SitesBLAST
Comparing Ac3H11_2278 FitnessBrowser__acidovorax_3H11:Ac3H11_2278 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)
65% identity, 97% coverage: 20:721/722 of query aligns to 43:743/750 of P22033
- Q50 (≠ S27) binding
- I69 (≠ V46) to V: in MMAM; likely benign; dbSNP:rs115923556
- P86 (= P65) 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 (= G66) to E: in MMAM; mut0; dbSNP:rs1554160986
- R93 (= R72) to H: in MMAM; mut0; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918251
- G94 (= G73) to R: in MMAM; mut0; dbSNP:rs727504022; to V: in MMAM; mut- and mut0; dbSNP:rs535411418
- P95 (= P74) to R: in MMAM; mut0; dbSNP:rs190834116
- YPTM 96:99 (≠ QATM 75:78) binding
- Y100 (= Y79) 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 (= W84) to R: in MMAM; mut0; dbSNP:rs121918249
- TIRQY 106:110 (= TIRQY 85:89) binding
- R108 (= R87) to C: in MMAM; mut0; dbSNP:rs121918257; to G: in MMAM; mut-; to H: in MMAM; mut0; dbSNP:rs483352778
- Q109 (= Q88) to R: in MMAM; mut0; dbSNP:rs1461110052
- G133 (= G112) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253828
- A137 (= A116) to V: in MMAM; mut0; dbSNP:rs941483851
- D139 (= D118) to N: in MMAM; uncertain significance; dbSNP:rs879253829
- L140 (= L119) to P: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- A141 (= A120) to T: in MMAM; decreased protein expression; dbSNP:rs1554160730
- H143 (= H122) to Y: in MMAM; mut0
- G145 (= G124) to S: in MMAM; mut0
- S148 (= S127) to L: in MMAM; mut0; dbSNP:rs1300547552
- D156 (= D135) to N: in MMAM; mut-
- G158 (= G137) to V: in MMAM; mut0
- G161 (= G140) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; to V: in MMAM; decreased protein expression
- F174 (= F153) to S: in MMAM; mut0; dbSNP:rs864309733
- M186 (= M165) to V: in MMAM; mut-; dbSNP:rs148331800
- T187 (= T166) to S: in MMAM; mut0; dbSNP:rs879253830
- N189 (= N168) to I: in MMAM; mut-; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs200908035; to K: in MMAM; mut-; dbSNP:rs1561959114
- A191 (= A170) to E: in MMAM; mut- and mut0; affects proper folding; reduced protein level; decreased methylmalonyl-CoA mutase activity; dbSNP:rs760782399
- A197 (= A176) to E: in MMAM; mut0
- G203 (≠ A182) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs778702777
- E205 (= E184) natural variant: Missing (in MMAM; mut0; dbSNP:rs879253831)
- G215 (= G194) to C: in MMAM; mut- and mut0; dbSNP:rs121918258; to S: in MMAM; mut0; dbSNP:rs121918258
- TIQ 216:218 (= TIQ 195:197) binding
- Q218 (= Q197) to H: in MMAM; mut0 and mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability; dbSNP:rs1446389693
- N219 (= N198) to Y: in MMAM; mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; dbSNP:rs121918256
- R228 (= R207) binding ; to Q: in MMAM; mut0; dbSNP:rs770810987
- T230 (= T209) to I: in MMAM; mut-; to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253833
- Y231 (= Y210) 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 (= K234) binding
- S262 (= S241) to N: in MMAM; mut0
- H265 (= H244) binding ; to Y: in MMAM; mut-
- E276 (= E255) to D: in MMAM; uncertain significance; mut-; dbSNP:rs12175488
- L281 (= L260) to S: in MMAM; mut0; dbSNP:rs796052007
- G284 (= G263) to E: in MMAM; mut0; dbSNP:rs879253835; to R: in MMAM; mut0; dbSNP:rs761477436
- S288 (≠ V267) to P: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1179778233
- G291 (≠ A270) to E: in MMAM; mut0
- Q293 (≠ A272) to P: in MMAM; mut0
- RLS 304:306 (= RLS 283:285) binding
- L305 (= L284) to S: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554160246
- S306 (= S285) to F: in MMAM; mut0; dbSNP:rs1085307929
- W309 (= W288) to G: in MMAM; decreased protein expression
- G312 (= G291) to V: in MMAM; mut0; dbSNP:rs864309734
- Y316 (= Y295) 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 (= A303) to T: in MMAM; mut-; dbSNP:rs780387525
- R326 (= R305) to K: in MMAM; uncertain significance; dbSNP:rs758577372
- L328 (= L307) 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 (= S322) 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 (≠ M324) natural variant: Missing (in MMAM; mut0)
- L347 (= L325) to R: in MMAM; mut0; dbSNP:rs1026703654
- H350 (= H328) to Y: in MMAM; mut0; dbSNP:rs1407914109
- L358 (= L336) to P: in MMAM; mut0
- N366 (= N344) 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 (= R347) 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 (= T348) to P: in MMAM; mut0; dbSNP:rs368790885
- A377 (= A355) to E: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918250
- Q383 (= Q361) to H: in MMAM; mut0; to P: in MMAM; mut0
- H386 (= H364) to N: in MMAM; mut0; dbSNP:rs1554159937; to R: in MMAM; mut0; dbSNP:rs866933356
- T387 (= T365) 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 (= N366) to H: in MMAM; mut0; dbSNP:rs766010704; to K: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253840
- S389 (≠ A367) natural variant: Missing (in MMAM; mut0)
- I412 (= I390) natural variant: Missing (in MMAM; mut0)
- P424 (= P402) to L: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253842
- G426 (≠ A404) 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 (= G405) to D: in MMAM; mut0; dbSNP:rs753288303
- G454 (= G432) to E: in MMAM; mut0
- A499 (≠ P477) to T: in dbSNP:rs2229385
- I505 (= I483) to T: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- Q514 (= Q492) to E: in MMAM; uncertain significance; to K: in MMAM; decreased protein expression
- L518 (= L496) to P: in MMAM; mut0; dbSNP:rs864309738
- R532 (≠ A510) to H: in dbSNP:rs1141321
- A535 (≠ D513) to P: in MMAM; mut0; dbSNP:rs760183775
- A552 (≠ S530) to V: in MMAM; uncertain significance; dbSNP:rs879253845
- C560 (≠ A538) to Y: in MMAM; mut0; dbSNP:rs1238333040
- T566 (≠ S544) to R: in MMAM; mut0
- F573 (= F551) 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 (= Y565) to C: in MMAM; mut-
- I597 (≠ W575) to R: in MMAM; no changed in protein expression; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554158951
- P615 (= P593) 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 (= R594) to C: in MMAM; mut0; dbSNP:rs765284825
- L617 (≠ V595) to R: in MMAM; mut0; dbSNP:rs1554158775
- K621 (= K599) to N: in MMAM; mut0
- G623 (= G601) to R: in MMAM; mut0; dbSNP:rs121918254
- Q624 (= Q602) to R: in MMAM; no effect on protein abundance; dbSNP:rs768521956
- D625 (= D603) 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 (= G604) to C: in MMAM; mut-; dbSNP:rs982110849
- H627 (= H605) binding axial binding residue; to R: in MMAM; mut0; dbSNP:rs372486357
- G630 (= G608) to E: in MMAM; mut0; dbSNP:rs143023066
- V633 (= V611) 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 (≠ A615) to E: in MMAM; mut-; to R: in MMAM; mut0; dbSNP:rs781501004
- F638 (= F616) to I: in MMAM; mut0
- D640 (= D618) to Y: in MMAM; mut0; dbSNP:rs865815395
- G642 (= G620) to R: in MMAM; mut-; dbSNP:rs747897332
- G648 (= G626) 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 (= V647) to E: in MMAM; mut0; dbSNP:rs1360470463
- I671 (≠ V649) to V: in dbSNP:rs8589
- L674 (= L652) to F: in MMAM; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1164271240
- H678 (= H656) to R: in MMAM; mut-; dbSNP:rs147094927
- E684 (≠ A662) natural variant: E -> EL (in MMAM; mut-)
- L685 (≠ I663) to R: in MMAM; mut-; dbSNP:rs864309739
- R694 (≠ A672) 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 (≠ F678) 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 (= G681) to R: in MMAM; mut0; dbSNP:rs121918255
- G717 (= G695) 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 (= G701) 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-)
- 152:750 natural variant: Missing (in MMAM; mut0)
- 228:750 natural variant: Missing (in MMAM; mut0)
2xiqA Crystal structure of human methylmalonyl-coa mutase in complex with adenosylcobalamin and malonyl-coa (see paper)
65% identity, 97% coverage: 20:721/722 of query aligns to 8:708/714 of 2xiqA
- active site: Y75 (= Y89), Y229 (= Y243), H230 (= H244), K586 (= K599), D590 (= D603), H592 (= H605)
- binding cobalamin: Y75 (= Y89), L105 (= L119), H108 (= H122), A125 (= A139), R193 (= R207), E233 (= E247), G320 (= G333), W321 (= W334), E357 (= E370), G360 (≠ A373), L361 (= L374), G591 (= G604), H592 (= H605), D593 (= D606), R594 (= R607), G595 (= G608), I599 (≠ V612), G635 (= G648), S637 (= S650), L639 (= L652), A641 (= A654), G667 (= G680), G668 (= G681), F687 (≠ Y700), G688 (= G701), T691 (= T704)
- binding malonyl-coenzyme a: Y61 (≠ Q75), T63 (= T77), M64 (= M78), R68 (= R82), T71 (= T85), R73 (= R87), Y75 (= Y89), S150 (= S164), T152 (= T166), T181 (= T195), R193 (= R207), K220 (= K234), H230 (= H244), R269 (= R283), S271 (= S285), F273 (= F287), R313 (= R326), A314 (≠ T327), H315 (= H328), Q317 (= Q330), Q348 (= Q361)
8dyjB Crystal structure of human methylmalonyl-coa mutase in complex with adp and cob(ii)alamin (see paper)
65% identity, 97% coverage: 20:721/722 of query aligns to 7:707/708 of 8dyjB
- binding adenosine-5'-diphosphate: Y74 (= Y89), T151 (= T166), R192 (= R207), Y228 (= Y243), H229 (= H244), F272 (= F287), Q316 (= Q330), N352 (= N366), E356 (= E370), L360 (= L374), P361 (= P375)
- binding cobalamin: F102 (= F117), L104 (= L119), H107 (= H122), A124 (= A139), V191 (= V206), R192 (= R207), H229 (= H244), E232 (= E247), G319 (= G333), W320 (= W334), E356 (= E370), G359 (≠ A373), L360 (= L374), G590 (= G604), H591 (= H605), D592 (= D606), R593 (= R607), G594 (= G608), I598 (≠ V612), S636 (= S650), L638 (= L652), A640 (= A654), G666 (= G680), G667 (= G681), V668 (= V682), F686 (≠ Y700), G687 (= G701), T690 (= T704)
8gjuJ Crystal structure of human methylmalonyl-coa mutase (mmut) in complex with methylmalonic acidemia type a protein (mmaa), coenzyme a, and gdp (see paper)
64% identity, 97% coverage: 20:721/722 of query aligns to 8:685/689 of 8gjuJ
- binding coenzyme a: Y61 (≠ Q75), T63 (= T77), R68 (= R82), T71 (= T85), R73 (= R87), S150 (= S164), T152 (= T166), T181 (= T195), Q183 (= Q197), N222 (= N236), R269 (= R283), S271 (= S285), R313 (= R326), A314 (≠ T327), H315 (= H328), Q348 (= Q361)
7reqA Methylmalonyl-coa mutase, 2-carboxypropyl-coa inhibitor complex (see paper)
61% identity, 95% coverage: 38:721/722 of query aligns to 35:723/725 of 7reqA
- active site: Y86 (= Y89), Y240 (= Y243), H241 (= H244), K601 (= K599), D605 (= D603), H607 (= H605)
- binding 2-carboxypropyl-coenzyme a: Y72 (≠ Q75), T74 (= T77), M75 (= M78), F78 (≠ V81), R79 (= R82), T82 (= T85), R84 (= R87), Y86 (= Y89), S161 (= S164), T163 (= T166), T192 (= T195), R204 (= R207), H241 (= H244), R280 (= R283), S282 (= S285), F284 (= F287), H325 (= H328), Q358 (= Q361)
- binding cobalamin: Y86 (= Y89), L116 (= L119), A136 (= A139), R204 (= R207), E244 (= E247), G330 (= G333), W331 (= W334), E367 (= E370), A368 (= A371), A370 (= A373), G606 (= G604), H607 (= H605), D608 (= D606), R609 (= R607), G610 (= G608), I614 (≠ V612), S652 (= S650), L654 (= L652), G682 (= G680), G683 (= G681), Y702 (= Y700), T703 (≠ G701), T706 (= T704)
3reqA Methylmalonyl-coa mutase, substrate-free state (poor quality structure) (see paper)
61% identity, 95% coverage: 38:721/722 of query aligns to 35:723/725 of 3reqA
- active site: Y86 (= Y89), Y240 (= Y243), H241 (= H244), K601 (= K599), D605 (= D603), H607 (= H605)
- binding adenosine: Y86 (= Y89), Y240 (= Y243), E244 (= E247), G330 (= G333)
- binding cobalamin: L116 (= L119), V203 (= V206), R204 (= R207), E244 (= E247), G330 (= G333), W331 (= W334), A368 (= A371), G606 (= G604), H607 (= H605), D608 (= D606), R609 (= R607), G610 (= G608), I614 (≠ V612), G650 (= G648), S652 (= S650), L654 (= L652), G682 (= G680), G683 (= G681), Y702 (= Y700), T703 (≠ G701), P704 (= P702), T706 (= T704)
2reqA Methylmalonyl-coa mutase, non-productive coa complex, in open conformation representing substrate-free state (see paper)
61% identity, 95% coverage: 38:721/722 of query aligns to 35:723/725 of 2reqA
- active site: Y86 (= Y89), Y240 (= Y243), H241 (= H244), K601 (= K599), D605 (= D603), H607 (= H605)
- binding cobalamin: V203 (= V206), R204 (= R207), E244 (= E247), A245 (= A248), W331 (= W334), A368 (= A371), G606 (= G604), H607 (= H605), D608 (= D606), R609 (= R607), G610 (= G608), I614 (≠ V612), G650 (= G648), S652 (= S650), L654 (= L652), A655 (= A653), G682 (= G680), G683 (= G681), Y702 (= Y700), T703 (≠ G701), T706 (= T704)
- binding coenzyme a: Y72 (≠ Q75), R79 (= R82), K318 (= K321)
P11653 Methylmalonyl-CoA mutase large subunit; MCM-alpha; EC 5.4.99.2 from Propionibacterium freudenreichii subsp. shermanii (see 4 papers)
61% identity, 95% coverage: 38:721/722 of query aligns to 38:726/728 of P11653
- Y75 (≠ Q75) binding
- M78 (= M78) binding
- R82 (= R82) binding
- T85 (= T85) binding
- R87 (= R87) binding
- Y89 (= Y89) binding ; mutation to F: Does not significantly affect affinity for succiny-CoA, but kcat is lowered about 580-fold.
- S114 (= S114) binding
- F117 (= F117) binding
- A139 (= A139) binding
- T195 (= T195) binding
- Q197 (= Q197) binding
- V206 (= V206) binding
- R207 (= R207) binding ; binding
- H244 (= H244) binding
- R283 (= R283) binding
- S285 (= S285) binding
- G333 (= G333) binding
- E370 (= E370) binding
- A373 (= A373) binding
- G609 (= G604) binding
- H610 (= H605) binding axial binding residue
- D611 (= D606) binding
- R612 (= R607) binding
- S655 (= S650) binding
- L657 (= L652) binding
- G686 (= G681) binding
- T709 (= T704) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
4reqA Methylmalonyl-coa mutase substrate complex (see paper)
61% identity, 95% coverage: 38:721/722 of query aligns to 36:724/726 of 4reqA
- active site: Y87 (= Y89), Y241 (= Y243), H242 (= H244), K602 (= K599), D606 (= D603), H608 (= H605)
- binding cobalamin: Y87 (= Y89), L117 (= L119), A137 (= A139), V204 (= V206), R205 (= R207), H242 (= H244), E245 (= E247), G331 (= G333), W332 (= W334), E368 (= E370), A369 (= A371), A371 (= A373), L372 (= L374), G607 (= G604), H608 (= H605), D609 (= D606), R610 (= R607), G611 (= G608), I615 (≠ V612), S653 (= S650), L655 (= L652), G683 (= G680), G684 (= G681), V685 (= V682), Y703 (= Y700), T704 (≠ G701), T707 (= T704)
- binding methylmalonyl-coenzyme a: Y73 (≠ Q75), M76 (= M78), F79 (≠ V81), R80 (= R82), T83 (= T85), R85 (= R87), Y87 (= Y89), S112 (= S114), S162 (= S164), T164 (= T166), T193 (= T195), R205 (= R207), N234 (= N236), Y241 (= Y243), H242 (= H244), R281 (= R283), S283 (= S285), F285 (= F287), H326 (= H328), Q328 (= Q330), Q359 (= Q361), S360 (= S362)
- binding succinyl-coenzyme a: Y73 (≠ Q75), M76 (= M78), F79 (≠ V81), R80 (= R82), T83 (= T85), R85 (= R87), Y87 (= Y89), S162 (= S164), T164 (= T166), T193 (= T195), Q195 (= Q197), R205 (= R207), N234 (= N236), Y241 (= Y243), H242 (= H244), R281 (= R283), S283 (= S285), F285 (= F287), R324 (= R326), H326 (= H328), Q359 (= Q361)
6reqA Methylmalonyl-coa mutase, 3-carboxypropyl-coa inhibitor complex (see paper)
61% identity, 95% coverage: 38:721/722 of query aligns to 37:725/727 of 6reqA
- active site: Y88 (= Y89), Y242 (= Y243), H243 (= H244), K603 (= K599), D607 (= D603), H609 (= H605)
- binding 3-carboxypropyl-coenzyme a: Y74 (≠ Q75), T76 (= T77), M77 (= M78), F80 (≠ V81), R81 (= R82), T84 (= T85), R86 (= R87), Y88 (= Y89), S113 (= S114), S163 (= S164), T165 (= T166), T194 (= T195), R206 (= R207), H243 (= H244), R282 (= R283), S284 (= S285), F286 (= F287), H327 (= H328), Q329 (= Q330), Q360 (= Q361)
- binding cobalamin: Y88 (= Y89), F116 (= F117), L118 (= L119), H121 (= H122), A138 (= A139), R206 (= R207), E246 (= E247), G332 (= G333), W333 (= W334), E369 (= E370), A370 (= A371), A372 (= A373), G608 (= G604), H609 (= H605), D610 (= D606), R611 (= R607), G612 (= G608), I616 (≠ V612), Y620 (≠ F616), S654 (= S650), L656 (= L652), G658 (≠ A654), G684 (= G680), G685 (= G681), Y704 (= Y700), T705 (≠ G701), T708 (= T704)
5reqA Methylmalonyl-coa mutase, y89f mutant, substrate complex (see paper)
61% identity, 95% coverage: 38:721/722 of query aligns to 35:723/725 of 5reqA
- active site: F86 (≠ Y89), Y240 (= Y243), H241 (= H244), K601 (= K599), D605 (= D603), H607 (= H605)
- binding cobalamin: L116 (= L119), A136 (= A139), R204 (= R207), H241 (= H244), E244 (= E247), G330 (= G333), W331 (= W334), E367 (= E370), A368 (= A371), A370 (= A373), G606 (= G604), H607 (= H605), D608 (= D606), R609 (= R607), G610 (= G608), I614 (≠ V612), S652 (= S650), L654 (= L652), G682 (= G680), G683 (= G681), V684 (= V682), Y702 (= Y700), T703 (≠ G701), T706 (= T704)
- binding methylmalonyl(carbadethia)-coenzyme a: Y72 (≠ Q75), T74 (= T77), M75 (= M78), R79 (= R82), T82 (= T85), R84 (= R87), F86 (≠ Y89), S111 (= S114), S161 (= S164), T163 (= T166), T192 (= T195), Q194 (= Q197), R204 (= R207), N233 (= N236), H241 (= H244), R280 (= R283), S282 (= S285), F284 (= F287), T324 (= T327), H325 (= H328), Q358 (= Q361), S359 (= S362)
- binding succinyl(carbadethia)-coenzyme a: Y72 (≠ Q75), T74 (= T77), M75 (= M78), R79 (= R82), T82 (= T85), R84 (= R87), F86 (≠ Y89), S161 (= S164), T163 (= T166), T192 (= T195), R204 (= R207), N233 (= N236), H241 (= H244), R280 (= R283), S282 (= S285), F284 (= F287), H325 (= H328), Q358 (= Q361)
1e1cA Methylmalonyl-coa mutase h244a mutant (see paper)
61% identity, 95% coverage: 38:721/722 of query aligns to 37:725/727 of 1e1cA
- active site: Y88 (= Y89), Y242 (= Y243), A243 (≠ H244), K603 (= K599), D607 (= D603), H609 (= H605)
- binding cobalamin: Y88 (= Y89), L118 (= L119), H121 (= H122), A138 (= A139), V205 (= V206), R206 (= R207), E246 (= E247), G332 (= G333), W333 (= W334), E369 (= E370), A370 (= A371), A372 (= A373), L373 (= L374), G608 (= G604), H609 (= H605), D610 (= D606), R611 (= R607), G612 (= G608), I616 (≠ V612), Y620 (≠ F616), S654 (= S650), L656 (= L652), G684 (= G680), G685 (= G681), V686 (= V682), Y704 (= Y700), T705 (≠ G701), T708 (= T704), S713 (= S709)
- binding desulfo-coenzyme a: Y74 (≠ Q75), M77 (= M78), F80 (≠ V81), R81 (= R82), T84 (= T85), R86 (= R87), S113 (= S114), S163 (= S164), T165 (= T166), T194 (= T195), R282 (= R283), S284 (= S285), H327 (= H328), Q360 (= Q361)
6oxdA Structure of mycobacterium tuberculosis methylmalonyl-coa mutase with adenosyl cobalamin (see paper)
62% identity, 94% coverage: 36:717/722 of query aligns to 43:728/736 of 6oxdA
- active site: Y100 (= Y89), Y254 (= Y243), H255 (= H244), K610 (= K599), D614 (= D603), H616 (= H605)
- binding cobalamin: Y100 (= Y89), L130 (= L119), H133 (= H122), A150 (= A139), R218 (= R207), E258 (= E247), G344 (= G333), W345 (= W334), E381 (= E370), A382 (= A371), A384 (= A373), L385 (= L374), G615 (= G604), H616 (= H605), D617 (= D606), R618 (= R607), S661 (= S650), L663 (= L652), A665 (= A654), G691 (= G680), G692 (= G681), F711 (≠ Y700), P712 (≠ G701), T715 (= T704)
- binding Itaconyl coenzyme A: Y86 (≠ Q75), T88 (= T77), M89 (= M78), Q93 (≠ R82), T96 (= T85), R98 (= R87), Y100 (= Y89), S175 (= S164), T177 (= T166), T206 (= T195), R218 (= R207), H255 (= H244), R294 (= R283), S296 (= S285), F298 (= F287), R337 (= R326), T338 (= T327), H339 (= H328), Q341 (= Q330), Q372 (= Q361)
4r3uA Crystal structure of 2-hydroxyisobutyryl-coa mutase (see paper)
46% identity, 71% coverage: 46:555/722 of query aligns to 45:556/557 of 4r3uA
- active site: I89 (≠ Y89), Y243 (= Y243), H244 (= H244)
- binding 3-hydroxybutanoyl-coenzyme a: Y75 (≠ Q75), T77 (= T77), M78 (= M78), R82 (= R82), T85 (= T85), R87 (= R87), I89 (≠ Y89), D116 (≠ A116), S164 (= S164), T166 (= T166), T195 (= T195), Q197 (= Q197), R234 (≠ K234), N236 (= N236), N239 (≠ S239), Y243 (= Y243), H244 (= H244), R283 (= R283), F287 (= F287), R327 (= R326), F328 (≠ T327), H329 (= H328), Q331 (= Q330), Q362 (= Q361)
- 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 (≠ Q75), T77 (= T77), M78 (= M78), R82 (= R82), T85 (= T85), R87 (= R87), I89 (≠ Y89), D116 (≠ A116), S164 (= S164), T166 (= T166), T195 (= T195), Q197 (= Q197), R234 (≠ K234), N236 (= N236), N239 (≠ S239), H244 (= H244), R283 (= R283), F287 (= F287), R327 (= R326), F328 (≠ T327), H329 (= H328), Q331 (= Q330), Q362 (= Q361)
- binding cobalamin: D116 (≠ A116), M119 (≠ L119), E139 (≠ A139), Q207 (≠ R207), E209 (≠ T209), E247 (= E247), A334 (≠ G333), E371 (= E370), A372 (= A371), A374 (= A373)
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)
46% identity, 71% coverage: 46:555/722 of query aligns to 46:557/562 of I3VE77
- YPTM 76:79 (≠ QATM 75:78) binding
- TMR 86:88 (≠ TIR 85:87) binding
- I90 (≠ Y89) 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 (≠ A116) 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 195:197) binding
- R235 (≠ K234) binding
- N240 (≠ S239) binding
- H245 (= H244) binding
- R284 (= R283) binding
Q5KUG0 Fused isobutyryl-CoA mutase; EC 5.4.99.13; EC 3.6.5.- from Geobacillus kaustophilus (strain HTA426) (see paper)
34% identity, 69% coverage: 60:557/722 of query aligns to 561:1085/1086 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)
34% identity, 69% coverage: 63:557/722 of query aligns to 544:1061/1062 of 5cjtA
- active site: F569 (≠ Y89), Y750 (= Y243), H751 (= H244)
- binding cobalamin: F598 (= F117), L603 (≠ H122), S621 (≠ A139), Q713 (≠ R207), H751 (= H244), E754 (= E247), A755 (= A248), G839 (= G333), R840 (≠ W334), E876 (= E370), A877 (= A371), T879 (≠ A373), H964 (≠ D458)
- binding isobutyryl-coenzyme a: F556 (≠ Q75), F558 (≠ T77), R560 (≠ Y79), R567 (= R87), F569 (≠ Y89), R593 (≠ G112), S648 (= S164), T650 (= T166), R699 (≠ S193), T701 (= T195), Q703 (= Q197), Y743 (≠ N236), Y750 (= Y243), H751 (= H244), S792 (= S285), F794 (= F287), R827 (≠ K321), K832 (≠ R326), H834 (= H328)
- binding guanosine-5'-diphosphate: E944 (≠ D438)
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
5cjwA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate pivalyl-coenzyme a (see paper)
34% identity, 69% coverage: 63:557/722 of query aligns to 546:1062/1063 of 5cjwA
- active site: F571 (≠ Y89), Y752 (= Y243), H753 (= H244)
- binding pivalyl-coenzyme A: F558 (≠ Q75), F560 (≠ T77), R562 (≠ Y79), R569 (= R87), F571 (≠ Y89), R595 (≠ G112), S650 (= S164), T652 (= T166), R701 (≠ S193), T703 (= T195), Q705 (= Q197), Y745 (≠ N236), Y752 (= Y243), H753 (= H244), S794 (= S285), F796 (= F287), R829 (≠ K321), K834 (≠ R326), H836 (= H328)
- binding cobalamin: F600 (= F117), L605 (≠ H122), S623 (≠ A139), Q715 (≠ R207), H753 (= H244), E756 (= E247), A757 (= A248), G841 (= G333), R842 (≠ W334), E878 (= E370), A879 (= A371), T881 (≠ A373), H966 (≠ D458)
- binding guanosine-5'-diphosphate: N1062 (≠ D557)
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
- binding magnesium ion: 203, 229, 242, 242, 290, 290
5cjvA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isovaleryl-coenzyme a (see paper)
34% identity, 69% coverage: 63:557/722 of query aligns to 544:1060/1061 of 5cjvA
- active site: F569 (≠ Y89), Y750 (= Y243), H751 (= H244)
- binding cobalamin: F598 (= F117), L603 (≠ H122), S621 (≠ A139), Q713 (≠ R207), E754 (= E247), A755 (= A248), G839 (= G333), R840 (≠ W334), E876 (= E370), A877 (= A371), T879 (≠ A373), H964 (≠ D458)
- binding guanosine-5'-diphosphate: E944 (≠ D438)
- binding Isovaleryl-coenzyme A: F556 (≠ Q75), F558 (≠ T77), R560 (≠ Y79), R567 (= R87), F569 (≠ Y89), R593 (≠ G112), S648 (= S164), T650 (= T166), R699 (≠ S193), T701 (= T195), Q703 (= Q197), Q713 (≠ R207), Y743 (≠ N236), H751 (= H244), S792 (= S285), F794 (= F287), K832 (≠ R326), H834 (= H328)
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
4xc6A Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, and mg (holo-icmf/gdp) (see paper)
34% identity, 69% coverage: 63:557/722 of query aligns to 547:1066/1067 of 4xc6A
- active site: F572 (≠ Y89), Y753 (= Y243), H754 (= H244)
- binding cobalamin: F601 (= F117), L606 (≠ H122), S624 (≠ A139), Q716 (≠ R207), H754 (= H244), E757 (= E247), A758 (= A248), G842 (= G333), R843 (≠ W334), E879 (= E370), A880 (= A371), T882 (≠ A373), H967 (≠ D458)
- binding guanosine-5'-diphosphate: E947 (≠ D438)
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
>Ac3H11_2278 FitnessBrowser__acidovorax_3H11:Ac3H11_2278
MSDKPTNNAPEFAAASLEAWAKAAAKSAPGGDVSALNWVTPDGITVKPLYTAEDTASLPY
ANTLPGFEPYLRGPQATMYAVRPWTIRQYAGFSTAEESNAFYRKALAAGGQGVSVAFDLA
THRGYDSDHPRVTGDVGKAGVAIDSVEDMKILFDQIPLDKVSVSMTMNGAVLPVLAGYVV
AAEEQGVSQDKLSGTIQNDILKEFMVRNTYIYPPKPSMRIIGDIIGYTAKNMPKFNSISI
SGYHMQEAGANQALELAFTLADGKEYVKTAMASGLDVDEFAGRLSFFWAIGMNFYLEVAK
MRAARLLWCRIMKETGAKNPKSLMLRTHCQTSGWSLTEQDPYNNVVRTTIEAMAAVFGGT
QSLHTNALDEAIALPTEFSARIARNTQLIIQEETHITNVIDPWAGSYMMEKLTQDMMDAA
WKIIEEVEAMGGMTQAVDSGWAKLKIEAAAAEKQARIDSGKDVIVGVNKYKLAKEDPVDI
LQIDNMKVRDGQIARLEKIRATRDAAKVQAALDALTAAAESGEGNLLELSINAVRLRATV
GEVSDALEKVFGRHRADTQKVTGVYAAAYDSAEGWDKLKTEINAFAEEQGRRPRVMIAKL
GQDGHDRGAKVVATAFADLGFDVDMGPLFQTPEECARQAIENDVHAVGVSTLAAGHKTLV
PAIIQSLRDQGADDIIVFVGGVIPAQDYDFLYESGVKGVYGPGTPIPASAKDVLEQIRKA
VA
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