SitesBLAST
Comparing AZOBR_RS24250 FitnessBrowser__azobra:AZOBR_RS24250 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)
6oxdA Structure of mycobacterium tuberculosis methylmalonyl-coa mutase with adenosyl cobalamin (see paper)
74% identity, 98% coverage: 7:727/732 of query aligns to 6:734/736 of 6oxdA
- active site: Y100 (= Y92), Y254 (= Y246), H255 (= H247), K610 (= K603), D614 (= D607), H616 (= H609)
- binding cobalamin: Y100 (= Y92), L130 (= L122), H133 (= H125), A150 (= A142), R218 (= R210), E258 (= E250), G344 (= G336), W345 (= W337), E381 (= E373), A382 (= A374), A384 (= A376), L385 (= L377), G615 (= G608), H616 (= H609), D617 (= D610), R618 (= R611), S661 (= S654), L663 (= L656), A665 (= A658), G691 (= G684), G692 (= G685), F711 (= F704), P712 (= P705), T715 (= T708)
- binding Itaconyl coenzyme A: Y86 (= Y78), T88 (= T80), M89 (= M81), Q93 (≠ K85), T96 (= T88), R98 (= R90), Y100 (= Y92), S175 (= S167), T177 (= T169), T206 (= T198), R218 (= R210), H255 (= H247), R294 (= R286), S296 (= S288), F298 (= F290), R337 (= R329), T338 (= T330), H339 (= H331), Q341 (= Q333), Q372 (= Q364)
P11653 Methylmalonyl-CoA mutase large subunit; MCM-alpha; EC 5.4.99.2 from Propionibacterium freudenreichii subsp. shermanii (see 4 papers)
70% identity, 98% coverage: 1:721/732 of query aligns to 1:722/728 of P11653
- M1 (= M1) modified: Initiator methionine, Removed
- Y75 (= Y78) binding
- M78 (= M81) binding
- R82 (≠ K85) binding
- T85 (= T88) binding
- R87 (= R90) binding
- Y89 (= Y92) binding ; mutation to F: Does not significantly affect affinity for succiny-CoA, but kcat is lowered about 580-fold.
- S114 (= S117) binding
- F117 (= F120) binding
- A139 (= A142) binding
- T195 (= T198) binding
- Q197 (= Q200) binding
- V206 (= V209) binding
- R207 (= R210) binding ; binding
- H244 (= H247) binding
- R283 (= R286) binding
- S285 (= S288) binding
- G333 (= G336) binding
- E370 (= E373) binding
- A373 (= A376) binding
- G609 (= G608) binding
- H610 (= H609) binding axial binding residue
- D611 (= D610) binding
- R612 (= R611) binding
- S655 (= S654) binding
- L657 (= L656) binding
- G686 (= G685) binding
- T709 (= T708) binding
6reqA Methylmalonyl-coa mutase, 3-carboxypropyl-coa inhibitor complex (see paper)
70% identity, 98% coverage: 2:721/732 of query aligns to 1:721/727 of 6reqA
- active site: Y88 (= Y92), Y242 (= Y246), H243 (= H247), K603 (= K603), D607 (= D607), H609 (= H609)
- binding 3-carboxypropyl-coenzyme a: Y74 (= Y78), T76 (= T80), M77 (= M81), F80 (≠ D84), R81 (≠ K85), T84 (= T88), R86 (= R90), Y88 (= Y92), S113 (= S117), S163 (= S167), T165 (= T169), T194 (= T198), R206 (= R210), H243 (= H247), R282 (= R286), S284 (= S288), F286 (= F290), H327 (= H331), Q329 (= Q333), Q360 (= Q364)
- binding cobalamin: Y88 (= Y92), F116 (= F120), L118 (= L122), H121 (= H125), A138 (= A142), R206 (= R210), E246 (= E250), G332 (= G336), W333 (= W337), E369 (= E373), A370 (= A374), A372 (= A376), G608 (= G608), H609 (= H609), D610 (= D610), R611 (= R611), G612 (= G612), I616 (= I616), Y620 (≠ F620), S654 (= S654), L656 (= L656), G658 (≠ A658), G684 (= G684), G685 (= G685), Y704 (≠ F704), T705 (≠ P705), T708 (= T708)
4reqA Methylmalonyl-coa mutase substrate complex (see paper)
70% identity, 98% coverage: 3:721/732 of query aligns to 1:720/726 of 4reqA
- active site: Y87 (= Y92), Y241 (= Y246), H242 (= H247), K602 (= K603), D606 (= D607), H608 (= H609)
- binding cobalamin: Y87 (= Y92), L117 (= L122), A137 (= A142), V204 (= V209), R205 (= R210), H242 (= H247), E245 (= E250), G331 (= G336), W332 (= W337), E368 (= E373), A369 (= A374), A371 (= A376), L372 (= L377), G607 (= G608), H608 (= H609), D609 (= D610), R610 (= R611), G611 (= G612), I615 (= I616), S653 (= S654), L655 (= L656), G683 (= G684), G684 (= G685), V685 (= V686), Y703 (≠ F704), T704 (≠ P705), T707 (= T708)
- binding methylmalonyl-coenzyme a: Y73 (= Y78), M76 (= M81), F79 (≠ D84), R80 (≠ K85), T83 (= T88), R85 (= R90), Y87 (= Y92), S112 (= S117), S162 (= S167), T164 (= T169), T193 (= T198), R205 (= R210), N234 (= N239), Y241 (= Y246), H242 (= H247), R281 (= R286), S283 (= S288), F285 (= F290), H326 (= H331), Q328 (= Q333), Q359 (= Q364), S360 (= S365)
- binding succinyl-coenzyme a: Y73 (= Y78), M76 (= M81), F79 (≠ D84), R80 (≠ K85), T83 (= T88), R85 (= R90), Y87 (= Y92), S162 (= S167), T164 (= T169), T193 (= T198), Q195 (= Q200), R205 (= R210), N234 (= N239), Y241 (= Y246), H242 (= H247), R281 (= R286), S283 (= S288), F285 (= F290), R324 (= R329), H326 (= H331), Q359 (= Q364)
7reqA Methylmalonyl-coa mutase, 2-carboxypropyl-coa inhibitor complex (see paper)
70% identity, 98% coverage: 4:721/732 of query aligns to 1:719/725 of 7reqA
- active site: Y86 (= Y92), Y240 (= Y246), H241 (= H247), K601 (= K603), D605 (= D607), H607 (= H609)
- binding 2-carboxypropyl-coenzyme a: Y72 (= Y78), T74 (= T80), M75 (= M81), F78 (≠ D84), R79 (≠ K85), T82 (= T88), R84 (= R90), Y86 (= Y92), S161 (= S167), T163 (= T169), T192 (= T198), R204 (= R210), H241 (= H247), R280 (= R286), S282 (= S288), F284 (= F290), H325 (= H331), Q358 (= Q364)
- binding cobalamin: Y86 (= Y92), L116 (= L122), A136 (= A142), R204 (= R210), E244 (= E250), G330 (= G336), W331 (= W337), E367 (= E373), A368 (= A374), A370 (= A376), G606 (= G608), H607 (= H609), D608 (= D610), R609 (= R611), G610 (= G612), I614 (= I616), S652 (= S654), L654 (= L656), G682 (= G684), G683 (= G685), Y702 (≠ F704), T703 (≠ P705), T706 (= T708)
3reqA Methylmalonyl-coa mutase, substrate-free state (poor quality structure) (see paper)
70% identity, 98% coverage: 4:721/732 of query aligns to 1:719/725 of 3reqA
- active site: Y86 (= Y92), Y240 (= Y246), H241 (= H247), K601 (= K603), D605 (= D607), H607 (= H609)
- binding adenosine: Y86 (= Y92), Y240 (= Y246), E244 (= E250), G330 (= G336)
- binding cobalamin: L116 (= L122), V203 (= V209), R204 (= R210), E244 (= E250), G330 (= G336), W331 (= W337), A368 (= A374), G606 (= G608), H607 (= H609), D608 (= D610), R609 (= R611), G610 (= G612), I614 (= I616), G650 (= G652), S652 (= S654), L654 (= L656), G682 (= G684), G683 (= G685), Y702 (≠ F704), T703 (≠ P705), P704 (= P706), T706 (= T708)
2reqA Methylmalonyl-coa mutase, non-productive coa complex, in open conformation representing substrate-free state (see paper)
70% identity, 98% coverage: 4:721/732 of query aligns to 1:719/725 of 2reqA
- active site: Y86 (= Y92), Y240 (= Y246), H241 (= H247), K601 (= K603), D605 (= D607), H607 (= H609)
- binding cobalamin: V203 (= V209), R204 (= R210), E244 (= E250), A245 (= A251), W331 (= W337), A368 (= A374), G606 (= G608), H607 (= H609), D608 (= D610), R609 (= R611), G610 (= G612), I614 (= I616), G650 (= G652), S652 (= S654), L654 (= L656), A655 (= A657), G682 (= G684), G683 (= G685), Y702 (≠ F704), T703 (≠ P705), T706 (= T708)
- binding coenzyme a: Y72 (= Y78), R79 (≠ K85), K318 (= K324)
1e1cA Methylmalonyl-coa mutase h244a mutant (see paper)
70% identity, 98% coverage: 2:721/732 of query aligns to 1:721/727 of 1e1cA
- active site: Y88 (= Y92), Y242 (= Y246), A243 (≠ H247), K603 (= K603), D607 (= D607), H609 (= H609)
- binding cobalamin: Y88 (= Y92), L118 (= L122), H121 (= H125), A138 (= A142), V205 (= V209), R206 (= R210), E246 (= E250), G332 (= G336), W333 (= W337), E369 (= E373), A370 (= A374), A372 (= A376), L373 (= L377), G608 (= G608), H609 (= H609), D610 (= D610), R611 (= R611), G612 (= G612), I616 (= I616), Y620 (≠ F620), S654 (= S654), L656 (= L656), G684 (= G684), G685 (= G685), V686 (= V686), Y704 (≠ F704), T705 (≠ P705), T708 (= T708), S713 (≠ A713)
- binding desulfo-coenzyme a: Y74 (= Y78), M77 (= M81), F80 (≠ D84), R81 (≠ K85), T84 (= T88), R86 (= R90), S113 (= S117), S163 (= S167), T165 (= T169), T194 (= T198), R282 (= R286), S284 (= S288), H327 (= H331), Q360 (= Q364)
5reqA Methylmalonyl-coa mutase, y89f mutant, substrate complex (see paper)
70% identity, 98% coverage: 4:721/732 of query aligns to 1:719/725 of 5reqA
- active site: F86 (≠ Y92), Y240 (= Y246), H241 (= H247), K601 (= K603), D605 (= D607), H607 (= H609)
- binding cobalamin: L116 (= L122), A136 (= A142), R204 (= R210), H241 (= H247), E244 (= E250), G330 (= G336), W331 (= W337), E367 (= E373), A368 (= A374), A370 (= A376), G606 (= G608), H607 (= H609), D608 (= D610), R609 (= R611), G610 (= G612), I614 (= I616), S652 (= S654), L654 (= L656), G682 (= G684), G683 (= G685), V684 (= V686), Y702 (≠ F704), T703 (≠ P705), T706 (= T708)
- binding methylmalonyl(carbadethia)-coenzyme a: Y72 (= Y78), T74 (= T80), M75 (= M81), R79 (≠ K85), T82 (= T88), R84 (= R90), F86 (≠ Y92), S111 (= S117), S161 (= S167), T163 (= T169), T192 (= T198), Q194 (= Q200), R204 (= R210), N233 (= N239), H241 (= H247), R280 (= R286), S282 (= S288), F284 (= F290), T324 (= T330), H325 (= H331), Q358 (= Q364), S359 (= S365)
- binding succinyl(carbadethia)-coenzyme a: Y72 (= Y78), T74 (= T80), M75 (= M81), R79 (≠ K85), T82 (= T88), R84 (= R90), F86 (≠ Y92), S161 (= S167), T163 (= T169), T192 (= T198), R204 (= R210), N233 (= N239), H241 (= H247), R280 (= R286), S282 (= S288), F284 (= F290), H325 (= H331), Q358 (= Q364)
P22033 Methylmalonyl-CoA mutase, mitochondrial; MCM; Methylmalonyl-CoA isomerase; EC 5.4.99.2 from Homo sapiens (Human) (see 28 papers)
65% identity, 94% coverage: 33:718/732 of query aligns to 53:736/750 of P22033
- I69 (≠ V49) to V: in MMAM; likely benign; dbSNP:rs115923556
- P86 (= P68) 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 (= G69) to E: in MMAM; mut0; dbSNP:rs1554160986
- R93 (= R75) to H: in MMAM; mut0; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918251
- G94 (= G76) to R: in MMAM; mut0; dbSNP:rs727504022; to V: in MMAM; mut- and mut0; dbSNP:rs535411418
- P95 (= P77) to R: in MMAM; mut0; dbSNP:rs190834116
- YPTM 96:99 (= YPTM 78:81) binding
- Y100 (= Y82) 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 (= W87) to R: in MMAM; mut0; dbSNP:rs121918249
- TIRQY 106:110 (≠ TVRQY 88:92) binding
- R108 (= R90) to C: in MMAM; mut0; dbSNP:rs121918257; to G: in MMAM; mut-; to H: in MMAM; mut0; dbSNP:rs483352778
- Q109 (= Q91) to R: in MMAM; mut0; dbSNP:rs1461110052
- G133 (= G115) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253828
- A137 (= A119) to V: in MMAM; mut0; dbSNP:rs941483851
- D139 (= D121) to N: in MMAM; uncertain significance; dbSNP:rs879253829
- L140 (= L122) to P: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- A141 (= A123) to T: in MMAM; decreased protein expression; dbSNP:rs1554160730
- H143 (= H125) to Y: in MMAM; mut0
- G145 (= G127) to S: in MMAM; mut0
- S148 (= S130) to L: in MMAM; mut0; dbSNP:rs1300547552
- D156 (= D138) to N: in MMAM; mut-
- G158 (= G140) to V: in MMAM; mut0
- G161 (= G143) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; to V: in MMAM; decreased protein expression
- F174 (= F156) to S: in MMAM; mut0; dbSNP:rs864309733
- M186 (= M168) to V: in MMAM; mut-; dbSNP:rs148331800
- T187 (= T169) to S: in MMAM; mut0; dbSNP:rs879253830
- N189 (= N171) to I: in MMAM; mut-; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs200908035; to K: in MMAM; mut-; dbSNP:rs1561959114
- A191 (= A173) to E: in MMAM; mut- and mut0; affects proper folding; reduced protein level; decreased methylmalonyl-CoA mutase activity; dbSNP:rs760782399
- A197 (= A179) to E: in MMAM; mut0
- G203 (≠ A185) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs778702777
- E205 (= E187) natural variant: Missing (in MMAM; mut0; dbSNP:rs879253831)
- G215 (= G197) to C: in MMAM; mut- and mut0; dbSNP:rs121918258; to S: in MMAM; mut0; dbSNP:rs121918258
- TIQ 216:218 (= TIQ 198:200) binding
- Q218 (= Q200) to H: in MMAM; mut0 and mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability; dbSNP:rs1446389693
- N219 (= N201) to Y: in MMAM; mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; dbSNP:rs121918256
- R228 (= R210) binding ; to Q: in MMAM; mut0; dbSNP:rs770810987
- T230 (= T212) to I: in MMAM; mut-; to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253833
- Y231 (= Y213) 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 (= K237) binding
- S262 (= S244) to N: in MMAM; mut0
- H265 (= H247) binding ; to Y: in MMAM; mut-
- E276 (= E258) to D: in MMAM; uncertain significance; mut-; dbSNP:rs12175488
- L281 (= L263) to S: in MMAM; mut0; dbSNP:rs796052007
- G284 (= G266) to E: in MMAM; mut0; dbSNP:rs879253835; to R: in MMAM; mut0; dbSNP:rs761477436
- S288 (≠ A270) to P: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1179778233
- G291 (= G273) to E: in MMAM; mut0
- Q293 (≠ A275) to P: in MMAM; mut0
- RLS 304:306 (= RLS 286:288) binding
- L305 (= L287) to S: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554160246
- S306 (= S288) to F: in MMAM; mut0; dbSNP:rs1085307929
- W309 (= W291) to G: in MMAM; decreased protein expression
- G312 (= G294) to V: in MMAM; mut0; dbSNP:rs864309734
- Y316 (≠ F298) 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 (= A306) to T: in MMAM; mut-; dbSNP:rs780387525
- R326 (= R308) to K: in MMAM; uncertain significance; dbSNP:rs758577372
- L328 (= L310) 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 (= S325) 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 (≠ S327) natural variant: Missing (in MMAM; mut0)
- L347 (= L328) to R: in MMAM; mut0; dbSNP:rs1026703654
- H350 (= H331) to Y: in MMAM; mut0; dbSNP:rs1407914109
- L358 (= L339) to P: in MMAM; mut0
- N366 (= N347) 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 (= R350) 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 (= T351) to P: in MMAM; mut0; dbSNP:rs368790885
- A377 (≠ S358) to E: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918250
- Q383 (= Q364) to H: in MMAM; mut0; to P: in MMAM; mut0
- H386 (= H367) to N: in MMAM; mut0; dbSNP:rs1554159937; to R: in MMAM; mut0; dbSNP:rs866933356
- T387 (= T368) 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 (= N369) to H: in MMAM; mut0; dbSNP:rs766010704; to K: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253840
- S389 (≠ A370) natural variant: Missing (in MMAM; mut0)
- I412 (≠ L393) natural variant: Missing (in MMAM; mut0)
- P424 (= P405) to L: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253842
- G426 (= G407) 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 (= G408) to D: in MMAM; mut0; dbSNP:rs753288303
- G454 (= G435) to E: in MMAM; mut0
- A499 (= A480) to T: in dbSNP:rs2229385
- I505 (≠ V486) to T: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- Q514 (= Q495) to E: in MMAM; uncertain significance; to K: in MMAM; decreased protein expression
- L518 (= L499) to P: in MMAM; mut0; dbSNP:rs864309738
- R532 (≠ Q513) to H: in dbSNP:rs1141321
- A535 (≠ E516) to P: in MMAM; mut0; dbSNP:rs760183775
- A552 (≠ S533) to V: in MMAM; uncertain significance; dbSNP:rs879253845
- C560 (≠ A541) to Y: in MMAM; mut0; dbSNP:rs1238333040
- T566 (≠ S547) to R: in MMAM; mut0
- F573 (≠ Y554) 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 (= Y568) to C: in MMAM; mut-
- I597 (≠ A578) to R: in MMAM; no changed in protein expression; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554158951
- P615 (= P597) 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 (= R598) to C: in MMAM; mut0; dbSNP:rs765284825
- L617 (≠ I599) to R: in MMAM; mut0; dbSNP:rs1554158775
- K621 (= K603) to N: in MMAM; mut0
- G623 (= G605) to R: in MMAM; mut0; dbSNP:rs121918254
- Q624 (= Q606) to R: in MMAM; no effect on protein abundance; dbSNP:rs768521956
- D625 (= D607) 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 (= G608) to C: in MMAM; mut-; dbSNP:rs982110849
- H627 (= H609) binding axial binding residue; to R: in MMAM; mut0; dbSNP:rs372486357
- G630 (= G612) to E: in MMAM; mut0; dbSNP:rs143023066
- V633 (= V615) 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 (≠ A619) to E: in MMAM; mut-; to R: in MMAM; mut0; dbSNP:rs781501004
- F638 (= F620) to I: in MMAM; mut0
- D640 (= D622) to Y: in MMAM; mut0; dbSNP:rs865815395
- G642 (= G624) to R: in MMAM; mut-; dbSNP:rs747897332
- G648 (= G630) 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 (= V651) to E: in MMAM; mut0; dbSNP:rs1360470463
- I671 (≠ V653) to V: in dbSNP:rs8589
- L674 (= L656) to F: in MMAM; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1164271240
- H678 (= H660) to R: in MMAM; mut-; dbSNP:rs147094927
- E684 (≠ Q666) natural variant: E -> EL (in MMAM; mut-)
- L685 (= L667) to R: in MMAM; mut-; dbSNP:rs864309739
- R694 (≠ A676) 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 (≠ V682) 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 (= G685) to R: in MMAM; mut0; dbSNP:rs121918255
- G717 (= G699) 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 (≠ P705) 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, 94% coverage: 33:718/732 of query aligns to 18:701/714 of 2xiqA
- active site: Y75 (= Y92), Y229 (= Y246), H230 (= H247), K586 (= K603), D590 (= D607), H592 (= H609)
- binding cobalamin: Y75 (= Y92), L105 (= L122), H108 (= H125), A125 (= A142), R193 (= R210), E233 (= E250), G320 (= G336), W321 (= W337), E357 (= E373), G360 (≠ A376), L361 (= L377), G591 (= G608), H592 (= H609), D593 (= D610), R594 (= R611), G595 (= G612), I599 (= I616), G635 (= G652), S637 (= S654), L639 (= L656), A641 (= A658), G667 (= G684), G668 (= G685), F687 (= F704), G688 (≠ P705), T691 (= T708)
- binding malonyl-coenzyme a: Y61 (= Y78), T63 (= T80), M64 (= M81), R68 (≠ K85), T71 (= T88), R73 (= R90), Y75 (= Y92), S150 (= S167), T152 (= T169), T181 (= T198), R193 (= R210), K220 (= K237), H230 (= H247), R269 (= R286), S271 (= S288), F273 (= F290), R313 (= R329), A314 (≠ T330), H315 (= H331), Q317 (= Q333), Q348 (= Q364)
8dyjB Crystal structure of human methylmalonyl-coa mutase in complex with adp and cob(ii)alamin (see paper)
65% identity, 94% coverage: 33:718/732 of query aligns to 17:700/708 of 8dyjB
- binding adenosine-5'-diphosphate: Y74 (= Y92), T151 (= T169), R192 (= R210), Y228 (= Y246), H229 (= H247), F272 (= F290), Q316 (= Q333), N352 (= N369), E356 (= E373), L360 (= L377), P361 (= P378)
- binding cobalamin: F102 (= F120), L104 (= L122), H107 (= H125), A124 (= A142), V191 (= V209), R192 (= R210), H229 (= H247), E232 (= E250), G319 (= G336), W320 (= W337), E356 (= E373), G359 (≠ A376), L360 (= L377), G590 (= G608), H591 (= H609), D592 (= D610), R593 (= R611), G594 (= G612), I598 (= I616), S636 (= S654), L638 (= L656), A640 (= A658), G666 (= G684), G667 (= G685), V668 (= V686), F686 (= F704), G687 (≠ P705), T690 (= T708)
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, 94% coverage: 33:718/732 of query aligns to 18:678/689 of 8gjuJ
- binding coenzyme a: Y61 (= Y78), T63 (= T80), R68 (≠ K85), T71 (= T88), R73 (= R90), S150 (= S167), T152 (= T169), T181 (= T198), Q183 (= Q200), N222 (= N239), R269 (= R286), S271 (= S288), R313 (= R329), A314 (≠ T330), H315 (= H331), Q348 (= Q364)
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, 70% coverage: 49:558/732 of query aligns to 46:557/562 of I3VE77
- YPTM 76:79 (= YPTM 78:81) binding
- TMR 86:88 (≠ TVR 88:90) binding
- I90 (≠ Y92) 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 (≠ A119) 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 198:200) binding
- R235 (≠ K237) binding
- N240 (≠ S242) binding
- H245 (= H247) binding
- R284 (= R286) binding
4r3uA Crystal structure of 2-hydroxyisobutyryl-coa mutase (see paper)
43% identity, 70% coverage: 49:558/732 of query aligns to 45:556/557 of 4r3uA
- active site: I89 (≠ Y92), Y243 (= Y246), H244 (= H247)
- binding 3-hydroxybutanoyl-coenzyme a: Y75 (= Y78), T77 (= T80), M78 (= M81), R82 (≠ K85), T85 (= T88), R87 (= R90), I89 (≠ Y92), D116 (≠ A119), S164 (= S167), T166 (= T169), T195 (= T198), Q197 (= Q200), R234 (≠ K237), N236 (= N239), N239 (≠ S242), Y243 (= Y246), H244 (= H247), R283 (= R286), F287 (= F290), R327 (= R329), F328 (≠ T330), H329 (= H331), Q331 (= Q333), Q362 (= Q364)
- 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 (= Y78), T77 (= T80), M78 (= M81), R82 (≠ K85), T85 (= T88), R87 (= R90), I89 (≠ Y92), D116 (≠ A119), S164 (= S167), T166 (= T169), T195 (= T198), Q197 (= Q200), R234 (≠ K237), N236 (= N239), N239 (≠ S242), H244 (= H247), R283 (= R286), F287 (= F290), R327 (= R329), F328 (≠ T330), H329 (= H331), Q331 (= Q333), Q362 (= Q364)
- binding cobalamin: D116 (≠ A119), M119 (≠ L122), E139 (≠ A142), Q207 (≠ R210), E209 (≠ T212), E247 (= E250), A334 (≠ G336), E371 (= E373), A372 (= A374), A374 (= A376)
5cjwA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate pivalyl-coenzyme a (see paper)
34% identity, 67% coverage: 67:558/732 of query aligns to 547:1060/1063 of 5cjwA
- active site: F571 (≠ Y92), Y752 (= Y246), H753 (= H247)
- binding pivalyl-coenzyme A: F558 (≠ Y78), F560 (≠ T80), R562 (≠ Y82), R569 (= R90), F571 (≠ Y92), R595 (≠ G115), S650 (= S167), T652 (= T169), R701 (≠ S196), T703 (= T198), Q705 (= Q200), Y745 (≠ N239), Y752 (= Y246), H753 (= H247), S794 (= S288), F796 (= F290), R829 (≠ K324), K834 (≠ R329), H836 (= H331)
- binding cobalamin: F600 (= F120), L605 (≠ H125), S623 (≠ A142), Q715 (≠ R210), H753 (= H247), E756 (= E250), A757 (= A251), G841 (= G336), R842 (≠ W337), E878 (= E373), A879 (= A374), T881 (≠ A376), H966 (≠ D461)
Sites not aligning to the query:
- active site: 6
- binding cobalamin: 18, 19, 20, 21, 22, 26, 66, 67, 94, 96, 98, 116, 117, 118
- binding guanosine-5'-diphosphate: 199, 201, 202, 203, 204, 245, 337, 338, 340, 375, 377, 1062
- binding magnesium ion: 203, 229, 242, 242, 290, 290
5cjvA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isovaleryl-coenzyme a (see paper)
34% identity, 67% coverage: 67:558/732 of query aligns to 545:1058/1061 of 5cjvA
- active site: F569 (≠ Y92), Y750 (= Y246), H751 (= H247)
- binding cobalamin: F598 (= F120), L603 (≠ H125), S621 (≠ A142), Q713 (≠ R210), E754 (= E250), A755 (= A251), G839 (= G336), R840 (≠ W337), E876 (= E373), A877 (= A374), T879 (≠ A376), H964 (≠ D461)
- binding guanosine-5'-diphosphate: E944 (= E441)
- binding Isovaleryl-coenzyme A: F556 (≠ Y78), F558 (≠ T80), R560 (≠ Y82), R567 (= R90), F569 (≠ Y92), R593 (≠ G115), S648 (= S167), T650 (= T169), R699 (≠ S196), T701 (= T198), Q703 (= Q200), Q713 (≠ R210), Y743 (≠ N239), H751 (= H247), S792 (= S288), F794 (= F290), K832 (≠ R329), H834 (= H331)
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, 67% coverage: 67:558/732 of query aligns to 545:1059/1062 of 5cjtA
- active site: F569 (≠ Y92), Y750 (= Y246), H751 (= H247)
- binding cobalamin: F598 (= F120), L603 (≠ H125), S621 (≠ A142), Q713 (≠ R210), H751 (= H247), E754 (= E250), A755 (= A251), G839 (= G336), R840 (≠ W337), E876 (= E373), A877 (= A374), T879 (≠ A376), H964 (≠ D461)
- binding isobutyryl-coenzyme a: F556 (≠ Y78), F558 (≠ T80), R560 (≠ Y82), R567 (= R90), F569 (≠ Y92), R593 (≠ G115), S648 (= S167), T650 (= T169), R699 (≠ S196), T701 (= T198), Q703 (= Q200), Y743 (≠ N239), Y750 (= Y246), H751 (= H247), S792 (= S288), F794 (= F290), R827 (≠ K324), K832 (≠ R329), H834 (= H331)
- binding guanosine-5'-diphosphate: E944 (= E441)
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, 67% coverage: 67:558/732 of query aligns to 574:1090/1093 of Q1LRY0
- F587 (≠ T80) binding
- F598 (≠ Y92) 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 (≠ G115) binding
- R728 (≠ S196) binding
- Y772 (≠ N239) binding
- S821 (= S288) binding
- R856 (≠ K324) binding
- K861 (≠ R329) binding
- E973 (= E441) binding
Sites not aligning to the query:
- 39 binding axial binding residue
- 169:417 GTPase chaperone MeaI
- 219:224 binding
- 223 binding
- 248 binding
- 249 binding
- 262 binding ; binding
- 265 binding
- 310 binding ; binding
- 311 binding
- 357:360 binding
- 418:579 Linker
- 1092 binding
4xc6A Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, and mg (holo-icmf/gdp) (see paper)
34% identity, 67% coverage: 67:558/732 of query aligns to 548:1064/1067 of 4xc6A
- active site: F572 (≠ Y92), Y753 (= Y246), H754 (= H247)
- binding cobalamin: F601 (= F120), L606 (≠ H125), S624 (≠ A142), Q716 (≠ R210), H754 (= H247), E757 (= E250), A758 (= A251), G842 (= G336), R843 (≠ W337), E879 (= E373), A880 (= A374), T882 (≠ A376), H967 (≠ D461)
- binding guanosine-5'-diphosphate: E947 (= E441)
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
Query Sequence
>AZOBR_RS24250 FitnessBrowser__azobra:AZOBR_RS24250
MTSLPDFSTLPLDAAVSNASPAEWSRRFAAETGTDPATALWRTPEMLDVKPLYTAADLDG
LDHLAAMPGMAPFLRGPYPTMYVDKPWTVRQYAGFSTAQESNAFYRRNLAAGQKGLSVAF
DLATHRGYDSDHPRVTGDVGMAGVAIDSILDMKTLFDGIPLDQMSVSMTMNGAVLPVLAG
YIVAAEEQGVSADKLSGTIQNDILKEFMVRNTYIYPPKPSMRIISDIFAFTSQHMPKFNS
ISISGYHLQEAGATADLELAYTLADGVEYARAGLAAGLTIDQFAPRLSFFWAIGMNFFME
VAKMRAGRMLWAKLIKEFAPKSDKSLSLRTHSQTSGWSLTAQDVFNNVTRTCIEAMASTQ
GHTQSLHTNALDEALALPTDFSARIARNTQLFLQQESGTCRVIDPWGGSYYVERLTRELA
ARAWGHIREVEETGGMAKAIETGIPKMRVEEAAARTQARIDSGRQTVVGVNKYRLEQEEA
IEVLKVDNSAVRAQQIAQLERLRAERDPIRCRQTLEALTNAAAAGDGNLLALSVDAIRAR
ATVGEISDALEKVYGRHKAEIRTITGIYAGEVGRQSDAIARVRALVAEFAERDGRRPRIM
VAKMGQDGHDRGQKVIATAFADLGFDVDVGPLFQTPEEAARQAVENDCHIVGVSSLAAGH
LTLVPQLKAELERHGAGDILIVVGGVVPPQDYDALYAAGATAIFPPGTVISEAAVDLLRI
LNERHGYAPKAA
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