SitesBLAST
Comparing WP_025273328.1 NCBI__GCF_000527155.1:WP_025273328.1 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)
P22033 Methylmalonyl-CoA mutase, mitochondrial; MCM; Methylmalonyl-CoA isomerase; EC 5.4.99.2 from Homo sapiens (Human) (see 28 papers)
49% identity, 97% coverage: 10:517/523 of query aligns to 66:576/750 of P22033
- I69 (= I13) to V: in MMAM; likely benign; dbSNP:rs115923556
- P86 (= P29) 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 (= G30) to E: in MMAM; mut0; dbSNP:rs1554160986
- R93 (= R36) to H: in MMAM; mut0; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918251
- G94 (= G37) to R: in MMAM; mut0; dbSNP:rs727504022; to V: in MMAM; mut- and mut0; dbSNP:rs535411418
- P95 (≠ A38) to R: in MMAM; mut0; dbSNP:rs190834116
- YPTM 96:99 (= YPTM 39:42) binding malonyl-CoA
- Y100 (= Y43) 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 (= W48) to R: in MMAM; mut0; dbSNP:rs121918249
- TIRQY 106:110 (≠ TMRQY 49:53) binding malonyl-CoA
- R108 (= R51) to C: in MMAM; mut0; dbSNP:rs121918257; to G: in MMAM; mut-; to H: in MMAM; mut0; dbSNP:rs483352778
- Q109 (= Q52) to R: in MMAM; mut0; dbSNP:rs1461110052
- G133 (= G76) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253828
- A137 (= A80) to V: in MMAM; mut0; dbSNP:rs941483851
- D139 (= D82) to N: in MMAM; uncertain significance; dbSNP:rs879253829
- L140 (= L83) to P: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- A141 (≠ P84) to T: in MMAM; decreased protein expression; dbSNP:rs1554160730
- H143 (≠ Q86) to Y: in MMAM; mut0
- G145 (= G88) to S: in MMAM; mut0
- S148 (= S91) to L: in MMAM; mut0; dbSNP:rs1300547552
- D156 (≠ E99) to N: in MMAM; mut-
- G158 (= G101) to V: in MMAM; mut0
- G161 (= G104) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; to V: in MMAM; decreased protein expression
- F174 (= F117) to S: in MMAM; mut0; dbSNP:rs864309733
- M186 (= M129) to V: in MMAM; mut-; dbSNP:rs148331800
- T187 (= T130) to S: in MMAM; mut0; dbSNP:rs879253830
- N189 (= N132) to I: in MMAM; mut-; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs200908035; to K: in MMAM; mut-; dbSNP:rs1561959114
- A191 (≠ P134) to E: in MMAM; mut- and mut0; affects proper folding; reduced protein level; decreased methylmalonyl-CoA mutase activity; dbSNP:rs760782399
- A197 (≠ L140) to E: in MMAM; mut0
- G203 (≠ A146) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs778702777
- E205 (= E148) natural variant: Missing (in MMAM; mut0; dbSNP:rs879253831)
- G215 (= G158) to C: in MMAM; mut- and mut0; dbSNP:rs121918258; to S: in MMAM; mut0; dbSNP:rs121918258
- TIQ 216:218 (= TIQ 159:161) binding malonyl-CoA
- Q218 (= Q161) to H: in MMAM; mut0 and mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability; dbSNP:rs1446389693
- N219 (= N162) to Y: in MMAM; mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; dbSNP:rs121918256
- R228 (= R171) binding malonyl-CoA; to Q: in MMAM; mut0; dbSNP:rs770810987
- T230 (= T173) to I: in MMAM; mut-; to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253833
- Y231 (= Y174) 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 (≠ Q198) binding malonyl-CoA
- S262 (= S205) to N: in MMAM; mut0
- H265 (= H208) binding malonyl-CoA; to Y: in MMAM; mut-
- E276 (= E219) to D: in MMAM; uncertain significance; mut-; dbSNP:rs12175488
- L281 (= L224) to S: in MMAM; mut0; dbSNP:rs796052007
- G284 (= G227) to E: in MMAM; mut0; dbSNP:rs879253835; to R: in MMAM; mut0; dbSNP:rs761477436
- S288 (≠ V231) to P: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1179778233
- G291 (≠ A234) to E: in MMAM; mut0
- Q293 (≠ D236) to P: in MMAM; mut0
- RLS 304:306 (= RLS 247:249) binding malonyl-CoA
- L305 (= L248) to S: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554160246
- S306 (= S249) to F: in MMAM; mut0; dbSNP:rs1085307929
- W309 (≠ F252) to G: in MMAM; decreased protein expression
- G312 (≠ R255) to V: in MMAM; mut0; dbSNP:rs864309734
- Y316 (≠ L259) 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 (= A267) to T: in MMAM; mut-; dbSNP:rs780387525
- R326 (= R269) to K: in MMAM; uncertain significance; dbSNP:rs758577372
- L328 (= L271) 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 (= S287) 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 (≠ R289) natural variant: Missing (in MMAM; mut0)
- L347 (= L290) to R: in MMAM; mut0; dbSNP:rs1026703654
- H350 (= H293) to Y: in MMAM; mut0; dbSNP:rs1407914109
- L358 (= L301) to P: in MMAM; mut0
- N366 (= N309) 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 (= R312) 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 (≠ V313) to P: in MMAM; mut0; dbSNP:rs368790885
- A377 (= A320) to E: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918250
- Q383 (= Q326) to H: in MMAM; mut0; to P: in MMAM; mut0
- H386 (= H329) to N: in MMAM; mut0; dbSNP:rs1554159937; to R: in MMAM; mut0; dbSNP:rs866933356
- T387 (= T330) 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 (= N331) to H: in MMAM; mut0; dbSNP:rs766010704; to K: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253840
- S389 (= S332) natural variant: Missing (in MMAM; mut0)
- I412 (= I355) natural variant: Missing (in MMAM; mut0)
- P424 (= P367) to L: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253842
- G426 (≠ A369) 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 (= G370) to D: in MMAM; mut0; dbSNP:rs753288303
- G454 (≠ S397) to E: in MMAM; mut0
- A499 (≠ P442) to T: in dbSNP:rs2229385
- I505 (≠ V448) to T: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- Q514 (= Q456) to E: in MMAM; uncertain significance; to K: in MMAM; decreased protein expression
- L518 (≠ V460) to P: in MMAM; mut0; dbSNP:rs864309738
- R532 (≠ D474) to H: in dbSNP:rs1141321
- A535 (= A477) to P: in MMAM; mut0; dbSNP:rs760183775
- A552 (≠ M493) to V: in MMAM; uncertain significance; dbSNP:rs879253845
- C560 (≠ A501) to Y: in MMAM; mut0; dbSNP:rs1238333040
- T566 (≠ S507) to R: in MMAM; mut0
- F573 (≠ W514) 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
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
- 7:750 natural variant: Missing (in MMAM; mut-)
- 50 binding malonyl-CoA
- 152:750 natural variant: Missing (in MMAM; mut0)
- 228:750 natural variant: Missing (in MMAM; mut0)
- 587 Y → C: in MMAM; mut-
- 597 I → R: in MMAM; no changed in protein expression; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554158951
- 615 P → L: in MMAM; mut0; affects proper folding; reduced strongly protein level; P → R: in MMAM; mut0; dbSNP:rs1554158777; P → T: in MMAM; mut0; affects proper folding; reduced strongly protein level; loss of methylmalonyl-CoA mutase activity; dbSNP:rs1302409621
- 616 R → C: in MMAM; mut0; dbSNP:rs765284825
- 617 L → R: in MMAM; mut0; dbSNP:rs1554158775
- 621 K → N: in MMAM; mut0
- 623 G → R: in MMAM; mut0; dbSNP:rs121918254
- 624 Q → R: in MMAM; no effect on protein abundance; dbSNP:rs768521956
- 625 D → G: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253847; D → V: in MMAM; mut0; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity
- 626 G → C: in MMAM; mut-; dbSNP:rs982110849
- 627 binding axial binding residue; H → R: in MMAM; mut0; dbSNP:rs372486357
- 630 G → E: in MMAM; mut0; dbSNP:rs143023066
- 633 V → 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
- 637 G → E: in MMAM; mut-; G → R: in MMAM; mut0; dbSNP:rs781501004
- 638 F → I: in MMAM; mut0
- 640 D → Y: in MMAM; mut0; dbSNP:rs865815395
- 642 G → R: in MMAM; mut-; dbSNP:rs747897332
- 648 G → 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
- 669 V → E: in MMAM; mut0; dbSNP:rs1360470463
- 671 I → V: in dbSNP:rs8589
- 674 L → F: in MMAM; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1164271240
- 678 H → R: in MMAM; mut-; dbSNP:rs147094927
- 684 natural variant: E -> EL (in MMAM; mut-)
- 685 L → R: in MMAM; mut-; dbSNP:rs864309739
- 694 R → L: in MMAM; mut-; decreased protein abundance; loss of methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability; R → 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
- 700 M → 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
- 703 G → R: in MMAM; mut0; dbSNP:rs121918255
- 717 G → 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
- 723 G → D: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity; dbSNP:rs755077681
8gjuJ Crystal structure of human methylmalonyl-coa mutase (mmut) in complex with methylmalonic acidemia type a protein (mmaa), coenzyme a, and gdp (see paper)
49% identity, 97% coverage: 10:517/523 of query aligns to 31:541/689 of 8gjuJ
- binding coenzyme a: Y61 (= Y39), T63 (= T41), R68 (≠ K46), T71 (= T49), R73 (= R51), S150 (= S128), T152 (= T130), T181 (= T159), Q183 (= Q161), N222 (= N200), R269 (= R247), S271 (= S249), R313 (= R291), A314 (≠ F292), H315 (= H293), Q348 (= Q326)
8dyjB Crystal structure of human methylmalonyl-coa mutase in complex with adp and cob(ii)alamin (see paper)
49% identity, 97% coverage: 10:517/523 of query aligns to 30:540/708 of 8dyjB
- binding adenosine-5'-diphosphate: Y74 (= Y53), T151 (= T130), R192 (= R171), Y228 (= Y207), H229 (= H208), F272 (= F251), Q316 (= Q295), N352 (= N331), E356 (= E335), L360 (= L339), P361 (= P340)
- binding cobalamin: F102 (= F81), L104 (= L83), H107 (≠ Q86), A124 (≠ V103), V191 (≠ A170), R192 (= R171), H229 (= H208), E232 (= E211), G319 (= G298), W320 (≠ V299), E356 (= E335), G359 (≠ A338), L360 (= L339)
Sites not aligning to the query:
- binding cobalamin: 590, 591, 592, 593, 594, 598, 636, 638, 640, 666, 667, 668, 686, 687, 690
2xiqA Crystal structure of human methylmalonyl-coa mutase in complex with adenosylcobalamin and malonyl-coa (see paper)
49% identity, 97% coverage: 10:517/523 of query aligns to 31:541/714 of 2xiqA
- active site: Y75 (= Y53), Y229 (= Y207), H230 (= H208)
- binding cobalamin: Y75 (= Y53), L105 (= L83), H108 (≠ Q86), A125 (≠ V103), R193 (= R171), E233 (= E211), G320 (= G298), W321 (≠ V299), E357 (= E335), G360 (≠ A338), L361 (= L339)
- binding malonyl-coenzyme a: Y61 (= Y39), T63 (= T41), M64 (= M42), R68 (≠ K46), T71 (= T49), R73 (= R51), Y75 (= Y53), S150 (= S128), T152 (= T130), T181 (= T159), R193 (= R171), K220 (≠ Q198), H230 (= H208), R269 (= R247), S271 (= S249), F273 (= F251), R313 (= R291), A314 (≠ F292), H315 (= H293), Q317 (= Q295), Q348 (= Q326)
Sites not aligning to the query:
- active site: 586, 590, 592
- binding cobalamin: 591, 592, 593, 594, 595, 599, 635, 637, 639, 641, 667, 668, 687, 688, 691
6reqA Methylmalonyl-coa mutase, 3-carboxypropyl-coa inhibitor complex (see paper)
53% identity, 93% coverage: 30:517/523 of query aligns to 65:558/727 of 6reqA
- active site: Y88 (= Y53), Y242 (= Y207), H243 (= H208)
- binding 3-carboxypropyl-coenzyme a: Y74 (= Y39), T76 (= T41), M77 (= M42), F80 (≠ T45), R81 (≠ K46), T84 (= T49), R86 (= R51), Y88 (= Y53), S113 (= S78), S163 (= S128), T165 (= T130), T194 (= T159), R206 (= R171), H243 (= H208), R282 (= R247), S284 (= S249), F286 (= F251), H327 (= H293), Q329 (= Q295), Q360 (= Q326)
- binding cobalamin: Y88 (= Y53), F116 (= F81), L118 (= L83), H121 (≠ Q86), A138 (≠ V103), R206 (= R171), E246 (= E211), G332 (= G298), W333 (≠ V299), E369 (= E335), A370 (= A336), A372 (= A338)
Sites not aligning to the query:
- active site: 603, 607, 609
- binding cobalamin: 608, 609, 610, 611, 612, 616, 620, 654, 656, 658, 684, 685, 704, 705, 708
P11653 Methylmalonyl-CoA mutase large subunit; MCM-alpha; EC 5.4.99.2 from Propionibacterium freudenreichii subsp. shermanii (see 4 papers)
53% identity, 93% coverage: 30:517/523 of query aligns to 66:559/728 of P11653
- Y75 (= Y39) binding (R)-methylmalonyl-CoA
- M78 (= M42) binding (R)-methylmalonyl-CoA
- R82 (≠ K46) binding (R)-methylmalonyl-CoA
- T85 (= T49) binding (R)-methylmalonyl-CoA
- R87 (= R51) binding (R)-methylmalonyl-CoA
- Y89 (= Y53) binding (R)-methylmalonyl-CoA; mutation to F: Does not significantly affect affinity for succiny-CoA, but kcat is lowered about 580-fold.
- S114 (= S78) binding (R)-methylmalonyl-CoA
- F117 (= F81) binding cob(II)alamin
- A139 (≠ V103) binding cob(II)alamin
- T195 (= T159) binding (R)-methylmalonyl-CoA
- Q197 (= Q161) binding (R)-methylmalonyl-CoA
- V206 (≠ A170) binding cob(II)alamin
- R207 (= R171) binding (R)-methylmalonyl-CoA; binding cob(II)alamin
- H244 (= H208) binding (R)-methylmalonyl-CoA
- R283 (= R247) binding (R)-methylmalonyl-CoA
- S285 (= S249) binding (R)-methylmalonyl-CoA
- G333 (= G298) binding cob(II)alamin
- E370 (= E335) binding cob(II)alamin
- A373 (= A338) binding cob(II)alamin
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 609 binding cob(II)alamin
- 610 binding axial binding residue
- 611 binding cob(II)alamin
- 612 binding cob(II)alamin
- 655 binding cob(II)alamin
- 657 binding cob(II)alamin
- 686 binding cob(II)alamin
- 709 binding cob(II)alamin
4reqA Methylmalonyl-coa mutase substrate complex (see paper)
53% identity, 93% coverage: 30:517/523 of query aligns to 64:557/726 of 4reqA
- active site: Y87 (= Y53), Y241 (= Y207), H242 (= H208)
- binding cobalamin: Y87 (= Y53), L117 (= L83), A137 (≠ V103), V204 (≠ A170), R205 (= R171), H242 (= H208), E245 (= E211), G331 (= G298), W332 (≠ V299), E368 (= E335), A369 (= A336), A371 (= A338), L372 (= L339)
- binding methylmalonyl-coenzyme a: Y73 (= Y39), M76 (= M42), F79 (≠ T45), R80 (≠ K46), T83 (= T49), R85 (= R51), Y87 (= Y53), S112 (= S78), S162 (= S128), T164 (= T130), T193 (= T159), R205 (= R171), N234 (= N200), Y241 (= Y207), H242 (= H208), R281 (= R247), S283 (= S249), F285 (= F251), H326 (= H293), Q328 (= Q295), Q359 (= Q326), S360 (= S327)
- binding succinyl-coenzyme a: Y73 (= Y39), M76 (= M42), F79 (≠ T45), R80 (≠ K46), T83 (= T49), R85 (= R51), Y87 (= Y53), S162 (= S128), T164 (= T130), T193 (= T159), Q195 (= Q161), R205 (= R171), N234 (= N200), Y241 (= Y207), H242 (= H208), R281 (= R247), S283 (= S249), F285 (= F251), R324 (= R291), H326 (= H293), Q359 (= Q326)
Sites not aligning to the query:
- active site: 602, 606, 608
- binding cobalamin: 607, 608, 609, 610, 611, 615, 653, 655, 683, 684, 685, 703, 704, 707
7reqA Methylmalonyl-coa mutase, 2-carboxypropyl-coa inhibitor complex (see paper)
53% identity, 93% coverage: 30:517/523 of query aligns to 63:556/725 of 7reqA
- active site: Y86 (= Y53), Y240 (= Y207), H241 (= H208)
- binding 2-carboxypropyl-coenzyme a: Y72 (= Y39), T74 (= T41), M75 (= M42), F78 (≠ T45), R79 (≠ K46), T82 (= T49), R84 (= R51), Y86 (= Y53), S161 (= S128), T163 (= T130), T192 (= T159), R204 (= R171), H241 (= H208), R280 (= R247), S282 (= S249), F284 (= F251), H325 (= H293), Q358 (= Q326)
- binding cobalamin: Y86 (= Y53), L116 (= L83), A136 (≠ V103), R204 (= R171), E244 (= E211), G330 (= G298), W331 (≠ V299), E367 (= E335), A368 (= A336), A370 (= A338)
Sites not aligning to the query:
- active site: 601, 605, 607
- binding cobalamin: 606, 607, 608, 609, 610, 614, 652, 654, 682, 683, 702, 703, 706
3reqA Methylmalonyl-coa mutase, substrate-free state (poor quality structure) (see paper)
53% identity, 93% coverage: 30:517/523 of query aligns to 63:556/725 of 3reqA
- active site: Y86 (= Y53), Y240 (= Y207), H241 (= H208)
- binding adenosine: Y86 (= Y53), Y240 (= Y207), E244 (= E211), G330 (= G298)
- binding cobalamin: L116 (= L83), V203 (≠ A170), R204 (= R171), E244 (= E211), G330 (= G298), W331 (≠ V299), A368 (= A336)
Sites not aligning to the query:
- active site: 601, 605, 607
- binding cobalamin: 606, 607, 608, 609, 610, 614, 650, 652, 654, 682, 683, 702, 703, 704, 706
2reqA Methylmalonyl-coa mutase, non-productive coa complex, in open conformation representing substrate-free state (see paper)
53% identity, 93% coverage: 30:517/523 of query aligns to 63:556/725 of 2reqA
Sites not aligning to the query:
- active site: 601, 605, 607
- binding cobalamin: 606, 607, 608, 609, 610, 614, 650, 652, 654, 655, 682, 683, 702, 703, 706
5reqA Methylmalonyl-coa mutase, y89f mutant, substrate complex (see paper)
53% identity, 93% coverage: 30:517/523 of query aligns to 63:556/725 of 5reqA
- active site: F86 (≠ Y53), Y240 (= Y207), H241 (= H208)
- binding cobalamin: L116 (= L83), A136 (≠ V103), R204 (= R171), H241 (= H208), E244 (= E211), G330 (= G298), W331 (≠ V299), E367 (= E335), A368 (= A336), A370 (= A338)
- binding methylmalonyl(carbadethia)-coenzyme a: Y72 (= Y39), T74 (= T41), M75 (= M42), R79 (≠ K46), T82 (= T49), R84 (= R51), F86 (≠ Y53), S111 (= S78), S161 (= S128), T163 (= T130), T192 (= T159), Q194 (= Q161), R204 (= R171), N233 (= N200), H241 (= H208), R280 (= R247), S282 (= S249), F284 (= F251), T324 (≠ F292), H325 (= H293), Q358 (= Q326), S359 (= S327)
- binding succinyl(carbadethia)-coenzyme a: Y72 (= Y39), T74 (= T41), M75 (= M42), R79 (≠ K46), T82 (= T49), R84 (= R51), F86 (≠ Y53), S161 (= S128), T163 (= T130), T192 (= T159), R204 (= R171), N233 (= N200), H241 (= H208), R280 (= R247), S282 (= S249), F284 (= F251), H325 (= H293), Q358 (= Q326)
Sites not aligning to the query:
- active site: 601, 605, 607
- binding cobalamin: 606, 607, 608, 609, 610, 614, 652, 654, 682, 683, 684, 702, 703, 706
1e1cA Methylmalonyl-coa mutase h244a mutant (see paper)
53% identity, 93% coverage: 30:517/523 of query aligns to 65:558/727 of 1e1cA
- active site: Y88 (= Y53), Y242 (= Y207), A243 (≠ H208)
- binding cobalamin: Y88 (= Y53), L118 (= L83), H121 (≠ Q86), A138 (≠ V103), V205 (≠ A170), R206 (= R171), E246 (= E211), G332 (= G298), W333 (≠ V299), E369 (= E335), A370 (= A336), A372 (= A338), L373 (= L339)
- binding desulfo-coenzyme a: Y74 (= Y39), M77 (= M42), F80 (≠ T45), R81 (≠ K46), T84 (= T49), R86 (= R51), S113 (= S78), S163 (= S128), T165 (= T130), T194 (= T159), R282 (= R247), S284 (= S249), H327 (= H293), Q360 (= Q326)
Sites not aligning to the query:
- active site: 603, 607, 609
- binding cobalamin: 608, 609, 610, 611, 612, 616, 620, 654, 656, 684, 685, 686, 704, 705, 708, 713
6oxdA Structure of mycobacterium tuberculosis methylmalonyl-coa mutase with adenosyl cobalamin (see paper)
52% identity, 93% coverage: 29:517/523 of query aligns to 76:565/736 of 6oxdA
- active site: Y100 (= Y53), Y254 (= Y207), H255 (= H208)
- binding cobalamin: Y100 (= Y53), L130 (= L83), H133 (≠ Q86), A150 (≠ V103), R218 (= R171), E258 (= E211), G344 (= G298), W345 (≠ V299), E381 (= E335), A382 (= A336), A384 (= A338), L385 (= L339)
- binding Itaconyl coenzyme A: Y86 (= Y39), T88 (= T41), M89 (= M42), Q93 (≠ K46), T96 (= T49), R98 (= R51), Y100 (= Y53), S175 (= S128), T177 (= T130), T206 (= T159), R218 (= R171), H255 (= H208), R294 (= R247), S296 (= S249), F298 (= F251), R337 (= R291), T338 (≠ F292), H339 (= H293), Q341 (= Q295), Q372 (= Q326)
Sites not aligning to the query:
- active site: 610, 614, 616
- binding cobalamin: 615, 616, 617, 618, 661, 663, 665, 691, 692, 711, 712, 715
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)
44% identity, 94% coverage: 25:517/523 of query aligns to 62:556/562 of I3VE77
- YPTM 76:79 (= YPTM 39:42) binding (3S)-3-hydroxybutanoyl-CoA
- TMR 86:88 (= TMR 49:51) binding (3S)-3-hydroxybutanoyl-CoA
- I90 (≠ Y53) 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 (≠ A80) 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 (≠ TIQ 159:161) binding (3S)-3-hydroxybutanoyl-CoA
- R235 (≠ Q198) binding (3S)-3-hydroxybutanoyl-CoA
- N240 (≠ S203) binding (3S)-3-hydroxybutanoyl-CoA
- H245 (= H208) binding (3S)-3-hydroxybutanoyl-CoA
- R284 (= R247) binding (3S)-3-hydroxybutanoyl-CoA
4r3uA Crystal structure of 2-hydroxyisobutyryl-coa mutase (see paper)
44% identity, 94% coverage: 25:517/523 of query aligns to 61:555/557 of 4r3uA
- active site: I89 (≠ Y53), Y243 (= Y207), H244 (= H208)
- binding 3-hydroxybutanoyl-coenzyme a: Y75 (= Y39), T77 (= T41), M78 (= M42), R82 (≠ K46), T85 (= T49), R87 (= R51), I89 (≠ Y53), D116 (≠ A80), S164 (= S128), T166 (= T130), T195 (= T159), Q197 (= Q161), R234 (≠ Q198), N236 (= N200), N239 (≠ S203), Y243 (= Y207), H244 (= H208), R283 (= R247), F287 (= F251), R327 (= R291), F328 (= F292), H329 (= H293), Q331 (= Q295), Q362 (= Q326)
- 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 (= Y39), T77 (= T41), M78 (= M42), R82 (≠ K46), T85 (= T49), R87 (= R51), I89 (≠ Y53), D116 (≠ A80), S164 (= S128), T166 (= T130), T195 (= T159), Q197 (= Q161), R234 (≠ Q198), N236 (= N200), N239 (≠ S203), H244 (= H208), R283 (= R247), F287 (= F251), R327 (= R291), F328 (= F292), H329 (= H293), Q331 (= Q295), Q362 (= Q326)
- binding cobalamin: D116 (≠ A80), M119 (≠ L83), E139 (≠ V103), Q207 (≠ R171), E209 (≠ T173), E247 (= E211), A334 (≠ G298), E371 (= E335), A372 (= A336), A374 (= A338)
Q5KUG0 Fused isobutyryl-CoA mutase; EC 5.4.99.13; EC 3.6.5.- from Geobacillus kaustophilus (strain HTA426) (see paper)
35% identity, 93% coverage: 29:517/523 of query aligns to 566:1082/1086 of Q5KUG0
Sites not aligning to the query:
- 213 K→A: Loss of GTPase and ATPase activities. No effect on the mutase activity.
5cjtA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isobutyryl-coenzyme a (see paper)
35% identity, 93% coverage: 29:517/523 of query aligns to 546:1058/1062 of 5cjtA
- active site: F569 (≠ Y53), Y750 (= Y207), H751 (= H208)
- binding cobalamin: F598 (= F81), L603 (≠ Q86), S621 (≠ V103), Q713 (≠ R171), H751 (= H208), E754 (= E211), A755 (= A212), G839 (= G298), R840 (≠ V299), E876 (= E335), A877 (= A336), T879 (≠ A338), H964 (≠ D423)
- binding isobutyryl-coenzyme a: F556 (≠ Y39), F558 (≠ T41), R560 (≠ Y43), R567 (= R51), F569 (≠ Y53), R593 (≠ G76), S648 (vs. gap), T650 (= T130), R699 (= R157), T701 (= T159), Q703 (= Q161), Y743 (≠ N200), Y750 (= Y207), H751 (= H208), S792 (= S249), F794 (= F251), R827 (≠ K286), K832 (≠ R291), H834 (= H293)
- binding guanosine-5'-diphosphate: E944 (= E403)
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
4xc7A Isobutyryl-coa mutase fused with bound butyryl-coa and without cobalamin or gdp (apo-icmf) (see paper)
35% identity, 93% coverage: 29:517/523 of query aligns to 543:1049/1053 of 4xc7A
- active site: F566 (≠ Y53), Y747 (= Y207), H748 (= H208)
- binding Butyryl Coenzyme A: F553 (≠ Y39), R557 (≠ Y43), R564 (= R51), F566 (≠ Y53), R590 (≠ G76), S645 (vs. gap), T647 (= T130), R696 (= R157), T698 (= T159), Y740 (≠ N200), S789 (= S249), F791 (= F251), R824 (≠ K286), K829 (≠ R291), H831 (= H293)
Sites not aligning to the query:
4xc6A Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, and mg (holo-icmf/gdp) (see paper)
35% identity, 93% coverage: 29:517/523 of query aligns to 549:1063/1067 of 4xc6A
- active site: F572 (≠ Y53), Y753 (= Y207), H754 (= H208)
- binding cobalamin: F601 (= F81), L606 (≠ Q86), S624 (≠ V103), Q716 (≠ R171), H754 (= H208), E757 (= E211), A758 (= A212), G842 (= G298), R843 (≠ V299), E879 (= E335), A880 (= A336), T882 (≠ A338), H967 (≠ D423)
- binding guanosine-5'-diphosphate: E947 (= E403)
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)
35% identity, 93% coverage: 29:517/523 of query aligns to 554:1068/1072 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
Query Sequence
>WP_025273328.1 NCBI__GCF_000527155.1:WP_025273328.1
MDRDVQGRTGVPIEPLYESYKREPELGKPGSFPYTRGAYPTMYTTKPWTMRQYAGFATAS
ESNQRYRELLANGSTGLSVAFDLPTQMGYDSDAAIAAGEVGKVGVAIDSIDDMRILFNEI
PLDQVSTSMTINAPASVLLLLYQLVAEEQGVSGDQLRGTIQNDVLKEYIARGTYIFPPEP
SLRLISDTFAYCSAEMPQWNTISISGYHMAEAGADAGQELGFTLANGIQYVQAAIDAGLD
IDTIAPRLSFFFVARSSILTEVAKFRAARRLWAHVMRDRFGTDNPKSQRLRFHTQTAGVE
LTAQQPEINLSRVTIQALAAVMGGTQSLHTNSFDEALALPTDKSARLALRTQQVIANETD
LTDTVDPFAGSYAVESLTDEIEAQATELIDAVFAHGSAVKAIEQGFQKTEIERTAYATAQ
RIDAEEQVIVGVNKYRTEDEEPYTPLRVDPEQEASQVKSVQATRNDRDNDVVADKLAALK
SAAGTDDNILYPMKEALAAKATVGEVSGALAEVWGRYVPPETF
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