Y620 (≠ L600), S654 (= S634), L656 (= L636), G684 (= G663), G685 (= G664), V686 (≠ I665), Y704 (≠ F683), T705 (≠ G684), T708 (= T687), S713 (≠ A695)
- binding desulfo-coenzyme a: Y74 (= Y57), M77 (= M60), F80 (≠ D63), R81 (= R64), T84 (= T67), R86 (= R69), S113 (= S96), S163 (= S146), T165 (= T148), T194 (= T177), R282 (= R265), S284 (= S267), H327 (= H310), Q360 (= Q343)
4r3uA Crystal structure of 2-hydroxyisobutyryl-coa mutase (see paper)
39% identity, 71% coverage: 27:534/713 of query aligns to 44:552/557 of 4r3uA
- active site: I89 (≠ Y71), Y243 (= Y225), H244 (= H226)
- binding 3-hydroxybutanoyl-coenzyme a: Y75 (= Y57), T77 (≠ S59), M78 (= M60), R82 (= R64), T85 (= T67), R87 (= R69), I89 (≠ Y71), D116 (≠ A98), S164 (= S146), T166 (= T148), T195 (= T177), Q197 (= Q179), R234 (= R216), N236 (= N218), N239 (≠ S221), Y243 (= Y225), H244 (= H226), R283 (= R265), F287 (= F269), R327 (= R308), F328 (≠ M309), H329 (= H310), Q331 (= Q312), Q362 (= Q343)
- 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 (= Y57), T77 (≠ S59), M78 (= M60), R82 (= R64), T85 (= T67), R87 (= R69), I89 (≠ Y71), D116 (≠ A98), S164 (= S146), T166 (= T148), T195 (= T177), Q197 (= Q179), R234 (= R216), N236 (= N218), N239 (≠ S221), H244 (= H226), R283 (= R265), F287 (= F269), R327 (= R308), F328 (≠ M309), H329 (= H310), Q331 (= Q312), Q362 (= Q343)
- binding cobalamin: D116 (≠ A98), M119 (≠ L101), E139 (≠ A121), Q207 (≠ R189), E209 (≠ T191), E247 (= E229), A334 (≠ G315), E371 (= E352), A372 (= A353), A374 (= A355)
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)
39% identity, 71% coverage: 27:534/713 of query aligns to 45:553/562 of I3VE77
- YPTM 76:79 (≠ YASM 57:60) binding (3S)-3-hydroxybutanoyl-CoA
- TMR 86:88 (≠ TIR 67:69) binding (3S)-3-hydroxybutanoyl-CoA
- I90 (≠ Y71) 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 (≠ A98) 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 177:179) binding (3S)-3-hydroxybutanoyl-CoA
- R235 (= R216) binding (3S)-3-hydroxybutanoyl-CoA
- N240 (≠ S221) binding (3S)-3-hydroxybutanoyl-CoA
- H245 (= H226) binding (3S)-3-hydroxybutanoyl-CoA
- R284 (= R265) binding (3S)-3-hydroxybutanoyl-CoA
4xc6A Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, and mg (holo-icmf/gdp) (see paper)
35% identity, 69% coverage: 45:533/713 of query aligns to 547:1059/1067 of 4xc6A
- active site: F572 (≠ Y71), Y753 (= Y225), H754 (= H226)
- binding cobalamin: F601 (= F99), L606 (≠ Q104), S624 (≠ A121), Q716 (≠ R189), H754 (= H226), E757 (= E229), A758 (= A230), G842 (= G315), R843 (≠ W316), E879 (= E352), A880 (= A353), T882 (≠ A355), H967 (≠ D440)
- binding guanosine-5'-diphosphate: E947 (= E420)
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
8sslA Isobutyryl-coa mutase fused q341a in the presence of gtp (see paper)
35% identity, 69% coverage: 45:533/713 of query aligns to 552:1064/1072 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
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)
35% identity, 69% coverage: 45:533/713 of query aligns to 573:1085/1093 of Q1LRY0
- F587 (≠ S59) binding substrate
- F598 (≠ Y71) 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 (≠ G94) binding substrate
- R728 (≠ G175) binding substrate
- Y772 (≠ N218) binding substrate
- S821 (= S267) binding substrate
- R856 (= R303) binding substrate
- K861 (≠ R308) binding substrate
- E973 (= E420) 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
Q5KUG0 Fused isobutyryl-CoA mutase; EC 5.4.99.13; EC 3.6.5.- from Geobacillus kaustophilus (strain HTA426) (see paper)
33% identity, 69% coverage: 45:533/713 of query aligns to 564:1078/1086 of Q5KUG0
Sites not aligning to the query:
- 213 K→A: Loss of GTPase and ATPase activities. No effect on the mutase activity.
5cjwA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate pivalyl-coenzyme a (see paper)
35% identity, 69% coverage: 45:533/713 of query aligns to 546:1055/1063 of 5cjwA
- active site: F571 (≠ Y71), Y752 (= Y225), H753 (= H226)
- binding pivalyl-coenzyme A: F558 (≠ Y57), F560 (≠ S59), R562 (≠ Y61), R569 (= R69), F571 (≠ Y71), R595 (≠ G94), S650 (= S146), T652 (= T148), R701 (≠ G175), T703 (= T177), Q705 (= Q179), Y745 (≠ N218), Y752 (= Y225), H753 (= H226), S794 (= S267), F796 (= F269), R829 (= R303), K834 (≠ R308), H836 (= H310)
- binding cobalamin: F600 (= F99), L605 (≠ Q104), S623 (≠ A121), Q715 (≠ R189), H753 (= H226), E756 (= E229), A757 (= A230), G841 (= G315), R842 (≠ W316), E878 (= E352), A879 (= A353), T881 (≠ A355), H966 (≠ D440)
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
Query Sequence
>WP_011880186.1 NCBI__GCF_000016205.1:WP_011880186.1
MNEAAIMAPDTEVERVGPNDRRARTVPLRKLYTQRDLEAVAHLGSMPGAWPYVRGPYASM
YTDRPWTIRQYTGHADAADSNLAFRTALEQGAQGLSVAFDLATQRGYDSDCVEAWADVGV
AGVAIDTADDMVRLFDGIALDATTVSMTMNGAVLPIMAAFVVVAEEQGVPPERIGGTIQN
DILKEYMVRNTWIFGPAPSMRIVADVALWLAEHAPRFNALSVSGYHFQEAGADAVLELAL
TLSNARAYVDTLAARGMPADEACSRLSFFFGVGSDFYTEIAKLRAARLLWAEIAHACGAR
SPRACALRMHCQTSGWSLTAQEAENNIVRVTAQAMAAAFGGTQSLHTNAYDEALALPSAA
AARLARNTQLILQHETGLCDTVDPWAGSYMMESLTDDIATRVRAELAAIDAQGGVIAAIE
SGWVKRRLLHAAAKTQAQVDSGRRTVVGVNRFVASDPTDEFTVREMDGRHVRAGQARRIA
AVKAARDPARVEAALWRLANAARDGGGNLLALAIDCMRARATVGECTRALESVWPRHTAA
VEANGAGAYGDHRRGDAAWRAAKGCVGRLAQRAGRRPRIVIAKLGQDGHDRGAAVVAAAL
EDAGFDVLRLPLFQQPICVAAAVQAYGADIVGVSSLSGGHRELVEGLLDELASLRAGIPV
VLGGIFPAADARHLKAKGVAASFGPGTPLDAIVEALCACIERARCVHPADHVG
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