SitesBLAST
Comparing WP_012330042.1 NCBI__GCF_000019365.1:WP_012330042.1 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)
4reqA Methylmalonyl-coa mutase substrate complex (see paper)
37% identity, 95% coverage: 2:639/675 of query aligns to 71:705/726 of 4reqA
- active site: Y87 (= Y20), Y241 (= Y174), H242 (= H175), K602 (= K536), D606 (= D540), H608 (= H542)
- binding cobalamin: Y87 (= Y20), L117 (= L50), A137 (≠ V70), V204 (≠ S137), R205 (= R138), H242 (= H175), E245 (= E178), G331 (≠ S269), W332 (≠ L270), E368 (= E309), A369 (= A310), A371 (≠ G312), L372 (= L313), G607 (= G541), H608 (= H542), D609 (≠ S543), R610 (≠ N544), G611 (= G545), I615 (= I549), S653 (= S587), L655 (= L589), G683 (= G617), G684 (= G618), V685 (≠ I619), Y703 (= Y637), T704 (= T638)
- binding methylmalonyl-coenzyme a: Y73 (≠ Q4), M76 (≠ R7), F79 (≠ Q10), R80 (= R11), T83 (≠ I16), R85 (= R18), Y87 (= Y20), S112 (= S45), S162 (= S95), T164 (= T97), T193 (= T126), R205 (= R138), N234 (= N167), Y241 (= Y174), H242 (= H175), R281 (= R218), S283 (= S220), F285 (= F222), H326 (≠ G264), Q328 (= Q266), Q359 (≠ R300), S360 (≠ A301)
- binding succinyl-coenzyme a: Y73 (≠ Q4), M76 (≠ R7), F79 (≠ Q10), R80 (= R11), T83 (≠ I16), R85 (= R18), Y87 (= Y20), S162 (= S95), T164 (= T97), T193 (= T126), Q195 (= Q128), R205 (= R138), N234 (= N167), Y241 (= Y174), H242 (= H175), R281 (= R218), S283 (= S220), F285 (= F222), R324 (= R262), H326 (≠ G264), Q359 (≠ R300)
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)
37% identity, 95% coverage: 2:639/675 of query aligns to 73:707/728 of P11653
- Y75 (≠ Q4) binding (R)-methylmalonyl-CoA
- M78 (≠ R7) binding (R)-methylmalonyl-CoA
- R82 (= R11) binding (R)-methylmalonyl-CoA
- T85 (≠ I16) binding (R)-methylmalonyl-CoA
- R87 (= R18) binding (R)-methylmalonyl-CoA
- Y89 (= Y20) binding (R)-methylmalonyl-CoA; mutation to F: Does not significantly affect affinity for succiny-CoA, but kcat is lowered about 580-fold.
- S114 (= S45) binding (R)-methylmalonyl-CoA
- F117 (= F48) binding cob(II)alamin
- A139 (≠ V70) binding cob(II)alamin
- T195 (= T126) binding (R)-methylmalonyl-CoA
- Q197 (= Q128) binding (R)-methylmalonyl-CoA
- V206 (≠ S137) binding cob(II)alamin
- R207 (= R138) binding (R)-methylmalonyl-CoA; binding cob(II)alamin
- H244 (= H175) binding (R)-methylmalonyl-CoA
- R283 (= R218) binding (R)-methylmalonyl-CoA
- S285 (= S220) binding (R)-methylmalonyl-CoA
- G333 (≠ S269) binding cob(II)alamin
- E370 (= E309) binding cob(II)alamin
- A373 (≠ G312) binding cob(II)alamin
- G609 (= G541) binding cob(II)alamin
- H610 (= H542) binding axial binding residue
- D611 (≠ S543) binding cob(II)alamin
- R612 (≠ N544) binding cob(II)alamin
- S655 (= S587) binding cob(II)alamin
- L657 (= L589) binding cob(II)alamin
- G686 (= G618) binding cob(II)alamin
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 709 binding cob(II)alamin
6reqA Methylmalonyl-coa mutase, 3-carboxypropyl-coa inhibitor complex (see paper)
37% identity, 95% coverage: 2:639/675 of query aligns to 72:706/727 of 6reqA
- active site: Y88 (= Y20), Y242 (= Y174), H243 (= H175), K603 (= K536), D607 (= D540), H609 (= H542)
- binding 3-carboxypropyl-coenzyme a: Y74 (≠ Q4), T76 (= T6), M77 (≠ R7), F80 (≠ Q10), R81 (= R11), T84 (≠ I16), R86 (= R18), Y88 (= Y20), S113 (= S45), S163 (= S95), T165 (= T97), T194 (= T126), R206 (= R138), H243 (= H175), R282 (= R218), S284 (= S220), F286 (= F222), H327 (≠ G264), Q329 (= Q266), Q360 (≠ R300)
- binding cobalamin: Y88 (= Y20), F116 (= F48), L118 (= L50), H121 (≠ Q53), A138 (≠ V70), R206 (= R138), E246 (= E178), G332 (≠ S269), W333 (≠ L270), E369 (= E309), A370 (= A310), A372 (≠ G312), G608 (= G541), H609 (= H542), D610 (≠ S543), R611 (≠ N544), G612 (= G545), I616 (= I549), Y620 (≠ A553), S654 (= S587), L656 (= L589), G658 (= G591), G684 (= G617), G685 (= G618), Y704 (= Y637), T705 (= T638)
Sites not aligning to the query:
7reqA Methylmalonyl-coa mutase, 2-carboxypropyl-coa inhibitor complex (see paper)
37% identity, 95% coverage: 2:639/675 of query aligns to 70:704/725 of 7reqA
- active site: Y86 (= Y20), Y240 (= Y174), H241 (= H175), K601 (= K536), D605 (= D540), H607 (= H542)
- binding 2-carboxypropyl-coenzyme a: Y72 (≠ Q4), T74 (= T6), M75 (≠ R7), F78 (≠ Q10), R79 (= R11), T82 (≠ I16), R84 (= R18), Y86 (= Y20), S161 (= S95), T163 (= T97), T192 (= T126), R204 (= R138), H241 (= H175), R280 (= R218), S282 (= S220), F284 (= F222), H325 (≠ G264), Q358 (≠ R300)
- binding cobalamin: Y86 (= Y20), L116 (= L50), A136 (≠ V70), R204 (= R138), E244 (= E178), G330 (≠ S269), W331 (≠ L270), E367 (= E309), A368 (= A310), A370 (≠ G312), G606 (= G541), H607 (= H542), D608 (≠ S543), R609 (≠ N544), G610 (= G545), I614 (= I549), S652 (= S587), L654 (= L589), G682 (= G617), G683 (= G618), Y702 (= Y637), T703 (= T638)
Sites not aligning to the query:
3reqA Methylmalonyl-coa mutase, substrate-free state (poor quality structure) (see paper)
37% identity, 95% coverage: 2:639/675 of query aligns to 70:704/725 of 3reqA
- active site: Y86 (= Y20), Y240 (= Y174), H241 (= H175), K601 (= K536), D605 (= D540), H607 (= H542)
- binding adenosine: Y86 (= Y20), Y240 (= Y174), E244 (= E178), G330 (≠ S269)
- binding cobalamin: L116 (= L50), V203 (≠ S137), R204 (= R138), E244 (= E178), G330 (≠ S269), W331 (≠ L270), A368 (= A310), G606 (= G541), H607 (= H542), D608 (≠ S543), R609 (≠ N544), G610 (= G545), I614 (= I549), G650 (= G585), S652 (= S587), L654 (= L589), G682 (= G617), G683 (= G618), Y702 (= Y637), T703 (= T638), P704 (= P639)
Sites not aligning to the query:
2reqA Methylmalonyl-coa mutase, non-productive coa complex, in open conformation representing substrate-free state (see paper)
37% identity, 95% coverage: 2:639/675 of query aligns to 70:704/725 of 2reqA
- active site: Y86 (= Y20), Y240 (= Y174), H241 (= H175), K601 (= K536), D605 (= D540), H607 (= H542)
- binding cobalamin: V203 (≠ S137), R204 (= R138), E244 (= E178), A245 (= A179), W331 (≠ L270), A368 (= A310), G606 (= G541), H607 (= H542), D608 (≠ S543), R609 (≠ N544), G610 (= G545), I614 (= I549), G650 (= G585), S652 (= S587), L654 (= L589), A655 (≠ S590), G682 (= G617), G683 (= G618), Y702 (= Y637), T703 (= T638)
- binding coenzyme a: Y72 (≠ Q4), R79 (= R11), K318 (= K257)
Sites not aligning to the query:
5reqA Methylmalonyl-coa mutase, y89f mutant, substrate complex (see paper)
37% identity, 95% coverage: 2:639/675 of query aligns to 70:704/725 of 5reqA
- active site: F86 (≠ Y20), Y240 (= Y174), H241 (= H175), K601 (= K536), D605 (= D540), H607 (= H542)
- binding cobalamin: L116 (= L50), A136 (≠ V70), R204 (= R138), H241 (= H175), E244 (= E178), G330 (≠ S269), W331 (≠ L270), E367 (= E309), A368 (= A310), A370 (≠ G312), G606 (= G541), H607 (= H542), D608 (≠ S543), R609 (≠ N544), G610 (= G545), I614 (= I549), S652 (= S587), L654 (= L589), G682 (= G617), G683 (= G618), V684 (≠ I619), Y702 (= Y637), T703 (= T638)
- binding methylmalonyl(carbadethia)-coenzyme a: Y72 (≠ Q4), T74 (= T6), M75 (≠ R7), R79 (= R11), T82 (≠ I16), R84 (= R18), F86 (≠ Y20), S111 (= S45), S161 (= S95), T163 (= T97), T192 (= T126), Q194 (= Q128), R204 (= R138), N233 (= N167), H241 (= H175), R280 (= R218), S282 (= S220), F284 (= F222), T324 (≠ Y263), H325 (≠ G264), Q358 (≠ R300), S359 (≠ A301)
- binding succinyl(carbadethia)-coenzyme a: Y72 (≠ Q4), T74 (= T6), M75 (≠ R7), R79 (= R11), T82 (≠ I16), R84 (= R18), F86 (≠ Y20), S161 (= S95), T163 (= T97), T192 (= T126), R204 (= R138), N233 (= N167), H241 (= H175), R280 (= R218), S282 (= S220), F284 (= F222), H325 (≠ G264), Q358 (≠ R300)
Sites not aligning to the query:
1e1cA Methylmalonyl-coa mutase h244a mutant (see paper)
37% identity, 95% coverage: 2:639/675 of query aligns to 72:706/727 of 1e1cA
- active site: Y88 (= Y20), Y242 (= Y174), A243 (≠ H175), K603 (= K536), D607 (= D540), H609 (= H542)
- binding cobalamin: Y88 (= Y20), L118 (= L50), H121 (≠ Q53), A138 (≠ V70), V205 (≠ S137), R206 (= R138), E246 (= E178), G332 (≠ S269), W333 (≠ L270), E369 (= E309), A370 (= A310), A372 (≠ G312), L373 (= L313), G608 (= G541), H609 (= H542), D610 (≠ S543), R611 (≠ N544), G612 (= G545), I616 (= I549), Y620 (≠ A553), S654 (= S587), L656 (= L589), G684 (= G617), G685 (= G618), V686 (≠ I619), Y704 (= Y637), T705 (= T638)
- binding desulfo-coenzyme a: Y74 (≠ Q4), M77 (≠ R7), F80 (≠ Q10), R81 (= R11), T84 (≠ I16), R86 (= R18), S113 (= S45), S163 (= S95), T165 (= T97), T194 (= T126), R282 (= R218), S284 (= S220), H327 (≠ G264), Q360 (≠ R300)
Sites not aligning to the query:
6oxdA Structure of mycobacterium tuberculosis methylmalonyl-coa mutase with adenosyl cobalamin (see paper)
38% identity, 96% coverage: 12:657/675 of query aligns to 92:731/736 of 6oxdA
- active site: Y100 (= Y20), Y254 (= Y174), H255 (= H175), K610 (= K536), D614 (= D540), H616 (= H542)
- binding cobalamin: Y100 (= Y20), L130 (= L50), H133 (≠ Q53), A150 (≠ V70), R218 (= R138), E258 (= E178), G344 (≠ S269), W345 (≠ L270), E381 (= E309), A382 (= A310), A384 (≠ G312), L385 (= L313), G615 (= G541), H616 (= H542), D617 (≠ S543), R618 (≠ N544), S661 (= S587), L663 (= L589), A665 (≠ G591), G691 (= G617), G692 (= G618), F711 (≠ Y637), P712 (≠ T638), T715 (≠ D641)
- binding Itaconyl coenzyme A: Q93 (≠ K13), T96 (≠ I16), R98 (= R18), Y100 (= Y20), S175 (= S95), T177 (= T97), T206 (= T126), R218 (= R138), H255 (= H175), R294 (= R218), S296 (= S220), F298 (= F222), R337 (= R262), T338 (≠ Y263), H339 (≠ G264), Q341 (= Q266), Q372 (≠ R300)
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)
35% identity, 93% coverage: 13:639/675 of query aligns to 103:724/750 of P22033
- W105 (= W15) to R: in MMAM; mut0; dbSNP:rs121918249
- TIRQY 106:110 (≠ IIRTY 16:20) binding malonyl-CoA
- R108 (= R18) to C: in MMAM; mut0; dbSNP:rs121918257; to G: in MMAM; mut-; to H: in MMAM; mut0; dbSNP:rs483352778
- Q109 (≠ T19) to R: in MMAM; mut0; dbSNP:rs1461110052
- G133 (= G43) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253828
- A137 (= A47) to V: in MMAM; mut0; dbSNP:rs941483851
- D139 (= D49) to N: in MMAM; uncertain significance; dbSNP:rs879253829
- L140 (= L50) to P: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- A141 (≠ P51) to T: in MMAM; decreased protein expression; dbSNP:rs1554160730
- H143 (≠ Q53) to Y: in MMAM; mut0
- G145 (= G55) to S: in MMAM; mut0
- S148 (≠ P58) to L: in MMAM; mut0; dbSNP:rs1300547552
- D156 (≠ E66) to N: in MMAM; mut-
- G158 (= G68) to V: in MMAM; mut0
- G161 (= G71) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; to V: in MMAM; decreased protein expression
- F174 (= F84) to S: in MMAM; mut0; dbSNP:rs864309733
- M186 (= M96) to V: in MMAM; mut-; dbSNP:rs148331800
- T187 (= T97) to S: in MMAM; mut0; dbSNP:rs879253830
- N189 (= N99) to I: in MMAM; mut-; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs200908035; to K: in MMAM; mut-; dbSNP:rs1561959114
- A191 (≠ T101) to E: in MMAM; mut- and mut0; affects proper folding; reduced protein level; decreased methylmalonyl-CoA mutase activity; dbSNP:rs760782399
- A197 (= A107) to E: in MMAM; mut0
- G203 (≠ A113) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs778702777
- E205 (= E115) natural variant: Missing (in MMAM; mut0; dbSNP:rs879253831)
- G215 (= G125) to C: in MMAM; mut- and mut0; dbSNP:rs121918258; to S: in MMAM; mut0; dbSNP:rs121918258
- TIQ 216:218 (≠ TTQ 126:128) binding malonyl-CoA
- Q218 (= Q128) to H: in MMAM; mut0 and mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability; dbSNP:rs1446389693
- N219 (= N129) to Y: in MMAM; mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; dbSNP:rs121918256
- R228 (= R138) binding malonyl-CoA; to Q: in MMAM; mut0; dbSNP:rs770810987
- T230 (= T140) to I: in MMAM; mut-; to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253833
- Y231 (= Y141) 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 (= K165) binding malonyl-CoA
- S262 (≠ C172) to N: in MMAM; mut0
- H265 (= H175) binding malonyl-CoA; to Y: in MMAM; mut-
- E276 (= E186) to D: in MMAM; uncertain significance; mut-; dbSNP:rs12175488
- L281 (= L191) to S: in MMAM; mut0; dbSNP:rs796052007
- G284 (≠ A194) to E: in MMAM; mut0; dbSNP:rs879253835; to R: in MMAM; mut0; dbSNP:rs761477436
- S288 (≠ L198) to P: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1179778233
- G291 (vs. gap) to E: in MMAM; mut0
- Q293 (≠ R202) to P: in MMAM; mut0
- RLS 304:306 (≠ RIS 218:220) binding malonyl-CoA
- L305 (≠ I219) to S: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554160246
- S306 (= S220) to F: in MMAM; mut0; dbSNP:rs1085307929
- W309 (≠ V223) to G: in MMAM; decreased protein expression
- G312 (= G226) to V: in MMAM; mut0; dbSNP:rs864309734
- Y316 (≠ I230) 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 (= A238) to T: in MMAM; mut-; dbSNP:rs780387525
- R326 (≠ S240) to K: in MMAM; uncertain significance; dbSNP:rs758577372
- L328 (= L242) 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 (≠ K258) 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 (≠ I260) natural variant: Missing (in MMAM; mut0)
- L347 (≠ F261) to R: in MMAM; mut0; dbSNP:rs1026703654
- H350 (≠ G264) to Y: in MMAM; mut0; dbSNP:rs1407914109
- L358 (= L272) to P: in MMAM; mut0
- N366 (= N280) 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 (= R283) 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 (≠ I284) to P: in MMAM; mut0; dbSNP:rs368790885
- A377 (≠ V291) to E: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918250
- Q383 (≠ R300) to H: in MMAM; mut0; to P: in MMAM; mut0
- H386 (≠ Q303) to N: in MMAM; mut0; dbSNP:rs1554159937; to R: in MMAM; mut0; dbSNP:rs866933356
- T387 (≠ L304) 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 (≠ P305) to H: in MMAM; mut0; dbSNP:rs766010704; to K: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253840
- S389 (≠ A306) natural variant: Missing (in MMAM; mut0)
- I412 (≠ L329) natural variant: Missing (in MMAM; mut0)
- P424 (≠ I341) to L: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253842
- G426 (≠ D343) 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 (= G344) to D: in MMAM; mut0; dbSNP:rs753288303
- G454 (= G371) to E: in MMAM; mut0
- A499 (≠ P416) to T: in dbSNP:rs2229385
- I505 (≠ V427) to T: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- Q514 (= Q436) to E: in MMAM; uncertain significance; to K: in MMAM; decreased protein expression
- L518 (≠ I439) to P: in MMAM; mut0; dbSNP:rs864309738
- R532 (= R453) to H: in dbSNP:rs1141321
- A535 (≠ D456) to P: in MMAM; mut0; dbSNP:rs760183775
- A552 (≠ S472) to V: in MMAM; uncertain significance; dbSNP:rs879253845
- C560 (≠ V480) to Y: in MMAM; mut0; dbSNP:rs1238333040
- T566 (≠ G486) to R: in MMAM; mut0
- F573 (= F493) 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 (≠ V507) to C: in MMAM; mut-
- I597 (≠ L517) to R: in MMAM; no changed in protein expression; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554158951
- P615 (= P530) 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 (≠ K531) to C: in MMAM; mut0; dbSNP:rs765284825
- L617 (= L532) to R: in MMAM; mut0; dbSNP:rs1554158775
- K621 (= K536) to N: in MMAM; mut0
- G623 (= G538) to R: in MMAM; mut0; dbSNP:rs121918254
- Q624 (≠ L539) to R: in MMAM; no effect on protein abundance; dbSNP:rs768521956
- D625 (= D540) 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 (= G541) to C: in MMAM; mut-; dbSNP:rs982110849
- H627 (= H542) binding axial binding residue; to R: in MMAM; mut0; dbSNP:rs372486357
- G630 (= G545) to E: in MMAM; mut0; dbSNP:rs143023066
- V633 (≠ Q548) 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 (≠ R552) to E: in MMAM; mut-; to R: in MMAM; mut0; dbSNP:rs781501004
- F638 (≠ A553) to I: in MMAM; mut0
- D640 (= D555) to Y: in MMAM; mut0; dbSNP:rs865815395
- G642 (= G557) to R: in MMAM; mut-; dbSNP:rs747897332
- G648 (≠ D563) 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 (≠ I584) to E: in MMAM; mut0; dbSNP:rs1360470463
- I671 (≠ L586) to V: in dbSNP:rs8589
- L674 (= L589) to F: in MMAM; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1164271240
- H678 (= H593) to R: in MMAM; mut-; dbSNP:rs147094927
- E684 (= E599) natural variant: E -> EL (in MMAM; mut-)
- L685 (≠ V600) to R: in MMAM; mut-; dbSNP:rs864309739
- R694 (≠ L609) 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 (≠ V615) 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 (= G618) to R: in MMAM; mut0; dbSNP:rs121918255
- G717 (= G632) 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 (≠ T638) 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 malonyl-CoA
- 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 malonyl-CoA
- 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)
8dyjB Crystal structure of human methylmalonyl-coa mutase in complex with adp and cob(ii)alamin (see paper)
35% identity, 93% coverage: 13:639/675 of query aligns to 67:688/708 of 8dyjB
- binding adenosine-5'-diphosphate: Y74 (= Y20), T151 (= T97), R192 (= R138), Y228 (= Y174), H229 (= H175), F272 (= F222), Q316 (= Q266), N352 (≠ P305), E356 (= E309), L360 (= L313), P361 (= P314)
- binding cobalamin: F102 (= F48), L104 (= L50), H107 (≠ Q53), A124 (≠ V70), V191 (≠ S137), R192 (= R138), H229 (= H175), E232 (= E178), G319 (≠ S269), W320 (≠ L270), E356 (= E309), G359 (= G312), L360 (= L313), G590 (= G541), H591 (= H542), D592 (≠ S543), R593 (≠ N544), G594 (= G545), I598 (= I549), S636 (= S587), L638 (= L589), A640 (≠ G591), G666 (= G617), G667 (= G618), V668 (≠ I619), F686 (≠ Y637), G687 (≠ T638)
Sites not aligning to the query:
2xiqA Crystal structure of human methylmalonyl-coa mutase in complex with adenosylcobalamin and malonyl-coa (see paper)
35% identity, 93% coverage: 13:639/675 of query aligns to 68:689/714 of 2xiqA
- active site: Y75 (= Y20), Y229 (= Y174), H230 (= H175), K586 (= K536), D590 (= D540), H592 (= H542)
- binding cobalamin: Y75 (= Y20), L105 (= L50), H108 (≠ Q53), A125 (≠ V70), R193 (= R138), E233 (= E178), G320 (≠ S269), W321 (≠ L270), E357 (= E309), G360 (= G312), L361 (= L313), G591 (= G541), H592 (= H542), D593 (≠ S543), R594 (≠ N544), G595 (= G545), I599 (= I549), G635 (= G585), S637 (= S587), L639 (= L589), A641 (≠ G591), G667 (= G617), G668 (= G618), F687 (≠ Y637), G688 (≠ T638)
- binding malonyl-coenzyme a: R68 (≠ K13), T71 (≠ I16), R73 (= R18), Y75 (= Y20), S150 (= S95), T152 (= T97), T181 (= T126), R193 (= R138), K220 (= K165), H230 (= H175), R269 (= R218), S271 (= S220), F273 (= F222), R313 (= R262), A314 (≠ Y263), H315 (≠ G264), Q317 (= Q266), Q348 (≠ R300)
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)
34% identity, 93% coverage: 13:639/675 of query aligns to 68:666/689 of 8gjuJ
- binding coenzyme a: R68 (≠ K13), T71 (≠ I16), R73 (= R18), S150 (= S95), T152 (= T97), T181 (= T126), Q183 (= Q128), N222 (= N167), R269 (= R218), S271 (= S220), R313 (= R262), A314 (≠ Y263), H315 (≠ G264), Q348 (≠ R300)
Sites not aligning to the query:
4r3uA Crystal structure of 2-hydroxyisobutyryl-coa mutase (see paper)
33% identity, 73% coverage: 8:497/675 of query aligns to 77:556/557 of 4r3uA
- active site: I89 (≠ Y20), Y243 (= Y174), H244 (= H175)
- binding 3-hydroxybutanoyl-coenzyme a: T77 (= T8), M78 (≠ A9), R82 (≠ K13), T85 (≠ I16), R87 (= R18), I89 (≠ Y20), D116 (≠ A47), S164 (= S95), T166 (= T97), T195 (= T126), Q197 (= Q128), R234 (≠ K165), N236 (= N167), N239 (= N170), Y243 (= Y174), H244 (= H175), R283 (= R218), F287 (= F222), R327 (= R262), F328 (≠ Y263), H329 (≠ G264), Q331 (= Q266), Q362 (≠ R300)
- 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: T77 (= T8), M78 (≠ A9), R82 (≠ K13), T85 (≠ I16), R87 (= R18), I89 (≠ Y20), D116 (≠ A47), S164 (= S95), T166 (= T97), T195 (= T126), Q197 (= Q128), R234 (≠ K165), N236 (= N167), N239 (= N170), H244 (= H175), R283 (= R218), F287 (= F222), R327 (= R262), F328 (≠ Y263), H329 (≠ G264), Q331 (= Q266), Q362 (≠ R300)
- binding cobalamin: D116 (≠ A47), M119 (≠ L50), E139 (≠ V70), Q207 (≠ R138), E209 (≠ T140), E247 (= E178), A334 (≠ S269), E371 (= E309), A372 (= A310), A374 (≠ G312)
Sites not aligning to the query:
- binding 3-hydroxybutanoyl-coenzyme a: 75
- 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: 75
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)
33% identity, 73% coverage: 8:497/675 of query aligns to 78:557/562 of I3VE77
- TMR 86:88 (≠ IIR 16:18) binding (3S)-3-hydroxybutanoyl-CoA
- I90 (≠ Y20) 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 (≠ A47) binding (3S)-3-hydroxybutanoyl-CoA; 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 (≠ TTQ 126:128) binding (3S)-3-hydroxybutanoyl-CoA
- R235 (≠ K165) binding (3S)-3-hydroxybutanoyl-CoA
- N240 (= N170) binding (3S)-3-hydroxybutanoyl-CoA
- H245 (= H175) binding (3S)-3-hydroxybutanoyl-CoA
- R284 (= R218) binding (3S)-3-hydroxybutanoyl-CoA
Sites not aligning to the query:
- 76:79 binding (3S)-3-hydroxybutanoyl-CoA
Q5KUG0 Fused isobutyryl-CoA mutase; EC 5.4.99.13; EC 3.6.5.- from Geobacillus kaustophilus (strain HTA426) (see paper)
26% identity, 71% coverage: 18:497/675 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.
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)
27% identity, 71% coverage: 18:497/675 of query aligns to 596:1090/1093 of Q1LRY0
- F598 (≠ Y20) 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 substrate
- R728 (≠ Q124) binding substrate
- Y772 (≠ N167) binding substrate
- S821 (= S220) binding substrate
- R856 (≠ P256) binding substrate
- K861 (≠ R262) binding substrate
- E973 (= E377) binding GTP
Sites not aligning to the query:
- 39 binding axial binding residue
- 169:417 GTPase chaperone MeaI
- 219:224 binding GTP
- 223 binding Mg(2+)
- 248 binding Mg(2+)
- 249 binding Mg(2+)
- 262 binding Mg(2+); binding Mg(2+)
- 265 binding GTP
- 310 binding Mg(2+); binding Mg(2+)
- 311 binding Mg(2+)
- 357:360 binding GTP
- 418:579 Linker
- 587 binding substrate
- 1092 binding GTP
4xc6A Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, and mg (holo-icmf/gdp) (see paper)
27% identity, 71% coverage: 18:497/675 of query aligns to 570:1064/1067 of 4xc6A
- active site: F572 (≠ Y20), Y753 (= Y174), H754 (= H175)
- binding cobalamin: F601 (= F48), L606 (≠ Q53), S624 (≠ V70), Q716 (≠ R138), H754 (= H175), E757 (= E178), A758 (= A179), G842 (≠ S269), R843 (≠ L270), E879 (= E309), A880 (= A310), T882 (≠ G312), H967 (≠ E397)
- binding guanosine-5'-diphosphate: E947 (= E377)
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
8sslA Isobutyryl-coa mutase fused q341a in the presence of gtp (see paper)
27% identity, 71% coverage: 18:497/675 of query aligns to 575:1069/1072 of 8sslA
Sites not aligning to the query:
- binding guanosine-5'-diphosphate: 200, 201, 202, 241, 244, 337, 339, 374, 375, 376, 1071
- binding magnesium ion: 201, 241
5cjtA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isobutyryl-coenzyme a (see paper)
26% identity, 71% coverage: 18:497/675 of query aligns to 567:1059/1062 of 5cjtA
- active site: F569 (≠ Y20), Y750 (= Y174), H751 (= H175)
- binding cobalamin: F598 (= F48), L603 (≠ Q53), S621 (≠ V70), Q713 (≠ R138), H751 (= H175), E754 (= E178), A755 (= A179), G839 (≠ S269), R840 (≠ L270), E876 (= E309), A877 (= A310), T879 (≠ G312), H964 (≠ E397)
- binding isobutyryl-coenzyme a: R567 (= R18), F569 (≠ Y20), R593 (vs. gap), S648 (vs. gap), T650 (= T97), R699 (≠ Q124), T701 (= T126), Q703 (= Q128), Y743 (≠ N167), Y750 (= Y174), H751 (= H175), S792 (= S220), F794 (= F222), R827 (≠ P256), K832 (≠ R262), H834 (≠ G264)
- binding guanosine-5'-diphosphate: E944 (= E377)
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
>WP_012330042.1 NCBI__GCF_000019365.1:WP_012330042.1
MGEQATRTAQRDKPWIIRTYAGHSTAADSNALYRKNLAKGQTGLSVAFDLPTQTGYDPDH
ELARGEVGKVGVSIAHLGDMRTLFRDIPLAQMNTSMTINATAPWLLALYLAVAEEQGAPI
AALQGTTQNDIIKEYLSRGTYVFPPAPSLRLTKDVILFTTKHVPKWNPMNVCSYHLQEAG
ATPVQELSYALAIAIAVLDTVRADPDFDEASFEEVVGRISFFVNAGLRFITEICKMRAFS
DLWDEITRDRYGIKDPKKRIFRYGVQVNSLGLTEQQPENNVHRILIEMLAVTLSKRARAR
AVQLPAWNEALGLPRPWDQQWSMRMQQILAYETDLLEFDDIFDGSRVIDAKVEELKARTR
AELERIGALGGAVAAVETGALKRALVESNAQRIAAIERGEQVVVGVNRFETGEPSPLTAG
DGAIFTVSETVEMEAQGRIRAWRAERDAQAVARALDELDAAARSGANIMPVSIACAKAGV
TTGEWGARLRAVFGEYRAPTGVTPETVTSGAAEEARLLIADLGERLGETPKLVVGKPGLD
GHSNGAEQIALRARDVGFDVSYDGIRQTPDEIVAKARERGAHVIGLSILSGSHVPLVREV
KARLRREGLDHVPVVVGGIISPEDELVLKNMGVAAVYTPKDYAIDAIMVGLAKVVERALA
AREAQGPVPNREQVF
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