SitesBLAST
Comparing H281DRAFT_01038 FitnessBrowser__Burk376:H281DRAFT_01038 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)
47% identity, 97% coverage: 12:694/703 of query aligns to 32:709/714 of 2xiqA
- active site: Y75 (= Y57), Y229 (= Y211), H230 (= H212), K586 (= K568), D590 (= D572), H592 (= H574)
- binding cobalamin: Y75 (= Y57), L105 (= L87), H108 (≠ Q90), A125 (≠ T107), R193 (= R175), E233 (= E215), G320 (= G301), W321 (= W302), E357 (= E338), G360 (≠ S341), L361 (= L342), G591 (= G573), H592 (= H574), D593 (= D575), R594 (= R576), G595 (= G577), I599 (= I581), G635 (= G617), S637 (= S619), L639 (= L621), A641 (≠ G623), G667 (= G648), G668 (= G649), F687 (= F668), G688 (≠ P669), T691 (= T672)
- binding malonyl-coenzyme a: Y61 (≠ F43), T63 (≠ S45), M64 (= M46), R68 (≠ K50), T71 (= T53), R73 (= R55), Y75 (= Y57), S150 (= S132), T152 (= T134), T181 (= T163), R193 (= R175), K220 (≠ R202), H230 (= H212), R269 (= R251), S271 (= S253), F273 (= F255), R313 (= R294), A314 (≠ M295), H315 (= H296), Q317 (= Q298), Q348 (= Q329)
P22033 Methylmalonyl-CoA mutase, mitochondrial; MCM; Methylmalonyl-CoA isomerase; EC 5.4.99.2 from Homo sapiens (Human) (see 28 papers)
47% identity, 97% coverage: 12:694/703 of query aligns to 67:744/750 of P22033
- I69 (≠ L14) to V: in MMAM; likely benign; dbSNP:rs115923556
- P86 (= P33) 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 (= G34) to E: in MMAM; mut0; dbSNP:rs1554160986
- R93 (= R40) to H: in MMAM; mut0; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918251
- G94 (= G41) to R: in MMAM; mut0; dbSNP:rs727504022; to V: in MMAM; mut- and mut0; dbSNP:rs535411418
- P95 (= P42) to R: in MMAM; mut0; dbSNP:rs190834116
- YPTM 96:99 (≠ FASM 43:46) binding
- Y100 (= Y47) 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 (= W52) to R: in MMAM; mut0; dbSNP:rs121918249
- TIRQY 106:110 (= TIRQY 53:57) binding
- R108 (= R55) to C: in MMAM; mut0; dbSNP:rs121918257; to G: in MMAM; mut-; to H: in MMAM; mut0; dbSNP:rs483352778
- Q109 (= Q56) to R: in MMAM; mut0; dbSNP:rs1461110052
- G133 (= G80) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253828
- A137 (= A84) to V: in MMAM; mut0; dbSNP:rs941483851
- D139 (= D86) to N: in MMAM; uncertain significance; dbSNP:rs879253829
- L140 (= L87) to P: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- A141 (≠ P88) to T: in MMAM; decreased protein expression; dbSNP:rs1554160730
- H143 (≠ Q90) to Y: in MMAM; mut0
- G145 (= G92) to S: in MMAM; mut0
- S148 (= S95) to L: in MMAM; mut0; dbSNP:rs1300547552
- D156 (= D103) to N: in MMAM; mut-
- G158 (= G105) to V: in MMAM; mut0
- G161 (= G108) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; to V: in MMAM; decreased protein expression
- F174 (= F121) to S: in MMAM; mut0; dbSNP:rs864309733
- M186 (= M133) to V: in MMAM; mut-; dbSNP:rs148331800
- T187 (= T134) to S: in MMAM; mut0; dbSNP:rs879253830
- N189 (= N136) to I: in MMAM; mut-; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs200908035; to K: in MMAM; mut-; dbSNP:rs1561959114
- A191 (= A138) to E: in MMAM; mut- and mut0; affects proper folding; reduced protein level; decreased methylmalonyl-CoA mutase activity; dbSNP:rs760782399
- A197 (= A144) to E: in MMAM; mut0
- G203 (≠ A150) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs778702777
- E205 (= E152) natural variant: Missing (in MMAM; mut0; dbSNP:rs879253831)
- G215 (= G162) to C: in MMAM; mut- and mut0; dbSNP:rs121918258; to S: in MMAM; mut0; dbSNP:rs121918258
- TIQ 216:218 (= TIQ 163:165) binding
- Q218 (= Q165) to H: in MMAM; mut0 and mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability; dbSNP:rs1446389693
- N219 (= N166) to Y: in MMAM; mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; dbSNP:rs121918256
- R228 (= R175) binding ; to Q: in MMAM; mut0; dbSNP:rs770810987
- T230 (= T177) to I: in MMAM; mut-; to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253833
- Y231 (≠ S178) 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 (≠ R202) binding
- S262 (= S209) to N: in MMAM; mut0
- H265 (= H212) binding ; to Y: in MMAM; mut-
- E276 (= E223) to D: in MMAM; uncertain significance; mut-; dbSNP:rs12175488
- L281 (≠ M228) to S: in MMAM; mut0; dbSNP:rs796052007
- G284 (≠ A231) to E: in MMAM; mut0; dbSNP:rs879253835; to R: in MMAM; mut0; dbSNP:rs761477436
- S288 (≠ I235) to P: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1179778233
- G291 (≠ L238) to E: in MMAM; mut0
- Q293 (≠ G240) to P: in MMAM; mut0
- RLS 304:306 (≠ RMS 251:253) binding
- L305 (≠ M252) to S: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554160246
- S306 (= S253) to F: in MMAM; mut0; dbSNP:rs1085307929
- W309 (≠ F256) to G: in MMAM; decreased protein expression
- G312 (= G259) to V: in MMAM; mut0; dbSNP:rs864309734
- Y316 (= Y263) 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 (= A271) to T: in MMAM; mut-; dbSNP:rs780387525
- R326 (= R273) to K: in MMAM; uncertain significance; dbSNP:rs758577372
- L328 (= L275) 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 (≠ A290) 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 (≠ A292) natural variant: Missing (in MMAM; mut0)
- L347 (= L293) to R: in MMAM; mut0; dbSNP:rs1026703654
- H350 (= H296) to Y: in MMAM; mut0; dbSNP:rs1407914109
- L358 (= L304) to P: in MMAM; mut0
- N366 (= N312) 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 (= R315) 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 (= T316) to P: in MMAM; mut0; dbSNP:rs368790885
- A377 (= A323) to E: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918250
- Q383 (= Q329) to H: in MMAM; mut0; to P: in MMAM; mut0
- H386 (= H332) to N: in MMAM; mut0; dbSNP:rs1554159937; to R: in MMAM; mut0; dbSNP:rs866933356
- T387 (= T333) 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 (= N334) to H: in MMAM; mut0; dbSNP:rs766010704; to K: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253840
- S389 (≠ G335) natural variant: Missing (in MMAM; mut0)
- I412 (≠ L358) natural variant: Missing (in MMAM; mut0)
- P424 (= P370) to L: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253842
- G426 (≠ A372) 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 (= G373) to D: in MMAM; mut0; dbSNP:rs753288303
- G454 (= G400) to E: in MMAM; mut0
- A499 (≠ L446) to T: in dbSNP:rs2229385
- I505 (≠ V452) to T: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- Q514 (= Q461) to E: in MMAM; uncertain significance; to K: in MMAM; decreased protein expression
- L518 (= L465) to P: in MMAM; mut0; dbSNP:rs864309738
- R532 (≠ N479) to H: in dbSNP:rs1141321
- A535 (≠ D482) to P: in MMAM; mut0; dbSNP:rs760183775
- A552 (≠ T499) to V: in MMAM; uncertain significance; dbSNP:rs879253845
- C560 (≠ A507) to Y: in MMAM; mut0; dbSNP:rs1238333040
- T566 (= T513) to R: in MMAM; mut0
- F573 (≠ W520) 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 (= Y534) to C: in MMAM; mut-
- I597 (≠ W544) to R: in MMAM; no changed in protein expression; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554158951
- P615 (= P562) 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 (= R563) to C: in MMAM; mut0; dbSNP:rs765284825
- L617 (≠ V564) to R: in MMAM; mut0; dbSNP:rs1554158775
- K621 (= K568) to N: in MMAM; mut0
- G623 (= G570) to R: in MMAM; mut0; dbSNP:rs121918254
- Q624 (= Q571) to R: in MMAM; no effect on protein abundance; dbSNP:rs768521956
- D625 (= D572) 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 (= G573) to C: in MMAM; mut-; dbSNP:rs982110849
- H627 (= H574) binding axial binding residue; to R: in MMAM; mut0; dbSNP:rs372486357
- G630 (= G577) to E: in MMAM; mut0; dbSNP:rs143023066
- V633 (≠ I580) 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 (≠ A584) to E: in MMAM; mut-; to R: in MMAM; mut0; dbSNP:rs781501004
- F638 (≠ L585) to I: in MMAM; mut0
- D640 (= D587) to Y: in MMAM; mut0; dbSNP:rs865815395
- G642 (= G589) to R: in MMAM; mut-; dbSNP:rs747897332
- G648 (= G595) 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 (≠ I616) to E: in MMAM; mut0; dbSNP:rs1360470463
- I671 (≠ V618) to V: in dbSNP:rs8589
- L674 (= L621) to F: in MMAM; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1164271240
- H678 (≠ Q625) to R: in MMAM; mut-; dbSNP:rs147094927
- E684 (≠ A631) natural variant: E -> EL (in MMAM; mut-)
- L685 (= L632) to R: in MMAM; mut-; dbSNP:rs864309739
- R694 (≠ L641) 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 (≠ V646) 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 (= G649) to R: in MMAM; mut0; dbSNP:rs121918255
- G717 (= G663) 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 (≠ P669) 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
- 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)
47% identity, 97% coverage: 12:694/703 of query aligns to 31:708/708 of 8dyjB
- binding adenosine-5'-diphosphate: Y74 (= Y57), T151 (= T134), R192 (= R175), Y228 (= Y211), H229 (= H212), F272 (= F255), Q316 (= Q298), N352 (= N334), E356 (= E338), L360 (= L342), P361 (= P343)
- binding cobalamin: F102 (= F85), L104 (= L87), H107 (≠ Q90), A124 (≠ T107), V191 (= V174), R192 (= R175), H229 (= H212), E232 (= E215), G319 (= G301), W320 (= W302), E356 (= E338), G359 (≠ S341), L360 (= L342), G590 (= G573), H591 (= H574), D592 (= D575), R593 (= R576), G594 (= G577), I598 (= I581), S636 (= S619), L638 (= L621), A640 (≠ G623), G666 (= G648), G667 (= G649), V668 (≠ I650), F686 (= F668), G687 (≠ P669), T690 (= T672)
6oxdA Structure of mycobacterium tuberculosis methylmalonyl-coa mutase with adenosyl cobalamin (see paper)
49% identity, 92% coverage: 29:674/703 of query aligns to 72:717/736 of 6oxdA
- active site: Y100 (= Y57), Y254 (= Y211), H255 (= H212), K610 (= K568), D614 (= D572), H616 (= H574)
- binding cobalamin: Y100 (= Y57), L130 (= L87), H133 (≠ Q90), A150 (≠ T107), R218 (= R175), E258 (= E215), G344 (= G301), W345 (= W302), E381 (= E338), A382 (= A339), A384 (≠ S341), L385 (= L342), G615 (= G573), H616 (= H574), D617 (= D575), R618 (= R576), S661 (= S619), L663 (= L621), A665 (≠ G623), G691 (= G648), G692 (= G649), F711 (= F668), P712 (= P669), T715 (= T672)
- binding Itaconyl coenzyme A: Y86 (≠ F43), T88 (≠ S45), M89 (= M46), Q93 (≠ K50), T96 (= T53), R98 (= R55), Y100 (= Y57), S175 (= S132), T177 (= T134), T206 (= T163), R218 (= R175), H255 (= H212), R294 (= R251), S296 (= S253), F298 (= F255), R337 (= R294), T338 (≠ M295), H339 (= H296), Q341 (= Q298), Q372 (= Q329)
P11653 Methylmalonyl-CoA mutase large subunit; MCM-alpha; EC 5.4.99.2 from Propionibacterium freudenreichii subsp. shermanii (see 4 papers)
47% identity, 92% coverage: 29:676/703 of query aligns to 61:713/728 of P11653
- Y75 (≠ F43) binding
- M78 (= M46) binding
- R82 (≠ K50) binding
- T85 (= T53) binding
- R87 (= R55) binding
- Y89 (= Y57) binding ; mutation to F: Does not significantly affect affinity for succiny-CoA, but kcat is lowered about 580-fold.
- S114 (= S82) binding
- F117 (= F85) binding
- A139 (≠ T107) binding
- T195 (= T163) binding
- Q197 (= Q165) binding
- V206 (= V174) binding
- R207 (= R175) binding ; binding
- H244 (= H212) binding
- R283 (= R251) binding
- S285 (= S253) binding
- G333 (= G301) binding
- E370 (= E338) binding
- A373 (≠ S341) binding
- G609 (= G573) binding
- H610 (= H574) binding axial binding residue
- D611 (= D575) binding
- R612 (= R576) binding
- S655 (= S619) binding
- L657 (= L621) binding
- G686 (= G649) binding
- T709 (= T672) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
4reqA Methylmalonyl-coa mutase substrate complex (see paper)
47% identity, 92% coverage: 29:676/703 of query aligns to 59:711/726 of 4reqA
- active site: Y87 (= Y57), Y241 (= Y211), H242 (= H212), K602 (= K568), D606 (= D572), H608 (= H574)
- binding cobalamin: Y87 (= Y57), L117 (= L87), A137 (≠ T107), V204 (= V174), R205 (= R175), H242 (= H212), E245 (= E215), G331 (= G301), W332 (= W302), E368 (= E338), A369 (= A339), A371 (≠ S341), L372 (= L342), G607 (= G573), H608 (= H574), D609 (= D575), R610 (= R576), G611 (= G577), I615 (= I581), S653 (= S619), L655 (= L621), G683 (= G648), G684 (= G649), V685 (≠ I650), Y703 (≠ F668), T704 (≠ P669), T707 (= T672)
- binding methylmalonyl-coenzyme a: Y73 (≠ F43), M76 (= M46), F79 (≠ Q49), R80 (≠ K50), T83 (= T53), R85 (= R55), Y87 (= Y57), S112 (= S82), S162 (= S132), T164 (= T134), T193 (= T163), R205 (= R175), N234 (= N204), Y241 (= Y211), H242 (= H212), R281 (= R251), S283 (= S253), F285 (= F255), H326 (= H296), Q328 (= Q298), Q359 (= Q329), S360 (= S330)
- binding succinyl-coenzyme a: Y73 (≠ F43), M76 (= M46), F79 (≠ Q49), R80 (≠ K50), T83 (= T53), R85 (= R55), Y87 (= Y57), S162 (= S132), T164 (= T134), T193 (= T163), Q195 (= Q165), R205 (= R175), N234 (= N204), Y241 (= Y211), H242 (= H212), R281 (= R251), S283 (= S253), F285 (= F255), R324 (= R294), H326 (= H296), Q359 (= Q329)
7reqA Methylmalonyl-coa mutase, 2-carboxypropyl-coa inhibitor complex (see paper)
47% identity, 92% coverage: 29:676/703 of query aligns to 58:710/725 of 7reqA
- active site: Y86 (= Y57), Y240 (= Y211), H241 (= H212), K601 (= K568), D605 (= D572), H607 (= H574)
- binding 2-carboxypropyl-coenzyme a: Y72 (≠ F43), T74 (≠ S45), M75 (= M46), F78 (≠ Q49), R79 (≠ K50), T82 (= T53), R84 (= R55), Y86 (= Y57), S161 (= S132), T163 (= T134), T192 (= T163), R204 (= R175), H241 (= H212), R280 (= R251), S282 (= S253), F284 (= F255), H325 (= H296), Q358 (= Q329)
- binding cobalamin: Y86 (= Y57), L116 (= L87), A136 (≠ T107), R204 (= R175), E244 (= E215), G330 (= G301), W331 (= W302), E367 (= E338), A368 (= A339), A370 (≠ S341), G606 (= G573), H607 (= H574), D608 (= D575), R609 (= R576), G610 (= G577), I614 (= I581), S652 (= S619), L654 (= L621), G682 (= G648), G683 (= G649), Y702 (≠ F668), T703 (≠ P669), T706 (= T672)
3reqA Methylmalonyl-coa mutase, substrate-free state (poor quality structure) (see paper)
47% identity, 92% coverage: 29:676/703 of query aligns to 58:710/725 of 3reqA
- active site: Y86 (= Y57), Y240 (= Y211), H241 (= H212), K601 (= K568), D605 (= D572), H607 (= H574)
- binding adenosine: Y86 (= Y57), Y240 (= Y211), E244 (= E215), G330 (= G301)
- binding cobalamin: L116 (= L87), V203 (= V174), R204 (= R175), E244 (= E215), G330 (= G301), W331 (= W302), A368 (= A339), G606 (= G573), H607 (= H574), D608 (= D575), R609 (= R576), G610 (= G577), I614 (= I581), G650 (= G617), S652 (= S619), L654 (= L621), G682 (= G648), G683 (= G649), Y702 (≠ F668), T703 (≠ P669), P704 (≠ A670), T706 (= T672)
2reqA Methylmalonyl-coa mutase, non-productive coa complex, in open conformation representing substrate-free state (see paper)
47% identity, 92% coverage: 29:676/703 of query aligns to 58:710/725 of 2reqA
- active site: Y86 (= Y57), Y240 (= Y211), H241 (= H212), K601 (= K568), D605 (= D572), H607 (= H574)
- binding cobalamin: V203 (= V174), R204 (= R175), E244 (= E215), A245 (= A216), W331 (= W302), A368 (= A339), G606 (= G573), H607 (= H574), D608 (= D575), R609 (= R576), G610 (= G577), I614 (= I581), G650 (= G617), S652 (= S619), L654 (= L621), A655 (= A622), G682 (= G648), G683 (= G649), Y702 (≠ F668), T703 (≠ P669), T706 (= T672)
- binding coenzyme a: Y72 (≠ F43), R79 (≠ K50), K318 (≠ R289)
6reqA Methylmalonyl-coa mutase, 3-carboxypropyl-coa inhibitor complex (see paper)
47% identity, 92% coverage: 29:676/703 of query aligns to 60:712/727 of 6reqA
- active site: Y88 (= Y57), Y242 (= Y211), H243 (= H212), K603 (= K568), D607 (= D572), H609 (= H574)
- binding 3-carboxypropyl-coenzyme a: Y74 (≠ F43), T76 (≠ S45), M77 (= M46), F80 (≠ Q49), R81 (≠ K50), T84 (= T53), R86 (= R55), Y88 (= Y57), S113 (= S82), S163 (= S132), T165 (= T134), T194 (= T163), R206 (= R175), H243 (= H212), R282 (= R251), S284 (= S253), F286 (= F255), H327 (= H296), Q329 (= Q298), Q360 (= Q329)
- binding cobalamin: Y88 (= Y57), F116 (= F85), L118 (= L87), H121 (≠ Q90), A138 (≠ T107), R206 (= R175), E246 (= E215), G332 (= G301), W333 (= W302), E369 (= E338), A370 (= A339), A372 (≠ S341), G608 (= G573), H609 (= H574), D610 (= D575), R611 (= R576), G612 (= G577), I616 (= I581), Y620 (≠ L585), S654 (= S619), L656 (= L621), G658 (= G623), G684 (= G648), G685 (= G649), Y704 (≠ F668), T705 (≠ P669), T708 (= T672)
5reqA Methylmalonyl-coa mutase, y89f mutant, substrate complex (see paper)
47% identity, 92% coverage: 29:676/703 of query aligns to 58:710/725 of 5reqA
- active site: F86 (≠ Y57), Y240 (= Y211), H241 (= H212), K601 (= K568), D605 (= D572), H607 (= H574)
- binding cobalamin: L116 (= L87), A136 (≠ T107), R204 (= R175), H241 (= H212), E244 (= E215), G330 (= G301), W331 (= W302), E367 (= E338), A368 (= A339), A370 (≠ S341), G606 (= G573), H607 (= H574), D608 (= D575), R609 (= R576), G610 (= G577), I614 (= I581), S652 (= S619), L654 (= L621), G682 (= G648), G683 (= G649), V684 (≠ I650), Y702 (≠ F668), T703 (≠ P669), T706 (= T672)
- binding methylmalonyl(carbadethia)-coenzyme a: Y72 (≠ F43), T74 (≠ S45), M75 (= M46), R79 (≠ K50), T82 (= T53), R84 (= R55), F86 (≠ Y57), S111 (= S82), S161 (= S132), T163 (= T134), T192 (= T163), Q194 (= Q165), R204 (= R175), N233 (= N204), H241 (= H212), R280 (= R251), S282 (= S253), F284 (= F255), T324 (≠ M295), H325 (= H296), Q358 (= Q329), S359 (= S330)
- binding succinyl(carbadethia)-coenzyme a: Y72 (≠ F43), T74 (≠ S45), M75 (= M46), R79 (≠ K50), T82 (= T53), R84 (= R55), F86 (≠ Y57), S161 (= S132), T163 (= T134), T192 (= T163), R204 (= R175), N233 (= N204), H241 (= H212), R280 (= R251), S282 (= S253), F284 (= F255), H325 (= H296), Q358 (= Q329)
8gjuJ Crystal structure of human methylmalonyl-coa mutase (mmut) in complex with methylmalonic acidemia type a protein (mmaa), coenzyme a, and gdp (see paper)
46% identity, 97% coverage: 12:694/703 of query aligns to 32:686/689 of 8gjuJ
- binding coenzyme a: Y61 (≠ F43), T63 (≠ S45), R68 (≠ K50), T71 (= T53), R73 (= R55), S150 (= S132), T152 (= T134), T181 (= T163), Q183 (= Q165), N222 (= N204), R269 (= R251), S271 (= S253), R313 (= R294), A314 (≠ M295), H315 (= H296), Q348 (= Q329)
1e1cA Methylmalonyl-coa mutase h244a mutant (see paper)
47% identity, 92% coverage: 29:676/703 of query aligns to 60:712/727 of 1e1cA
- active site: Y88 (= Y57), Y242 (= Y211), A243 (≠ H212), K603 (= K568), D607 (= D572), H609 (= H574)
- binding cobalamin: Y88 (= Y57), L118 (= L87), H121 (≠ Q90), A138 (≠ T107), V205 (= V174), R206 (= R175), E246 (= E215), G332 (= G301), W333 (= W302), E369 (= E338), A370 (= A339), A372 (≠ S341), L373 (= L342), G608 (= G573), H609 (= H574), D610 (= D575), R611 (= R576), G612 (= G577), I616 (= I581), Y620 (≠ L585), S654 (= S619), L656 (= L621), G684 (= G648), G685 (= G649), V686 (≠ I650), Y704 (≠ F668), T705 (≠ P669), T708 (= T672)
- binding desulfo-coenzyme a: Y74 (≠ F43), M77 (= M46), F80 (≠ Q49), R81 (≠ K50), T84 (= T53), R86 (= R55), S113 (= S82), S163 (= S132), T165 (= T134), T194 (= T163), R282 (= R251), S284 (= S253), H327 (= H296), Q360 (= Q329)
Sites not aligning to the query:
4r3uA Crystal structure of 2-hydroxyisobutyryl-coa mutase (see paper)
41% identity, 73% coverage: 14:524/703 of query aligns to 45:556/557 of 4r3uA
- active site: I89 (≠ Y57), Y243 (= Y211), H244 (= H212)
- binding 3-hydroxybutanoyl-coenzyme a: Y75 (≠ F43), T77 (≠ S45), M78 (= M46), R82 (≠ K50), T85 (= T53), R87 (= R55), I89 (≠ Y57), D116 (≠ A84), S164 (= S132), T166 (= T134), T195 (= T163), Q197 (= Q165), R234 (= R202), N236 (= N204), N239 (≠ S207), Y243 (= Y211), H244 (= H212), R283 (= R251), F287 (= F255), R327 (= R294), F328 (≠ M295), H329 (= H296), Q331 (= Q298), Q362 (= Q329)
- 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 (≠ F43), T77 (≠ S45), M78 (= M46), R82 (≠ K50), T85 (= T53), R87 (= R55), I89 (≠ Y57), D116 (≠ A84), S164 (= S132), T166 (= T134), T195 (= T163), Q197 (= Q165), R234 (= R202), N236 (= N204), N239 (≠ S207), H244 (= H212), R283 (= R251), F287 (= F255), R327 (= R294), F328 (≠ M295), H329 (= H296), Q331 (= Q298), Q362 (= Q329)
- binding cobalamin: D116 (≠ A84), M119 (≠ L87), E139 (≠ T107), Q207 (≠ R175), E209 (≠ T177), E247 (= E215), A334 (≠ G301), E371 (= E338), A372 (= A339), A374 (≠ S341)
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)
41% identity, 73% coverage: 14:524/703 of query aligns to 46:557/562 of I3VE77
- YPTM 76:79 (≠ FASM 43:46) binding
- TMR 86:88 (≠ TIR 53:55) binding
- I90 (≠ Y57) 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 (≠ A84) binding ; mutation to A: 2-fold increase in catalytic efficiency with 2-hydroxyisobutyryl-CoA as substrate. Small increase in catalytic efficiency with (S)-3-hydroxybuytryl-CoA as substrate. 1800-fold increase in catalytic efficiency with (R)-3-hydroxybutyryl-CoA as substrate.; mutation to V: 1.5-fold increase in catalytic efficiency with 2-hydroxyisobutyryl-CoA as substrate. 3-fold decrease in catalytic efficiency with (S)-3-hydroxybuytryl-CoA as substrate. 1300-fold increase in catalytic efficiency with (R)-3-hydroxybutyryl-CoA as substrate. 74-fold increase in catalytic efficiency with pivalyl-CoA as substrate.
- TVQ 196:198 (≠ TIQ 163:165) binding
- R235 (= R202) binding
- N240 (≠ S207) binding
- H245 (= H212) binding
- R284 (= R251) binding
5cjtA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isobutyryl-coenzyme a (see paper)
34% identity, 73% coverage: 11:524/703 of query aligns to 524:1059/1062 of 5cjtA
- active site: F569 (≠ Y57), Y750 (= Y211), H751 (= H212)
- binding cobalamin: F598 (= F85), L603 (≠ Q90), S621 (≠ T107), Q713 (≠ R175), H751 (= H212), E754 (= E215), A755 (= A216), G839 (= G301), R840 (≠ W302), E876 (= E338), A877 (= A339), T879 (≠ S341), H964 (≠ E426)
- binding isobutyryl-coenzyme a: F556 (= F43), F558 (≠ S45), R560 (≠ Y47), R567 (= R55), F569 (≠ Y57), R593 (≠ G80), S648 (= S132), T650 (= T134), R699 (= R161), T701 (= T163), Q703 (= Q165), Y743 (≠ N204), Y750 (= Y211), H751 (= H212), S792 (= S253), F794 (= F255), R827 (= R289), K832 (≠ R294), H834 (= H296)
- binding guanosine-5'-diphosphate: E944 (= E406)
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)
34% identity, 73% coverage: 11:524/703 of query aligns to 527:1064/1067 of 4xc6A
- active site: F572 (≠ Y57), Y753 (= Y211), H754 (= H212)
- binding cobalamin: F601 (= F85), L606 (≠ Q90), S624 (≠ T107), Q716 (≠ R175), H754 (= H212), E757 (= E215), A758 (= A216), G842 (= G301), R843 (≠ W302), E879 (= E338), A880 (= A339), T882 (≠ S341), H967 (≠ E426)
- binding guanosine-5'-diphosphate: E947 (= E406)
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
5cjwA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate pivalyl-coenzyme a (see paper)
37% identity, 61% coverage: 11:438/703 of query aligns to 526:978/1063 of 5cjwA
- active site: F571 (≠ Y57), Y752 (= Y211), H753 (= H212)
- binding pivalyl-coenzyme A: F558 (= F43), F560 (≠ S45), R562 (≠ Y47), R569 (= R55), F571 (≠ Y57), R595 (≠ G80), S650 (= S132), T652 (= T134), R701 (= R161), T703 (= T163), Q705 (= Q165), Y745 (≠ N204), Y752 (= Y211), H753 (= H212), S794 (= S253), F796 (= F255), R829 (= R289), K834 (≠ R294), H836 (= H296)
- binding cobalamin: F600 (= F85), L605 (≠ Q90), S623 (≠ T107), Q715 (≠ R175), H753 (= H212), E756 (= E215), A757 (= A216), G841 (= G301), R842 (≠ W302), E878 (= E338), A879 (= A339), T881 (≠ S341), H966 (≠ E426)
Sites not aligning to the query:
- active site: 6
- binding cobalamin: 18, 19, 20, 21, 22, 26, 66, 67, 94, 96, 98, 116, 117, 118
- binding guanosine-5'-diphosphate: 199, 201, 202, 203, 204, 245, 337, 338, 340, 375, 377, 1062
- binding magnesium ion: 203, 229, 242, 242, 290, 290
Q1LRY0 Fused isobutyryl-CoA mutase; EC 5.4.99.13; EC 3.6.5.- from Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34) (Ralstonia metallidurans) (see 2 papers)
34% identity, 73% coverage: 11:524/703 of query aligns to 553:1090/1093 of Q1LRY0
- F587 (≠ S45) binding
- F598 (≠ Y57) 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 (≠ G80) binding
- R728 (= R161) binding
- Y772 (≠ N204) binding
- S821 (= S253) binding
- R856 (= R289) binding
- K861 (≠ R294) binding
- E973 (= E406) binding
Sites not aligning to the query:
- 39 binding axial binding residue
- 169:417 GTPase chaperone MeaI
- 219:224 binding
- 223 binding
- 248 binding
- 249 binding
- 262 binding ; binding
- 265 binding
- 310 binding ; binding
- 311 binding
- 357:360 binding
- 418:579 Linker
- 1092 binding
5cjvA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isovaleryl-coenzyme a (see paper)
37% identity, 61% coverage: 11:438/703 of query aligns to 524:976/1061 of 5cjvA
- active site: F569 (≠ Y57), Y750 (= Y211), H751 (= H212)
- binding cobalamin: F598 (= F85), L603 (≠ Q90), S621 (≠ T107), Q713 (≠ R175), E754 (= E215), A755 (= A216), G839 (= G301), R840 (≠ W302), E876 (= E338), A877 (= A339), T879 (≠ S341), H964 (≠ E426)
- binding guanosine-5'-diphosphate: E944 (= E406)
- binding Isovaleryl-coenzyme A: F556 (= F43), F558 (≠ S45), R560 (≠ Y47), R567 (= R55), F569 (≠ Y57), R593 (≠ G80), S648 (= S132), T650 (= T134), R699 (= R161), T701 (= T163), Q703 (= Q165), Q713 (≠ R175), Y743 (≠ N204), H751 (= H212), S792 (= S253), F794 (= F255), K832 (≠ R294), H834 (= H296)
Sites not aligning to the query:
- active site: 6
- binding cobalamin: 18, 19, 20, 21, 22, 26, 66, 67, 94, 96, 98, 116, 117, 129
- binding guanosine-5'-diphosphate: 199, 201, 202, 203, 204, 245, 336, 338, 373, 375
- binding magnesium ion: 203, 229, 242, 242, 288, 288
Query Sequence
>H281DRAFT_01038 FitnessBrowser__Burk376:H281DRAFT_01038
MNTQRRRRSDRVKLKRVYTRADIEGIAHIDSMPGEAPFVRGPFASMYTQKPWTIRQYAGY
AQASDTNLAFRTALAEGAQGLSVAFDLPTQRGYDSDDPAVSADVGMTGVAIDTVEDMTRL
FEDIALDRVSVSMTMNGAVLPVLAAFIVAAEESGVGASQLRGTIQNDILKEFMVRNTSIF
APEPSLRIAADVVEYLGKNVPRFNALSVSGYHFQEAGADPVLELALTMANARKYITALAG
RGMQADDVCQRMSFFFGVGMDFYVEIAKLRAARILWADIASASGATSDRARALRMHCQTS
GWSLTAQKPMNNVVRTTVEALAAVFGGTQSLHTNGYDEALSLPCADASRLARDTQLVLQH
ETGVCDVVDPWAGSYMMEKFTAEICQKALTVMAEIERRGGVVDVVESGWVRDQIHRSALN
IQAEIESRKRTVVGVNDFMTGCDEDLGEPQTVDGRRVRVLQTQRLAHIKARRDPTRVRNT
LDALTRAARGRDGNLLELTVACMRARATVGECTQALEAVWPRYQIGLPLLRDHYGANLES
DKDWQDTCRAVADATKRLGRAPRVLIAKLGQDGHDRGARIIAAALSDAGFAVFTGSMFAS
PSDTVQLAEGERVDVIGVSSLAGAQNDLITALHDQLTVRGLRIPIVVGGIIDQASQLVLR
RSGVAACFPAGTPIKKIVTLLAAIAVASAEKCVEGGHPLHESA
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