SitesBLAST
Comparing 351618 FitnessBrowser__Btheta:351618 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)
P11653 Methylmalonyl-CoA mutase large subunit; MCM-alpha; EC 5.4.99.2 from Propionibacterium freudenreichii subsp. shermanii (see 4 papers)
64% identity, 99% coverage: 5:711/715 of query aligns to 7:722/728 of P11653
- Y75 (= Y69) binding
- M78 (= M72) binding
- R82 (= R76) binding
- T85 (= T79) binding
- R87 (= R81) binding
- Y89 (= Y83) binding ; mutation to F: Does not significantly affect affinity for succiny-CoA, but kcat is lowered about 580-fold.
- S114 (= S108) binding
- F117 (= F111) binding
- A139 (= A133) binding
- T195 (= T189) binding
- Q197 (= Q191) binding
- V206 (= V200) binding
- R207 (= R201) binding ; binding
- H244 (= H238) binding
- R283 (= R277) binding
- S285 (= S279) binding
- G333 (= G327) binding
- E370 (= E364) binding
- A373 (= A367) binding
- G609 (= G598) binding
- H610 (= H599) binding axial binding residue
- D611 (= D600) binding
- R612 (= R601) binding
- S655 (= S644) binding
- L657 (= L646) binding
- G686 (= G675) binding
- T709 (= T698) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
6reqA Methylmalonyl-coa mutase, 3-carboxypropyl-coa inhibitor complex (see paper)
64% identity, 99% coverage: 5:711/715 of query aligns to 6:721/727 of 6reqA
- active site: Y88 (= Y83), Y242 (= Y237), H243 (= H238), K603 (= K593), D607 (= D597), H609 (= H599)
- binding 3-carboxypropyl-coenzyme a: Y74 (= Y69), T76 (≠ V71), M77 (= M72), F80 (≠ L75), R81 (= R76), T84 (= T79), R86 (= R81), Y88 (= Y83), S113 (= S108), S163 (= S158), T165 (= T160), T194 (= T189), R206 (= R201), H243 (= H238), R282 (= R277), S284 (= S279), F286 (= F281), H327 (= H322), Q329 (= Q324), Q360 (= Q355)
- binding cobalamin: Y88 (= Y83), F116 (= F111), L118 (= L113), H121 (= H116), A138 (= A133), R206 (= R201), E246 (= E241), G332 (= G327), W333 (= W328), E369 (= E364), A370 (= A365), A372 (= A367), G608 (= G598), H609 (= H599), D610 (= D600), R611 (= R601), G612 (= G602), I616 (≠ V606), Y620 (= Y610), S654 (= S644), L656 (= L646), G658 (≠ A648), G684 (= G674), G685 (= G675), Y704 (≠ F694), T705 (≠ G695), T708 (= T698)
4reqA Methylmalonyl-coa mutase substrate complex (see paper)
64% identity, 99% coverage: 5:711/715 of query aligns to 5:720/726 of 4reqA
- active site: Y87 (= Y83), Y241 (= Y237), H242 (= H238), K602 (= K593), D606 (= D597), H608 (= H599)
- binding cobalamin: Y87 (= Y83), L117 (= L113), A137 (= A133), V204 (= V200), R205 (= R201), H242 (= H238), E245 (= E241), G331 (= G327), W332 (= W328), E368 (= E364), A369 (= A365), A371 (= A367), L372 (= L368), G607 (= G598), H608 (= H599), D609 (= D600), R610 (= R601), G611 (= G602), I615 (≠ V606), S653 (= S644), L655 (= L646), G683 (= G674), G684 (= G675), V685 (= V676), Y703 (≠ F694), T704 (≠ G695), T707 (= T698)
- binding methylmalonyl-coenzyme a: Y73 (= Y69), M76 (= M72), F79 (≠ L75), R80 (= R76), T83 (= T79), R85 (= R81), Y87 (= Y83), S112 (= S108), S162 (= S158), T164 (= T160), T193 (= T189), R205 (= R201), N234 (= N230), Y241 (= Y237), H242 (= H238), R281 (= R277), S283 (= S279), F285 (= F281), H326 (= H322), Q328 (= Q324), Q359 (= Q355), S360 (= S356)
- binding succinyl-coenzyme a: Y73 (= Y69), M76 (= M72), F79 (≠ L75), R80 (= R76), T83 (= T79), R85 (= R81), Y87 (= Y83), S162 (= S158), T164 (= T160), T193 (= T189), Q195 (= Q191), R205 (= R201), N234 (= N230), Y241 (= Y237), H242 (= H238), R281 (= R277), S283 (= S279), F285 (= F281), R324 (= R320), H326 (= H322), Q359 (= Q355)
7reqA Methylmalonyl-coa mutase, 2-carboxypropyl-coa inhibitor complex (see paper)
64% identity, 99% coverage: 5:711/715 of query aligns to 4:719/725 of 7reqA
- active site: Y86 (= Y83), Y240 (= Y237), H241 (= H238), K601 (= K593), D605 (= D597), H607 (= H599)
- binding 2-carboxypropyl-coenzyme a: Y72 (= Y69), T74 (≠ V71), M75 (= M72), F78 (≠ L75), R79 (= R76), T82 (= T79), R84 (= R81), Y86 (= Y83), S161 (= S158), T163 (= T160), T192 (= T189), R204 (= R201), H241 (= H238), R280 (= R277), S282 (= S279), F284 (= F281), H325 (= H322), Q358 (= Q355)
- binding cobalamin: Y86 (= Y83), L116 (= L113), A136 (= A133), R204 (= R201), E244 (= E241), G330 (= G327), W331 (= W328), E367 (= E364), A368 (= A365), A370 (= A367), G606 (= G598), H607 (= H599), D608 (= D600), R609 (= R601), G610 (= G602), I614 (≠ V606), S652 (= S644), L654 (= L646), G682 (= G674), G683 (= G675), Y702 (≠ F694), T703 (≠ G695), T706 (= T698)
3reqA Methylmalonyl-coa mutase, substrate-free state (poor quality structure) (see paper)
64% identity, 99% coverage: 5:711/715 of query aligns to 4:719/725 of 3reqA
- active site: Y86 (= Y83), Y240 (= Y237), H241 (= H238), K601 (= K593), D605 (= D597), H607 (= H599)
- binding adenosine: Y86 (= Y83), Y240 (= Y237), E244 (= E241), G330 (= G327)
- binding cobalamin: L116 (= L113), V203 (= V200), R204 (= R201), E244 (= E241), G330 (= G327), W331 (= W328), A368 (= A365), G606 (= G598), H607 (= H599), D608 (= D600), R609 (= R601), G610 (= G602), I614 (≠ V606), G650 (= G642), S652 (= S644), L654 (= L646), G682 (= G674), G683 (= G675), Y702 (≠ F694), T703 (≠ G695), P704 (= P696), T706 (= T698)
2reqA Methylmalonyl-coa mutase, non-productive coa complex, in open conformation representing substrate-free state (see paper)
64% identity, 99% coverage: 5:711/715 of query aligns to 4:719/725 of 2reqA
- active site: Y86 (= Y83), Y240 (= Y237), H241 (= H238), K601 (= K593), D605 (= D597), H607 (= H599)
- binding cobalamin: V203 (= V200), R204 (= R201), E244 (= E241), A245 (= A242), W331 (= W328), A368 (= A365), G606 (= G598), H607 (= H599), D608 (= D600), R609 (= R601), G610 (= G602), I614 (≠ V606), G650 (= G642), S652 (= S644), L654 (= L646), A655 (= A647), G682 (= G674), G683 (= G675), Y702 (≠ F694), T703 (≠ G695), T706 (= T698)
- binding coenzyme a: Y72 (= Y69), R79 (= R76), K318 (= K315)
5reqA Methylmalonyl-coa mutase, y89f mutant, substrate complex (see paper)
64% identity, 99% coverage: 5:711/715 of query aligns to 4:719/725 of 5reqA
- active site: F86 (≠ Y83), Y240 (= Y237), H241 (= H238), K601 (= K593), D605 (= D597), H607 (= H599)
- binding cobalamin: L116 (= L113), A136 (= A133), R204 (= R201), H241 (= H238), E244 (= E241), G330 (= G327), W331 (= W328), E367 (= E364), A368 (= A365), A370 (= A367), G606 (= G598), H607 (= H599), D608 (= D600), R609 (= R601), G610 (= G602), I614 (≠ V606), S652 (= S644), L654 (= L646), G682 (= G674), G683 (= G675), V684 (= V676), Y702 (≠ F694), T703 (≠ G695), T706 (= T698)
- binding methylmalonyl(carbadethia)-coenzyme a: Y72 (= Y69), T74 (≠ V71), M75 (= M72), R79 (= R76), T82 (= T79), R84 (= R81), F86 (≠ Y83), S111 (= S108), S161 (= S158), T163 (= T160), T192 (= T189), Q194 (= Q191), R204 (= R201), N233 (= N230), H241 (= H238), R280 (= R277), S282 (= S279), F284 (= F281), T324 (= T321), H325 (= H322), Q358 (= Q355), S359 (= S356)
- binding succinyl(carbadethia)-coenzyme a: Y72 (= Y69), T74 (≠ V71), M75 (= M72), R79 (= R76), T82 (= T79), R84 (= R81), F86 (≠ Y83), S161 (= S158), T163 (= T160), T192 (= T189), R204 (= R201), N233 (= N230), H241 (= H238), R280 (= R277), S282 (= S279), F284 (= F281), H325 (= H322), Q358 (= Q355)
1e1cA Methylmalonyl-coa mutase h244a mutant (see paper)
64% identity, 99% coverage: 5:711/715 of query aligns to 6:721/727 of 1e1cA
- active site: Y88 (= Y83), Y242 (= Y237), A243 (≠ H238), K603 (= K593), D607 (= D597), H609 (= H599)
- binding cobalamin: Y88 (= Y83), L118 (= L113), H121 (= H116), A138 (= A133), V205 (= V200), R206 (= R201), E246 (= E241), G332 (= G327), W333 (= W328), E369 (= E364), A370 (= A365), A372 (= A367), L373 (= L368), G608 (= G598), H609 (= H599), D610 (= D600), R611 (= R601), G612 (= G602), I616 (≠ V606), Y620 (= Y610), S654 (= S644), L656 (= L646), G684 (= G674), G685 (= G675), V686 (= V676), Y704 (≠ F694), T705 (≠ G695), T708 (= T698), S713 (≠ A703)
- binding desulfo-coenzyme a: Y74 (= Y69), M77 (= M72), F80 (≠ L75), R81 (= R76), T84 (= T79), R86 (= R81), S113 (= S108), S163 (= S158), T165 (= T160), T194 (= T189), R282 (= R277), S284 (= S279), H327 (= H322), Q360 (= Q355)
6oxdA Structure of mycobacterium tuberculosis methylmalonyl-coa mutase with adenosyl cobalamin (see paper)
66% identity, 95% coverage: 32:713/715 of query aligns to 45:730/736 of 6oxdA
- active site: Y100 (= Y83), Y254 (= Y237), H255 (= H238), K610 (= K593), D614 (= D597), H616 (= H599)
- binding cobalamin: Y100 (= Y83), L130 (= L113), H133 (= H116), A150 (= A133), R218 (= R201), E258 (= E241), G344 (= G327), W345 (= W328), E381 (= E364), A382 (= A365), A384 (= A367), L385 (= L368), G615 (= G598), H616 (= H599), D617 (= D600), R618 (= R601), S661 (= S644), L663 (= L646), A665 (= A648), G691 (= G674), G692 (= G675), F711 (= F694), P712 (≠ G695), T715 (= T698)
- binding Itaconyl coenzyme A: Y86 (= Y69), T88 (≠ V71), M89 (= M72), Q93 (≠ R76), T96 (= T79), R98 (= R81), Y100 (= Y83), S175 (= S158), T177 (= T160), T206 (= T189), R218 (= R201), H255 (= H238), R294 (= R277), S296 (= S279), F298 (= F281), R337 (= R320), T338 (= T321), H339 (= H322), Q341 (= Q324), Q372 (= Q355)
P22033 Methylmalonyl-CoA mutase, mitochondrial; MCM; Methylmalonyl-CoA isomerase; EC 5.4.99.2 from Homo sapiens (Human) (see 28 papers)
65% identity, 95% coverage: 32:709/715 of query aligns to 61:737/750 of P22033
- I69 (≠ V40) to V: in MMAM; likely benign; dbSNP:rs115923556
- P86 (≠ A59) 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 (= G60) to E: in MMAM; mut0; dbSNP:rs1554160986
- R93 (= R66) to H: in MMAM; mut0; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918251
- G94 (= G67) to R: in MMAM; mut0; dbSNP:rs727504022; to V: in MMAM; mut- and mut0; dbSNP:rs535411418
- P95 (= P68) to R: in MMAM; mut0; dbSNP:rs190834116
- YPTM 96:99 (≠ YSVM 69:72) binding
- Y100 (= Y73) 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 (= W78) to R: in MMAM; mut0; dbSNP:rs121918249
- TIRQY 106:110 (= TIRQY 79:83) binding
- R108 (= R81) to C: in MMAM; mut0; dbSNP:rs121918257; to G: in MMAM; mut-; to H: in MMAM; mut0; dbSNP:rs483352778
- Q109 (= Q82) to R: in MMAM; mut0; dbSNP:rs1461110052
- G133 (= G106) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253828
- A137 (= A110) to V: in MMAM; mut0; dbSNP:rs941483851
- D139 (= D112) to N: in MMAM; uncertain significance; dbSNP:rs879253829
- L140 (= L113) to P: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- A141 (= A114) to T: in MMAM; decreased protein expression; dbSNP:rs1554160730
- H143 (= H116) to Y: in MMAM; mut0
- G145 (= G118) to S: in MMAM; mut0
- S148 (≠ P121) to L: in MMAM; mut0; dbSNP:rs1300547552
- D156 (= D129) to N: in MMAM; mut-
- G158 (= G131) to V: in MMAM; mut0
- G161 (= G134) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; to V: in MMAM; decreased protein expression
- F174 (= F147) to S: in MMAM; mut0; dbSNP:rs864309733
- M186 (= M159) to V: in MMAM; mut-; dbSNP:rs148331800
- T187 (= T160) to S: in MMAM; mut0; dbSNP:rs879253830
- N189 (= N162) to I: in MMAM; mut-; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs200908035; to K: in MMAM; mut-; dbSNP:rs1561959114
- A191 (= A164) to E: in MMAM; mut- and mut0; affects proper folding; reduced protein level; decreased methylmalonyl-CoA mutase activity; dbSNP:rs760782399
- A197 (= A170) to E: in MMAM; mut0
- G203 (= G176) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs778702777
- E205 (= E178) natural variant: Missing (in MMAM; mut0; dbSNP:rs879253831)
- G215 (= G188) to C: in MMAM; mut- and mut0; dbSNP:rs121918258; to S: in MMAM; mut0; dbSNP:rs121918258
- TIQ 216:218 (= TIQ 189:191) binding
- Q218 (= Q191) to H: in MMAM; mut0 and mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability; dbSNP:rs1446389693
- N219 (= N192) to Y: in MMAM; mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; dbSNP:rs121918256
- R228 (= R201) binding ; to Q: in MMAM; mut0; dbSNP:rs770810987
- T230 (= T203) to I: in MMAM; mut-; to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253833
- Y231 (= Y204) 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 (= K228) binding
- S262 (= S235) to N: in MMAM; mut0
- H265 (= H238) binding ; to Y: in MMAM; mut-
- E276 (= E249) to D: in MMAM; uncertain significance; mut-; dbSNP:rs12175488
- L281 (= L254) to S: in MMAM; mut0; dbSNP:rs796052007
- G284 (= G257) to E: in MMAM; mut0; dbSNP:rs879253835; to R: in MMAM; mut0; dbSNP:rs761477436
- S288 (≠ L261) to P: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1179778233
- G291 (= G264) to E: in MMAM; mut0
- Q293 (≠ A266) to P: in MMAM; mut0
- RLS 304:306 (= RLS 277:279) binding
- L305 (= L278) to S: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554160246
- S306 (= S279) to F: in MMAM; mut0; dbSNP:rs1085307929
- W309 (= W282) to G: in MMAM; decreased protein expression
- G312 (= G285) to V: in MMAM; mut0; dbSNP:rs864309734
- Y316 (≠ F289) 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 (= A297) to T: in MMAM; mut-; dbSNP:rs780387525
- R326 (= R299) to K: in MMAM; uncertain significance; dbSNP:rs758577372
- L328 (= L301) 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 (= S316) 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 (≠ A318) natural variant: Missing (in MMAM; mut0)
- L347 (= L319) to R: in MMAM; mut0; dbSNP:rs1026703654
- H350 (= H322) to Y: in MMAM; mut0; dbSNP:rs1407914109
- L358 (= L330) to P: in MMAM; mut0
- N366 (= N338) 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 (= R341) 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 (= T342) to P: in MMAM; mut0; dbSNP:rs368790885
- A377 (= A349) to E: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918250
- Q383 (= Q355) to H: in MMAM; mut0; to P: in MMAM; mut0
- H386 (= H358) to N: in MMAM; mut0; dbSNP:rs1554159937; to R: in MMAM; mut0; dbSNP:rs866933356
- T387 (= T359) 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 (= N360) to H: in MMAM; mut0; dbSNP:rs766010704; to K: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253840
- S389 (≠ A361) natural variant: Missing (in MMAM; mut0)
- I412 (= I384) natural variant: Missing (in MMAM; mut0)
- P424 (= P396) to L: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253842
- G426 (= G398) 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 (= G399) to D: in MMAM; mut0; dbSNP:rs753288303
- G454 (= G426) to E: in MMAM; mut0
- A499 (≠ P471) to T: in dbSNP:rs2229385
- I505 (= I477) to T: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- Q514 (= Q486) to E: in MMAM; uncertain significance; to K: in MMAM; decreased protein expression
- L518 (= L490) to P: in MMAM; mut0; dbSNP:rs864309738
- R532 (≠ K504) to H: in dbSNP:rs1141321
- A535 (= A507) to P: in MMAM; mut0; dbSNP:rs760183775
- A552 (= A524) to V: in MMAM; uncertain significance; dbSNP:rs879253845
- C560 (≠ A532) to Y: in MMAM; mut0; dbSNP:rs1238333040
- T566 (≠ S538) to R: in MMAM; mut0
- F573 (≠ V545) 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 (= Y559) to C: in MMAM; mut-
- I597 (≠ F569) to R: in MMAM; no changed in protein expression; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554158951
- P615 (= P587) 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 (= R588) to C: in MMAM; mut0; dbSNP:rs765284825
- L617 (≠ I589) to R: in MMAM; mut0; dbSNP:rs1554158775
- K621 (= K593) to N: in MMAM; mut0
- G623 (= G595) to R: in MMAM; mut0; dbSNP:rs121918254
- Q624 (= Q596) to R: in MMAM; no effect on protein abundance; dbSNP:rs768521956
- D625 (= D597) 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 (= G598) to C: in MMAM; mut-; dbSNP:rs982110849
- H627 (= H599) binding axial binding residue; to R: in MMAM; mut0; dbSNP:rs372486357
- G630 (= G602) to E: in MMAM; mut0; dbSNP:rs143023066
- V633 (= V605) 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 (= G609) to E: in MMAM; mut-; to R: in MMAM; mut0; dbSNP:rs781501004
- F638 (≠ Y610) to I: in MMAM; mut0
- D640 (= D612) to Y: in MMAM; mut0; dbSNP:rs865815395
- G642 (= G614) to R: in MMAM; mut-; dbSNP:rs747897332
- G648 (= G620) 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 (= V641) to E: in MMAM; mut0; dbSNP:rs1360470463
- I671 (≠ V643) to V: in dbSNP:rs8589
- L674 (= L646) to F: in MMAM; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1164271240
- H678 (= H650) to R: in MMAM; mut-; dbSNP:rs147094927
- E684 (≠ Q656) natural variant: E -> EL (in MMAM; mut-)
- L685 (≠ I657) to R: in MMAM; mut-; dbSNP:rs864309739
- R694 (= R666) 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 (≠ I672) 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 (= G675) to R: in MMAM; mut0; dbSNP:rs121918255
- G717 (= G689) 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 (= G695) 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)
2xiqA Crystal structure of human methylmalonyl-coa mutase in complex with adenosylcobalamin and malonyl-coa (see paper)
65% identity, 95% coverage: 32:709/715 of query aligns to 26:702/714 of 2xiqA
- active site: Y75 (= Y83), Y229 (= Y237), H230 (= H238), K586 (= K593), D590 (= D597), H592 (= H599)
- binding cobalamin: Y75 (= Y83), L105 (= L113), H108 (= H116), A125 (= A133), R193 (= R201), E233 (= E241), G320 (= G327), W321 (= W328), E357 (= E364), G360 (≠ A367), L361 (= L368), G591 (= G598), H592 (= H599), D593 (= D600), R594 (= R601), G595 (= G602), I599 (≠ V606), G635 (= G642), S637 (= S644), L639 (= L646), A641 (= A648), G667 (= G674), G668 (= G675), F687 (= F694), G688 (= G695), T691 (= T698)
- binding malonyl-coenzyme a: Y61 (= Y69), T63 (≠ V71), M64 (= M72), R68 (= R76), T71 (= T79), R73 (= R81), Y75 (= Y83), S150 (= S158), T152 (= T160), T181 (= T189), R193 (= R201), K220 (= K228), H230 (= H238), R269 (= R277), S271 (= S279), F273 (= F281), R313 (= R320), A314 (≠ T321), H315 (= H322), Q317 (= Q324), Q348 (= Q355)
8dyjB Crystal structure of human methylmalonyl-coa mutase in complex with adp and cob(ii)alamin (see paper)
65% identity, 95% coverage: 32:709/715 of query aligns to 25:701/708 of 8dyjB
- binding adenosine-5'-diphosphate: Y74 (= Y83), T151 (= T160), R192 (= R201), Y228 (= Y237), H229 (= H238), F272 (= F281), Q316 (= Q324), N352 (= N360), E356 (= E364), L360 (= L368), P361 (= P369)
- binding cobalamin: F102 (= F111), L104 (= L113), H107 (= H116), A124 (= A133), V191 (= V200), R192 (= R201), H229 (= H238), E232 (= E241), G319 (= G327), W320 (= W328), E356 (= E364), G359 (≠ A367), L360 (= L368), G590 (= G598), H591 (= H599), D592 (= D600), R593 (= R601), G594 (= G602), I598 (≠ V606), S636 (= S644), L638 (= L646), A640 (= A648), G666 (= G674), G667 (= G675), V668 (= V676), F686 (= F694), G687 (= G695), T690 (= T698)
8gjuJ Crystal structure of human methylmalonyl-coa mutase (mmut) in complex with methylmalonic acidemia type a protein (mmaa), coenzyme a, and gdp (see paper)
64% identity, 95% coverage: 32:709/715 of query aligns to 26:679/689 of 8gjuJ
- binding coenzyme a: Y61 (= Y69), T63 (≠ V71), R68 (= R76), T71 (= T79), R73 (= R81), S150 (= S158), T152 (= T160), T181 (= T189), Q183 (= Q191), N222 (= N230), R269 (= R277), S271 (= S279), R313 (= R320), A314 (≠ T321), H315 (= H322), Q348 (= Q355)
4r3uA Crystal structure of 2-hydroxyisobutyryl-coa mutase (see paper)
40% identity, 74% coverage: 19:549/715 of query aligns to 24:556/557 of 4r3uA
- active site: I89 (≠ Y83), Y243 (= Y237), H244 (= H238)
- binding 3-hydroxybutanoyl-coenzyme a: Y75 (= Y69), T77 (≠ V71), M78 (= M72), R82 (= R76), T85 (= T79), R87 (= R81), I89 (≠ Y83), D116 (≠ A110), S164 (= S158), T166 (= T160), T195 (= T189), Q197 (= Q191), R234 (≠ K228), N236 (= N230), N239 (≠ S233), Y243 (= Y237), H244 (= H238), R283 (= R277), F287 (= F281), R327 (= R320), F328 (≠ T321), H329 (= H322), Q331 (= Q324), Q362 (= Q355)
- 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 (= Y69), T77 (≠ V71), M78 (= M72), R82 (= R76), T85 (= T79), R87 (= R81), I89 (≠ Y83), D116 (≠ A110), S164 (= S158), T166 (= T160), T195 (= T189), Q197 (= Q191), R234 (≠ K228), N236 (= N230), N239 (≠ S233), H244 (= H238), R283 (= R277), F287 (= F281), R327 (= R320), F328 (≠ T321), H329 (= H322), Q331 (= Q324), Q362 (= Q355)
- binding cobalamin: D116 (≠ A110), M119 (≠ L113), E139 (≠ A133), Q207 (≠ R201), E209 (≠ T203), E247 (= E241), A334 (≠ G327), E371 (= E364), A372 (= A365), A374 (= A367)
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)
40% identity, 74% coverage: 19:549/715 of query aligns to 25:557/562 of I3VE77
- YPTM 76:79 (≠ YSVM 69:72) binding
- TMR 86:88 (≠ TIR 79:81) binding
- I90 (≠ Y83) 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 (≠ A110) 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 189:191) binding
- R235 (≠ K228) binding
- N240 (≠ S233) binding
- H245 (= H238) binding
- R284 (= R277) binding
4xc6A Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, and mg (holo-icmf/gdp) (see paper)
37% identity, 66% coverage: 81:549/715 of query aligns to 570:1064/1067 of 4xc6A
- active site: F572 (≠ Y83), Y753 (= Y237), H754 (= H238)
- binding cobalamin: F601 (= F111), L606 (≠ H116), S624 (≠ A133), Q716 (≠ R201), H754 (= H238), E757 (= E241), A758 (= A242), G842 (= G327), R843 (≠ W328), E879 (= E364), A880 (= A365), T882 (≠ A367), H967 (≠ D452)
- binding guanosine-5'-diphosphate: E947 (= E432)
Sites not aligning to the query:
- active site: 6
- binding cobalamin: 18, 19, 20, 21, 22, 26, 66, 67, 94, 96, 98, 116, 117, 118, 129
- binding guanosine-5'-diphosphate: 199, 201, 202, 203, 204, 245, 337, 338, 340, 375, 377
- binding magnesium ion: 203, 229, 242, 242, 290, 290
5cjtA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isobutyryl-coenzyme a (see paper)
37% identity, 66% coverage: 81:549/715 of query aligns to 567:1059/1062 of 5cjtA
- active site: F569 (≠ Y83), Y750 (= Y237), H751 (= H238)
- binding cobalamin: F598 (= F111), L603 (≠ H116), S621 (≠ A133), Q713 (≠ R201), H751 (= H238), E754 (= E241), A755 (= A242), G839 (= G327), R840 (≠ W328), E876 (= E364), A877 (= A365), T879 (≠ A367), H964 (≠ D452)
- binding isobutyryl-coenzyme a: R567 (= R81), F569 (≠ Y83), R593 (≠ G106), S648 (= S158), T650 (= T160), R699 (≠ A187), T701 (= T189), Q703 (= Q191), Y743 (≠ N230), Y750 (= Y237), H751 (= H238), S792 (= S279), F794 (= F281), R827 (≠ K315), K832 (≠ R320), H834 (= H322)
- binding guanosine-5'-diphosphate: E944 (= E432)
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
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)
37% identity, 66% coverage: 81:549/715 of query aligns to 596:1090/1093 of Q1LRY0
- F598 (≠ Y83) 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 (≠ G106) binding
- R728 (≠ A187) binding
- Y772 (≠ N230) binding
- S821 (= S279) binding
- R856 (≠ K315) binding
- K861 (≠ R320) binding
- E973 (= E432) 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
Q5KUG0 Fused isobutyryl-CoA mutase; EC 5.4.99.13; EC 3.6.5.- from Geobacillus kaustophilus (strain HTA426) (see paper)
34% identity, 70% coverage: 46:549/715 of query aligns to 562:1083/1086 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)
36% identity, 66% coverage: 81:549/715 of query aligns to 564:1050/1053 of 4xc7A
- active site: F566 (≠ Y83), Y747 (= Y237), H748 (= H238)
- binding Butyryl Coenzyme A: R564 (= R81), F566 (≠ Y83), R590 (≠ G106), S645 (= S158), T647 (= T160), R696 (≠ A187), T698 (= T189), Y740 (≠ N230), S789 (= S279), F791 (= F281), R824 (≠ K315), K829 (≠ R320), H831 (= H322)
Sites not aligning to the query:
Query Sequence
>351618 FitnessBrowser__Btheta:351618
MRKDFKNLDIYAAFQPANGAEWQKANGISADWNTPEHIDVKPVYTKEDLEGMEHLGYAAG
LPPYLRGPYSVMYTLRPWTIRQYAGFSTAEESNAFYRRNLASGQKGLSVAFDLATHRGYD
PDHERVVGDVGKAGVSICSLENMKVLFDGIPLSKMSVSMTMNGAVLPIMAFYINAGLEQG
AKLEEMAGTIQNDILKEFMVRNTYIYPPAFSMKIISDIFEYTSQKMPKFNSISISGYHMQ
EAGATADIELAYTLADGLEYLRAGTAAGIDIDAFAPRLSFFWAIGTNHFMEIAKMRAARM
LWAKIVKQFNPKNPKSLALRTHSQTSGWSLTEQDPFNNVGRTCIEAMAAALGHTQSLHTN
ALDEAIALPTDFSARIARNTQIYIQEETYICKNVDPWGGSYYVEALTNELAHKAWERIEE
VEKLGGMAKAIETGIPKMRIEEAAARTQARIDSGSQTIVGVNKYRLEKEAPIDILEIDNT
AVRLEQIENLKRLKEGRNQAEVDKALAAITECVETGKGNLLELAVEAARVRATLGEISYA
CEKVVGRYKAIIRTISGVYSSESKNDGDFKRACELAEKFAKKEGRQPRIMVAKMGQDGHD
RGAKVVATGYADCGFDVDMGPLFQTPAEAAREAVENDVHVVGVSSLAAGHKTLIPQIMEE
LKKLGREDIVVIAGGVIPAQDYDFLYKAGVAAIFGPGTPVAKAACQILEILMDEE
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