SitesBLAST
Comparing YP_428144.1 NCBI__GCF_000013085.1:YP_428144.1 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)
36% identity, 95% coverage: 9:647/671 of query aligns to 95:724/750 of P22033
- P95 (= P9) to R: in MMAM; mut0; dbSNP:rs190834116
- YPTM 96:99 (≠ KPKL 10:13) binding malonyl-CoA
- Y100 (≠ Q14) 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 (= W20) to R: in MMAM; mut0; dbSNP:rs121918249
- TIRQY 106:110 (≠ LFRTY 21:25) binding malonyl-CoA
- R108 (= R23) to C: in MMAM; mut0; dbSNP:rs121918257; to G: in MMAM; mut-; to H: in MMAM; mut0; dbSNP:rs483352778
- Q109 (≠ T24) to R: in MMAM; mut0; dbSNP:rs1461110052
- G133 (= G48) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253828
- A137 (= A52) to V: in MMAM; mut0; dbSNP:rs941483851
- D139 (= D54) to N: in MMAM; uncertain significance; dbSNP:rs879253829
- L140 (= L55) to P: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- A141 (≠ P56) to T: in MMAM; decreased protein expression; dbSNP:rs1554160730
- H143 (≠ Q58) to Y: in MMAM; mut0
- G145 (= G60) to S: in MMAM; mut0
- S148 (= S63) to L: in MMAM; mut0; dbSNP:rs1300547552
- D156 (≠ E71) to N: in MMAM; mut-
- G158 (= G73) to V: in MMAM; mut0
- G161 (= G76) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; to V: in MMAM; decreased protein expression
- F174 (= F89) to S: in MMAM; mut0; dbSNP:rs864309733
- M186 (= M101) to V: in MMAM; mut-; dbSNP:rs148331800
- T187 (= T102) to S: in MMAM; mut0; dbSNP:rs879253830
- N189 (= N104) to I: in MMAM; mut-; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs200908035; to K: in MMAM; mut-; dbSNP:rs1561959114
- A191 (≠ P106) to E: in MMAM; mut- and mut0; affects proper folding; reduced protein level; decreased methylmalonyl-CoA mutase activity; dbSNP:rs760782399
- A197 (= A112) to E: in MMAM; mut0
- G203 (≠ A118) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs778702777
- E205 (≠ R120) natural variant: Missing (in MMAM; mut0; dbSNP:rs879253831)
- G215 (= G130) to C: in MMAM; mut- and mut0; dbSNP:rs121918258; to S: in MMAM; mut0; dbSNP:rs121918258
- TIQ 216:218 (≠ TVQ 131:133) binding malonyl-CoA
- Q218 (= Q133) to H: in MMAM; mut0 and mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability; dbSNP:rs1446389693
- N219 (= N134) to Y: in MMAM; mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; dbSNP:rs121918256
- R228 (= R143) binding malonyl-CoA; to Q: in MMAM; mut0; dbSNP:rs770810987
- T230 (= T145) to I: in MMAM; mut-; to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253833
- Y231 (= Y146) 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 (= K170) binding malonyl-CoA
- S262 (≠ C177) to N: in MMAM; mut0
- H265 (= H180) binding malonyl-CoA; to Y: in MMAM; mut-
- E276 (= E191) to D: in MMAM; uncertain significance; mut-; dbSNP:rs12175488
- L281 (= L196) to S: in MMAM; mut0; dbSNP:rs796052007
- G284 (≠ A199) to E: in MMAM; mut0; dbSNP:rs879253835; to R: in MMAM; mut0; dbSNP:rs761477436
- S288 (≠ L203) to P: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1179778233
- G291 (vs. gap) to E: in MMAM; mut0
- Q293 (≠ K207) to P: in MMAM; mut0
- RLS 304:306 (≠ RIS 223:225) binding malonyl-CoA
- L305 (≠ I224) to S: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554160246
- S306 (= S225) to F: in MMAM; mut0; dbSNP:rs1085307929
- W309 (≠ V228) to G: in MMAM; decreased protein expression
- G312 (= G231) to V: in MMAM; mut0; dbSNP:rs864309734
- Y316 (≠ I235) 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 (= A243) to T: in MMAM; mut-; dbSNP:rs780387525
- R326 (≠ C245) to K: in MMAM; uncertain significance; dbSNP:rs758577372
- L328 (= L247) 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 (≠ F263) 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 (≠ R265) natural variant: Missing (in MMAM; mut0)
- L347 (≠ F266) to R: in MMAM; mut0; dbSNP:rs1026703654
- H350 (≠ G269) to Y: in MMAM; mut0; dbSNP:rs1407914109
- L358 (= L277) to P: in MMAM; mut0
- N366 (= N285) 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 (= R288) 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 (≠ I289) to P: in MMAM; mut0; dbSNP:rs368790885
- A377 (≠ V296) to E: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918250
- Q383 (≠ R305) to H: in MMAM; mut0; to P: in MMAM; mut0
- H386 (≠ Q308) to N: in MMAM; mut0; dbSNP:rs1554159937; to R: in MMAM; mut0; dbSNP:rs866933356
- T387 (≠ L309) 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 (≠ P310) to H: in MMAM; mut0; dbSNP:rs766010704; to K: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253840
- S389 (≠ A311) natural variant: Missing (in MMAM; mut0)
- I412 (≠ V334) natural variant: Missing (in MMAM; mut0)
- P424 (≠ I346) to L: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253842
- G426 (≠ D348) 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 (= G349) to D: in MMAM; mut0; dbSNP:rs753288303
- G454 (= G376) to E: in MMAM; mut0
- A499 (≠ P421) to T: in dbSNP:rs2229385
- I505 (≠ V432) to T: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- Q514 (= Q440) to E: in MMAM; uncertain significance; to K: in MMAM; decreased protein expression
- L518 (= L444) to P: in MMAM; mut0; dbSNP:rs864309738
- R532 (≠ A458) to H: in dbSNP:rs1141321
- A535 (≠ D461) to P: in MMAM; mut0; dbSNP:rs760183775
- A552 (≠ T477) to V: in MMAM; uncertain significance; dbSNP:rs879253845
- C560 (≠ V485) to Y: in MMAM; mut0; dbSNP:rs1238333040
- T566 (≠ S491) to R: in MMAM; mut0
- F573 (= F498) 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 (≠ A512) to C: in MMAM; mut-
- I597 (≠ L520) to R: in MMAM; no changed in protein expression; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554158951
- P615 (≠ L538) 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 (≠ K539) to C: in MMAM; mut0; dbSNP:rs765284825
- L617 (≠ I540) to R: in MMAM; mut0; dbSNP:rs1554158775
- K621 (= K544) to N: in MMAM; mut0
- G623 (= G546) to R: in MMAM; mut0; dbSNP:rs121918254
- Q624 (≠ L547) to R: in MMAM; no effect on protein abundance; dbSNP:rs768521956
- D625 (= D548) 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 (= G549) to C: in MMAM; mut-; dbSNP:rs982110849
- H627 (= H550) binding axial binding residue; to R: in MMAM; mut0; dbSNP:rs372486357
- G630 (= G553) to E: in MMAM; mut0; dbSNP:rs143023066
- V633 (≠ Q556) 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 (≠ R560) to E: in MMAM; mut-; to R: in MMAM; mut0; dbSNP:rs781501004
- F638 (≠ A561) to I: in MMAM; mut0
- D640 (= D563) to Y: in MMAM; mut0; dbSNP:rs865815395
- G642 (= G565) to R: in MMAM; mut-; dbSNP:rs747897332
- G648 (≠ E571) 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 (= V592) to E: in MMAM; mut0; dbSNP:rs1360470463
- I671 (≠ L594) to V: in dbSNP:rs8589
- L674 (= L597) to F: in MMAM; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1164271240
- H678 (= H601) to R: in MMAM; mut-; dbSNP:rs147094927
- E684 (≠ D607) natural variant: E -> EL (in MMAM; mut-)
- L685 (≠ V608) to R: in MMAM; mut-; dbSNP:rs864309739
- R694 (≠ L617) 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 (≠ I623) 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 (= G626) to R: in MMAM; mut0; dbSNP:rs121918255
- G717 (= G640) 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 (≠ T646) 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
- 69 I → V: in MMAM; likely benign; dbSNP:rs115923556
- 86 P → 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
- 87 G → E: in MMAM; mut0; dbSNP:rs1554160986
- 93 R → H: in MMAM; mut0; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918251
- 94 G → R: in MMAM; mut0; dbSNP:rs727504022; G → V: in MMAM; mut- and mut0; dbSNP:rs535411418
- 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)
36% identity, 95% coverage: 9:647/671 of query aligns to 60:689/714 of 2xiqA
- active site: Y75 (= Y25), Y229 (= Y179), H230 (= H180), K586 (= K544), D590 (= D548), H592 (= H550)
- binding cobalamin: Y75 (= Y25), L105 (= L55), H108 (≠ Q58), A125 (≠ V75), R193 (= R143), E233 (= E183), G320 (≠ S274), W321 (≠ L275), E357 (= E314), G360 (= G317), L361 (= L318), G591 (= G549), H592 (= H550), D593 (≠ S551), R594 (≠ N552), G595 (= G553), I599 (= I557), G635 (= G593), S637 (= S595), L639 (= L597), A641 (≠ G599), G667 (= G625), G668 (= G626), F687 (≠ Y645), G688 (≠ T646)
- binding malonyl-coenzyme a: Y61 (≠ K10), T63 (≠ K12), M64 (≠ L13), R68 (≠ K18), T71 (≠ L21), R73 (= R23), Y75 (= Y25), S150 (= S100), T152 (= T102), T181 (= T131), R193 (= R143), K220 (= K170), H230 (= H180), R269 (= R223), S271 (= S225), F273 (= F227), R313 (= R267), A314 (≠ Y268), H315 (≠ G269), Q317 (= Q271), Q348 (≠ R305)
Sites not aligning to the query:
8dyjB Crystal structure of human methylmalonyl-coa mutase in complex with adp and cob(ii)alamin (see paper)
36% identity, 95% coverage: 9:647/671 of query aligns to 59:688/708 of 8dyjB
- binding adenosine-5'-diphosphate: Y74 (= Y25), T151 (= T102), R192 (= R143), Y228 (= Y179), H229 (= H180), F272 (= F227), Q316 (= Q271), N352 (≠ P310), E356 (= E314), L360 (= L318), P361 (= P319)
- binding cobalamin: F102 (= F53), L104 (= L55), H107 (≠ Q58), A124 (≠ V75), V191 (≠ S142), R192 (= R143), H229 (= H180), E232 (= E183), G319 (≠ S274), W320 (≠ L275), E356 (= E314), G359 (= G317), L360 (= L318), G590 (= G549), H591 (= H550), D592 (≠ S551), R593 (≠ N552), G594 (= G553), I598 (= I557), S636 (= S595), L638 (= L597), A640 (≠ G599), G666 (= G625), G667 (= G626), V668 (≠ I627), F686 (≠ Y645), G687 (≠ T646)
Sites not aligning to the query:
6oxdA Structure of mycobacterium tuberculosis methylmalonyl-coa mutase with adenosyl cobalamin (see paper)
38% identity, 95% coverage: 9:647/671 of query aligns to 85:713/736 of 6oxdA
- active site: Y100 (= Y25), Y254 (= Y179), H255 (= H180), K610 (= K544), D614 (= D548), H616 (= H550)
- binding cobalamin: Y100 (= Y25), L130 (= L55), H133 (≠ Q58), A150 (≠ V75), R218 (= R143), E258 (= E183), G344 (≠ S274), W345 (≠ L275), E381 (= E314), A382 (= A315), A384 (≠ G317), L385 (= L318), G615 (= G549), H616 (= H550), D617 (≠ S551), R618 (≠ N552), S661 (= S595), L663 (= L597), A665 (≠ G599), G691 (= G625), G692 (= G626), F711 (≠ Y645), P712 (≠ T646)
- binding Itaconyl coenzyme A: Y86 (≠ K10), T88 (≠ K12), M89 (≠ L13), Q93 (≠ K18), T96 (≠ L21), R98 (= R23), Y100 (= Y25), S175 (= S100), T177 (= T102), T206 (= T131), R218 (= R143), H255 (= H180), R294 (= R223), S296 (= S225), F298 (= F227), R337 (= R267), T338 (≠ Y268), H339 (≠ G269), Q341 (= Q271), Q372 (≠ R305)
Sites not aligning to the query:
6reqA Methylmalonyl-coa mutase, 3-carboxypropyl-coa inhibitor complex (see paper)
37% identity, 94% coverage: 18:647/671 of query aligns to 81:706/727 of 6reqA
- active site: Y88 (= Y25), Y242 (= Y179), H243 (= H180), K603 (= K544), D607 (= D548), H609 (= H550)
- binding 3-carboxypropyl-coenzyme a: R81 (≠ K18), T84 (≠ L21), R86 (= R23), Y88 (= Y25), S113 (= S50), S163 (= S100), T165 (= T102), T194 (= T131), R206 (= R143), H243 (= H180), R282 (= R223), S284 (= S225), F286 (= F227), H327 (≠ G269), Q329 (= Q271), Q360 (≠ R305)
- binding cobalamin: Y88 (= Y25), F116 (= F53), L118 (= L55), H121 (≠ Q58), A138 (≠ V75), R206 (= R143), E246 (= E183), G332 (≠ S274), W333 (≠ L275), E369 (= E314), A370 (= A315), A372 (≠ G317), G608 (= G549), H609 (= H550), D610 (≠ S551), R611 (≠ N552), G612 (= G553), I616 (= I557), Y620 (≠ A561), S654 (= S595), L656 (= L597), G658 (= G599), G684 (= G625), G685 (= G626), Y704 (= Y645), T705 (= T646)
Sites not aligning to the query:
P11653 Methylmalonyl-CoA mutase large subunit; MCM-alpha; EC 5.4.99.2 from Propionibacterium freudenreichii subsp. shermanii (see 4 papers)
37% identity, 94% coverage: 18:647/671 of query aligns to 82:707/728 of P11653
- R82 (≠ K18) binding (R)-methylmalonyl-CoA
- T85 (≠ L21) binding (R)-methylmalonyl-CoA
- R87 (= R23) binding (R)-methylmalonyl-CoA
- Y89 (= Y25) binding (R)-methylmalonyl-CoA; mutation to F: Does not significantly affect affinity for succiny-CoA, but kcat is lowered about 580-fold.
- S114 (= S50) binding (R)-methylmalonyl-CoA
- F117 (= F53) binding cob(II)alamin
- A139 (≠ V75) binding cob(II)alamin
- T195 (= T131) binding (R)-methylmalonyl-CoA
- Q197 (= Q133) binding (R)-methylmalonyl-CoA
- V206 (≠ S142) binding cob(II)alamin
- R207 (= R143) binding (R)-methylmalonyl-CoA; binding cob(II)alamin
- H244 (= H180) binding (R)-methylmalonyl-CoA
- R283 (= R223) binding (R)-methylmalonyl-CoA
- S285 (= S225) binding (R)-methylmalonyl-CoA
- G333 (≠ S274) binding cob(II)alamin
- E370 (= E314) binding cob(II)alamin
- A373 (≠ G317) binding cob(II)alamin
- G609 (= G549) binding cob(II)alamin
- H610 (= H550) binding axial binding residue
- D611 (≠ S551) binding cob(II)alamin
- R612 (≠ N552) binding cob(II)alamin
- S655 (= S595) binding cob(II)alamin
- L657 (= L597) binding cob(II)alamin
- G686 (= G626) binding cob(II)alamin
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 75 binding (R)-methylmalonyl-CoA
- 78 binding (R)-methylmalonyl-CoA
- 709 binding cob(II)alamin
4reqA Methylmalonyl-coa mutase substrate complex (see paper)
37% identity, 94% coverage: 18:647/671 of query aligns to 80:705/726 of 4reqA
- active site: Y87 (= Y25), Y241 (= Y179), H242 (= H180), K602 (= K544), D606 (= D548), H608 (= H550)
- binding cobalamin: Y87 (= Y25), L117 (= L55), A137 (≠ V75), V204 (≠ S142), R205 (= R143), H242 (= H180), E245 (= E183), G331 (≠ S274), W332 (≠ L275), E368 (= E314), A369 (= A315), A371 (≠ G317), L372 (= L318), G607 (= G549), H608 (= H550), D609 (≠ S551), R610 (≠ N552), G611 (= G553), I615 (= I557), S653 (= S595), L655 (= L597), G683 (= G625), G684 (= G626), V685 (≠ I627), Y703 (= Y645), T704 (= T646)
- binding methylmalonyl-coenzyme a: R80 (≠ K18), T83 (≠ L21), R85 (= R23), Y87 (= Y25), S112 (= S50), S162 (= S100), T164 (= T102), T193 (= T131), R205 (= R143), N234 (= N172), Y241 (= Y179), H242 (= H180), R281 (= R223), S283 (= S225), F285 (= F227), H326 (≠ G269), Q328 (= Q271), Q359 (≠ R305), S360 (≠ A306)
- binding succinyl-coenzyme a: R80 (≠ K18), T83 (≠ L21), R85 (= R23), Y87 (= Y25), S162 (= S100), T164 (= T102), T193 (= T131), Q195 (= Q133), R205 (= R143), N234 (= N172), Y241 (= Y179), H242 (= H180), R281 (= R223), S283 (= S225), F285 (= F227), R324 (= R267), H326 (≠ G269), Q359 (≠ R305)
Sites not aligning to the query:
7reqA Methylmalonyl-coa mutase, 2-carboxypropyl-coa inhibitor complex (see paper)
37% identity, 94% coverage: 18:647/671 of query aligns to 79:704/725 of 7reqA
- active site: Y86 (= Y25), Y240 (= Y179), H241 (= H180), K601 (= K544), D605 (= D548), H607 (= H550)
- binding 2-carboxypropyl-coenzyme a: R79 (≠ K18), T82 (≠ L21), R84 (= R23), Y86 (= Y25), S161 (= S100), T163 (= T102), T192 (= T131), R204 (= R143), H241 (= H180), R280 (= R223), S282 (= S225), F284 (= F227), H325 (≠ G269), Q358 (≠ R305)
- binding cobalamin: Y86 (= Y25), L116 (= L55), A136 (≠ V75), R204 (= R143), E244 (= E183), G330 (≠ S274), W331 (≠ L275), E367 (= E314), A368 (= A315), A370 (≠ G317), G606 (= G549), H607 (= H550), D608 (≠ S551), R609 (≠ N552), G610 (= G553), I614 (= I557), S652 (= S595), L654 (= L597), G682 (= G625), G683 (= G626), Y702 (= Y645), T703 (= T646)
Sites not aligning to the query:
3reqA Methylmalonyl-coa mutase, substrate-free state (poor quality structure) (see paper)
37% identity, 94% coverage: 18:647/671 of query aligns to 79:704/725 of 3reqA
- active site: Y86 (= Y25), Y240 (= Y179), H241 (= H180), K601 (= K544), D605 (= D548), H607 (= H550)
- binding adenosine: Y86 (= Y25), Y240 (= Y179), E244 (= E183), G330 (≠ S274)
- binding cobalamin: L116 (= L55), V203 (≠ S142), R204 (= R143), E244 (= E183), G330 (≠ S274), W331 (≠ L275), A368 (= A315), G606 (= G549), H607 (= H550), D608 (≠ S551), R609 (≠ N552), G610 (= G553), I614 (= I557), G650 (= G593), S652 (= S595), L654 (= L597), G682 (= G625), G683 (= G626), Y702 (= Y645), T703 (= T646), P704 (= P647)
Sites not aligning to the query:
2reqA Methylmalonyl-coa mutase, non-productive coa complex, in open conformation representing substrate-free state (see paper)
37% identity, 94% coverage: 18:647/671 of query aligns to 79:704/725 of 2reqA
- active site: Y86 (= Y25), Y240 (= Y179), H241 (= H180), K601 (= K544), D605 (= D548), H607 (= H550)
- binding cobalamin: V203 (≠ S142), R204 (= R143), E244 (= E183), A245 (= A184), W331 (≠ L275), A368 (= A315), G606 (= G549), H607 (= H550), D608 (≠ S551), R609 (≠ N552), G610 (= G553), I614 (= I557), G650 (= G593), S652 (= S595), L654 (= L597), A655 (≠ S598), G682 (= G625), G683 (= G626), Y702 (= Y645), T703 (= T646)
- binding coenzyme a: R79 (≠ K18), K318 (= K262)
Sites not aligning to the query:
5reqA Methylmalonyl-coa mutase, y89f mutant, substrate complex (see paper)
37% identity, 94% coverage: 18:647/671 of query aligns to 79:704/725 of 5reqA
- active site: F86 (≠ Y25), Y240 (= Y179), H241 (= H180), K601 (= K544), D605 (= D548), H607 (= H550)
- binding cobalamin: L116 (= L55), A136 (≠ V75), R204 (= R143), H241 (= H180), E244 (= E183), G330 (≠ S274), W331 (≠ L275), E367 (= E314), A368 (= A315), A370 (≠ G317), G606 (= G549), H607 (= H550), D608 (≠ S551), R609 (≠ N552), G610 (= G553), I614 (= I557), S652 (= S595), L654 (= L597), G682 (= G625), G683 (= G626), V684 (≠ I627), Y702 (= Y645), T703 (= T646)
- binding methylmalonyl(carbadethia)-coenzyme a: R79 (≠ K18), T82 (≠ L21), R84 (= R23), F86 (≠ Y25), S111 (= S50), S161 (= S100), T163 (= T102), T192 (= T131), Q194 (= Q133), R204 (= R143), N233 (= N172), H241 (= H180), R280 (= R223), S282 (= S225), F284 (= F227), T324 (≠ Y268), H325 (≠ G269), Q358 (≠ R305), S359 (≠ A306)
- binding succinyl(carbadethia)-coenzyme a: R79 (≠ K18), T82 (≠ L21), R84 (= R23), F86 (≠ Y25), S161 (= S100), T163 (= T102), T192 (= T131), R204 (= R143), N233 (= N172), H241 (= H180), R280 (= R223), S282 (= S225), F284 (= F227), H325 (≠ G269), Q358 (≠ R305)
Sites not aligning to the query:
1e1cA Methylmalonyl-coa mutase h244a mutant (see paper)
37% identity, 94% coverage: 18:647/671 of query aligns to 81:706/727 of 1e1cA
- active site: Y88 (= Y25), Y242 (= Y179), A243 (≠ H180), K603 (= K544), D607 (= D548), H609 (= H550)
- binding cobalamin: Y88 (= Y25), L118 (= L55), H121 (≠ Q58), A138 (≠ V75), V205 (≠ S142), R206 (= R143), E246 (= E183), G332 (≠ S274), W333 (≠ L275), E369 (= E314), A370 (= A315), A372 (≠ G317), L373 (= L318), G608 (= G549), H609 (= H550), D610 (≠ S551), R611 (≠ N552), G612 (= G553), I616 (= I557), Y620 (≠ A561), S654 (= S595), L656 (= L597), G684 (= G625), G685 (= G626), V686 (≠ I627), Y704 (= Y645), T705 (= T646)
- binding desulfo-coenzyme a: R81 (≠ K18), T84 (≠ L21), R86 (= R23), S113 (= S50), S163 (= S100), T165 (= T102), T194 (= T131), R282 (= R223), S284 (= S225), H327 (≠ G269), Q360 (≠ R305)
Sites not aligning to the query:
8gjuJ Crystal structure of human methylmalonyl-coa mutase (mmut) in complex with methylmalonic acidemia type a protein (mmaa), coenzyme a, and gdp (see paper)
35% identity, 95% coverage: 9:647/671 of query aligns to 60:666/689 of 8gjuJ
- binding coenzyme a: Y61 (≠ K10), T63 (≠ K12), R68 (≠ K18), T71 (≠ L21), R73 (= R23), S150 (= S100), T152 (= T102), T181 (= T131), Q183 (= Q133), N222 (= N172), R269 (= R223), S271 (= S225), R313 (= R267), A314 (≠ Y268), H315 (≠ G269), Q348 (≠ R305)
4r3uA Crystal structure of 2-hydroxyisobutyryl-coa mutase (see paper)
34% identity, 74% coverage: 9:502/671 of query aligns to 74:556/557 of 4r3uA
- active site: I89 (≠ Y25), Y243 (= Y179), H244 (= H180)
- binding 3-hydroxybutanoyl-coenzyme a: Y75 (≠ K10), T77 (≠ K12), M78 (≠ L13), R82 (≠ K18), T85 (≠ L21), R87 (= R23), I89 (≠ Y25), D116 (≠ A52), S164 (= S100), T166 (= T102), T195 (= T131), Q197 (= Q133), R234 (≠ K170), N236 (= N172), N239 (= N175), Y243 (= Y179), H244 (= H180), R283 (= R223), F287 (= F227), R327 (= R267), F328 (≠ Y268), H329 (≠ G269), Q331 (= Q271), Q362 (≠ R305)
- 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 (≠ K10), T77 (≠ K12), M78 (≠ L13), R82 (≠ K18), T85 (≠ L21), R87 (= R23), I89 (≠ Y25), D116 (≠ A52), S164 (= S100), T166 (= T102), T195 (= T131), Q197 (= Q133), R234 (≠ K170), N236 (= N172), N239 (= N175), H244 (= H180), R283 (= R223), F287 (= F227), R327 (= R267), F328 (≠ Y268), H329 (≠ G269), Q331 (= Q271), Q362 (≠ R305)
- binding cobalamin: D116 (≠ A52), M119 (≠ L55), E139 (≠ V75), Q207 (≠ R143), E209 (≠ T145), E247 (= E183), A334 (≠ S274), E371 (= E314), A372 (= A315), A374 (≠ G317)
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)
34% identity, 74% coverage: 9:502/671 of query aligns to 75:557/562 of I3VE77
- YPTM 76:79 (≠ KPKL 10:13) binding (3S)-3-hydroxybutanoyl-CoA
- TMR 86:88 (≠ LFR 21:23) binding (3S)-3-hydroxybutanoyl-CoA
- I90 (≠ Y25) 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 (≠ A52) 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 (= TVQ 131:133) binding (3S)-3-hydroxybutanoyl-CoA
- R235 (≠ K170) binding (3S)-3-hydroxybutanoyl-CoA
- N240 (= N175) binding (3S)-3-hydroxybutanoyl-CoA
- H245 (= H180) binding (3S)-3-hydroxybutanoyl-CoA
- R284 (= R223) binding (3S)-3-hydroxybutanoyl-CoA
8sslA Isobutyryl-coa mutase fused q341a in the presence of gtp (see paper)
28% identity, 72% coverage: 23:502/671 of query aligns to 575:1069/1072 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
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)
28% identity, 72% coverage: 23:502/671 of query aligns to 596:1090/1093 of Q1LRY0
- F598 (≠ Y25) 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 (≠ Q129) binding substrate
- Y772 (≠ N172) binding substrate
- S821 (= S225) binding substrate
- R856 (≠ K262) binding substrate
- K861 (≠ R267) binding substrate
- E973 (= E382) 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
- 587 binding substrate
- 1092 binding GTP
4xc6A Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, and mg (holo-icmf/gdp) (see paper)
28% identity, 72% coverage: 23:502/671 of query aligns to 570:1064/1067 of 4xc6A
- active site: F572 (≠ Y25), Y753 (= Y179), H754 (= H180)
- binding cobalamin: F601 (= F53), L606 (≠ Q58), S624 (≠ V75), Q716 (≠ R143), H754 (= H180), E757 (= E183), A758 (= A184), G842 (≠ S274), R843 (≠ L275), E879 (= E314), A880 (= A315), T882 (≠ G317), H967 (≠ E402)
- binding guanosine-5'-diphosphate: E947 (= E382)
Sites not aligning to the query:
- active site: 6
- binding cobalamin: 18, 19, 20, 21, 22, 26, 66, 67, 94, 96, 98, 116, 117, 118, 129
- binding guanosine-5'-diphosphate: 199, 201, 202, 203, 204, 245, 337, 338, 340, 375, 377
- binding magnesium ion: 203, 229, 242, 242, 290, 290
5cjtA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isobutyryl-coenzyme a (see paper)
28% identity, 72% coverage: 23:502/671 of query aligns to 567:1059/1062 of 5cjtA
- active site: F569 (≠ Y25), Y750 (= Y179), H751 (= H180)
- binding cobalamin: F598 (= F53), L603 (≠ Q58), S621 (≠ V75), Q713 (≠ R143), H751 (= H180), E754 (= E183), A755 (= A184), G839 (≠ S274), R840 (≠ L275), E876 (= E314), A877 (= A315), T879 (≠ G317), H964 (≠ E402)
- binding isobutyryl-coenzyme a: R567 (= R23), F569 (≠ Y25), R593 (vs. gap), S648 (vs. gap), T650 (= T102), R699 (≠ Q129), T701 (= T131), Q703 (= Q133), Y743 (≠ N172), Y750 (= Y179), H751 (= H180), S792 (= S225), F794 (= F227), R827 (≠ K262), K832 (≠ R267), H834 (≠ G269)
- binding guanosine-5'-diphosphate: E944 (= E382)
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 isobutyryl-coenzyme a: 556, 558, 560
- 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)
27% identity, 72% coverage: 23:502/671 of query aligns to 564:1050/1053 of 4xc7A
- active site: F566 (≠ Y25), Y747 (= Y179), H748 (= H180)
- binding Butyryl Coenzyme A: R564 (= R23), F566 (≠ Y25), R590 (vs. gap), S645 (vs. gap), T647 (= T102), R696 (≠ Q129), T698 (= T131), Y740 (≠ N172), S789 (= S225), F791 (= F227), R824 (≠ K262), K829 (≠ R267), H831 (≠ G269)
Sites not aligning to the query:
Query Sequence
>YP_428144.1 NCBI__GCF_000013085.1:YP_428144.1
MSGDAASTPKPKLQTRDKPWLFRTYSGHSSARASNALYRTNLARGQTGLSVAFDLPTQTG
YDSDHVLARGEVGKVGVPISHLGDMQTLFEGIPLEKMNTSMTINAPAPWLLALYVATAER
QGADRAALQGTVQNDLIKEYLSRGTYIFPPEPSLRLIGDVIAFTYREIPKWNPTNVCSYH
LQEAGATPEQELAFALATAIAVLDTVKAGGQVPEADFPEVVGRISFFVNAGIRFITEMCK
MRAFCDLWDEICLTRYGVTDEKFRRFRYGVQVNSLGLTEQQPENNVYRILLEMLAVVLSK
NARARAVQLPAWNEALGLPRPWDQQWSLRLQQIVAFETDLLDYGDIFDGSREIAAKVEEL
KTAARDELARIAAMGGAEAAVEAGYMKQKLVESNSRRIGGIESGEQIVVGVNKYTEGADS
PLVGGDGAIMTVDPAVEAEQIAALTAWKAARDAKDVGAALDGLRRAAAEGTNIMEPTIAC
AHAGVTTGEWSQTLREVFGEYRAPTGVGRAAAQPEAGGRLAEVRLRVDDLSTRLGRRLKI
LVGKPGLDGHSNGAEQIAVRARDSGMEVVYEGIRLTPAQIVNAALEESVHVVGLSILSGS
HVPLVSDVLDRMRAEGLADIPVIVGGIIPPEDEKILLAAGVARVYTPKDYDITAIMADIV
GIVDLTTRQAA
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