SitesBLAST
Comparing 351619 FitnessBrowser__Btheta:351619 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)
7reqD Methylmalonyl-coa mutase, 2-carboxypropyl-coa inhibitor complex (see paper)
29% identity, 91% coverage: 8:581/633 of query aligns to 8:564/623 of 7reqD
Sites not aligning to the query:
6reqB Methylmalonyl-coa mutase, 3-carboxypropyl-coa inhibitor complex (see paper)
29% identity, 91% coverage: 8:581/633 of query aligns to 4:560/619 of 6reqB
Sites not aligning to the query:
5reqD Methylmalonyl-coa mutase, y89f mutant, substrate complex (see paper)
29% identity, 91% coverage: 8:581/633 of query aligns to 4:560/619 of 5reqD
Sites not aligning to the query:
1e1cB Methylmalonyl-coa mutase h244a mutant (see paper)
29% identity, 91% coverage: 8:581/633 of query aligns to 4:560/619 of 1e1cB
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)
28% identity, 71% coverage: 5:456/633 of query aligns to 29:492/750 of P22033
- Q50 (≠ D27) binding
- I69 (≠ V47) to V: in MMAM; likely benign; dbSNP:rs115923556
- P86 (= P66) 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 (= G67) to E: in MMAM; mut0; dbSNP:rs1554160986
- R93 (= R73) to H: in MMAM; mut0; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918251
- G94 (= G74) to R: in MMAM; mut0; dbSNP:rs727504022; to V: in MMAM; mut- and mut0; dbSNP:rs535411418
- P95 (vs. gap) to R: in MMAM; mut0; dbSNP:rs190834116
- YPTM 96:99 (≠ --TK 75:76) binding
- Y100 (≠ K77) 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 (= W82) to R: in MMAM; mut0; dbSNP:rs121918249
- TIRQY 106:110 (≠ LVRQE 83:87) binding
- R108 (= R85) to C: in MMAM; mut0; dbSNP:rs121918257; to G: in MMAM; mut-; to H: in MMAM; mut0; dbSNP:rs483352778
- Q109 (= Q86) to R: in MMAM; mut0; dbSNP:rs1461110052
- G133 (vs. gap) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253828
- A137 (= A100) to V: in MMAM; mut0; dbSNP:rs941483851
- D139 (= D102) to N: in MMAM; uncertain significance; dbSNP:rs879253829
- L140 (≠ I103) to P: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- A141 (vs. gap) to T: in MMAM; decreased protein expression; dbSNP:rs1554160730
- H143 (≠ N105) to Y: in MMAM; mut0
- G145 (= G107) to S: in MMAM; mut0
- S148 (= S110) to L: in MMAM; mut0; dbSNP:rs1300547552
- D156 (≠ K118) to N: in MMAM; mut-
- G158 (≠ L120) to V: in MMAM; mut0
- G161 (vs. gap) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; to V: in MMAM; decreased protein expression
- F174 (≠ L129) to S: in MMAM; mut0; dbSNP:rs864309733
- M186 (≠ F141) to V: in MMAM; mut-; dbSNP:rs148331800
- T187 (= T143) to S: in MMAM; mut0; dbSNP:rs879253830
- N189 (≠ Q145) to I: in MMAM; mut-; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs200908035; to K: in MMAM; mut-; dbSNP:rs1561959114
- A191 (≠ H147) to E: in MMAM; mut- and mut0; affects proper folding; reduced protein level; decreased methylmalonyl-CoA mutase activity; dbSNP:rs760782399
- A197 (≠ G153) to E: in MMAM; mut0
- G203 (≠ F159) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs778702777
- E205 (≠ K161) natural variant: Missing (in MMAM; mut0; dbSNP:rs879253831)
- G215 (= G171) to C: in MMAM; mut- and mut0; dbSNP:rs121918258; to S: in MMAM; mut0; dbSNP:rs121918258
- TIQ 216:218 (≠ SVN 172:174) binding
- Q218 (≠ N174) to H: in MMAM; mut0 and mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability; dbSNP:rs1446389693
- N219 (≠ Y175) to Y: in MMAM; mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; dbSNP:rs121918256
- R228 (= R184) binding ; to Q: in MMAM; mut0; dbSNP:rs770810987
- T230 (vs. gap) to I: in MMAM; mut-; to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253833
- Y231 (vs. gap) 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 (≠ F207) binding
- S262 (≠ N214) to N: in MMAM; mut0
- H265 (≠ S217) binding ; to Y: in MMAM; mut-
- E276 (= E228) to D: in MMAM; uncertain significance; mut-; dbSNP:rs12175488
- L281 (= L233) to S: in MMAM; mut0; dbSNP:rs796052007
- G284 (= G236) to E: in MMAM; mut0; dbSNP:rs879253835; to R: in MMAM; mut0; dbSNP:rs761477436
- S288 (≠ M240) to P: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1179778233
- G291 (≠ L243) to E: in MMAM; mut0
- Q293 (≠ D245) to P: in MMAM; mut0
- RLS 304:306 (≠ KIK 256:258) binding
- L305 (≠ I257) to S: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554160246
- S306 (≠ K258) to F: in MMAM; mut0; dbSNP:rs1085307929
- W309 (≠ F261) to G: in MMAM; decreased protein expression
- G312 (≠ S264) to V: in MMAM; mut0; dbSNP:rs864309734
- Y316 (≠ F268) 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 (= A276) to T: in MMAM; mut-; dbSNP:rs780387525
- R326 (= R278) to K: in MMAM; uncertain significance; dbSNP:rs758577372
- L328 (= L280) 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 (≠ A308) 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 (≠ K310) natural variant: Missing (in MMAM; mut0)
- L347 (≠ M311) to R: in MMAM; mut0; dbSNP:rs1026703654
- H350 (= H314) to Y: in MMAM; mut0; dbSNP:rs1407914109
- L358 (= L322) to P: in MMAM; mut0
- N366 (= N330) 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 (= R333) 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 (= T334) to P: in MMAM; mut0; dbSNP:rs368790885
- A377 (= A341) to E: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918250
- Q383 (≠ D347) to H: in MMAM; mut0; to P: in MMAM; mut0
- H386 (≠ T350) to N: in MMAM; mut0; dbSNP:rs1554159937; to R: in MMAM; mut0; dbSNP:rs866933356
- T387 (≠ V351) 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 (≠ V352) to H: in MMAM; mut0; dbSNP:rs766010704; to K: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253840
- S389 (≠ P353) natural variant: Missing (in MMAM; mut0)
- I412 (≠ L376) natural variant: Missing (in MMAM; mut0)
- P424 (= P388) to L: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253842
- G426 (≠ A390) 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 (= G391) to D: in MMAM; mut0; dbSNP:rs753288303
- G454 (= G418) to E: in MMAM; mut0
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
- 7:750 natural variant: Missing (in MMAM; mut-)
- 152:750 natural variant: Missing (in MMAM; mut0)
- 228:750 natural variant: Missing (in MMAM; mut0)
- 499 A → T: in dbSNP:rs2229385
- 505 I → T: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- 514 Q → E: in MMAM; uncertain significance; Q → K: in MMAM; decreased protein expression
- 518 L → P: in MMAM; mut0; dbSNP:rs864309738
- 532 R → H: in dbSNP:rs1141321
- 535 A → P: in MMAM; mut0; dbSNP:rs760183775
- 552 A → V: in MMAM; uncertain significance; dbSNP:rs879253845
- 560 C → Y: in MMAM; mut0; dbSNP:rs1238333040
- 566 T → R: in MMAM; mut0
- 573 F → 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
- 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
2xiqA Crystal structure of human methylmalonyl-coa mutase in complex with adenosylcobalamin and malonyl-coa (see paper)
28% identity, 69% coverage: 19:456/633 of query aligns to 7:457/714 of 2xiqA
- active site: Y75 (≠ E87), Y229 (≠ I216), H230 (≠ S217)
- binding cobalamin: Y75 (≠ E87), L105 (≠ I103), H108 (≠ N105), A125 (= A122), R193 (= R184), E233 (≠ N220), G320 (≠ T319), W321 (≠ F320), E357 (≠ K356), G360 (≠ S359), L361 (≠ T360)
- binding malonyl-coenzyme a: Y61 (vs. gap), T63 (= T75), M64 (≠ K76), R68 (≠ N80), T71 (≠ L83), R73 (= R85), Y75 (≠ E87), S150 (≠ N140), T152 (= T143), T181 (≠ S172), R193 (= R184), K220 (≠ F207), H230 (≠ S217), R269 (≠ K256), S271 (≠ K258), F273 (≠ N260), R313 (≠ A312), A314 (≠ V313), H315 (= H314), Q317 (≠ E316), Q348 (≠ D347)
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
8dyjB Crystal structure of human methylmalonyl-coa mutase in complex with adp and cob(ii)alamin (see paper)
28% identity, 69% coverage: 19:456/633 of query aligns to 6:456/708 of 8dyjB
- binding adenosine-5'-diphosphate: Y74 (≠ E87), T151 (= T143), R192 (= R184), Y228 (≠ I216), H229 (≠ S217), F272 (≠ N260), Q316 (≠ E316), N352 (≠ V352), E356 (≠ K356), L360 (≠ T360), P361 (= P361)
- binding cobalamin: F102 (≠ L101), L104 (≠ I103), H107 (≠ N105), A124 (= A122), V191 (≠ T183), R192 (= R184), H229 (≠ S217), E232 (≠ N220), G319 (≠ T319), W320 (≠ F320), E356 (≠ K356), G359 (≠ S359), L360 (≠ T360)
Sites not aligning to the query:
- binding cobalamin: 590, 591, 592, 593, 594, 598, 636, 638, 640, 666, 667, 668, 686, 687, 690
8gjuJ Crystal structure of human methylmalonyl-coa mutase (mmut) in complex with methylmalonic acidemia type a protein (mmaa), coenzyme a, and gdp (see paper)
28% identity, 69% coverage: 19:456/633 of query aligns to 7:457/689 of 8gjuJ
- binding coenzyme a: Y61 (vs. gap), T63 (= T75), R68 (≠ N80), T71 (≠ L83), R73 (= R85), S150 (≠ N140), T152 (= T143), T181 (≠ S172), Q183 (≠ N174), N222 (≠ R209), R269 (≠ K256), S271 (≠ K258), R313 (≠ A312), A314 (≠ V313), H315 (= H314), Q348 (≠ D347)
6oxdA Structure of mycobacterium tuberculosis methylmalonyl-coa mutase with adenosyl cobalamin (see paper)
27% identity, 67% coverage: 35:456/633 of query aligns to 41:481/736 of 6oxdA
- active site: Y100 (≠ E87), Y254 (≠ I216), H255 (≠ S217)
- binding cobalamin: Y100 (≠ E87), L130 (vs. gap), H133 (≠ N105), A150 (= A122), R218 (= R184), E258 (≠ N220), G344 (≠ T319), W345 (≠ F320), E381 (≠ K356), A382 (≠ T357), A384 (≠ S359), L385 (≠ T360)
- binding Itaconyl coenzyme A: Y86 (vs. gap), T88 (= T75), M89 (≠ K76), Q93 (≠ N80), T96 (≠ L83), R98 (= R85), Y100 (≠ E87), S175 (≠ N140), T177 (= T143), T206 (≠ S172), R218 (= R184), H255 (≠ S217), R294 (≠ K256), S296 (≠ K258), F298 (≠ N260), R337 (≠ A312), T338 (≠ V313), H339 (= H314), Q341 (≠ E316), Q372 (≠ D347)
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
1e1cA Methylmalonyl-coa mutase h244a mutant (see paper)
26% identity, 66% coverage: 39:456/633 of query aligns to 37:469/727 of 1e1cA
- active site: Y88 (≠ E87), Y242 (≠ I216), A243 (≠ S217)
- binding cobalamin: Y88 (≠ E87), L118 (vs. gap), H121 (≠ N105), A138 (vs. gap), V205 (≠ T183), R206 (= R184), E246 (≠ N220), G332 (≠ T319), W333 (≠ F320), E369 (≠ K356), A370 (≠ T357), A372 (≠ S359), L373 (≠ T360)
- binding desulfo-coenzyme a: Y74 (vs. gap), M77 (≠ K76), F80 (≠ N79), R81 (≠ N80), T84 (≠ L83), R86 (= R85), S113 (≠ D102), S163 (≠ N140), T165 (= T143), T194 (≠ S172), R282 (≠ K256), S284 (≠ K258), H327 (= H314), Q360 (≠ D347)
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
6reqA Methylmalonyl-coa mutase, 3-carboxypropyl-coa inhibitor complex (see paper)
26% identity, 66% coverage: 39:456/633 of query aligns to 37:469/727 of 6reqA
- active site: Y88 (≠ E87), Y242 (≠ I216), H243 (≠ S217)
- binding 3-carboxypropyl-coenzyme a: Y74 (vs. gap), T76 (= T75), M77 (≠ K76), F80 (≠ N79), R81 (≠ N80), T84 (≠ L83), R86 (= R85), Y88 (≠ E87), S113 (≠ D102), S163 (≠ N140), T165 (= T143), T194 (≠ S172), R206 (= R184), H243 (≠ S217), R282 (≠ K256), S284 (≠ K258), F286 (≠ N260), H327 (= H314), Q329 (≠ E316), Q360 (≠ D347)
- binding cobalamin: Y88 (≠ E87), F116 (vs. gap), L118 (vs. gap), H121 (≠ N105), A138 (vs. gap), R206 (= R184), E246 (≠ N220), G332 (≠ T319), W333 (≠ F320), E369 (≠ K356), A370 (≠ T357), A372 (≠ S359)
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)
26% identity, 66% coverage: 39:456/633 of query aligns to 36:468/726 of 4reqA
- active site: Y87 (≠ E87), Y241 (≠ I216), H242 (≠ S217)
- binding cobalamin: Y87 (≠ E87), L117 (vs. gap), A137 (vs. gap), V204 (≠ T183), R205 (= R184), H242 (≠ S217), E245 (≠ N220), G331 (≠ T319), W332 (≠ F320), E368 (≠ K356), A369 (≠ T357), A371 (≠ S359), L372 (≠ T360)
- binding methylmalonyl-coenzyme a: Y73 (vs. gap), M76 (≠ K76), F79 (≠ N79), R80 (≠ N80), T83 (≠ L83), R85 (= R85), Y87 (≠ E87), S112 (≠ D102), S162 (≠ N140), T164 (= T143), T193 (≠ S172), R205 (= R184), N234 (≠ R209), Y241 (≠ I216), H242 (≠ S217), R281 (≠ K256), S283 (≠ K258), F285 (≠ N260), H326 (= H314), Q328 (≠ E316), Q359 (≠ D347), S360 (= S348)
- binding succinyl-coenzyme a: Y73 (vs. gap), M76 (≠ K76), F79 (≠ N79), R80 (≠ N80), T83 (≠ L83), R85 (= R85), Y87 (≠ E87), S162 (≠ N140), T164 (= T143), T193 (≠ S172), Q195 (≠ N174), R205 (= R184), N234 (≠ R209), Y241 (≠ I216), H242 (≠ S217), R281 (≠ K256), S283 (≠ K258), F285 (≠ N260), R324 (≠ A312), H326 (= H314), Q359 (≠ D347)
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
P11653 Methylmalonyl-CoA mutase large subunit; MCM-alpha; EC 5.4.99.2 from Propionibacterium freudenreichii subsp. shermanii (see 4 papers)
26% identity, 66% coverage: 39:456/633 of query aligns to 38:470/728 of P11653
- Y75 (vs. gap) binding
- M78 (≠ K76) binding
- R82 (≠ N80) binding
- T85 (≠ L83) binding
- R87 (= R85) binding
- Y89 (≠ E87) binding ; mutation to F: Does not significantly affect affinity for succiny-CoA, but kcat is lowered about 580-fold.
- S114 (≠ D102) binding
- F117 (vs. gap) binding
- A139 (vs. gap) binding
- T195 (≠ S172) binding
- Q197 (≠ N174) binding
- V206 (≠ T183) binding
- R207 (= R184) binding ; binding
- H244 (≠ S217) binding
- R283 (≠ K256) binding
- S285 (≠ K258) binding
- G333 (≠ T319) binding
- E370 (≠ K356) binding
- A373 (≠ S359) 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
7reqA Methylmalonyl-coa mutase, 2-carboxypropyl-coa inhibitor complex (see paper)
26% identity, 66% coverage: 39:456/633 of query aligns to 35:467/725 of 7reqA
- active site: Y86 (≠ E87), Y240 (≠ I216), H241 (≠ S217)
- binding 2-carboxypropyl-coenzyme a: Y72 (vs. gap), T74 (= T75), M75 (≠ K76), F78 (≠ N79), R79 (≠ N80), T82 (≠ L83), R84 (= R85), Y86 (≠ E87), S161 (≠ N140), T163 (= T143), T192 (≠ S172), R204 (= R184), H241 (≠ S217), R280 (≠ K256), S282 (≠ K258), F284 (≠ N260), H325 (= H314), Q358 (≠ D347)
- binding cobalamin: Y86 (≠ E87), L116 (vs. gap), A136 (vs. gap), R204 (= R184), E244 (≠ N220), G330 (≠ T319), W331 (≠ F320), E367 (≠ K356), A368 (≠ T357), A370 (≠ S359)
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)
26% identity, 66% coverage: 39:456/633 of query aligns to 35:467/725 of 3reqA
- active site: Y86 (≠ E87), Y240 (≠ I216), H241 (≠ S217)
- binding adenosine: Y86 (≠ E87), Y240 (≠ I216), E244 (≠ N220), G330 (≠ T319)
- binding cobalamin: L116 (vs. gap), V203 (≠ T183), R204 (= R184), E244 (≠ N220), G330 (≠ T319), W331 (≠ F320), A368 (≠ T357)
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)
26% identity, 66% coverage: 39:456/633 of query aligns to 35:467/725 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)
26% identity, 66% coverage: 39:456/633 of query aligns to 35:467/725 of 5reqA
- active site: F86 (≠ E87), Y240 (≠ I216), H241 (≠ S217)
- binding cobalamin: L116 (vs. gap), A136 (vs. gap), R204 (= R184), H241 (≠ S217), E244 (≠ N220), G330 (≠ T319), W331 (≠ F320), E367 (≠ K356), A368 (≠ T357), A370 (≠ S359)
- binding methylmalonyl(carbadethia)-coenzyme a: Y72 (vs. gap), T74 (= T75), M75 (≠ K76), R79 (≠ N80), T82 (≠ L83), R84 (= R85), F86 (≠ E87), S111 (≠ D102), S161 (≠ N140), T163 (= T143), T192 (≠ S172), Q194 (≠ N174), R204 (= R184), N233 (≠ R209), H241 (≠ S217), R280 (≠ K256), S282 (≠ K258), F284 (≠ N260), T324 (≠ V313), H325 (= H314), Q358 (≠ D347), S359 (= S348)
- binding succinyl(carbadethia)-coenzyme a: Y72 (vs. gap), T74 (= T75), M75 (≠ K76), R79 (≠ N80), T82 (≠ L83), R84 (= R85), F86 (≠ E87), S161 (≠ N140), T163 (= T143), T192 (≠ S172), R204 (= R184), N233 (≠ R209), H241 (≠ S217), R280 (≠ K256), S282 (≠ K258), F284 (≠ N260), H325 (= H314), Q358 (≠ D347)
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
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)
26% identity, 69% coverage: 23:456/633 of query aligns to 23:472/562 of I3VE77
- YPTM 76:79 (≠ --TK 75:76) binding
- TMR 86:88 (≠ LVR 83:85) binding
- I90 (≠ E87) 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 (≠ H114) 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 (≠ SVN 172:174) binding
- R235 (≠ F207) binding
- N240 (= N212) binding
- H245 (≠ S217) binding
- R284 (≠ K256) binding
4r3uA Crystal structure of 2-hydroxyisobutyryl-coa mutase (see paper)
26% identity, 69% coverage: 23:456/633 of query aligns to 22:471/557 of 4r3uA
- active site: I89 (≠ E87), Y243 (≠ I216), H244 (≠ S217)
- binding 3-hydroxybutanoyl-coenzyme a: Y75 (vs. gap), T77 (= T75), M78 (≠ K76), R82 (≠ N80), T85 (≠ L83), R87 (= R85), I89 (≠ E87), D116 (≠ H114), S164 (≠ N140), T166 (≠ S142), T195 (≠ S172), Q197 (≠ N174), R234 (≠ F207), N236 (≠ R209), N239 (= N212), Y243 (≠ I216), H244 (≠ S217), R283 (≠ K256), F287 (≠ N260), R327 (≠ A312), F328 (≠ V313), H329 (= H314), Q331 (≠ E316), Q362 (≠ D347)
- 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 (vs. gap), T77 (= T75), M78 (≠ K76), R82 (≠ N80), T85 (≠ L83), R87 (= R85), I89 (≠ E87), D116 (≠ H114), S164 (≠ N140), T166 (≠ S142), T195 (≠ S172), Q197 (≠ N174), R234 (≠ F207), N236 (≠ R209), N239 (= N212), H244 (≠ S217), R283 (≠ K256), F287 (≠ N260), R327 (≠ A312), F328 (≠ V313), H329 (= H314), Q331 (≠ E316), Q362 (≠ D347)
- binding cobalamin: D116 (≠ H114), M119 (≠ A117), E139 (vs. gap), Q207 (≠ R184), E209 (≠ K186), E247 (≠ N220), A334 (≠ T319), E371 (≠ K356), A372 (≠ T357), A374 (≠ S359)
5cjtA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isobutyryl-coenzyme a (see paper)
26% identity, 42% coverage: 207:470/633 of query aligns to 742:987/1062 of 5cjtA
- active site: Y750 (≠ I216), H751 (≠ S217)
- binding cobalamin: H751 (≠ S217), E754 (≠ N220), A755 (= A221), G839 (≠ T319), R840 (≠ F320), E876 (≠ K356), A877 (≠ T357), T879 (≠ S359), H964 (≠ A444)
- binding isobutyryl-coenzyme a: Y743 (= Y208), Y750 (≠ I216), H751 (≠ S217), S792 (≠ K258), F794 (≠ N260), R827 (≠ E304), K832 (≠ A312), H834 (= H314)
- binding guanosine-5'-diphosphate: E944 (≠ K424)
Sites not aligning to the query:
- active site: 6, 569
- binding cobalamin: 18, 19, 20, 21, 22, 26, 66, 67, 94, 96, 98, 116, 117, 598, 603, 621, 713
- binding isobutyryl-coenzyme a: 556, 558, 560, 567, 569, 593, 648, 650, 699, 701, 703
- 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
>351619 FitnessBrowser__Btheta:351619
MADKKEKLFSDFSPVSTEQWMEKVTADLKGADFEKKLVWKTNEGFKVKPFYRMEDLEGLK
TTDALPGEFPYLRGTKKSNNEWLVRQEIKVECPKEANAKALDILNKGVDSLSFHVKAKEL
NAEYIETLLNGIQAECVELNFSTCQGHVVELAGLLVAYFQKKDYDVKKLRGSVNYDFFNK
MLTRGKEKGDMVQTAKALIEAIQPLPFYRVLNVNAISLNNAGAYISQELGYALAWGNEYM
NQLTDAGIPAATVAKKIKFNFGISSNYFLEIAKFRAARMLWANIVASYHPECLRDCDNKG
ANGECRCAAKMAVHAETSTFNLTLFDAHVNLLRTQTEAMSAALAGVDSMTVVPFDKTYST
PDEFSERLARNQQLLLKEESHFDKVIDPAAGSYYIENLTVSIAKQAWELFLAVEEAGGFY
AALKAGTVQAAVNESNKARHKAVAQRREVLLGTNQFPNFNEKAGEKQPIEAKCCCGGDAH
TCEKDVDTLVFDRAASEFEALRLETEASGKRPKAFMLTIGNLAMRQARAQYSCNFLACAG
YEVIDNLGFETVEAGVEAAMAAKADIVVLCSSDDEYAEYAVPAFKALDGRAMFIVAGAPA
CMDELKAAGIENFIHVRVNVLDTLKEFNAKLLK
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