SitesBLAST
Comparing CA265_RS25460 FitnessBrowser__Pedo557:CA265_RS25460 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)
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)
49% identity, 99% coverage: 8:515/515 of query aligns to 40:556/562 of I3VE77
- YPTM 76:79 (≠ QKDM 38:41) binding
- TMR 86:88 (= TMR 48:50) binding
- I90 (≠ Y52) 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 (≠ A79) 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 158:160) binding
- R235 (≠ K197) binding
- N240 (≠ S202) binding
- H245 (= H207) binding
- R284 (= R246) binding
4r3uA Crystal structure of 2-hydroxyisobutyryl-coa mutase (see paper)
49% identity, 99% coverage: 8:515/515 of query aligns to 39:555/557 of 4r3uA
- active site: I89 (≠ Y52), Y243 (= Y206), H244 (= H207)
- binding 3-hydroxybutanoyl-coenzyme a: Y75 (≠ Q38), T77 (≠ D40), M78 (= M41), R82 (= R45), T85 (= T48), R87 (= R50), I89 (≠ Y52), D116 (≠ A79), S164 (= S127), T166 (= T129), T195 (= T158), Q197 (= Q160), R234 (≠ K197), N236 (= N199), N239 (≠ S202), Y243 (= Y206), H244 (= H207), R283 (= R246), F287 (= F250), R327 (= R289), F328 (= F290), H329 (= H291), Q331 (= Q293), Q362 (= Q324)
- 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 (≠ Q38), T77 (≠ D40), M78 (= M41), R82 (= R45), T85 (= T48), R87 (= R50), I89 (≠ Y52), D116 (≠ A79), S164 (= S127), T166 (= T129), T195 (= T158), Q197 (= Q160), R234 (≠ K197), N236 (= N199), N239 (≠ S202), H244 (= H207), R283 (= R246), F287 (= F250), R327 (= R289), F328 (= F290), H329 (= H291), Q331 (= Q293), Q362 (= Q324)
- binding cobalamin: D116 (≠ A79), M119 (≠ L82), E139 (≠ V102), Q207 (≠ R170), E209 (≠ T172), E247 (= E210), A334 (≠ G296), E371 (= E333), A372 (= A334), A374 (≠ S336)
2xiqA Crystal structure of human methylmalonyl-coa mutase in complex with adenosylcobalamin and malonyl-coa (see paper)
49% identity, 98% coverage: 8:513/515 of query aligns to 28:539/714 of 2xiqA
- active site: Y75 (= Y52), Y229 (= Y206), H230 (= H207)
- binding cobalamin: Y75 (= Y52), L105 (= L82), H108 (≠ Q85), A125 (≠ V102), R193 (= R170), E233 (= E210), G320 (= G296), W321 (≠ S297), E357 (= E333), G360 (≠ S336), L361 (= L337)
- binding malonyl-coenzyme a: Y61 (≠ Q38), T63 (≠ D40), M64 (= M41), R68 (= R45), T71 (= T48), R73 (= R50), Y75 (= Y52), S150 (= S127), T152 (= T129), T181 (= T158), R193 (= R170), K220 (= K197), H230 (= H207), R269 (= R246), S271 (= S248), F273 (= F250), R313 (= R289), A314 (≠ F290), H315 (= H291), Q317 (= Q293), Q348 (= Q324)
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
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, 98% coverage: 8:513/515 of query aligns to 28:539/689 of 8gjuJ
- binding coenzyme a: Y61 (≠ Q38), T63 (≠ D40), R68 (= R45), T71 (= T48), R73 (= R50), S150 (= S127), T152 (= T129), T181 (= T158), Q183 (= Q160), N222 (= N199), R269 (= R246), S271 (= S248), R313 (= R289), A314 (≠ F290), H315 (= H291), Q348 (= Q324)
P22033 Methylmalonyl-CoA mutase, mitochondrial; MCM; Methylmalonyl-CoA isomerase; EC 5.4.99.2 from Homo sapiens (Human) (see 28 papers)
49% identity, 98% coverage: 8:513/515 of query aligns to 63:574/750 of P22033
- I69 (= I14) to V: in MMAM; likely benign; dbSNP:rs115923556
- P86 (= P28) 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 (= G29) to E: in MMAM; mut0; dbSNP:rs1554160986
- R93 (= R35) to H: in MMAM; mut0; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918251
- G94 (= G36) to R: in MMAM; mut0; dbSNP:rs727504022; to V: in MMAM; mut- and mut0; dbSNP:rs535411418
- P95 (≠ I37) to R: in MMAM; mut0; dbSNP:rs190834116
- YPTM 96:99 (≠ QKDM 38:41) binding
- Y100 (= Y42) 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 (= W47) to R: in MMAM; mut0; dbSNP:rs121918249
- TIRQY 106:110 (≠ TMRQY 48:52) binding
- R108 (= R50) to C: in MMAM; mut0; dbSNP:rs121918257; to G: in MMAM; mut-; to H: in MMAM; mut0; dbSNP:rs483352778
- Q109 (= Q51) to R: in MMAM; mut0; dbSNP:rs1461110052
- G133 (= G75) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253828
- A137 (= A79) to V: in MMAM; mut0; dbSNP:rs941483851
- D139 (= D81) to N: in MMAM; uncertain significance; dbSNP:rs879253829
- L140 (= L82) to P: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- A141 (≠ P83) to T: in MMAM; decreased protein expression; dbSNP:rs1554160730
- H143 (≠ Q85) to Y: in MMAM; mut0
- G145 (= G87) to S: in MMAM; mut0
- S148 (= S90) to L: in MMAM; mut0; dbSNP:rs1300547552
- D156 (≠ E98) to N: in MMAM; mut-
- G158 (= G100) to V: in MMAM; mut0
- G161 (= G103) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; to V: in MMAM; decreased protein expression
- F174 (= F116) to S: in MMAM; mut0; dbSNP:rs864309733
- M186 (= M128) to V: in MMAM; mut-; dbSNP:rs148331800
- T187 (= T129) to S: in MMAM; mut0; dbSNP:rs879253830
- N189 (= N131) to I: in MMAM; mut-; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs200908035; to K: in MMAM; mut-; dbSNP:rs1561959114
- A191 (≠ T133) to E: in MMAM; mut- and mut0; affects proper folding; reduced protein level; decreased methylmalonyl-CoA mutase activity; dbSNP:rs760782399
- A197 (= A139) to E: in MMAM; mut0
- G203 (≠ A145) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs778702777
- E205 (≠ K147) natural variant: Missing (in MMAM; mut0; dbSNP:rs879253831)
- G215 (= G157) to C: in MMAM; mut- and mut0; dbSNP:rs121918258; to S: in MMAM; mut0; dbSNP:rs121918258
- TIQ 216:218 (= TIQ 158:160) binding
- Q218 (= Q160) to H: in MMAM; mut0 and mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability; dbSNP:rs1446389693
- N219 (= N161) to Y: in MMAM; mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; dbSNP:rs121918256
- R228 (= R170) binding ; to Q: in MMAM; mut0; dbSNP:rs770810987
- T230 (= T172) to I: in MMAM; mut-; to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253833
- Y231 (= Y173) 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 (= K197) binding
- S262 (= S204) to N: in MMAM; mut0
- H265 (= H207) binding ; to Y: in MMAM; mut-
- E276 (= E218) to D: in MMAM; uncertain significance; mut-; dbSNP:rs12175488
- L281 (= L223) to S: in MMAM; mut0; dbSNP:rs796052007
- G284 (= G226) to E: in MMAM; mut0; dbSNP:rs879253835; to R: in MMAM; mut0; dbSNP:rs761477436
- S288 (≠ L230) to P: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1179778233
- G291 (≠ A233) to E: in MMAM; mut0
- Q293 (≠ D235) to P: in MMAM; mut0
- RLS 304:306 (= RLS 246:248) binding
- L305 (= L247) to S: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554160246
- S306 (= S248) to F: in MMAM; mut0; dbSNP:rs1085307929
- W309 (≠ F251) to G: in MMAM; decreased protein expression
- G312 (≠ H254) to V: in MMAM; mut0; dbSNP:rs864309734
- Y316 (≠ F258) 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 (= A266) to T: in MMAM; mut-; dbSNP:rs780387525
- R326 (= R268) to K: in MMAM; uncertain significance; dbSNP:rs758577372
- L328 (≠ M270) 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 (≠ A285) 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 (≠ M287) natural variant: Missing (in MMAM; mut0)
- L347 (= L288) to R: in MMAM; mut0; dbSNP:rs1026703654
- H350 (= H291) to Y: in MMAM; mut0; dbSNP:rs1407914109
- L358 (= L299) to P: in MMAM; mut0
- N366 (= N307) 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 (= R310) 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 (≠ V311) to P: in MMAM; mut0; dbSNP:rs368790885
- A377 (= A318) to E: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918250
- Q383 (= Q324) to H: in MMAM; mut0; to P: in MMAM; mut0
- H386 (= H327) to N: in MMAM; mut0; dbSNP:rs1554159937; to R: in MMAM; mut0; dbSNP:rs866933356
- T387 (= T328) 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 (= N329) to H: in MMAM; mut0; dbSNP:rs766010704; to K: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253840
- S389 (≠ G330) natural variant: Missing (in MMAM; mut0)
- I412 (= I353) natural variant: Missing (in MMAM; mut0)
- P424 (= P365) to L: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253842
- G426 (≠ A367) 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 (= G368) to D: in MMAM; mut0; dbSNP:rs753288303
- G454 (= G395) to E: in MMAM; mut0
- A499 (≠ L440) to T: in dbSNP:rs2229385
- I505 (= I446) to T: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- Q514 (= Q454) to E: in MMAM; uncertain significance; to K: in MMAM; decreased protein expression
- L518 (= L458) to P: in MMAM; mut0; dbSNP:rs864309738
- R532 (≠ K472) to H: in dbSNP:rs1141321
- A535 (≠ Q475) to P: in MMAM; mut0; dbSNP:rs760183775
- A552 (≠ I491) to V: in MMAM; uncertain significance; dbSNP:rs879253845
- C560 (≠ A499) to Y: in MMAM; mut0; dbSNP:rs1238333040
- T566 (≠ A505) to R: in MMAM; mut0
- F573 (= F512) 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
- 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
8dyjB Crystal structure of human methylmalonyl-coa mutase in complex with adp and cob(ii)alamin (see paper)
49% identity, 98% coverage: 8:513/515 of query aligns to 27:538/708 of 8dyjB
- binding adenosine-5'-diphosphate: Y74 (= Y52), T151 (= T129), R192 (= R170), Y228 (= Y206), H229 (= H207), F272 (= F250), Q316 (= Q293), N352 (= N329), E356 (= E333), L360 (= L337), P361 (= P338)
- binding cobalamin: F102 (= F80), L104 (= L82), H107 (≠ Q85), A124 (≠ V102), V191 (≠ A169), R192 (= R170), H229 (= H207), E232 (= E210), G319 (= G296), W320 (≠ S297), E356 (= E333), G359 (≠ S336), L360 (= L337)
Sites not aligning to the query:
- binding cobalamin: 590, 591, 592, 593, 594, 598, 636, 638, 640, 666, 667, 668, 686, 687, 690
6oxdA Structure of mycobacterium tuberculosis methylmalonyl-coa mutase with adenosyl cobalamin (see paper)
48% identity, 98% coverage: 8:513/515 of query aligns to 47:563/736 of 6oxdA
- active site: Y100 (= Y52), Y254 (= Y206), H255 (= H207)
- binding cobalamin: Y100 (= Y52), L130 (= L82), H133 (≠ Q85), A150 (≠ V102), R218 (= R170), E258 (= E210), G344 (= G296), W345 (≠ S297), E381 (= E333), A382 (= A334), A384 (≠ S336), L385 (= L337)
- binding Itaconyl coenzyme A: Y86 (≠ Q38), T88 (≠ D40), M89 (= M41), Q93 (≠ R45), T96 (= T48), R98 (= R50), Y100 (= Y52), S175 (= S127), T177 (= T129), T206 (= T158), R218 (= R170), H255 (= H207), R294 (= R246), S296 (= S248), F298 (= F250), R337 (= R289), T338 (≠ F290), H339 (= H291), Q341 (= Q293), Q372 (= Q324)
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
P11653 Methylmalonyl-CoA mutase large subunit; MCM-alpha; EC 5.4.99.2 from Propionibacterium freudenreichii subsp. shermanii (see 4 papers)
48% identity, 94% coverage: 32:515/515 of query aligns to 69:559/728 of P11653
- Y75 (≠ Q38) binding
- M78 (= M41) binding
- R82 (= R45) binding
- T85 (= T48) binding
- R87 (= R50) binding
- Y89 (= Y52) binding ; mutation to F: Does not significantly affect affinity for succiny-CoA, but kcat is lowered about 580-fold.
- S114 (= S77) binding
- F117 (= F80) binding
- A139 (≠ V102) binding
- T195 (= T158) binding
- Q197 (= Q160) binding
- V206 (≠ A169) binding
- R207 (= R170) binding ; binding
- H244 (= H207) binding
- R283 (= R246) binding
- S285 (= S248) binding
- G333 (= G296) binding
- E370 (= E333) binding
- A373 (≠ S336) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 609 binding
- 610 binding axial binding residue
- 611 binding
- 612 binding
- 655 binding
- 657 binding
- 686 binding
- 709 binding
6reqA Methylmalonyl-coa mutase, 3-carboxypropyl-coa inhibitor complex (see paper)
48% identity, 94% coverage: 32:515/515 of query aligns to 68:558/727 of 6reqA
- active site: Y88 (= Y52), Y242 (= Y206), H243 (= H207)
- binding 3-carboxypropyl-coenzyme a: Y74 (≠ Q38), T76 (≠ D40), M77 (= M41), F80 (≠ G44), R81 (= R45), T84 (= T48), R86 (= R50), Y88 (= Y52), S113 (= S77), S163 (= S127), T165 (= T129), T194 (= T158), R206 (= R170), H243 (= H207), R282 (= R246), S284 (= S248), F286 (= F250), H327 (= H291), Q329 (= Q293), Q360 (= Q324)
- binding cobalamin: Y88 (= Y52), F116 (= F80), L118 (= L82), H121 (≠ Q85), A138 (≠ V102), R206 (= R170), E246 (= E210), G332 (= G296), W333 (≠ S297), E369 (= E333), A370 (= A334), A372 (≠ S336)
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
4reqA Methylmalonyl-coa mutase substrate complex (see paper)
48% identity, 94% coverage: 32:515/515 of query aligns to 67:557/726 of 4reqA
- active site: Y87 (= Y52), Y241 (= Y206), H242 (= H207)
- binding cobalamin: Y87 (= Y52), L117 (= L82), A137 (≠ V102), V204 (≠ A169), R205 (= R170), H242 (= H207), E245 (= E210), G331 (= G296), W332 (≠ S297), E368 (= E333), A369 (= A334), A371 (≠ S336), L372 (= L337)
- binding methylmalonyl-coenzyme a: Y73 (≠ Q38), M76 (= M41), F79 (≠ G44), R80 (= R45), T83 (= T48), R85 (= R50), Y87 (= Y52), S112 (= S77), S162 (= S127), T164 (= T129), T193 (= T158), R205 (= R170), N234 (= N199), Y241 (= Y206), H242 (= H207), R281 (= R246), S283 (= S248), F285 (= F250), H326 (= H291), Q328 (= Q293), Q359 (= Q324), S360 (= S325)
- binding succinyl-coenzyme a: Y73 (≠ Q38), M76 (= M41), F79 (≠ G44), R80 (= R45), T83 (= T48), R85 (= R50), Y87 (= Y52), S162 (= S127), T164 (= T129), T193 (= T158), Q195 (= Q160), R205 (= R170), N234 (= N199), Y241 (= Y206), H242 (= H207), R281 (= R246), S283 (= S248), F285 (= F250), R324 (= R289), H326 (= H291), Q359 (= Q324)
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)
48% identity, 94% coverage: 32:515/515 of query aligns to 66:556/725 of 7reqA
- active site: Y86 (= Y52), Y240 (= Y206), H241 (= H207)
- binding 2-carboxypropyl-coenzyme a: Y72 (≠ Q38), T74 (≠ D40), M75 (= M41), F78 (≠ G44), R79 (= R45), T82 (= T48), R84 (= R50), Y86 (= Y52), S161 (= S127), T163 (= T129), T192 (= T158), R204 (= R170), H241 (= H207), R280 (= R246), S282 (= S248), F284 (= F250), H325 (= H291), Q358 (= Q324)
- binding cobalamin: Y86 (= Y52), L116 (= L82), A136 (≠ V102), R204 (= R170), E244 (= E210), G330 (= G296), W331 (≠ S297), E367 (= E333), A368 (= A334), A370 (≠ S336)
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)
48% identity, 94% coverage: 32:515/515 of query aligns to 66:556/725 of 3reqA
- active site: Y86 (= Y52), Y240 (= Y206), H241 (= H207)
- binding adenosine: Y86 (= Y52), Y240 (= Y206), E244 (= E210), G330 (= G296)
- binding cobalamin: L116 (= L82), V203 (≠ A169), R204 (= R170), E244 (= E210), G330 (= G296), W331 (≠ S297), A368 (= A334)
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)
48% identity, 94% coverage: 32:515/515 of query aligns to 66:556/725 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)
47% identity, 94% coverage: 32:515/515 of query aligns to 66:556/725 of 5reqA
- active site: F86 (≠ Y52), Y240 (= Y206), H241 (= H207)
- binding cobalamin: L116 (= L82), A136 (≠ V102), R204 (= R170), H241 (= H207), E244 (= E210), G330 (= G296), W331 (≠ S297), E367 (= E333), A368 (= A334), A370 (≠ S336)
- binding methylmalonyl(carbadethia)-coenzyme a: Y72 (≠ Q38), T74 (≠ D40), M75 (= M41), R79 (= R45), T82 (= T48), R84 (= R50), F86 (≠ Y52), S111 (= S77), S161 (= S127), T163 (= T129), T192 (= T158), Q194 (= Q160), R204 (= R170), N233 (= N199), H241 (= H207), R280 (= R246), S282 (= S248), F284 (= F250), T324 (≠ F290), H325 (= H291), Q358 (= Q324), S359 (= S325)
- binding succinyl(carbadethia)-coenzyme a: Y72 (≠ Q38), T74 (≠ D40), M75 (= M41), R79 (= R45), T82 (= T48), R84 (= R50), F86 (≠ Y52), S161 (= S127), T163 (= T129), T192 (= T158), R204 (= R170), N233 (= N199), H241 (= H207), R280 (= R246), S282 (= S248), F284 (= F250), H325 (= H291), Q358 (= Q324)
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)
47% identity, 94% coverage: 32:515/515 of query aligns to 68:558/727 of 1e1cA
- active site: Y88 (= Y52), Y242 (= Y206), A243 (≠ H207)
- binding cobalamin: Y88 (= Y52), L118 (= L82), H121 (≠ Q85), A138 (≠ V102), V205 (≠ A169), R206 (= R170), E246 (= E210), G332 (= G296), W333 (≠ S297), E369 (= E333), A370 (= A334), A372 (≠ S336), L373 (= L337)
- binding desulfo-coenzyme a: Y74 (≠ Q38), M77 (= M41), F80 (≠ G44), R81 (= R45), T84 (= T48), R86 (= R50), S113 (= S77), S163 (= S127), T165 (= T129), T194 (= T158), R282 (= R246), S284 (= S248), H327 (= H291), Q360 (= Q324)
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
Q5KUG0 Fused isobutyryl-CoA mutase; EC 5.4.99.13; EC 3.6.5.- from Geobacillus kaustophilus (strain HTA426) (see paper)
36% identity, 95% coverage: 25:515/515 of query aligns to 563:1082/1086 of Q5KUG0
Sites not aligning to the query:
- 213 K→A: Loss of GTPase and ATPase activities. No effect on the mutase activity.
5cjwA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate pivalyl-coenzyme a (see paper)
36% identity, 95% coverage: 25:515/515 of query aligns to 545:1059/1063 of 5cjwA
- active site: F571 (≠ Y52), Y752 (= Y206), H753 (= H207)
- binding pivalyl-coenzyme A: F558 (≠ Q38), F560 (≠ D40), R562 (≠ Y42), R569 (= R50), F571 (≠ Y52), R595 (vs. gap), S650 (vs. gap), T652 (= T129), R701 (≠ S156), T703 (= T158), Q705 (= Q160), Y745 (≠ N199), Y752 (= Y206), H753 (= H207), S794 (= S248), F796 (= F250), R829 (≠ K284), K834 (≠ R289), H836 (= H291)
- binding cobalamin: F600 (= F80), L605 (≠ Q85), S623 (≠ V102), Q715 (≠ R170), H753 (= H207), E756 (= E210), A757 (= A211), G841 (= G296), R842 (≠ S297), E878 (= E333), A879 (= A334), T881 (≠ S336), H966 (≠ E421)
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)
36% identity, 95% coverage: 25:515/515 of query aligns to 543:1057/1061 of 5cjvA
- active site: F569 (≠ Y52), Y750 (= Y206), H751 (= H207)
- binding cobalamin: F598 (= F80), L603 (≠ Q85), S621 (≠ V102), Q713 (≠ R170), E754 (= E210), A755 (= A211), G839 (= G296), R840 (≠ S297), E876 (= E333), A877 (= A334), T879 (≠ S336), H964 (≠ E421)
- binding guanosine-5'-diphosphate: E944 (= E401)
- binding Isovaleryl-coenzyme A: F556 (≠ Q38), F558 (≠ D40), R560 (≠ Y42), R567 (= R50), F569 (≠ Y52), R593 (vs. gap), S648 (vs. gap), T650 (= T129), R699 (≠ S156), T701 (= T158), Q703 (= Q160), Q713 (≠ R170), Y743 (≠ N199), H751 (= H207), S792 (= S248), F794 (= F250), K832 (≠ R289), H834 (= H291)
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
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)
36% identity, 95% coverage: 25:515/515 of query aligns to 572:1089/1093 of Q1LRY0
- F587 (≠ D40) binding
- F598 (≠ Y52) mutation to A: Switches the substrate specificity and enhances the catalytic efficiency of the isovaleryl-CoA mutase over the native isobutyryl-CoA mutase activity about 4000-fold. Is even more susceptible to inactivation than wild-type during turnover.
- R622 (vs. gap) binding
- R728 (≠ S156) binding
- Y772 (≠ N199) binding
- S821 (= S248) binding
- R856 (≠ K284) binding
- K861 (≠ R289) binding
- E973 (= E401) 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)
36% identity, 95% coverage: 25:515/515 of query aligns to 546:1063/1067 of 4xc6A
- active site: F572 (≠ Y52), Y753 (= Y206), H754 (= H207)
- binding cobalamin: F601 (= F80), L606 (≠ Q85), S624 (≠ V102), Q716 (≠ R170), H754 (= H207), E757 (= E210), A758 (= A211), G842 (= G296), R843 (≠ S297), E879 (= E333), A880 (= A334), T882 (≠ S336), H967 (≠ E421)
- binding guanosine-5'-diphosphate: E947 (= E401)
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
>CA265_RS25460 FitnessBrowser__Pedo557:CA265_RS25460
MSEKKHTTTSGIEIKALYTKAKPMEELPGEFPFTRGIQKDMYRGRLWTMRQYAGFSTAEE
SNKRYHYLLAQGTTGLSVAFDLPTQIGYDSDHEMADGEVGKVGVAIDSLKDIEILFDGIQ
LKDITTSMTINATASILLAMYIALAKKQGADLKQISGTIQNDILKEYAARGTYIYPPKQS
MRLITDIFEFCSKEVPKWNTISISGYHIREAGSTAVQELAFTLANGKTYLKAALDKGLDI
NVFAKRLSFFFNCHNNFFEEIAKFRAARRMWAKITKDLGATDEKAQMLRFHTQTGGSTLT
AQQPLNNVIRVSNQAMAAVLGGTQSLHTNGYDEALSLPTESAAKIALRTQQIIAFESGVT
DTVDPLAGSFFVENLTDEVETAAWAYIDRIDAMGGSVNAIESDYMQNEIAGASYQYQKEI
ESGERISVGVNKFTQEEEGLTEVFNIDDSIRKLQSEKLEILKTTRDNDAVEKALQSLHEA
AKGETNLMPLIIDAVEKYATLGEIADVFRGTFGVY
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