SitesBLAST
Comparing CCNA_03177 FitnessBrowser__Caulo:CCNA_03177 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)
6oxdA Structure of mycobacterium tuberculosis methylmalonyl-coa mutase with adenosyl cobalamin (see paper)
38% identity, 96% coverage: 5:638/662 of query aligns to 80:713/736 of 6oxdA
- active site: Y100 (= Y19), Y254 (= Y173), H255 (= H174), K610 (= K535), D614 (= D539), H616 (= H541)
- binding cobalamin: Y100 (= Y19), L130 (= L49), H133 (≠ Q52), A150 (≠ V69), R218 (= R137), E258 (= E177), G344 (≠ S268), W345 (≠ L269), E381 (= E308), A382 (= A309), A384 (≠ G311), L385 (= L312), G615 (= G540), H616 (= H541), D617 (≠ S542), R618 (≠ N543), S661 (= S586), L663 (= L588), A665 (≠ G590), G691 (= G616), G692 (= G617), F711 (≠ Y636), P712 (≠ T637)
- binding Itaconyl coenzyme A: Y86 (≠ D11), T88 (vs. gap), M89 (vs. gap), Q93 (vs. gap), T96 (≠ I15), R98 (= R17), Y100 (= Y19), S175 (= S94), T177 (= T96), T206 (= T125), R218 (= R137), H255 (= H174), R294 (= R217), S296 (= S219), F298 (= F221), R337 (= R261), T338 (≠ Y262), H339 (≠ G263), Q341 (= Q265), Q372 (≠ R299)
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)
34% identity, 98% coverage: 4:655/662 of query aligns to 89:744/750 of P22033
- R93 (≠ H8) to H: in MAMM; mut0; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918251
- G94 (≠ A9) to R: in MAMM; mut0; dbSNP:rs727504022; to V: in MAMM; mut- and mut0; dbSNP:rs535411418
- P95 (= P10) to R: in MAMM; mut0; dbSNP:rs190834116
- YPTM 96:99 (≠ DP-- 11:12) binding malonyl-CoA
- Y100 (vs. gap) to C: in MAMM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability; dbSNP:rs864309735
- W105 (= W14) to R: in MAMM; mut0; dbSNP:rs121918249
- TIRQY 106:110 (≠ IFRTY 15:19) binding malonyl-CoA
- R108 (= R17) to C: in MAMM; mut0; dbSNP:rs121918257; to G: in MAMM; mut-; dbSNP:rs121918257; to H: in MAMM; mut0; dbSNP:rs483352778
- Q109 (≠ T18) to R: in MAMM; mut0; dbSNP:rs1461110052
- G133 (= G42) to R: in MAMM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253828
- A137 (= A46) to V: in MAMM; mut0; dbSNP:rs941483851
- D139 (= D48) to N: in MAMM; uncertain significance; dbSNP:rs879253829
- L140 (= L49) to P: in MAMM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- A141 (≠ P50) to T: in MAMM; decreased protein expression; dbSNP:rs1554160730
- H143 (≠ Q52) to Y: in MAMM; mut0
- G145 (= G54) to S: in MAMM; mut0; dbSNP:rs1237080100
- S148 (≠ P57) to L: in MAMM; mut0; dbSNP:rs1300547552
- D156 (≠ E65) to N: in MAMM; mut-
- G158 (= G67) to V: in MAMM; mut0
- G161 (= G70) to R: in MAMM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs2127420039; to V: in MAMM; decreased protein expression
- F174 (= F83) to S: in MAMM; mut0; dbSNP:rs864309733
- M186 (= M95) to V: in MAMM; mut-; dbSNP:rs148331800
- T187 (= T96) to S: in MAMM; mut0; dbSNP:rs879253830
- N189 (= N98) to I: in MAMM; mut-; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs200908035; to K: in MAMM; mut-; dbSNP:rs1561959114
- A191 (≠ P100) to E: in MAMM; mut- and mut0; affects proper folding; reduced protein level; decreased methylmalonyl-CoA mutase activity; dbSNP:rs760782399
- A197 (= A106) to E: in MAMM; mut0
- G203 (≠ A112) to R: in MAMM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs778702777
- E205 (= E114) natural variant: Missing (in MAMM; mut0; dbSNP:rs879253831)
- G215 (= G124) to C: in MAMM; mut- and mut0; dbSNP:rs121918258; to S: in MAMM; mut0; dbSNP:rs121918258
- TIQ 216:218 (≠ TTQ 125:127) binding malonyl-CoA
- Q218 (= Q127) to H: in MAMM; mut0 and mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability; dbSNP:rs1446389693
- N219 (= N128) to Y: in MAMM; mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; dbSNP:rs121918256
- R228 (= R137) binding malonyl-CoA; to Q: in MAMM; mut0; dbSNP:rs770810987
- T230 (= T139) to I: in MAMM; mut-; dbSNP:rs879253833; to R: in MAMM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253833
- Y231 (= Y140) to N: in MAMM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; strong decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability; dbSNP:rs864309736
- K255 (= K164) binding malonyl-CoA
- S262 (≠ C171) to N: in MAMM; mut0; dbSNP:rs1767683356
- H265 (= H174) binding malonyl-CoA; to Y: in MAMM; mut-
- E276 (= E185) to D: in MAMM; uncertain significance; mut-; dbSNP:rs12175488
- L281 (= L190) to S: in MAMM; mut0; dbSNP:rs796052007
- G284 (≠ A193) to E: in MAMM; mut0; dbSNP:rs879253835; to R: in MAMM; mut0; dbSNP:rs761477436
- S288 (≠ L197) to P: in MAMM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1179778233
- G291 (≠ V200) to E: in MAMM; mut0
- Q293 (≠ A202) to P: in MAMM; mut0; dbSNP:rs138374956
- RLS 304:306 (≠ RIS 217:219) binding malonyl-CoA
- L305 (≠ I218) to S: in MAMM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554160246
- S306 (= S219) to F: in MAMM; mut0; dbSNP:rs1085307929
- W309 (≠ V222) to G: in MAMM; decreased protein expression; dbSNP:rs2127418704
- G312 (= G225) to V: in MAMM; mut0; dbSNP:rs864309734
- Y316 (≠ V229) to C: in MAMM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; no decreased affinity for adenosylcob(III)alamin; dbSNP:rs781474200
- A324 (≠ S237) to T: in MAMM; mut-; dbSNP:rs780387525
- R326 (≠ T239) to K: in MAMM; uncertain significance; dbSNP:rs758577372
- L328 (= L241) to F: in MAMM; mut0; affects proper folding; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; dbSNP:rs796052002; to P: in MAMM; mut0; dbSNP:rs965316043
- S344 (≠ A257) to F: in MAMM; mut-; affects proper folding; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin
- L346 (≠ R259) natural variant: Missing (in MAMM; mut0)
- L347 (≠ F260) to R: in MAMM; mut0; dbSNP:rs1026703654
- H350 (≠ G263) to Y: in MAMM; mut0; dbSNP:rs1407914109
- L358 (= L271) to P: in MAMM; mut0; dbSNP:rs1767612147
- N366 (= N279) to S: in MAMM; mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability; dbSNP:rs864309737
- R369 (= R282) to C: in MAMM; mut0; dbSNP:rs772552898; to H: in MAMM; mut- and mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability; dbSNP:rs564069299
- T370 (≠ I283) to P: in MAMM; mut0; dbSNP:rs368790885
- A377 (≠ V290) to E: in MAMM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918250
- Q383 (≠ R299) to H: in MAMM; mut0; to P: in MAMM; mut0
- H386 (≠ Q302) to N: in MAMM; mut0; dbSNP:rs1554159937; to R: in MAMM; mut0; dbSNP:rs866933356
- T387 (≠ L303) to I: in MAMM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability; dbSNP:rs1400022403
- N388 (≠ P304) to H: in MAMM; mut0; dbSNP:rs766010704; to K: in MAMM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253840
- S389 (≠ A305) natural variant: Missing (in MAMM; mut0)
- I412 (≠ L328) natural variant: Missing (in MAMM; mut0)
- P424 (≠ L340) to L: in MAMM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253842
- G426 (≠ D342) to E: in MAMM; mut-; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs533755473; to R: in MAMM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; strong decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability; dbSNP:rs769922244
- G427 (= G343) to D: in MAMM; mut0; dbSNP:rs753288303
- G454 (= G370) to E: in MAMM; mut0
- A499 (= A420) to T: in dbSNP:rs2229385
- I505 (vs. gap) to T: in MAMM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- Q514 (≠ V432) to E: in MAMM; uncertain significance; to K: in MAMM; decreased protein expression; dbSNP:rs2127416800
- L518 (≠ I436) to P: in MAMM; mut0; dbSNP:rs864309738
- R532 (≠ A450) to H: in dbSNP:rs1141321
- A535 (= A453) to P: in MAMM; mut0; dbSNP:rs760183775
- A552 (≠ S469) to V: in MAMM; uncertain significance; dbSNP:rs879253845
- C560 (≠ V477) to Y: in MAMM; mut0; dbSNP:rs1238333040
- T566 (≠ S483) to R: in MAMM; mut0; dbSNP:rs1767288356
- F573 (= F490) to S: in MAMM; 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 (≠ V501) to C: in MAMM; mut-
- I597 (≠ V511) to R: in MAMM; no changed in protein expression; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554158951
- P615 (≠ L529) to L: in MAMM; mut0; affects proper folding; reduced strongly protein level; dbSNP:rs1554158777; to R: in MAMM; mut0; dbSNP:rs1554158777; to T: in MAMM; mut0; affects proper folding; reduced strongly protein level; loss of methylmalonyl-CoA mutase activity; dbSNP:rs1302409621
- R616 (≠ T530) to C: in MAMM; mut0; dbSNP:rs765284825
- L617 (≠ Y531) to R: in MAMM; mut0; dbSNP:rs1554158775
- K621 (= K535) to N: in MAMM; mut0
- G623 (= G537) to R: in MAMM; mut0; dbSNP:rs121918254
- Q624 (≠ L538) to R: in MAMM; no effect on protein abundance; dbSNP:rs768521956
- D625 (= D539) to G: in MAMM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253847; to V: in MAMM; mut0; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity
- G626 (= G540) to C: in MAMM; mut-; dbSNP:rs982110849
- H627 (= H541) binding axial binding residue; to R: in MAMM; mut0; dbSNP:rs372486357
- G630 (= G544) to E: in MAMM; mut0; dbSNP:rs143023066
- V633 (≠ Q547) to G: in MAMM; 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 (≠ R551) to E: in MAMM; mut-; to R: in MAMM; mut0; dbSNP:rs781501004
- F638 (≠ A552) to I: in MAMM; mut0
- D640 (≠ A554) to Y: in MAMM; mut0; dbSNP:rs865815395
- G642 (= G556) to R: in MAMM; mut-; dbSNP:rs747897332
- G648 (≠ D562) to D: in MAMM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; strong decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability; dbSNP:rs766721811
- V669 (= V583) to E: in MAMM; mut0; dbSNP:rs1360470463
- I671 (≠ L585) to V: in dbSNP:rs8589
- L674 (= L588) to F: in MAMM; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1164271240
- H678 (= H592) to R: in MAMM; mut-; dbSNP:rs147094927
- E684 (= E598) natural variant: E -> EL (in MAMM; mut-)
- L685 (≠ V599) to R: in MAMM; mut-; dbSNP:rs864309739
- R694 (≠ L608) to L: in MAMM; mut-; decreased protein abundance; loss of methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability; dbSNP:rs756225782; to W: in MAMM; 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 (≠ V614) to K: in MAMM; mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability; dbSNP:rs140600746
- G703 (= G617) to R: in MAMM; mut0; dbSNP:rs121918255
- G717 (= G631) to V: in MAMM; 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 (≠ T637) to D: in MAMM; 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 MAMM; mut-)
- 50 binding malonyl-CoA
- 69 I → V: in MAMM; likely benign; dbSNP:rs115923556
- 86 P → L: in MAMM; mut0 and mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability; dbSNP:rs769348060
- 87 G → E: in MAMM; mut0; dbSNP:rs1554160986
- 152:750 natural variant: Missing (in MAMM; mut0)
- 228:750 natural variant: Missing (in MAMM; mut0)
2xiqA Crystal structure of human methylmalonyl-coa mutase in complex with adenosylcobalamin and malonyl-coa (see paper)
34% identity, 98% coverage: 4:655/662 of query aligns to 54:709/714 of 2xiqA
- active site: Y75 (= Y19), Y229 (= Y173), H230 (= H174), K586 (= K535), D590 (= D539), H592 (= H541)
- binding cobalamin: Y75 (= Y19), L105 (= L49), H108 (≠ Q52), A125 (≠ V69), R193 (= R137), E233 (= E177), G320 (≠ S268), W321 (≠ L269), E357 (= E308), G360 (= G311), L361 (= L312), G591 (= G540), H592 (= H541), D593 (≠ S542), R594 (≠ N543), G595 (= G544), I599 (= I548), G635 (= G584), S637 (= S586), L639 (= L588), A641 (≠ G590), G667 (= G616), G668 (= G617), F687 (≠ Y636), G688 (≠ T637), T691 (≠ D640)
- binding malonyl-coenzyme a: Y61 (≠ D11), T63 (vs. gap), M64 (vs. gap), R68 (vs. gap), T71 (≠ I15), R73 (= R17), Y75 (= Y19), S150 (= S94), T152 (= T96), T181 (= T125), R193 (= R137), K220 (= K164), H230 (= H174), R269 (= R217), S271 (= S219), F273 (= F221), R313 (= R261), A314 (≠ Y262), H315 (≠ G263), Q317 (= Q265), Q348 (≠ R299)
8dyjB Crystal structure of human methylmalonyl-coa mutase in complex with adp and cob(ii)alamin (see paper)
34% identity, 98% coverage: 4:655/662 of query aligns to 53:708/708 of 8dyjB
- binding adenosine-5'-diphosphate: Y74 (= Y19), T151 (= T96), R192 (= R137), Y228 (= Y173), H229 (= H174), F272 (= F221), Q316 (= Q265), N352 (≠ P304), E356 (= E308), L360 (= L312), P361 (= P313)
- binding cobalamin: F102 (= F47), L104 (= L49), H107 (≠ Q52), A124 (≠ V69), V191 (≠ S136), R192 (= R137), H229 (= H174), E232 (= E177), G319 (≠ S268), W320 (≠ L269), E356 (= E308), G359 (= G311), L360 (= L312), G590 (= G540), H591 (= H541), D592 (≠ S542), R593 (≠ N543), G594 (= G544), I598 (= I548), S636 (= S586), L638 (= L588), A640 (≠ G590), G666 (= G616), G667 (= G617), V668 (≠ I618), F686 (≠ Y636), G687 (≠ T637), T690 (≠ D640)
7reqA Methylmalonyl-coa mutase, 2-carboxypropyl-coa inhibitor complex (see paper)
37% identity, 96% coverage: 5:638/662 of query aligns to 66:704/725 of 7reqA
- active site: Y86 (= Y19), Y240 (= Y173), H241 (= H174), K601 (= K535), D605 (= D539), H607 (= H541)
- binding 2-carboxypropyl-coenzyme a: Y72 (≠ D11), T74 (vs. gap), M75 (vs. gap), F78 (vs. gap), R79 (vs. gap), T82 (≠ I15), R84 (= R17), Y86 (= Y19), S161 (= S94), T163 (= T96), T192 (= T125), R204 (= R137), H241 (= H174), R280 (= R217), S282 (= S219), F284 (= F221), H325 (≠ G263), Q358 (≠ R299)
- binding cobalamin: Y86 (= Y19), L116 (= L49), A136 (≠ V69), R204 (= R137), E244 (= E177), G330 (≠ S268), W331 (≠ L269), E367 (= E308), A368 (= A309), A370 (≠ G311), G606 (= G540), H607 (= H541), D608 (≠ S542), R609 (≠ N543), G610 (= G544), I614 (= I548), S652 (= S586), L654 (= L588), G682 (= G616), G683 (= G617), Y702 (= Y636), T703 (= T637)
Sites not aligning to the query:
3reqA Methylmalonyl-coa mutase, substrate-free state (poor quality structure) (see paper)
37% identity, 96% coverage: 5:638/662 of query aligns to 66:704/725 of 3reqA
- active site: Y86 (= Y19), Y240 (= Y173), H241 (= H174), K601 (= K535), D605 (= D539), H607 (= H541)
- binding adenosine: Y86 (= Y19), Y240 (= Y173), E244 (= E177), G330 (≠ S268)
- binding cobalamin: L116 (= L49), V203 (≠ S136), R204 (= R137), E244 (= E177), G330 (≠ S268), W331 (≠ L269), A368 (= A309), G606 (= G540), H607 (= H541), D608 (≠ S542), R609 (≠ N543), G610 (= G544), I614 (= I548), G650 (= G584), S652 (= S586), L654 (= L588), G682 (= G616), G683 (= G617), Y702 (= Y636), T703 (= T637), P704 (= P638)
Sites not aligning to the query:
2reqA Methylmalonyl-coa mutase, non-productive coa complex, in open conformation representing substrate-free state (see paper)
37% identity, 96% coverage: 5:638/662 of query aligns to 66:704/725 of 2reqA
- active site: Y86 (= Y19), Y240 (= Y173), H241 (= H174), K601 (= K535), D605 (= D539), H607 (= H541)
- binding cobalamin: V203 (≠ S136), R204 (= R137), E244 (= E177), A245 (= A178), W331 (≠ L269), A368 (= A309), G606 (= G540), H607 (= H541), D608 (≠ S542), R609 (≠ N543), G610 (= G544), I614 (= I548), G650 (= G584), S652 (= S586), L654 (= L588), A655 (≠ S589), G682 (= G616), G683 (= G617), Y702 (= Y636), T703 (= T637)
- binding coenzyme a: Y72 (≠ D11), R79 (vs. gap), K318 (= K256)
Sites not aligning to the query:
P11653 Methylmalonyl-CoA mutase large subunit; MCM-alpha; EC 5.4.99.2 from Propionibacterium freudenreichii subsp. shermanii (see 4 papers)
37% identity, 96% coverage: 5:638/662 of query aligns to 69:707/728 of P11653
- Y75 (≠ D11) binding (R)-methylmalonyl-CoA
- M78 (vs. gap) binding (R)-methylmalonyl-CoA
- R82 (vs. gap) binding (R)-methylmalonyl-CoA
- T85 (≠ I15) binding (R)-methylmalonyl-CoA
- R87 (= R17) binding (R)-methylmalonyl-CoA
- Y89 (= Y19) binding (R)-methylmalonyl-CoA; mutation to F: Does not significantly affect affinity for succiny-CoA, but kcat is lowered about 580-fold.
- S114 (= S44) binding (R)-methylmalonyl-CoA
- F117 (= F47) binding cob(II)alamin
- A139 (≠ V69) binding cob(II)alamin
- T195 (= T125) binding (R)-methylmalonyl-CoA
- Q197 (= Q127) binding (R)-methylmalonyl-CoA
- V206 (≠ S136) binding cob(II)alamin
- R207 (= R137) binding (R)-methylmalonyl-CoA; binding cob(II)alamin
- H244 (= H174) binding (R)-methylmalonyl-CoA
- R283 (= R217) binding (R)-methylmalonyl-CoA
- S285 (= S219) binding (R)-methylmalonyl-CoA
- G333 (≠ S268) binding cob(II)alamin
- E370 (= E308) binding cob(II)alamin
- A373 (≠ G311) binding cob(II)alamin
- G609 (= G540) binding cob(II)alamin
- H610 (= H541) binding axial binding residue
- D611 (≠ S542) binding cob(II)alamin
- R612 (≠ N543) binding cob(II)alamin
- S655 (= S586) binding cob(II)alamin
- L657 (= L588) binding cob(II)alamin
- G686 (= G617) binding cob(II)alamin
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 709 binding cob(II)alamin
4reqA Methylmalonyl-coa mutase substrate complex (see paper)
37% identity, 96% coverage: 5:638/662 of query aligns to 67:705/726 of 4reqA
- active site: Y87 (= Y19), Y241 (= Y173), H242 (= H174), K602 (= K535), D606 (= D539), H608 (= H541)
- binding cobalamin: Y87 (= Y19), L117 (= L49), A137 (≠ V69), V204 (≠ S136), R205 (= R137), H242 (= H174), E245 (= E177), G331 (≠ S268), W332 (≠ L269), E368 (= E308), A369 (= A309), A371 (≠ G311), L372 (= L312), G607 (= G540), H608 (= H541), D609 (≠ S542), R610 (≠ N543), G611 (= G544), I615 (= I548), S653 (= S586), L655 (= L588), G683 (= G616), G684 (= G617), V685 (≠ I618), Y703 (= Y636), T704 (= T637)
- binding methylmalonyl-coenzyme a: Y73 (≠ D11), M76 (vs. gap), F79 (vs. gap), R80 (vs. gap), T83 (≠ I15), R85 (= R17), Y87 (= Y19), S112 (= S44), S162 (= S94), T164 (= T96), T193 (= T125), R205 (= R137), N234 (= N166), Y241 (= Y173), H242 (= H174), R281 (= R217), S283 (= S219), F285 (= F221), H326 (≠ G263), Q328 (= Q265), Q359 (≠ R299), S360 (≠ A300)
- binding succinyl-coenzyme a: Y73 (≠ D11), M76 (vs. gap), F79 (vs. gap), R80 (vs. gap), T83 (≠ I15), R85 (= R17), Y87 (= Y19), S162 (= S94), T164 (= T96), T193 (= T125), Q195 (= Q127), R205 (= R137), N234 (= N166), Y241 (= Y173), H242 (= H174), R281 (= R217), S283 (= S219), F285 (= F221), R324 (= R261), H326 (≠ G263), Q359 (≠ R299)
Sites not aligning to the query:
6reqA Methylmalonyl-coa mutase, 3-carboxypropyl-coa inhibitor complex (see paper)
37% identity, 96% coverage: 5:638/662 of query aligns to 68:706/727 of 6reqA
- active site: Y88 (= Y19), Y242 (= Y173), H243 (= H174), K603 (= K535), D607 (= D539), H609 (= H541)
- binding 3-carboxypropyl-coenzyme a: Y74 (≠ D11), T76 (vs. gap), M77 (vs. gap), F80 (vs. gap), R81 (vs. gap), T84 (≠ I15), R86 (= R17), Y88 (= Y19), S113 (= S44), S163 (= S94), T165 (= T96), T194 (= T125), R206 (= R137), H243 (= H174), R282 (= R217), S284 (= S219), F286 (= F221), H327 (≠ G263), Q329 (= Q265), Q360 (≠ R299)
- binding cobalamin: Y88 (= Y19), F116 (= F47), L118 (= L49), H121 (≠ Q52), A138 (≠ V69), R206 (= R137), E246 (= E177), G332 (≠ S268), W333 (≠ L269), E369 (= E308), A370 (= A309), A372 (≠ G311), G608 (= G540), H609 (= H541), D610 (≠ S542), R611 (≠ N543), G612 (= G544), I616 (= I548), Y620 (≠ A552), S654 (= S586), L656 (= L588), G658 (= G590), G684 (= G616), G685 (= G617), Y704 (= Y636), T705 (= T637)
Sites not aligning to the query:
5reqA Methylmalonyl-coa mutase, y89f mutant, substrate complex (see paper)
37% identity, 96% coverage: 5:638/662 of query aligns to 66:704/725 of 5reqA
- active site: F86 (≠ Y19), Y240 (= Y173), H241 (= H174), K601 (= K535), D605 (= D539), H607 (= H541)
- binding cobalamin: L116 (= L49), A136 (≠ V69), R204 (= R137), H241 (= H174), E244 (= E177), G330 (≠ S268), W331 (≠ L269), E367 (= E308), A368 (= A309), A370 (≠ G311), G606 (= G540), H607 (= H541), D608 (≠ S542), R609 (≠ N543), G610 (= G544), I614 (= I548), S652 (= S586), L654 (= L588), G682 (= G616), G683 (= G617), V684 (≠ I618), Y702 (= Y636), T703 (= T637)
- binding methylmalonyl(carbadethia)-coenzyme a: Y72 (≠ D11), T74 (vs. gap), M75 (vs. gap), R79 (vs. gap), T82 (≠ I15), R84 (= R17), F86 (≠ Y19), S111 (= S44), S161 (= S94), T163 (= T96), T192 (= T125), Q194 (= Q127), R204 (= R137), N233 (= N166), H241 (= H174), R280 (= R217), S282 (= S219), F284 (= F221), T324 (≠ Y262), H325 (≠ G263), Q358 (≠ R299), S359 (≠ A300)
- binding succinyl(carbadethia)-coenzyme a: Y72 (≠ D11), T74 (vs. gap), M75 (vs. gap), R79 (vs. gap), T82 (≠ I15), R84 (= R17), F86 (≠ Y19), S161 (= S94), T163 (= T96), T192 (= T125), R204 (= R137), N233 (= N166), H241 (= H174), R280 (= R217), S282 (= S219), F284 (= F221), H325 (≠ G263), Q358 (≠ R299)
Sites not aligning to the query:
1e1cA Methylmalonyl-coa mutase h244a mutant (see paper)
37% identity, 96% coverage: 5:638/662 of query aligns to 68:706/727 of 1e1cA
- active site: Y88 (= Y19), Y242 (= Y173), A243 (≠ H174), K603 (= K535), D607 (= D539), H609 (= H541)
- binding cobalamin: Y88 (= Y19), L118 (= L49), H121 (≠ Q52), A138 (≠ V69), V205 (≠ S136), R206 (= R137), E246 (= E177), G332 (≠ S268), W333 (≠ L269), E369 (= E308), A370 (= A309), A372 (≠ G311), L373 (= L312), G608 (= G540), H609 (= H541), D610 (≠ S542), R611 (≠ N543), G612 (= G544), I616 (= I548), Y620 (≠ A552), S654 (= S586), L656 (= L588), G684 (= G616), G685 (= G617), V686 (≠ I618), Y704 (= Y636), T705 (= T637)
- binding desulfo-coenzyme a: Y74 (≠ D11), M77 (vs. gap), F80 (vs. gap), R81 (vs. gap), T84 (≠ I15), R86 (= R17), S113 (= S44), S163 (= S94), T165 (= T96), T194 (= T125), R282 (= R217), S284 (= S219), H327 (≠ G263), Q360 (≠ R299)
Sites not aligning to the query:
8gjuJ Crystal structure of human methylmalonyl-coa mutase (mmut) in complex with methylmalonic acidemia type a protein (mmaa), coenzyme a, and gdp (see paper)
34% identity, 98% coverage: 4:655/662 of query aligns to 54:686/689 of 8gjuJ
- binding coenzyme a: Y61 (≠ D11), T63 (vs. gap), R68 (vs. gap), T71 (≠ I15), R73 (= R17), S150 (= S94), T152 (= T96), T181 (= T125), Q183 (= Q127), N222 (= N166), R269 (= R217), S271 (= S219), R313 (= R261), A314 (≠ Y262), H315 (≠ G263), Q348 (≠ R299)
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)
35% identity, 74% coverage: 5:494/662 of query aligns to 70:557/562 of I3VE77
- YPTM 76:79 (≠ DPP- 11:13) binding (3S)-3-hydroxybutanoyl-CoA
- TMR 86:88 (≠ IFR 15:17) binding (3S)-3-hydroxybutanoyl-CoA
- I90 (≠ Y19) 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 (≠ A46) binding (3S)-3-hydroxybutanoyl-CoA; mutation to A: 2-fold increase in catalytic efficiency with 2-hydroxyisobutyryl-CoA as substrate. Small increase in catalytic efficiency with (S)-3-hydroxybuytryl-CoA as substrate. 1800-fold increase in catalytic efficiency with (R)-3-hydroxybutyryl-CoA as substrate.; mutation to V: 1.5-fold increase in catalytic efficiency with 2-hydroxyisobutyryl-CoA as substrate. 3-fold decrease in catalytic efficiency with (S)-3-hydroxybuytryl-CoA as substrate. 1300-fold increase in catalytic efficiency with (R)-3-hydroxybutyryl-CoA as substrate. 74-fold increase in catalytic efficiency with pivalyl-CoA as substrate.
- TVQ 196:198 (≠ TTQ 125:127) binding (3S)-3-hydroxybutanoyl-CoA
- R235 (≠ K164) binding (3S)-3-hydroxybutanoyl-CoA
- N240 (= N169) binding (3S)-3-hydroxybutanoyl-CoA
- H245 (= H174) binding (3S)-3-hydroxybutanoyl-CoA
- R284 (= R217) binding (3S)-3-hydroxybutanoyl-CoA
4r3uA Crystal structure of 2-hydroxyisobutyryl-coa mutase (see paper)
35% identity, 74% coverage: 5:494/662 of query aligns to 69:556/557 of 4r3uA
- active site: I89 (≠ Y19), Y243 (= Y173), H244 (= H174)
- binding 3-hydroxybutanoyl-coenzyme a: Y75 (≠ D11), T77 (≠ P13), M78 (vs. gap), R82 (vs. gap), T85 (≠ I15), R87 (= R17), I89 (≠ Y19), D116 (≠ A46), S164 (= S94), T166 (= T96), T195 (= T125), Q197 (= Q127), R234 (≠ K164), N236 (= N166), N239 (= N169), Y243 (= Y173), H244 (= H174), R283 (= R217), F287 (= F221), R327 (= R261), F328 (≠ Y262), H329 (≠ G263), Q331 (= Q265), Q362 (≠ R299)
- 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 (≠ D11), T77 (≠ P13), M78 (vs. gap), R82 (vs. gap), T85 (≠ I15), R87 (= R17), I89 (≠ Y19), D116 (≠ A46), S164 (= S94), T166 (= T96), T195 (= T125), Q197 (= Q127), R234 (≠ K164), N236 (= N166), N239 (= N169), H244 (= H174), R283 (= R217), F287 (= F221), R327 (= R261), F328 (≠ Y262), H329 (≠ G263), Q331 (= Q265), Q362 (≠ R299)
- binding cobalamin: D116 (≠ A46), M119 (≠ L49), E139 (≠ V69), Q207 (≠ R137), E209 (≠ T139), E247 (= E177), A334 (≠ S268), E371 (= E308), A372 (= A309), A374 (≠ G311)
Q5KUG0 Fused isobutyryl-CoA mutase; EC 5.4.99.13; EC 3.6.5.- from Geobacillus kaustophilus (strain HTA426) (see paper)
26% identity, 74% coverage: 5:494/662 of query aligns to 577:1083/1086 of Q5KUG0
Sites not aligning to the query:
- 213 K→A: Loss of GTPase and ATPase activities. No effect on the mutase activity.
4xc7A Isobutyryl-coa mutase fused with bound butyryl-coa and without cobalamin or gdp (apo-icmf) (see paper)
27% identity, 72% coverage: 17:494/662 of query aligns to 564:1050/1053 of 4xc7A
- active site: F566 (≠ Y19), Y747 (= Y173), H748 (= H174)
- binding Butyryl Coenzyme A: R564 (= R17), F566 (≠ Y19), R590 (vs. gap), S645 (vs. gap), T647 (= T96), R696 (≠ Q123), T698 (= T125), Y740 (≠ N166), S789 (= S219), F791 (= F221), R824 (≠ K256), K829 (≠ R261), H831 (≠ G263)
Sites not aligning to the query:
5cjtA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isobutyryl-coenzyme a (see paper)
28% identity, 72% coverage: 17:494/662 of query aligns to 567:1059/1062 of 5cjtA
- active site: F569 (≠ Y19), Y750 (= Y173), H751 (= H174)
- binding cobalamin: F598 (= F47), L603 (≠ Q52), S621 (≠ V69), Q713 (≠ R137), H751 (= H174), E754 (= E177), A755 (= A178), G839 (≠ S268), R840 (≠ L269), E876 (= E308), A877 (= A309), T879 (≠ G311), H964 (≠ E394)
- binding isobutyryl-coenzyme a: R567 (= R17), F569 (≠ Y19), R593 (vs. gap), S648 (vs. gap), T650 (= T96), R699 (≠ Q123), T701 (= T125), Q703 (= Q127), Y743 (≠ N166), Y750 (= Y173), H751 (= H174), S792 (= S219), F794 (= F221), R827 (≠ K256), K832 (≠ R261), H834 (≠ G263)
- binding guanosine-5'-diphosphate: E944 (≠ D376)
Sites not aligning to the query:
- active site: 6
- binding cobalamin: 18, 19, 20, 21, 22, 26, 66, 67, 94, 96, 98, 116, 117
- binding isobutyryl-coenzyme a: 556, 558, 560
- binding guanosine-5'-diphosphate: 199, 201, 202, 203, 204, 245, 336, 337, 339, 374, 376
- binding magnesium ion: 203, 229, 242, 242, 289, 289
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)
28% identity, 72% coverage: 17:494/662 of query aligns to 596:1090/1093 of Q1LRY0
- F598 (≠ Y19) mutation to A: Switches the substrate specificity and enhances the catalytic efficiency of the isovaleryl-CoA mutase over the native isobutyryl-CoA mutase activity about 4000-fold. Is even more susceptible to inactivation than wild-type during turnover.
- R622 (vs. gap) binding substrate
- R728 (≠ Q123) binding substrate
- Y772 (≠ N166) binding substrate
- S821 (= S219) binding substrate
- R856 (≠ K256) binding substrate
- K861 (≠ R261) binding substrate
- E973 (≠ D376) binding GTP
Sites not aligning to the query:
- 39 binding axial binding residue
- 169:417 GTPase chaperone MeaI
- 219:224 binding GTP
- 223 binding Mg(2+)
- 248 binding Mg(2+)
- 249 binding Mg(2+)
- 262 binding Mg(2+); binding Mg(2+)
- 265 binding GTP
- 310 binding Mg(2+); binding Mg(2+)
- 311 binding Mg(2+)
- 357:360 binding GTP
- 418:579 Linker
- 587 binding substrate
- 1092 binding GTP
8sslA Isobutyryl-coa mutase fused q341a in the presence of gtp (see paper)
28% identity, 72% coverage: 17:494/662 of query aligns to 575:1069/1072 of 8sslA
Sites not aligning to the query:
- binding guanosine-5'-diphosphate: 200, 201, 202, 241, 244, 337, 339, 374, 375, 376, 1071
- binding magnesium ion: 201, 241
Query Sequence
>CCNA_03177 FitnessBrowser__Caulo:CCNA_03177
MSAKPYQHAPDPPWIFRTYAGHSTAEKSNALYRANLAKGQTGLSVAFDLPTQTGYDPDHI
LARGEVGKVGVPISHLGDMRQLFSEIPLEKMNTSMTINAPAAWLLAMYVALADEQGADRK
LLQGTTQNDLIKEYLSRGTYIFPPGPSLRLIGDMIAWCYREVPKWNPMNVCSYHLQEAGA
TPEQELAFALATAISVLDTVKAGGQVPDEDFEIVASRISFFVNAGVRFVTELCKMRSFTK
LWDQILLERYGVQDPKARRFRYGVQVNSLGLTEQQPENNVYRILIEALAVTLSKDARCRA
LQLPAWNEALGLPRPFDQQWSLRLQQVLAYETDLLEYEDLFDGSHVVEAKVAELSKGALA
QLTLIDEMGGAQNAIDYMKSELVASNAKRVRAVETGEMTVVGVNRWTETEASPLSAGESA
IETVDPRLEAGVVERIKAWREARDAVAVEAALAALKAAAREGRNVMEPSIAAAKAGVTTG
EWSGALREVFGEYRGPTGVAVVVSTGEAEDVEAVKREVERVSELLGRTLTYLVGKPGLDG
HSNGAEQIATRARACGMEVVYDGIRSTPEEIVRRAKESRAHVVGLSILSGSHLDLVQEVI
RVMRAEGLGHIPVVAGGIIPPEDALILKQMGVARIYTPKDFKITQIMGDVVKLVEATALT
EA
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