SitesBLAST
Comparing 3609471 FitnessBrowser__Dino:3609471 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)
6reqA Methylmalonyl-coa mutase, 3-carboxypropyl-coa inhibitor complex (see paper)
38% identity, 95% coverage: 10:633/657 of query aligns to 81:706/727 of 6reqA
- active site: Y88 (= Y17), Y242 (= Y171), H243 (= H172), K603 (= K530), D607 (= D534), H609 (= H536)
- binding 3-carboxypropyl-coenzyme a: R81 (= R10), T84 (≠ L13), R86 (= R15), Y88 (= Y17), S113 (= S42), S163 (= S92), T165 (= T94), T194 (= T123), R206 (= R135), H243 (= H172), R282 (= R213), S284 (= S215), F286 (= F217), H327 (≠ G259), Q329 (= Q261), Q360 (≠ R295)
- binding cobalamin: Y88 (= Y17), F116 (= F45), L118 (= L47), H121 (≠ Q50), A138 (≠ V67), R206 (= R135), E246 (= E175), G332 (≠ S264), W333 (≠ L265), E369 (= E304), A370 (= A305), A372 (≠ G307), G608 (= G535), H609 (= H536), D610 (≠ S537), R611 (≠ N538), G612 (= G539), I616 (= I543), Y620 (≠ A547), S654 (= S581), L656 (= L583), G658 (= G585), G684 (= G611), G685 (= G612), Y704 (= Y631), T705 (= T632)
Sites not aligning to the query:
4reqA Methylmalonyl-coa mutase substrate complex (see paper)
38% identity, 95% coverage: 10:633/657 of query aligns to 80:705/726 of 4reqA
- active site: Y87 (= Y17), Y241 (= Y171), H242 (= H172), K602 (= K530), D606 (= D534), H608 (= H536)
- binding cobalamin: Y87 (= Y17), L117 (= L47), A137 (≠ V67), V204 (≠ S134), R205 (= R135), H242 (= H172), E245 (= E175), G331 (≠ S264), W332 (≠ L265), E368 (= E304), A369 (= A305), A371 (≠ G307), L372 (= L308), G607 (= G535), H608 (= H536), D609 (≠ S537), R610 (≠ N538), G611 (= G539), I615 (= I543), S653 (= S581), L655 (= L583), G683 (= G611), G684 (= G612), V685 (≠ I613), Y703 (= Y631), T704 (= T632)
- binding methylmalonyl-coenzyme a: R80 (= R10), T83 (≠ L13), R85 (= R15), Y87 (= Y17), S112 (= S42), S162 (= S92), T164 (= T94), T193 (= T123), R205 (= R135), N234 (= N164), Y241 (= Y171), H242 (= H172), R281 (= R213), S283 (= S215), F285 (= F217), H326 (≠ G259), Q328 (= Q261), Q359 (≠ R295), S360 (≠ A296)
- binding succinyl-coenzyme a: R80 (= R10), T83 (≠ L13), R85 (= R15), Y87 (= Y17), S162 (= S92), T164 (= T94), T193 (= T123), Q195 (= Q125), R205 (= R135), N234 (= N164), Y241 (= Y171), H242 (= H172), R281 (= R213), S283 (= S215), F285 (= F217), R324 (= R257), H326 (≠ G259), Q359 (≠ R295)
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)
38% identity, 95% coverage: 10:633/657 of query aligns to 82:707/728 of P11653
- R82 (= R10) binding
- T85 (≠ L13) binding
- R87 (= R15) binding
- Y89 (= Y17) binding ; mutation to F: Does not significantly affect affinity for succiny-CoA, but kcat is lowered about 580-fold.
- S114 (= S42) binding
- F117 (= F45) binding
- A139 (≠ V67) binding
- T195 (= T123) binding
- Q197 (= Q125) binding
- V206 (≠ S134) binding
- R207 (= R135) binding ; binding
- H244 (= H172) binding
- R283 (= R213) binding
- S285 (= S215) binding
- G333 (≠ S264) binding
- E370 (= E304) binding
- A373 (≠ G307) binding
- G609 (= G535) binding
- H610 (= H536) binding axial binding residue
- D611 (≠ S537) binding
- R612 (≠ N538) binding
- S655 (= S581) binding
- L657 (= L583) binding
- G686 (= G612) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 75 binding
- 78 binding
- 709 binding
7reqA Methylmalonyl-coa mutase, 2-carboxypropyl-coa inhibitor complex (see paper)
38% identity, 95% coverage: 10:633/657 of query aligns to 79:704/725 of 7reqA
- active site: Y86 (= Y17), Y240 (= Y171), H241 (= H172), K601 (= K530), D605 (= D534), H607 (= H536)
- binding 2-carboxypropyl-coenzyme a: R79 (= R10), T82 (≠ L13), R84 (= R15), Y86 (= Y17), S161 (= S92), T163 (= T94), T192 (= T123), R204 (= R135), H241 (= H172), R280 (= R213), S282 (= S215), F284 (= F217), H325 (≠ G259), Q358 (≠ R295)
- binding cobalamin: Y86 (= Y17), L116 (= L47), A136 (≠ V67), R204 (= R135), E244 (= E175), G330 (≠ S264), W331 (≠ L265), E367 (= E304), A368 (= A305), A370 (≠ G307), G606 (= G535), H607 (= H536), D608 (≠ S537), R609 (≠ N538), G610 (= G539), I614 (= I543), S652 (= S581), L654 (= L583), G682 (= G611), G683 (= G612), Y702 (= Y631), T703 (= T632)
Sites not aligning to the query:
3reqA Methylmalonyl-coa mutase, substrate-free state (poor quality structure) (see paper)
38% identity, 95% coverage: 10:633/657 of query aligns to 79:704/725 of 3reqA
- active site: Y86 (= Y17), Y240 (= Y171), H241 (= H172), K601 (= K530), D605 (= D534), H607 (= H536)
- binding adenosine: Y86 (= Y17), Y240 (= Y171), E244 (= E175), G330 (≠ S264)
- binding cobalamin: L116 (= L47), V203 (≠ S134), R204 (= R135), E244 (= E175), G330 (≠ S264), W331 (≠ L265), A368 (= A305), G606 (= G535), H607 (= H536), D608 (≠ S537), R609 (≠ N538), G610 (= G539), I614 (= I543), G650 (= G579), S652 (= S581), L654 (= L583), G682 (= G611), G683 (= G612), Y702 (= Y631), T703 (= T632), P704 (= P633)
Sites not aligning to the query:
2reqA Methylmalonyl-coa mutase, non-productive coa complex, in open conformation representing substrate-free state (see paper)
38% identity, 95% coverage: 10:633/657 of query aligns to 79:704/725 of 2reqA
- active site: Y86 (= Y17), Y240 (= Y171), H241 (= H172), K601 (= K530), D605 (= D534), H607 (= H536)
- binding cobalamin: V203 (≠ S134), R204 (= R135), E244 (= E175), A245 (= A176), W331 (≠ L265), A368 (= A305), G606 (= G535), H607 (= H536), D608 (≠ S537), R609 (≠ N538), G610 (= G539), I614 (= I543), G650 (= G579), S652 (= S581), L654 (= L583), A655 (≠ S584), G682 (= G611), G683 (= G612), Y702 (= Y631), T703 (= T632)
- binding coenzyme a: R79 (= R10), K318 (= K252)
Sites not aligning to the query:
5reqA Methylmalonyl-coa mutase, y89f mutant, substrate complex (see paper)
37% identity, 95% coverage: 10:633/657 of query aligns to 79:704/725 of 5reqA
- active site: F86 (≠ Y17), Y240 (= Y171), H241 (= H172), K601 (= K530), D605 (= D534), H607 (= H536)
- binding cobalamin: L116 (= L47), A136 (≠ V67), R204 (= R135), H241 (= H172), E244 (= E175), G330 (≠ S264), W331 (≠ L265), E367 (= E304), A368 (= A305), A370 (≠ G307), G606 (= G535), H607 (= H536), D608 (≠ S537), R609 (≠ N538), G610 (= G539), I614 (= I543), S652 (= S581), L654 (= L583), G682 (= G611), G683 (= G612), V684 (≠ I613), Y702 (= Y631), T703 (= T632)
- binding methylmalonyl(carbadethia)-coenzyme a: R79 (= R10), T82 (≠ L13), R84 (= R15), F86 (≠ Y17), S111 (= S42), S161 (= S92), T163 (= T94), T192 (= T123), Q194 (= Q125), R204 (= R135), N233 (= N164), H241 (= H172), R280 (= R213), S282 (= S215), F284 (= F217), T324 (≠ Y258), H325 (≠ G259), Q358 (≠ R295), S359 (≠ A296)
- binding succinyl(carbadethia)-coenzyme a: R79 (= R10), T82 (≠ L13), R84 (= R15), F86 (≠ Y17), S161 (= S92), T163 (= T94), T192 (= T123), R204 (= R135), N233 (= N164), H241 (= H172), R280 (= R213), S282 (= S215), F284 (= F217), H325 (≠ G259), Q358 (≠ R295)
Sites not aligning to the query:
1e1cA Methylmalonyl-coa mutase h244a mutant (see paper)
37% identity, 95% coverage: 10:633/657 of query aligns to 81:706/727 of 1e1cA
- active site: Y88 (= Y17), Y242 (= Y171), A243 (≠ H172), K603 (= K530), D607 (= D534), H609 (= H536)
- binding cobalamin: Y88 (= Y17), L118 (= L47), H121 (≠ Q50), A138 (≠ V67), V205 (≠ S134), R206 (= R135), E246 (= E175), G332 (≠ S264), W333 (≠ L265), E369 (= E304), A370 (= A305), A372 (≠ G307), L373 (= L308), G608 (= G535), H609 (= H536), D610 (≠ S537), R611 (≠ N538), G612 (= G539), I616 (= I543), Y620 (≠ A547), S654 (= S581), L656 (= L583), G684 (= G611), G685 (= G612), V686 (≠ I613), Y704 (= Y631), T705 (= T632)
- binding desulfo-coenzyme a: R81 (= R10), T84 (≠ L13), R86 (= R15), S113 (= S42), S163 (= S92), T165 (= T94), T194 (= T123), R282 (= R213), S284 (= S215), H327 (≠ G259), Q360 (≠ R295)
Sites not aligning to the query:
6oxdA Structure of mycobacterium tuberculosis methylmalonyl-coa mutase with adenosyl cobalamin (see paper)
38% identity, 96% coverage: 2:633/657 of query aligns to 85:713/736 of 6oxdA
- active site: Y100 (= Y17), Y254 (= Y171), H255 (= H172), K610 (= K530), D614 (= D534), H616 (= H536)
- binding cobalamin: Y100 (= Y17), L130 (= L47), H133 (≠ Q50), A150 (≠ V67), R218 (= R135), E258 (= E175), G344 (≠ S264), W345 (≠ L265), E381 (= E304), A382 (= A305), A384 (≠ G307), L385 (= L308), G615 (= G535), H616 (= H536), D617 (≠ S537), R618 (≠ N538), S661 (= S581), L663 (= L583), A665 (≠ G585), G691 (= G611), G692 (= G612), F711 (≠ Y631), P712 (≠ T632)
- binding Itaconyl coenzyme A: Y86 (≠ M3), T88 (≠ E5), M89 (≠ T6), Q93 (≠ R10), T96 (≠ L13), R98 (= R15), Y100 (= Y17), S175 (= S92), T177 (= T94), T206 (= T123), R218 (= R135), H255 (= H172), R294 (= R213), S296 (= S215), F298 (= F217), R337 (= R257), T338 (≠ Y258), H339 (≠ G259), Q341 (= Q261), Q372 (≠ R295)
Sites not aligning to the query:
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: 10:633/657 of query aligns to 103:724/750 of P22033
- W105 (= W12) to R: in MMAM; mut0; dbSNP:rs121918249
- TIRQY 106:110 (≠ LFRTY 13:17) binding
- R108 (= R15) to C: in MMAM; mut0; dbSNP:rs121918257; to G: in MMAM; mut-; to H: in MMAM; mut0; dbSNP:rs483352778
- Q109 (≠ T16) to R: in MMAM; mut0; dbSNP:rs1461110052
- G133 (= G40) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253828
- A137 (= A44) to V: in MMAM; mut0; dbSNP:rs941483851
- D139 (= D46) to N: in MMAM; uncertain significance; dbSNP:rs879253829
- L140 (= L47) to P: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- A141 (≠ P48) to T: in MMAM; decreased protein expression; dbSNP:rs1554160730
- H143 (≠ Q50) to Y: in MMAM; mut0
- G145 (= G52) to S: in MMAM; mut0
- S148 (= S55) to L: in MMAM; mut0; dbSNP:rs1300547552
- D156 (≠ E63) to N: in MMAM; mut-
- G158 (= G65) to V: in MMAM; mut0
- G161 (= G68) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; to V: in MMAM; decreased protein expression
- F174 (= F81) to S: in MMAM; mut0; dbSNP:rs864309733
- M186 (= M93) to V: in MMAM; mut-; dbSNP:rs148331800
- T187 (= T94) to S: in MMAM; mut0; dbSNP:rs879253830
- N189 (= N96) to I: in MMAM; mut-; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs200908035; to K: in MMAM; mut-; dbSNP:rs1561959114
- A191 (≠ T98) to E: in MMAM; mut- and mut0; affects proper folding; reduced protein level; decreased methylmalonyl-CoA mutase activity; dbSNP:rs760782399
- A197 (≠ S104) to E: in MMAM; mut0
- G203 (≠ A110) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs778702777
- E205 (= E112) natural variant: Missing (in MMAM; mut0; dbSNP:rs879253831)
- G215 (= G122) to C: in MMAM; mut- and mut0; dbSNP:rs121918258; to S: in MMAM; mut0; dbSNP:rs121918258
- TIQ 216:218 (≠ TVQ 123:125) binding
- Q218 (= Q125) to H: in MMAM; mut0 and mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability; dbSNP:rs1446389693
- N219 (= N126) to Y: in MMAM; mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; dbSNP:rs121918256
- R228 (= R135) binding ; to Q: in MMAM; mut0; dbSNP:rs770810987
- T230 (= T137) to I: in MMAM; mut-; to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253833
- Y231 (= Y138) 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 (= K162) binding
- S262 (≠ C169) to N: in MMAM; mut0
- H265 (= H172) binding ; to Y: in MMAM; mut-
- E276 (= E183) to D: in MMAM; uncertain significance; mut-; dbSNP:rs12175488
- L281 (= L188) to S: in MMAM; mut0; dbSNP:rs796052007
- G284 (≠ A191) to E: in MMAM; mut0; dbSNP:rs879253835; to R: in MMAM; mut0; dbSNP:rs761477436
- S288 (vs. gap) to P: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1179778233
- G291 (≠ D197) to E: in MMAM; mut0
- Q293 (≠ K199) to P: in MMAM; mut0
- RLS 304:306 (≠ RIS 213:215) binding
- L305 (≠ I214) to S: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554160246
- S306 (= S215) to F: in MMAM; mut0; dbSNP:rs1085307929
- W309 (≠ V218) to G: in MMAM; decreased protein expression
- G312 (= G221) to V: in MMAM; mut0; dbSNP:rs864309734
- Y316 (≠ V225) 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 (= A233) to T: in MMAM; mut-; dbSNP:rs780387525
- R326 (≠ V235) to K: in MMAM; uncertain significance; dbSNP:rs758577372
- L328 (= L237) 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 (≠ F253) 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 (≠ R255) natural variant: Missing (in MMAM; mut0)
- L347 (≠ F256) to R: in MMAM; mut0; dbSNP:rs1026703654
- H350 (≠ G259) to Y: in MMAM; mut0; dbSNP:rs1407914109
- L358 (= L267) to P: in MMAM; mut0
- N366 (= N275) 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 (= R278) 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 (≠ I279) to P: in MMAM; mut0; dbSNP:rs368790885
- A377 (≠ V286) to E: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918250
- Q383 (≠ R295) to H: in MMAM; mut0; to P: in MMAM; mut0
- H386 (≠ Q298) to N: in MMAM; mut0; dbSNP:rs1554159937; to R: in MMAM; mut0; dbSNP:rs866933356
- T387 (≠ L299) 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 (≠ P300) to H: in MMAM; mut0; dbSNP:rs766010704; to K: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253840
- S389 (≠ A301) natural variant: Missing (in MMAM; mut0)
- I412 (≠ M324) natural variant: Missing (in MMAM; mut0)
- P424 (≠ L336) to L: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253842
- G426 (≠ D338) 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 (= G339) to D: in MMAM; mut0; dbSNP:rs753288303
- G454 (= G366) to E: in MMAM; mut0
- A499 (= A413) to T: in dbSNP:rs2229385
- I505 (≠ V419) to T: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- Q514 (= Q428) to E: in MMAM; uncertain significance; to K: in MMAM; decreased protein expression
- L518 (= L432) to P: in MMAM; mut0; dbSNP:rs864309738
- R532 (≠ K446) to H: in dbSNP:rs1141321
- A535 (= A449) to P: in MMAM; mut0; dbSNP:rs760183775
- A552 (≠ S465) to V: in MMAM; uncertain significance; dbSNP:rs879253845
- C560 (≠ V473) to Y: in MMAM; mut0; dbSNP:rs1238333040
- T566 (≠ G479) to R: in MMAM; mut0
- F573 (= F486) 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 (≠ S500) to C: in MMAM; mut-
- I597 (= I509) to R: in MMAM; no changed in protein expression; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554158951
- P615 (≠ L524) 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 (≠ K525) to C: in MMAM; mut0; dbSNP:rs765284825
- L617 (≠ F526) to R: in MMAM; mut0; dbSNP:rs1554158775
- K621 (= K530) to N: in MMAM; mut0
- G623 (= G532) to R: in MMAM; mut0; dbSNP:rs121918254
- Q624 (≠ L533) to R: in MMAM; no effect on protein abundance; dbSNP:rs768521956
- D625 (= D534) 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 (= G535) to C: in MMAM; mut-; dbSNP:rs982110849
- H627 (= H536) binding axial binding residue; to R: in MMAM; mut0; dbSNP:rs372486357
- G630 (= G539) to E: in MMAM; mut0; dbSNP:rs143023066
- V633 (≠ Q542) 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 (≠ R546) to E: in MMAM; mut-; to R: in MMAM; mut0; dbSNP:rs781501004
- F638 (≠ A547) to I: in MMAM; mut0
- D640 (= D549) to Y: in MMAM; mut0; dbSNP:rs865815395
- G642 (= G551) to R: in MMAM; mut-; dbSNP:rs747897332
- G648 (≠ E557) 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 (= V578) to E: in MMAM; mut0; dbSNP:rs1360470463
- I671 (≠ L580) to V: in dbSNP:rs8589
- L674 (= L583) to F: in MMAM; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1164271240
- H678 (= H587) to R: in MMAM; mut-; dbSNP:rs147094927
- E684 (= E593) natural variant: E -> EL (in MMAM; mut-)
- L685 (= L594) to R: in MMAM; mut-; dbSNP:rs864309739
- R694 (≠ L603) 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 (≠ I609) 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 (= G612) to R: in MMAM; mut0; dbSNP:rs121918255
- G717 (= G626) 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 (≠ T632) 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
- 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
- 95 P → R: in MMAM; mut0; dbSNP:rs190834116
- 96:99 binding
- 100 Y → 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
- 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: 10:633/657 of query aligns to 68:689/714 of 2xiqA
- active site: Y75 (= Y17), Y229 (= Y171), H230 (= H172), K586 (= K530), D590 (= D534), H592 (= H536)
- binding cobalamin: Y75 (= Y17), L105 (= L47), H108 (≠ Q50), A125 (≠ V67), R193 (= R135), E233 (= E175), G320 (≠ S264), W321 (≠ L265), E357 (= E304), G360 (= G307), L361 (= L308), G591 (= G535), H592 (= H536), D593 (≠ S537), R594 (≠ N538), G595 (= G539), I599 (= I543), G635 (= G579), S637 (= S581), L639 (= L583), A641 (≠ G585), G667 (= G611), G668 (= G612), F687 (≠ Y631), G688 (≠ T632)
- binding malonyl-coenzyme a: R68 (= R10), T71 (≠ L13), R73 (= R15), Y75 (= Y17), S150 (= S92), T152 (= T94), T181 (= T123), R193 (= R135), K220 (= K162), H230 (= H172), R269 (= R213), S271 (= S215), F273 (= F217), R313 (= R257), A314 (≠ Y258), H315 (≠ G259), Q317 (= Q261), Q348 (≠ R295)
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: 10:633/657 of query aligns to 67:688/708 of 8dyjB
- binding adenosine-5'-diphosphate: Y74 (= Y17), T151 (= T94), R192 (= R135), Y228 (= Y171), H229 (= H172), F272 (= F217), Q316 (= Q261), N352 (≠ P300), E356 (= E304), L360 (= L308), P361 (= P309)
- binding cobalamin: F102 (= F45), L104 (= L47), H107 (≠ Q50), A124 (≠ V67), V191 (≠ S134), R192 (= R135), H229 (= H172), E232 (= E175), G319 (≠ S264), W320 (≠ L265), E356 (= E304), G359 (= G307), L360 (= L308), G590 (= G535), H591 (= H536), D592 (≠ S537), R593 (≠ N538), G594 (= G539), I598 (= I543), S636 (= S581), L638 (= L583), A640 (≠ G585), G666 (= G611), G667 (= G612), V668 (≠ I613), F686 (≠ Y631), G687 (≠ T632)
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: 10:633/657 of query aligns to 68:666/689 of 8gjuJ
- binding coenzyme a: R68 (= R10), T71 (≠ L13), R73 (= R15), S150 (= S92), T152 (= T94), T181 (= T123), Q183 (= Q125), N222 (= N164), R269 (= R213), S271 (= S215), R313 (= R257), A314 (≠ Y258), H315 (≠ G259), Q348 (≠ R295)
Sites not aligning to the query:
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: 2:490/657 of query aligns to 75:557/562 of I3VE77
- YPTM 76:79 (≠ MTET 3:6) binding
- TMR 86:88 (≠ LFR 13:15) binding
- I90 (≠ Y17) 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 (≠ A44) 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 (= TVQ 123:125) binding
- R235 (≠ K162) binding
- N240 (= N167) binding
- H245 (= H172) binding
- R284 (= R213) binding
4r3uA Crystal structure of 2-hydroxyisobutyryl-coa mutase (see paper)
34% identity, 74% coverage: 2:490/657 of query aligns to 74:556/557 of 4r3uA
- active site: I89 (≠ Y17), Y243 (= Y171), H244 (= H172)
- binding 3-hydroxybutanoyl-coenzyme a: Y75 (≠ M3), T77 (≠ E5), M78 (≠ T6), R82 (= R10), T85 (≠ L13), R87 (= R15), I89 (≠ Y17), D116 (≠ A44), S164 (= S92), T166 (= T94), T195 (= T123), Q197 (= Q125), R234 (≠ K162), N236 (= N164), N239 (= N167), Y243 (= Y171), H244 (= H172), R283 (= R213), F287 (= F217), R327 (= R257), F328 (≠ Y258), H329 (≠ G259), Q331 (= Q261), Q362 (≠ R295)
- 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 (≠ M3), T77 (≠ E5), M78 (≠ T6), R82 (= R10), T85 (≠ L13), R87 (= R15), I89 (≠ Y17), D116 (≠ A44), S164 (= S92), T166 (= T94), T195 (= T123), Q197 (= Q125), R234 (≠ K162), N236 (= N164), N239 (= N167), H244 (= H172), R283 (= R213), F287 (= F217), R327 (= R257), F328 (≠ Y258), H329 (≠ G259), Q331 (= Q261), Q362 (≠ R295)
- binding cobalamin: D116 (≠ A44), M119 (≠ L47), E139 (≠ V67), Q207 (≠ R135), E209 (≠ T137), E247 (= E175), A334 (≠ S264), E371 (= E304), A372 (= A305), A374 (≠ G307)
Q5KUG0 Fused isobutyryl-CoA mutase; EC 5.4.99.13; EC 3.6.5.- from Geobacillus kaustophilus (strain HTA426) (see paper)
25% identity, 72% coverage: 15:490/657 of query aligns to 587:1083/1086 of Q5KUG0
Sites not aligning to the query:
- 213 K→A: Loss of GTPase and ATPase activities. No effect on the mutase activity.
4xc7A Isobutyryl-coa mutase fused with bound butyryl-coa and without cobalamin or gdp (apo-icmf) (see paper)
25% identity, 72% coverage: 15:490/657 of query aligns to 564:1050/1053 of 4xc7A
- active site: F566 (≠ Y17), Y747 (= Y171), H748 (= H172)
- binding Butyryl Coenzyme A: R564 (= R15), F566 (≠ Y17), R590 (vs. gap), S645 (= S92), T647 (= T94), R696 (≠ Q121), T698 (= T123), Y740 (≠ N164), S789 (= S215), F791 (= F217), R824 (≠ K252), K829 (≠ R257), H831 (≠ G259)
Sites not aligning to the query:
4xc6A Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, and mg (holo-icmf/gdp) (see paper)
25% identity, 72% coverage: 15:490/657 of query aligns to 570:1064/1067 of 4xc6A
- active site: F572 (≠ Y17), Y753 (= Y171), H754 (= H172)
- binding cobalamin: F601 (= F45), L606 (≠ Q50), S624 (≠ V67), Q716 (≠ R135), H754 (= H172), E757 (= E175), A758 (= A176), G842 (≠ S264), R843 (≠ L265), E879 (= E304), A880 (= A305), T882 (≠ G307), H967 (≠ E390)
- binding guanosine-5'-diphosphate: E947 (= E372)
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
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)
25% identity, 72% coverage: 15:490/657 of query aligns to 596:1090/1093 of Q1LRY0
- F598 (≠ Y17) 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
- R728 (≠ Q121) binding
- Y772 (≠ N164) binding
- S821 (= S215) binding
- R856 (≠ K252) binding
- K861 (≠ R257) binding
- E973 (= E372) 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
- 587 binding
- 1092 binding
5cjtA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isobutyryl-coenzyme a (see paper)
25% identity, 72% coverage: 15:490/657 of query aligns to 567:1059/1062 of 5cjtA
- active site: F569 (≠ Y17), Y750 (= Y171), H751 (= H172)
- binding cobalamin: F598 (= F45), L603 (≠ Q50), S621 (≠ V67), Q713 (≠ R135), H751 (= H172), E754 (= E175), A755 (= A176), G839 (≠ S264), R840 (≠ L265), E876 (= E304), A877 (= A305), T879 (≠ G307), H964 (≠ E390)
- binding isobutyryl-coenzyme a: R567 (= R15), F569 (≠ Y17), R593 (vs. gap), S648 (= S92), T650 (= T94), R699 (≠ Q121), T701 (= T123), Q703 (= Q125), Y743 (≠ N164), Y750 (= Y171), H751 (= H172), S792 (= S215), F794 (= F217), R827 (≠ K252), K832 (≠ R257), H834 (≠ G259)
- binding guanosine-5'-diphosphate: E944 (= E372)
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
Query Sequence
>3609471 FitnessBrowser__Dino:3609471
MPMTETKKDRPWLFRTYAGHSTAEASNALYRGNLAKGQTGLSVAFDLPTQTGYDSDHVLS
RGEVGKVGVPVAHLGDMRALFKDIPLDQMNTSMTINATAPWLLSLYIAVAEEQGADVTKL
QGTVQNDIIKEYLSRGTYICPPKPSLRMITDVAAYTREHLPKWNPMNVCSYHLQEAGATP
EQELAFALATATAVLDDLKGKVPAEHFPAMVGRISFFVNAGIRFVTEMCKMRAFVTLWDE
ICRDRYGVEDPKFRRFRYGVQVNSLGLTEQQPENNVYRILIEMLAVTLSKNARARAVQLP
AWNEALGLPRPWDQQWSLRMQQIMALETDLLEFDDLFDGNPAVDRKVAELMEGARAELAT
IDGMGGAVAAIEYMKSRLVEANSDRLGRIEGGETVVVGVNKYQQGEPSPLMDADGGIMVV
DPAVEADQIARLQAWRAARDEDAAQKALADLREAALSGANVMPASIAAAKAGVTTGEWGL
EIRKSFGEYRAPTGVSANPSNRTEGLDEIRDAVSAVSAKLGRKLKFLVGKPGLDGHSNGA
EQIAARARDCGMDITYEGIRLTPEEIVRAAREQDAHVVGLSILSGSHIPLIEELMGRMRE
ADLTHIPVIVGGIIPEDDAERLRAMGVAKVYTPKDFELNRIMFDIVGLVDDTPIAAE
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