SitesBLAST
Comparing Dsui_0519 FitnessBrowser__PS:Dsui_0519 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)
66% identity, 97% coverage: 19:719/721 of query aligns to 8:707/714 of 2xiqA
- active site: Y75 (= Y88), Y229 (= Y242), H230 (= H243), K586 (= K598), D590 (= D602), H592 (= H604)
- binding cobalamin: Y75 (= Y88), L105 (= L118), H108 (= H121), A125 (= A138), R193 (= R206), E233 (= E246), G320 (= G332), W321 (= W333), E357 (= E369), G360 (≠ A372), L361 (= L373), G591 (= G603), H592 (= H604), D593 (= D605), R594 (= R606), G595 (= G607), I599 (≠ V611), G635 (= G647), S637 (= S649), L639 (= L651), A641 (= A653), G667 (= G679), G668 (= G680), F687 (= F699), G688 (= G700), T691 (= T703)
- binding malonyl-coenzyme a: Y61 (≠ Q74), T63 (= T76), M64 (= M77), R68 (= R81), T71 (= T84), R73 (= R86), Y75 (= Y88), S150 (= S163), T152 (= T165), T181 (= T194), R193 (= R206), K220 (= K233), H230 (= H243), R269 (= R282), S271 (= S284), F273 (= F286), R313 (= R325), A314 (≠ T326), H315 (= H327), Q317 (= Q329), Q348 (= Q360)
P22033 Methylmalonyl-CoA mutase, mitochondrial; MCM; Methylmalonyl-CoA isomerase; EC 5.4.99.2 from Homo sapiens (Human) (see 28 papers)
66% identity, 97% coverage: 19:719/721 of query aligns to 43:742/750 of P22033
- Q50 (≠ S26) binding
- I69 (≠ V45) to V: in MMAM; likely benign; dbSNP:rs115923556
- P86 (= P64) 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 (= G65) to E: in MMAM; mut0; dbSNP:rs1554160986
- R93 (= R71) to H: in MMAM; mut0; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918251
- G94 (= G72) to R: in MMAM; mut0; dbSNP:rs727504022; to V: in MMAM; mut- and mut0; dbSNP:rs535411418
- P95 (= P73) to R: in MMAM; mut0; dbSNP:rs190834116
- YPTM 96:99 (≠ QATM 74:77) binding
- Y100 (= Y78) 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 (= W83) to R: in MMAM; mut0; dbSNP:rs121918249
- TIRQY 106:110 (= TIRQY 84:88) binding
- R108 (= R86) to C: in MMAM; mut0; dbSNP:rs121918257; to G: in MMAM; mut-; to H: in MMAM; mut0; dbSNP:rs483352778
- Q109 (= Q87) to R: in MMAM; mut0; dbSNP:rs1461110052
- G133 (= G111) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253828
- A137 (= A115) to V: in MMAM; mut0; dbSNP:rs941483851
- D139 (= D117) to N: in MMAM; uncertain significance; dbSNP:rs879253829
- L140 (= L118) to P: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- A141 (= A119) to T: in MMAM; decreased protein expression; dbSNP:rs1554160730
- H143 (= H121) to Y: in MMAM; mut0
- G145 (= G123) to S: in MMAM; mut0
- S148 (= S126) to L: in MMAM; mut0; dbSNP:rs1300547552
- D156 (= D134) to N: in MMAM; mut-
- G158 (= G136) to V: in MMAM; mut0
- G161 (= G139) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; to V: in MMAM; decreased protein expression
- F174 (= F152) to S: in MMAM; mut0; dbSNP:rs864309733
- M186 (= M164) to V: in MMAM; mut-; dbSNP:rs148331800
- T187 (= T165) to S: in MMAM; mut0; dbSNP:rs879253830
- N189 (= N167) to I: in MMAM; mut-; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs200908035; to K: in MMAM; mut-; dbSNP:rs1561959114
- A191 (= A169) to E: in MMAM; mut- and mut0; affects proper folding; reduced protein level; decreased methylmalonyl-CoA mutase activity; dbSNP:rs760782399
- A197 (= A175) to E: in MMAM; mut0
- G203 (≠ A181) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs778702777
- E205 (= E183) natural variant: Missing (in MMAM; mut0; dbSNP:rs879253831)
- G215 (= G193) to C: in MMAM; mut- and mut0; dbSNP:rs121918258; to S: in MMAM; mut0; dbSNP:rs121918258
- TIQ 216:218 (= TIQ 194:196) binding
- Q218 (= Q196) to H: in MMAM; mut0 and mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability; dbSNP:rs1446389693
- N219 (= N197) to Y: in MMAM; mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; dbSNP:rs121918256
- R228 (= R206) binding ; to Q: in MMAM; mut0; dbSNP:rs770810987
- T230 (= T208) to I: in MMAM; mut-; to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253833
- Y231 (= Y209) 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 (= K233) binding
- S262 (= S240) to N: in MMAM; mut0
- H265 (= H243) binding ; to Y: in MMAM; mut-
- E276 (= E254) to D: in MMAM; uncertain significance; mut-; dbSNP:rs12175488
- L281 (= L259) to S: in MMAM; mut0; dbSNP:rs796052007
- G284 (= G262) to E: in MMAM; mut0; dbSNP:rs879253835; to R: in MMAM; mut0; dbSNP:rs761477436
- S288 (≠ V266) to P: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1179778233
- G291 (= G269) to E: in MMAM; mut0
- Q293 (≠ A271) to P: in MMAM; mut0
- RLS 304:306 (= RLS 282:284) binding
- L305 (= L283) to S: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554160246
- S306 (= S284) to F: in MMAM; mut0; dbSNP:rs1085307929
- W309 (= W287) to G: in MMAM; decreased protein expression
- G312 (= G290) to V: in MMAM; mut0; dbSNP:rs864309734
- Y316 (= Y294) 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 (= A302) to T: in MMAM; mut-; dbSNP:rs780387525
- R326 (= R304) to K: in MMAM; uncertain significance; dbSNP:rs758577372
- L328 (= L306) 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 (= S321) 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 (≠ M323) natural variant: Missing (in MMAM; mut0)
- L347 (= L324) to R: in MMAM; mut0; dbSNP:rs1026703654
- H350 (= H327) to Y: in MMAM; mut0; dbSNP:rs1407914109
- L358 (= L335) to P: in MMAM; mut0
- N366 (= N343) 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 (= R346) 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 (= T347) to P: in MMAM; mut0; dbSNP:rs368790885
- A377 (= A354) to E: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918250
- Q383 (= Q360) to H: in MMAM; mut0; to P: in MMAM; mut0
- H386 (= H363) to N: in MMAM; mut0; dbSNP:rs1554159937; to R: in MMAM; mut0; dbSNP:rs866933356
- T387 (= T364) 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 (= N365) to H: in MMAM; mut0; dbSNP:rs766010704; to K: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253840
- S389 (≠ A366) natural variant: Missing (in MMAM; mut0)
- I412 (= I389) natural variant: Missing (in MMAM; mut0)
- P424 (= P401) to L: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253842
- G426 (≠ A403) 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 (= G404) to D: in MMAM; mut0; dbSNP:rs753288303
- G454 (= G431) to E: in MMAM; mut0
- A499 (≠ Q476) to T: in dbSNP:rs2229385
- I505 (= I482) to T: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- Q514 (= Q491) to E: in MMAM; uncertain significance; to K: in MMAM; decreased protein expression
- L518 (= L495) to P: in MMAM; mut0; dbSNP:rs864309738
- R532 (≠ A509) to H: in dbSNP:rs1141321
- A535 (≠ D512) to P: in MMAM; mut0; dbSNP:rs760183775
- A552 (≠ S529) to V: in MMAM; uncertain significance; dbSNP:rs879253845
- C560 (≠ A537) to Y: in MMAM; mut0; dbSNP:rs1238333040
- T566 (≠ S543) to R: in MMAM; mut0
- F573 (= F550) 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 (= Y564) to C: in MMAM; mut-
- I597 (≠ S573) to R: in MMAM; no changed in protein expression; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554158951
- P615 (= P592) 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 (= R593) to C: in MMAM; mut0; dbSNP:rs765284825
- L617 (≠ I594) to R: in MMAM; mut0; dbSNP:rs1554158775
- K621 (= K598) to N: in MMAM; mut0
- G623 (= G600) to R: in MMAM; mut0; dbSNP:rs121918254
- Q624 (= Q601) to R: in MMAM; no effect on protein abundance; dbSNP:rs768521956
- D625 (= D602) 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 (= G603) to C: in MMAM; mut-; dbSNP:rs982110849
- H627 (= H604) binding axial binding residue; to R: in MMAM; mut0; dbSNP:rs372486357
- G630 (= G607) to E: in MMAM; mut0; dbSNP:rs143023066
- V633 (= V610) 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 (≠ A614) to E: in MMAM; mut-; to R: in MMAM; mut0; dbSNP:rs781501004
- F638 (= F615) to I: in MMAM; mut0
- D640 (= D617) to Y: in MMAM; mut0; dbSNP:rs865815395
- G642 (= G619) to R: in MMAM; mut-; dbSNP:rs747897332
- G648 (= G625) 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 (≠ I646) to E: in MMAM; mut0; dbSNP:rs1360470463
- I671 (≠ V648) to V: in dbSNP:rs8589
- L674 (= L651) to F: in MMAM; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1164271240
- H678 (= H655) to R: in MMAM; mut-; dbSNP:rs147094927
- E684 (≠ A661) natural variant: E -> EL (in MMAM; mut-)
- L685 (= L662) to R: in MMAM; mut-; dbSNP:rs864309739
- R694 (≠ A671) 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 (≠ F677) 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 (= G680) to R: in MMAM; mut0; dbSNP:rs121918255
- G717 (= G694) 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 (= G700) to D: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity; dbSNP:rs755077681
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
- 7:750 natural variant: Missing (in MMAM; mut-)
- 152:750 natural variant: Missing (in MMAM; mut0)
- 228:750 natural variant: Missing (in MMAM; mut0)
8dyjB Crystal structure of human methylmalonyl-coa mutase in complex with adp and cob(ii)alamin (see paper)
66% identity, 97% coverage: 19:719/721 of query aligns to 7:706/708 of 8dyjB
- binding adenosine-5'-diphosphate: Y74 (= Y88), T151 (= T165), R192 (= R206), Y228 (= Y242), H229 (= H243), F272 (= F286), Q316 (= Q329), N352 (= N365), E356 (= E369), L360 (= L373), P361 (= P374)
- binding cobalamin: F102 (= F116), L104 (= L118), H107 (= H121), A124 (= A138), V191 (= V205), R192 (= R206), H229 (= H243), E232 (= E246), G319 (= G332), W320 (= W333), E356 (= E369), G359 (≠ A372), L360 (= L373), G590 (= G603), H591 (= H604), D592 (= D605), R593 (= R606), G594 (= G607), I598 (≠ V611), S636 (= S649), L638 (= L651), A640 (= A653), G666 (= G679), G667 (= G680), V668 (= V681), F686 (= F699), G687 (= G700), T690 (= T703)
8gjuJ Crystal structure of human methylmalonyl-coa mutase (mmut) in complex with methylmalonic acidemia type a protein (mmaa), coenzyme a, and gdp (see paper)
65% identity, 97% coverage: 19:719/721 of query aligns to 8:684/689 of 8gjuJ
- binding coenzyme a: Y61 (≠ Q74), T63 (= T76), R68 (= R81), T71 (= T84), R73 (= R86), S150 (= S163), T152 (= T165), T181 (= T194), Q183 (= Q196), N222 (= N235), R269 (= R282), S271 (= S284), R313 (= R325), A314 (≠ T326), H315 (= H327), Q348 (= Q360)
P11653 Methylmalonyl-CoA mutase large subunit; MCM-alpha; EC 5.4.99.2 from Propionibacterium freudenreichii subsp. shermanii (see 4 papers)
63% identity, 95% coverage: 37:719/721 of query aligns to 38:725/728 of P11653
- Y75 (≠ Q74) binding
- M78 (= M77) binding
- R82 (= R81) binding
- T85 (= T84) binding
- R87 (= R86) binding
- Y89 (= Y88) binding ; mutation to F: Does not significantly affect affinity for succiny-CoA, but kcat is lowered about 580-fold.
- S114 (= S113) binding
- F117 (= F116) binding
- A139 (= A138) binding
- T195 (= T194) binding
- Q197 (= Q196) binding
- V206 (= V205) binding
- R207 (= R206) binding ; binding
- H244 (= H243) binding
- R283 (= R282) binding
- S285 (= S284) binding
- G333 (= G332) binding
- E370 (= E369) binding
- A373 (= A372) binding
- G609 (= G603) binding
- H610 (= H604) binding axial binding residue
- D611 (= D605) binding
- R612 (= R606) binding
- S655 (= S649) binding
- L657 (= L651) binding
- G686 (= G680) binding
- T709 (= T703) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
6reqA Methylmalonyl-coa mutase, 3-carboxypropyl-coa inhibitor complex (see paper)
63% identity, 95% coverage: 37:719/721 of query aligns to 37:724/727 of 6reqA
- active site: Y88 (= Y88), Y242 (= Y242), H243 (= H243), K603 (= K598), D607 (= D602), H609 (= H604)
- binding 3-carboxypropyl-coenzyme a: Y74 (≠ Q74), T76 (= T76), M77 (= M77), F80 (≠ V80), R81 (= R81), T84 (= T84), R86 (= R86), Y88 (= Y88), S113 (= S113), S163 (= S163), T165 (= T165), T194 (= T194), R206 (= R206), H243 (= H243), R282 (= R282), S284 (= S284), F286 (= F286), H327 (= H327), Q329 (= Q329), Q360 (= Q360)
- binding cobalamin: Y88 (= Y88), F116 (= F116), L118 (= L118), H121 (= H121), A138 (= A138), R206 (= R206), E246 (= E246), G332 (= G332), W333 (= W333), E369 (= E369), A370 (= A370), A372 (= A372), G608 (= G603), H609 (= H604), D610 (= D605), R611 (= R606), G612 (= G607), I616 (≠ V611), Y620 (≠ F615), S654 (= S649), L656 (= L651), G658 (≠ A653), G684 (= G679), G685 (= G680), Y704 (≠ F699), T705 (≠ G700), T708 (= T703)
4reqA Methylmalonyl-coa mutase substrate complex (see paper)
63% identity, 95% coverage: 37:719/721 of query aligns to 36:723/726 of 4reqA
- active site: Y87 (= Y88), Y241 (= Y242), H242 (= H243), K602 (= K598), D606 (= D602), H608 (= H604)
- binding cobalamin: Y87 (= Y88), L117 (= L118), A137 (= A138), V204 (= V205), R205 (= R206), H242 (= H243), E245 (= E246), G331 (= G332), W332 (= W333), E368 (= E369), A369 (= A370), A371 (= A372), L372 (= L373), G607 (= G603), H608 (= H604), D609 (= D605), R610 (= R606), G611 (= G607), I615 (≠ V611), S653 (= S649), L655 (= L651), G683 (= G679), G684 (= G680), V685 (= V681), Y703 (≠ F699), T704 (≠ G700), T707 (= T703)
- binding methylmalonyl-coenzyme a: Y73 (≠ Q74), M76 (= M77), F79 (≠ V80), R80 (= R81), T83 (= T84), R85 (= R86), Y87 (= Y88), S112 (= S113), S162 (= S163), T164 (= T165), T193 (= T194), R205 (= R206), N234 (= N235), Y241 (= Y242), H242 (= H243), R281 (= R282), S283 (= S284), F285 (= F286), H326 (= H327), Q328 (= Q329), Q359 (= Q360), S360 (= S361)
- binding succinyl-coenzyme a: Y73 (≠ Q74), M76 (= M77), F79 (≠ V80), R80 (= R81), T83 (= T84), R85 (= R86), Y87 (= Y88), S162 (= S163), T164 (= T165), T193 (= T194), Q195 (= Q196), R205 (= R206), N234 (= N235), Y241 (= Y242), H242 (= H243), R281 (= R282), S283 (= S284), F285 (= F286), R324 (= R325), H326 (= H327), Q359 (= Q360)
7reqA Methylmalonyl-coa mutase, 2-carboxypropyl-coa inhibitor complex (see paper)
63% identity, 95% coverage: 37:719/721 of query aligns to 35:722/725 of 7reqA
- active site: Y86 (= Y88), Y240 (= Y242), H241 (= H243), K601 (= K598), D605 (= D602), H607 (= H604)
- binding 2-carboxypropyl-coenzyme a: Y72 (≠ Q74), T74 (= T76), M75 (= M77), F78 (≠ V80), R79 (= R81), T82 (= T84), R84 (= R86), Y86 (= Y88), S161 (= S163), T163 (= T165), T192 (= T194), R204 (= R206), H241 (= H243), R280 (= R282), S282 (= S284), F284 (= F286), H325 (= H327), Q358 (= Q360)
- binding cobalamin: Y86 (= Y88), L116 (= L118), A136 (= A138), R204 (= R206), E244 (= E246), G330 (= G332), W331 (= W333), E367 (= E369), A368 (= A370), A370 (= A372), G606 (= G603), H607 (= H604), D608 (= D605), R609 (= R606), G610 (= G607), I614 (≠ V611), S652 (= S649), L654 (= L651), G682 (= G679), G683 (= G680), Y702 (≠ F699), T703 (≠ G700), T706 (= T703)
3reqA Methylmalonyl-coa mutase, substrate-free state (poor quality structure) (see paper)
63% identity, 95% coverage: 37:719/721 of query aligns to 35:722/725 of 3reqA
- active site: Y86 (= Y88), Y240 (= Y242), H241 (= H243), K601 (= K598), D605 (= D602), H607 (= H604)
- binding adenosine: Y86 (= Y88), Y240 (= Y242), E244 (= E246), G330 (= G332)
- binding cobalamin: L116 (= L118), V203 (= V205), R204 (= R206), E244 (= E246), G330 (= G332), W331 (= W333), A368 (= A370), G606 (= G603), H607 (= H604), D608 (= D605), R609 (= R606), G610 (= G607), I614 (≠ V611), G650 (= G647), S652 (= S649), L654 (= L651), G682 (= G679), G683 (= G680), Y702 (≠ F699), T703 (≠ G700), P704 (= P701), T706 (= T703)
2reqA Methylmalonyl-coa mutase, non-productive coa complex, in open conformation representing substrate-free state (see paper)
63% identity, 95% coverage: 37:719/721 of query aligns to 35:722/725 of 2reqA
- active site: Y86 (= Y88), Y240 (= Y242), H241 (= H243), K601 (= K598), D605 (= D602), H607 (= H604)
- binding cobalamin: V203 (= V205), R204 (= R206), E244 (= E246), A245 (= A247), W331 (= W333), A368 (= A370), G606 (= G603), H607 (= H604), D608 (= D605), R609 (= R606), G610 (= G607), I614 (≠ V611), G650 (= G647), S652 (= S649), L654 (= L651), A655 (= A652), G682 (= G679), G683 (= G680), Y702 (≠ F699), T703 (≠ G700), T706 (= T703)
- binding coenzyme a: Y72 (≠ Q74), R79 (= R81), K318 (= K320)
5reqA Methylmalonyl-coa mutase, y89f mutant, substrate complex (see paper)
63% identity, 95% coverage: 37:719/721 of query aligns to 35:722/725 of 5reqA
- active site: F86 (≠ Y88), Y240 (= Y242), H241 (= H243), K601 (= K598), D605 (= D602), H607 (= H604)
- binding cobalamin: L116 (= L118), A136 (= A138), R204 (= R206), H241 (= H243), E244 (= E246), G330 (= G332), W331 (= W333), E367 (= E369), A368 (= A370), A370 (= A372), G606 (= G603), H607 (= H604), D608 (= D605), R609 (= R606), G610 (= G607), I614 (≠ V611), S652 (= S649), L654 (= L651), G682 (= G679), G683 (= G680), V684 (= V681), Y702 (≠ F699), T703 (≠ G700), T706 (= T703)
- binding methylmalonyl(carbadethia)-coenzyme a: Y72 (≠ Q74), T74 (= T76), M75 (= M77), R79 (= R81), T82 (= T84), R84 (= R86), F86 (≠ Y88), S111 (= S113), S161 (= S163), T163 (= T165), T192 (= T194), Q194 (= Q196), R204 (= R206), N233 (= N235), H241 (= H243), R280 (= R282), S282 (= S284), F284 (= F286), T324 (= T326), H325 (= H327), Q358 (= Q360), S359 (= S361)
- binding succinyl(carbadethia)-coenzyme a: Y72 (≠ Q74), T74 (= T76), M75 (= M77), R79 (= R81), T82 (= T84), R84 (= R86), F86 (≠ Y88), S161 (= S163), T163 (= T165), T192 (= T194), R204 (= R206), N233 (= N235), H241 (= H243), R280 (= R282), S282 (= S284), F284 (= F286), H325 (= H327), Q358 (= Q360)
6oxdA Structure of mycobacterium tuberculosis methylmalonyl-coa mutase with adenosyl cobalamin (see paper)
63% identity, 95% coverage: 35:721/721 of query aligns to 43:733/736 of 6oxdA
- active site: Y100 (= Y88), Y254 (= Y242), H255 (= H243), K610 (= K598), D614 (= D602), H616 (= H604)
- binding cobalamin: Y100 (= Y88), L130 (= L118), H133 (= H121), A150 (= A138), R218 (= R206), E258 (= E246), G344 (= G332), W345 (= W333), E381 (= E369), A382 (= A370), A384 (= A372), L385 (= L373), G615 (= G603), H616 (= H604), D617 (= D605), R618 (= R606), S661 (= S649), L663 (= L651), A665 (= A653), G691 (= G679), G692 (= G680), F711 (= F699), P712 (≠ G700), T715 (= T703)
- binding Itaconyl coenzyme A: Y86 (≠ Q74), T88 (= T76), M89 (= M77), Q93 (≠ R81), T96 (= T84), R98 (= R86), Y100 (= Y88), S175 (= S163), T177 (= T165), T206 (= T194), R218 (= R206), H255 (= H243), R294 (= R282), S296 (= S284), F298 (= F286), R337 (= R325), T338 (= T326), H339 (= H327), Q341 (= Q329), Q372 (= Q360)
1e1cA Methylmalonyl-coa mutase h244a mutant (see paper)
63% identity, 95% coverage: 37:719/721 of query aligns to 37:724/727 of 1e1cA
- active site: Y88 (= Y88), Y242 (= Y242), A243 (≠ H243), K603 (= K598), D607 (= D602), H609 (= H604)
- binding cobalamin: Y88 (= Y88), L118 (= L118), H121 (= H121), A138 (= A138), V205 (= V205), R206 (= R206), E246 (= E246), G332 (= G332), W333 (= W333), E369 (= E369), A370 (= A370), A372 (= A372), L373 (= L373), G608 (= G603), H609 (= H604), D610 (= D605), R611 (= R606), G612 (= G607), I616 (≠ V611), Y620 (≠ F615), S654 (= S649), L656 (= L651), G684 (= G679), G685 (= G680), V686 (= V681), Y704 (≠ F699), T705 (≠ G700), T708 (= T703), S713 (= S708)
- binding desulfo-coenzyme a: Y74 (≠ Q74), M77 (= M77), F80 (≠ V80), R81 (= R81), T84 (= T84), R86 (= R86), S113 (= S113), S163 (= S163), T165 (= T165), T194 (= T194), R282 (= R282), S284 (= S284), H327 (= H327), Q360 (= Q360)
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)
43% identity, 71% coverage: 45:554/721 of query aligns to 46:557/562 of I3VE77
- YPTM 76:79 (≠ QATM 74:77) binding
- TMR 86:88 (≠ TIR 84:86) binding
- I90 (≠ Y88) 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 (≠ A115) 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 194:196) binding
- R235 (≠ K233) binding
- N240 (≠ S238) binding
- H245 (= H243) binding
- R284 (= R282) binding
4r3uA Crystal structure of 2-hydroxyisobutyryl-coa mutase (see paper)
43% identity, 71% coverage: 45:554/721 of query aligns to 45:556/557 of 4r3uA
- active site: I89 (≠ Y88), Y243 (= Y242), H244 (= H243)
- binding 3-hydroxybutanoyl-coenzyme a: Y75 (≠ Q74), T77 (= T76), M78 (= M77), R82 (= R81), T85 (= T84), R87 (= R86), I89 (≠ Y88), D116 (≠ A115), S164 (= S163), T166 (= T165), T195 (= T194), Q197 (= Q196), R234 (≠ K233), N236 (= N235), N239 (≠ S238), Y243 (= Y242), H244 (= H243), R283 (= R282), F287 (= F286), R327 (= R325), F328 (≠ T326), H329 (= H327), Q331 (= Q329), Q362 (= Q360)
- 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 (≠ Q74), T77 (= T76), M78 (= M77), R82 (= R81), T85 (= T84), R87 (= R86), I89 (≠ Y88), D116 (≠ A115), S164 (= S163), T166 (= T165), T195 (= T194), Q197 (= Q196), R234 (≠ K233), N236 (= N235), N239 (≠ S238), H244 (= H243), R283 (= R282), F287 (= F286), R327 (= R325), F328 (≠ T326), H329 (= H327), Q331 (= Q329), Q362 (= Q360)
- binding cobalamin: D116 (≠ A115), M119 (≠ L118), E139 (≠ A138), Q207 (≠ R206), E209 (≠ T208), E247 (= E246), A334 (≠ G332), E371 (= E369), A372 (= A370), A374 (= A372)
Q5KUG0 Fused isobutyryl-CoA mutase; EC 5.4.99.13; EC 3.6.5.- from Geobacillus kaustophilus (strain HTA426) (see paper)
34% identity, 69% coverage: 59:556/721 of query aligns to 561:1085/1086 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)
34% identity, 69% coverage: 61:556/721 of query aligns to 545:1062/1063 of 5cjwA
- active site: F571 (≠ Y88), Y752 (= Y242), H753 (= H243)
- binding pivalyl-coenzyme A: F558 (≠ Q74), F560 (≠ T76), R562 (≠ Y78), R569 (= R86), F571 (≠ Y88), R595 (≠ G111), S650 (= S163), T652 (= T165), R701 (≠ S192), T703 (= T194), Q705 (= Q196), Y745 (≠ N235), Y752 (= Y242), H753 (= H243), S794 (= S284), F796 (= F286), R829 (≠ K320), K834 (≠ R325), H836 (= H327)
- binding cobalamin: F600 (= F116), L605 (≠ H121), S623 (≠ A138), Q715 (≠ R206), H753 (= H243), E756 (= E246), A757 (= A247), G841 (= G332), R842 (≠ W333), E878 (= E369), A879 (= A370), T881 (≠ A372), H966 (≠ D457)
- binding guanosine-5'-diphosphate: N1062 (= N556)
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
- binding magnesium ion: 203, 229, 242, 242, 290, 290
5cjvA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isovaleryl-coenzyme a (see paper)
34% identity, 69% coverage: 61:556/721 of query aligns to 543:1060/1061 of 5cjvA
- active site: F569 (≠ Y88), Y750 (= Y242), H751 (= H243)
- binding cobalamin: F598 (= F116), L603 (≠ H121), S621 (≠ A138), Q713 (≠ R206), E754 (= E246), A755 (= A247), G839 (= G332), R840 (≠ W333), E876 (= E369), A877 (= A370), T879 (≠ A372), H964 (≠ D457)
- binding guanosine-5'-diphosphate: E944 (= E437)
- binding Isovaleryl-coenzyme A: F556 (≠ Q74), F558 (≠ T76), R560 (≠ Y78), R567 (= R86), F569 (≠ Y88), R593 (≠ G111), S648 (= S163), T650 (= T165), R699 (≠ S192), T701 (= T194), Q703 (= Q196), Q713 (≠ R206), Y743 (≠ N235), H751 (= H243), S792 (= S284), F794 (= F286), K832 (≠ R325), H834 (= H327)
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
5cjtA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isobutyryl-coenzyme a (see paper)
34% identity, 69% coverage: 61:556/721 of query aligns to 543:1061/1062 of 5cjtA
- active site: F569 (≠ Y88), Y750 (= Y242), H751 (= H243)
- binding cobalamin: F598 (= F116), L603 (≠ H121), S621 (≠ A138), Q713 (≠ R206), H751 (= H243), E754 (= E246), A755 (= A247), G839 (= G332), R840 (≠ W333), E876 (= E369), A877 (= A370), T879 (≠ A372), H964 (≠ D457)
- binding isobutyryl-coenzyme a: F556 (≠ Q74), F558 (≠ T76), R560 (≠ Y78), R567 (= R86), F569 (≠ Y88), R593 (≠ G111), S648 (= S163), T650 (= T165), R699 (≠ S192), T701 (= T194), Q703 (= Q196), Y743 (≠ N235), Y750 (= Y242), H751 (= H243), S792 (= S284), F794 (= F286), R827 (≠ K320), K832 (≠ R325), H834 (= H327)
- binding guanosine-5'-diphosphate: E944 (= E437)
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
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, 69% coverage: 61:556/721 of query aligns to 572:1092/1093 of Q1LRY0
- F587 (≠ T76) binding
- F598 (≠ Y88) 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 (≠ G111) binding
- R728 (≠ S192) binding
- Y772 (≠ N235) binding
- S821 (= S284) binding
- R856 (≠ K320) binding
- K861 (≠ R325) binding
- E973 (= E437) binding
- N1092 (= N556) 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
Query Sequence
>Dsui_0519 FitnessBrowser__PS:Dsui_0519
MSADASKPQLPNSDNLDAWAKAAAKSAPGGDVNALNWITPEGLTVKPLYTKKDVEDLPYA
DTLPGFAPYLRGPQATMYAVRPWTIRQYAGFSTAEESNAFYRKALAAGGQGVSVAFDLAT
HRGYDSDNPRVLGDVGKAGVAIDSVEDMKILFDGIPLDKISVSMTMNGAVLPILAGYIVA
AEEQGVSQEQLSGTIQNDILKEFMVRNTYIYPPKPSMKIISDIFGYTAQHMPKFNSISIS
GYHIQEAGANQAIELAFTLADGMEYVRTGIASGLDVDAFAGRLSFFWAVGMNFYLEIAKM
RAGRMLWHRIMSQFNPKSAKSLMLRTHSQTSGWSLTEQDPYNNVVRTTIEAMAAVFGGTQ
SLHTNALDEAIALPTEFSARIARNTQLIIQEETHICNVVDPWAGSYMMEKLTQDMADKAW
SIIQEIEAMGGMTKAVESGWAKMQVETCAADKQARIDSGKDVIVGVNKYKLAKEDQIDIL
DIDNHAVREAQIARLKKIRASRDSAAVQAALDALTQCAESGEGNLLDLSVKAIRLRATVG
EVSDALEKVFGRFRANNQTISGVYGGVVEGQESWESIKADIAKFAEEEGRRPRIMIAKLG
QDGHDRGAKVVATAFADLGFDIDMGPLFQTPEEAARQAVENDVHAIGVSSLAAGHKTLLP
ALVNSLKEQGADDIIVFAGGVIPAQDYDTLYAAGAKAIFGPGTRIEDSAKRVLEEIRKSR
G
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