SitesBLAST
Comparing WP_011382757.1 AMB_RS01570 protein meaA 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, 94% coverage: 16:642/665 of query aligns to 93:713/736 of 6oxdA
- active site: Y100 (= Y23), Y254 (= Y177), H255 (= H178), K610 (= K539), D614 (= D543), H616 (= H545)
- binding cobalamin: Y100 (= Y23), L130 (= L53), H133 (≠ Q56), A150 (≠ V73), R218 (= R141), E258 (= E181), G344 (≠ S270), W345 (≠ L271), E381 (= E310), A382 (= A311), A384 (≠ G313), L385 (= L314), G615 (= G544), H616 (= H545), D617 (≠ S546), R618 (≠ N547), S661 (= S590), L663 (= L592), A665 (≠ G594), G691 (= G620), G692 (= G621), F711 (≠ Y640), P712 (≠ T641)
- binding Itaconyl coenzyme A: Q93 (≠ K16), T96 (≠ L19), R98 (= R21), Y100 (= Y23), S175 (= S98), T177 (= T100), T206 (= T129), R218 (= R141), H255 (= H178), R294 (= R219), S296 (= S221), F298 (= F223), R337 (= R263), T338 (≠ Y264), H339 (≠ G265), Q341 (= Q267), Q372 (≠ R301)
Sites not aligning to the query:
2xiqA Crystal structure of human methylmalonyl-coa mutase in complex with adenosylcobalamin and malonyl-coa (see paper)
35% identity, 94% coverage: 16:642/665 of query aligns to 68:689/714 of 2xiqA
- active site: Y75 (= Y23), Y229 (= Y177), H230 (= H178), K586 (= K539), D590 (= D543), H592 (= H545)
- binding cobalamin: Y75 (= Y23), L105 (= L53), H108 (≠ Q56), A125 (≠ V73), R193 (= R141), E233 (= E181), G320 (≠ S270), W321 (≠ L271), E357 (= E310), G360 (= G313), L361 (= L314), G591 (= G544), H592 (= H545), D593 (≠ S546), R594 (≠ N547), G595 (= G548), I599 (= I552), G635 (= G588), S637 (= S590), L639 (= L592), A641 (≠ G594), G667 (= G620), G668 (= G621), F687 (≠ Y640), G688 (≠ T641)
- binding malonyl-coenzyme a: R68 (≠ K16), T71 (≠ L19), R73 (= R21), Y75 (= Y23), S150 (= S98), T152 (= T100), T181 (= T129), R193 (= R141), K220 (= K168), H230 (= H178), R269 (= R219), S271 (= S221), F273 (= F223), R313 (= R263), A314 (≠ Y264), H315 (≠ G265), Q317 (= Q267), Q348 (≠ R301)
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)
35% identity, 94% coverage: 16:642/665 of query aligns to 103:724/750 of P22033
- W105 (= W18) to R: in MMAM; mut0; dbSNP:rs121918249
- TIRQY 106:110 (≠ LFRTY 19:23) binding
- R108 (= R21) to C: in MMAM; mut0; dbSNP:rs121918257; to G: in MMAM; mut-; to H: in MMAM; mut0; dbSNP:rs483352778
- Q109 (≠ T22) to R: in MMAM; mut0; dbSNP:rs1461110052
- G133 (= G46) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253828
- A137 (= A50) to V: in MMAM; mut0; dbSNP:rs941483851
- D139 (= D52) to N: in MMAM; uncertain significance; dbSNP:rs879253829
- L140 (= L53) to P: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- A141 (≠ P54) to T: in MMAM; decreased protein expression; dbSNP:rs1554160730
- H143 (≠ Q56) to Y: in MMAM; mut0
- G145 (= G58) to S: in MMAM; mut0
- S148 (= S61) to L: in MMAM; mut0; dbSNP:rs1300547552
- D156 (≠ E69) to N: in MMAM; mut-
- G158 (= G71) to V: in MMAM; mut0
- G161 (= G74) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; to V: in MMAM; decreased protein expression
- F174 (= F87) to S: in MMAM; mut0; dbSNP:rs864309733
- M186 (= M99) to V: in MMAM; mut-; dbSNP:rs148331800
- T187 (= T100) to S: in MMAM; mut0; dbSNP:rs879253830
- N189 (= N102) to I: in MMAM; mut-; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs200908035; to K: in MMAM; mut-; dbSNP:rs1561959114
- A191 (≠ P104) to E: in MMAM; mut- and mut0; affects proper folding; reduced protein level; decreased methylmalonyl-CoA mutase activity; dbSNP:rs760782399
- A197 (≠ S110) to E: in MMAM; mut0
- G203 (≠ A116) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs778702777
- E205 (≠ R118) natural variant: Missing (in MMAM; mut0; dbSNP:rs879253831)
- G215 (= G128) to C: in MMAM; mut- and mut0; dbSNP:rs121918258; to S: in MMAM; mut0; dbSNP:rs121918258
- TIQ 216:218 (≠ TTQ 129:131) binding
- Q218 (= Q131) to H: in MMAM; mut0 and mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability; dbSNP:rs1446389693
- N219 (= N132) to Y: in MMAM; mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; dbSNP:rs121918256
- R228 (= R141) binding ; to Q: in MMAM; mut0; dbSNP:rs770810987
- T230 (= T143) to I: in MMAM; mut-; to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253833
- Y231 (= Y144) 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 (= K168) binding
- S262 (≠ C175) to N: in MMAM; mut0
- H265 (= H178) binding ; to Y: in MMAM; mut-
- E276 (= E189) to D: in MMAM; uncertain significance; mut-; dbSNP:rs12175488
- L281 (= L194) to S: in MMAM; mut0; dbSNP:rs796052007
- G284 (≠ A197) to E: in MMAM; mut0; dbSNP:rs879253835; to R: in MMAM; mut0; dbSNP:rs761477436
- S288 (≠ V204) to P: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1179778233
- G291 (≠ T207) to E: in MMAM; mut0
- Q293 (≠ P209) to P: in MMAM; mut0
- RLS 304:306 (≠ RIS 219:221) binding
- L305 (≠ I220) to S: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554160246
- S306 (= S221) to F: in MMAM; mut0; dbSNP:rs1085307929
- W309 (≠ V224) to G: in MMAM; decreased protein expression
- G312 (= G227) to V: in MMAM; mut0; dbSNP:rs864309734
- Y316 (≠ V231) 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 (= A239) to T: in MMAM; mut-; dbSNP:rs780387525
- R326 (≠ T241) to K: in MMAM; uncertain significance; dbSNP:rs758577372
- L328 (= L243) 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 (≠ A259) 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 (≠ R261) natural variant: Missing (in MMAM; mut0)
- L347 (≠ F262) to R: in MMAM; mut0; dbSNP:rs1026703654
- H350 (≠ G265) to Y: in MMAM; mut0; dbSNP:rs1407914109
- L358 (= L273) to P: in MMAM; mut0
- N366 (= N281) 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 (= R284) 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 (≠ I285) to P: in MMAM; mut0; dbSNP:rs368790885
- A377 (≠ V292) to E: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918250
- Q383 (≠ R301) to H: in MMAM; mut0; to P: in MMAM; mut0
- H386 (≠ Q304) to N: in MMAM; mut0; dbSNP:rs1554159937; to R: in MMAM; mut0; dbSNP:rs866933356
- T387 (≠ L305) 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 (≠ P306) to H: in MMAM; mut0; dbSNP:rs766010704; to K: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253840
- S389 (≠ A307) natural variant: Missing (in MMAM; mut0)
- I412 (≠ M330) natural variant: Missing (in MMAM; mut0)
- P424 (≠ I342) to L: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253842
- G426 (≠ D344) 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 (= G345) to D: in MMAM; mut0; dbSNP:rs753288303
- G454 (= G372) to E: in MMAM; mut0
- A499 (≠ P417) to T: in dbSNP:rs2229385
- I505 (≠ V428) to T: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- Q514 (= Q436) to E: in MMAM; uncertain significance; to K: in MMAM; decreased protein expression
- L518 (= L440) to P: in MMAM; mut0; dbSNP:rs864309738
- R532 (≠ K454) to H: in dbSNP:rs1141321
- A535 (= A457) to P: in MMAM; mut0; dbSNP:rs760183775
- A552 (≠ S473) to V: in MMAM; uncertain significance; dbSNP:rs879253845
- C560 (≠ V481) to Y: in MMAM; mut0; dbSNP:rs1238333040
- T566 (≠ A487) to R: in MMAM; mut0
- F573 (= F494) 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 (≠ A504) to C: in MMAM; mut-
- I597 (≠ K514) to R: in MMAM; no changed in protein expression; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554158951
- P615 (≠ V533) 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 (≠ K534) to C: in MMAM; mut0; dbSNP:rs765284825
- L617 (≠ I535) to R: in MMAM; mut0; dbSNP:rs1554158775
- K621 (= K539) to N: in MMAM; mut0
- G623 (= G541) to R: in MMAM; mut0; dbSNP:rs121918254
- Q624 (≠ L542) to R: in MMAM; no effect on protein abundance; dbSNP:rs768521956
- D625 (= D543) 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 (= G544) to C: in MMAM; mut-; dbSNP:rs982110849
- H627 (= H545) binding axial binding residue; to R: in MMAM; mut0; dbSNP:rs372486357
- G630 (= G548) to E: in MMAM; mut0; dbSNP:rs143023066
- V633 (≠ Q551) 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 (≠ R555) to E: in MMAM; mut-; to R: in MMAM; mut0; dbSNP:rs781501004
- F638 (≠ A556) to I: in MMAM; mut0
- D640 (= D558) to Y: in MMAM; mut0; dbSNP:rs865815395
- G642 (= G560) to R: in MMAM; mut-; dbSNP:rs747897332
- G648 (≠ E566) 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 (= V587) to E: in MMAM; mut0; dbSNP:rs1360470463
- I671 (≠ L589) to V: in dbSNP:rs8589
- L674 (= L592) to F: in MMAM; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1164271240
- H678 (= H596) to R: in MMAM; mut-; dbSNP:rs147094927
- E684 (= E602) natural variant: E -> EL (in MMAM; mut-)
- L685 (≠ V603) to R: in MMAM; mut-; dbSNP:rs864309739
- R694 (≠ L612) 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 (≠ V618) 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 (= G621) to R: in MMAM; mut0; dbSNP:rs121918255
- G717 (= G635) 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 (≠ T641) 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-)
- 50 binding
- 69 I → V: in MMAM; likely benign; dbSNP:rs115923556
- 86 P → 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
- 87 G → E: in MMAM; mut0; dbSNP:rs1554160986
- 93 R → H: in MMAM; mut0; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918251
- 94 G → R: in MMAM; mut0; dbSNP:rs727504022; G → V: in MMAM; mut- and mut0; dbSNP:rs535411418
- 95 P → R: in MMAM; mut0; dbSNP:rs190834116
- 96:99 binding
- 100 Y → 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
- 152:750 natural variant: Missing (in MMAM; mut0)
- 228:750 natural variant: Missing (in MMAM; mut0)
8dyjB Crystal structure of human methylmalonyl-coa mutase in complex with adp and cob(ii)alamin (see paper)
35% identity, 94% coverage: 16:642/665 of query aligns to 67:688/708 of 8dyjB
- binding adenosine-5'-diphosphate: Y74 (= Y23), T151 (= T100), R192 (= R141), Y228 (= Y177), H229 (= H178), F272 (= F223), Q316 (= Q267), N352 (≠ P306), E356 (= E310), L360 (= L314), P361 (= P315)
- binding cobalamin: F102 (= F51), L104 (= L53), H107 (≠ Q56), A124 (≠ V73), V191 (≠ S140), R192 (= R141), H229 (= H178), E232 (= E181), G319 (≠ S270), W320 (≠ L271), E356 (= E310), G359 (= G313), L360 (= L314), G590 (= G544), H591 (= H545), D592 (≠ S546), R593 (≠ N547), G594 (= G548), I598 (= I552), S636 (= S590), L638 (= L592), A640 (≠ G594), G666 (= G620), G667 (= G621), V668 (≠ I622), F686 (≠ Y640), G687 (≠ T641)
Sites not aligning to the query:
4reqA Methylmalonyl-coa mutase substrate complex (see paper)
36% identity, 94% coverage: 16:642/665 of query aligns to 80:705/726 of 4reqA
- active site: Y87 (= Y23), Y241 (= Y177), H242 (= H178), K602 (= K539), D606 (= D543), H608 (= H545)
- binding cobalamin: Y87 (= Y23), L117 (= L53), A137 (≠ V73), V204 (≠ S140), R205 (= R141), H242 (= H178), E245 (= E181), G331 (≠ S270), W332 (≠ L271), E368 (= E310), A369 (= A311), A371 (≠ G313), L372 (= L314), G607 (= G544), H608 (= H545), D609 (≠ S546), R610 (≠ N547), G611 (= G548), I615 (= I552), S653 (= S590), L655 (= L592), G683 (= G620), G684 (= G621), V685 (≠ I622), Y703 (= Y640), T704 (= T641)
- binding methylmalonyl-coenzyme a: R80 (≠ K16), T83 (≠ L19), R85 (= R21), Y87 (= Y23), S112 (= S48), S162 (= S98), T164 (= T100), T193 (= T129), R205 (= R141), N234 (= N170), Y241 (= Y177), H242 (= H178), R281 (= R219), S283 (= S221), F285 (= F223), H326 (≠ G265), Q328 (= Q267), Q359 (≠ R301), S360 (≠ A302)
- binding succinyl-coenzyme a: R80 (≠ K16), T83 (≠ L19), R85 (= R21), Y87 (= Y23), S162 (= S98), T164 (= T100), T193 (= T129), Q195 (= Q131), R205 (= R141), N234 (= N170), Y241 (= Y177), H242 (= H178), R281 (= R219), S283 (= S221), F285 (= F223), R324 (= R263), H326 (≠ G265), Q359 (≠ R301)
Sites not aligning to the query:
6reqA Methylmalonyl-coa mutase, 3-carboxypropyl-coa inhibitor complex (see paper)
36% identity, 94% coverage: 16:642/665 of query aligns to 81:706/727 of 6reqA
- active site: Y88 (= Y23), Y242 (= Y177), H243 (= H178), K603 (= K539), D607 (= D543), H609 (= H545)
- binding 3-carboxypropyl-coenzyme a: R81 (≠ K16), T84 (≠ L19), R86 (= R21), Y88 (= Y23), S113 (= S48), S163 (= S98), T165 (= T100), T194 (= T129), R206 (= R141), H243 (= H178), R282 (= R219), S284 (= S221), F286 (= F223), H327 (≠ G265), Q329 (= Q267), Q360 (≠ R301)
- binding cobalamin: Y88 (= Y23), F116 (= F51), L118 (= L53), H121 (≠ Q56), A138 (≠ V73), R206 (= R141), E246 (= E181), G332 (≠ S270), W333 (≠ L271), E369 (= E310), A370 (= A311), A372 (≠ G313), G608 (= G544), H609 (= H545), D610 (≠ S546), R611 (≠ N547), G612 (= G548), I616 (= I552), Y620 (≠ A556), S654 (= S590), L656 (= L592), G658 (= G594), G684 (= G620), G685 (= G621), Y704 (= Y640), T705 (= T641)
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)
36% identity, 94% coverage: 16:642/665 of query aligns to 82:707/728 of P11653
- R82 (≠ K16) binding
- T85 (≠ L19) binding
- R87 (= R21) binding
- Y89 (= Y23) binding ; mutation to F: Does not significantly affect affinity for succiny-CoA, but kcat is lowered about 580-fold.
- S114 (= S48) binding
- F117 (= F51) binding
- A139 (≠ V73) binding
- T195 (= T129) binding
- Q197 (= Q131) binding
- V206 (≠ S140) binding
- R207 (= R141) binding ; binding
- H244 (= H178) binding
- R283 (= R219) binding
- S285 (= S221) binding
- G333 (≠ S270) binding
- E370 (= E310) binding
- A373 (≠ G313) binding
- G609 (= G544) binding
- H610 (= H545) binding axial binding residue
- D611 (≠ S546) binding
- R612 (≠ N547) binding
- S655 (= S590) binding
- L657 (= L592) binding
- G686 (= G621) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 75 binding
- 78 binding
- 709 binding
7reqA Methylmalonyl-coa mutase, 2-carboxypropyl-coa inhibitor complex (see paper)
36% identity, 94% coverage: 16:642/665 of query aligns to 79:704/725 of 7reqA
- active site: Y86 (= Y23), Y240 (= Y177), H241 (= H178), K601 (= K539), D605 (= D543), H607 (= H545)
- binding 2-carboxypropyl-coenzyme a: R79 (≠ K16), T82 (≠ L19), R84 (= R21), Y86 (= Y23), S161 (= S98), T163 (= T100), T192 (= T129), R204 (= R141), H241 (= H178), R280 (= R219), S282 (= S221), F284 (= F223), H325 (≠ G265), Q358 (≠ R301)
- binding cobalamin: Y86 (= Y23), L116 (= L53), A136 (≠ V73), R204 (= R141), E244 (= E181), G330 (≠ S270), W331 (≠ L271), E367 (= E310), A368 (= A311), A370 (≠ G313), G606 (= G544), H607 (= H545), D608 (≠ S546), R609 (≠ N547), G610 (= G548), I614 (= I552), S652 (= S590), L654 (= L592), G682 (= G620), G683 (= G621), Y702 (= Y640), T703 (= T641)
Sites not aligning to the query:
3reqA Methylmalonyl-coa mutase, substrate-free state (poor quality structure) (see paper)
36% identity, 94% coverage: 16:642/665 of query aligns to 79:704/725 of 3reqA
- active site: Y86 (= Y23), Y240 (= Y177), H241 (= H178), K601 (= K539), D605 (= D543), H607 (= H545)
- binding adenosine: Y86 (= Y23), Y240 (= Y177), E244 (= E181), G330 (≠ S270)
- binding cobalamin: L116 (= L53), V203 (≠ S140), R204 (= R141), E244 (= E181), G330 (≠ S270), W331 (≠ L271), A368 (= A311), G606 (= G544), H607 (= H545), D608 (≠ S546), R609 (≠ N547), G610 (= G548), I614 (= I552), G650 (= G588), S652 (= S590), L654 (= L592), G682 (= G620), G683 (= G621), Y702 (= Y640), T703 (= T641), P704 (= P642)
Sites not aligning to the query:
2reqA Methylmalonyl-coa mutase, non-productive coa complex, in open conformation representing substrate-free state (see paper)
36% identity, 94% coverage: 16:642/665 of query aligns to 79:704/725 of 2reqA
- active site: Y86 (= Y23), Y240 (= Y177), H241 (= H178), K601 (= K539), D605 (= D543), H607 (= H545)
- binding cobalamin: V203 (≠ S140), R204 (= R141), E244 (= E181), A245 (= A182), W331 (≠ L271), A368 (= A311), G606 (= G544), H607 (= H545), D608 (≠ S546), R609 (≠ N547), G610 (= G548), I614 (= I552), G650 (= G588), S652 (= S590), L654 (= L592), A655 (≠ S593), G682 (= G620), G683 (= G621), Y702 (= Y640), T703 (= T641)
- binding coenzyme a: R79 (≠ K16), K318 (= K258)
Sites not aligning to the query:
5reqA Methylmalonyl-coa mutase, y89f mutant, substrate complex (see paper)
36% identity, 94% coverage: 16:642/665 of query aligns to 79:704/725 of 5reqA
- active site: F86 (≠ Y23), Y240 (= Y177), H241 (= H178), K601 (= K539), D605 (= D543), H607 (= H545)
- binding cobalamin: L116 (= L53), A136 (≠ V73), R204 (= R141), H241 (= H178), E244 (= E181), G330 (≠ S270), W331 (≠ L271), E367 (= E310), A368 (= A311), A370 (≠ G313), G606 (= G544), H607 (= H545), D608 (≠ S546), R609 (≠ N547), G610 (= G548), I614 (= I552), S652 (= S590), L654 (= L592), G682 (= G620), G683 (= G621), V684 (≠ I622), Y702 (= Y640), T703 (= T641)
- binding methylmalonyl(carbadethia)-coenzyme a: R79 (≠ K16), T82 (≠ L19), R84 (= R21), F86 (≠ Y23), S111 (= S48), S161 (= S98), T163 (= T100), T192 (= T129), Q194 (= Q131), R204 (= R141), N233 (= N170), H241 (= H178), R280 (= R219), S282 (= S221), F284 (= F223), T324 (≠ Y264), H325 (≠ G265), Q358 (≠ R301), S359 (≠ A302)
- binding succinyl(carbadethia)-coenzyme a: R79 (≠ K16), T82 (≠ L19), R84 (= R21), F86 (≠ Y23), S161 (= S98), T163 (= T100), T192 (= T129), R204 (= R141), N233 (= N170), H241 (= H178), R280 (= R219), S282 (= S221), F284 (= F223), H325 (≠ G265), Q358 (≠ R301)
Sites not aligning to the query:
1e1cA Methylmalonyl-coa mutase h244a mutant (see paper)
36% identity, 94% coverage: 16:642/665 of query aligns to 81:706/727 of 1e1cA
- active site: Y88 (= Y23), Y242 (= Y177), A243 (≠ H178), K603 (= K539), D607 (= D543), H609 (= H545)
- binding cobalamin: Y88 (= Y23), L118 (= L53), H121 (≠ Q56), A138 (≠ V73), V205 (≠ S140), R206 (= R141), E246 (= E181), G332 (≠ S270), W333 (≠ L271), E369 (= E310), A370 (= A311), A372 (≠ G313), L373 (= L314), G608 (= G544), H609 (= H545), D610 (≠ S546), R611 (≠ N547), G612 (= G548), I616 (= I552), Y620 (≠ A556), S654 (= S590), L656 (= L592), G684 (= G620), G685 (= G621), V686 (≠ I622), Y704 (= Y640), T705 (= T641)
- binding desulfo-coenzyme a: R81 (≠ K16), T84 (≠ L19), R86 (= R21), S113 (= S48), S163 (= S98), T165 (= T100), T194 (= T129), R282 (= R219), S284 (= S221), H327 (≠ G265), Q360 (≠ R301)
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, 94% coverage: 16:642/665 of query aligns to 68:666/689 of 8gjuJ
- binding coenzyme a: R68 (≠ K16), T71 (≠ L19), R73 (= R21), S150 (= S98), T152 (= T100), T181 (= T129), Q183 (= Q131), N222 (= N170), R269 (= R219), S271 (= S221), R313 (= R263), A314 (≠ Y264), H315 (≠ G265), Q348 (≠ R301)
Sites not aligning to the query:
4r3uA Crystal structure of 2-hydroxyisobutyryl-coa mutase (see paper)
31% identity, 73% coverage: 14:498/665 of query aligns to 80:556/557 of 4r3uA
- active site: I89 (≠ Y23), Y243 (= Y177), H244 (= H178)
- binding 3-hydroxybutanoyl-coenzyme a: R82 (≠ K16), T85 (≠ L19), R87 (= R21), I89 (≠ Y23), D116 (≠ A50), S164 (= S98), T166 (= T100), T195 (= T129), Q197 (= Q131), R234 (≠ K168), N236 (= N170), N239 (= N173), Y243 (= Y177), H244 (= H178), R283 (= R219), F287 (= F223), R327 (= R263), F328 (≠ Y264), H329 (≠ G265), Q331 (= Q267), Q362 (≠ R301)
- 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: R82 (≠ K16), T85 (≠ L19), R87 (= R21), I89 (≠ Y23), D116 (≠ A50), S164 (= S98), T166 (= T100), T195 (= T129), Q197 (= Q131), R234 (≠ K168), N236 (= N170), N239 (= N173), H244 (= H178), R283 (= R219), F287 (= F223), R327 (= R263), F328 (≠ Y264), H329 (≠ G265), Q331 (= Q267), Q362 (≠ R301)
- binding cobalamin: D116 (≠ A50), M119 (≠ L53), E139 (≠ V73), Q207 (≠ R141), E209 (≠ T143), E247 (= E181), A334 (≠ S270), E371 (= E310), A372 (= A311), A374 (≠ G313)
Sites not aligning to the query:
- binding 3-hydroxybutanoyl-coenzyme a: 75, 77, 78
- 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: 75, 77, 78
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)
31% identity, 73% coverage: 14:498/665 of query aligns to 81:557/562 of I3VE77
- TMR 86:88 (≠ LFR 19:21) binding
- I90 (≠ Y23) 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 (≠ A50) 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 (≠ TTQ 129:131) binding
- R235 (≠ K168) binding
- N240 (= N173) binding
- H245 (= H178) binding
- R284 (= R219) binding
Sites not aligning to the query:
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)
26% identity, 72% coverage: 21:498/665 of query aligns to 596:1090/1093 of Q1LRY0
- F598 (≠ Y23) 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 (≠ N127) binding
- Y772 (≠ N170) binding
- S821 (= S221) binding
- R856 (≠ K258) binding
- K861 (≠ R263) binding
- E973 (= E378) 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
- 587 binding
- 1092 binding
5cjtA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isobutyryl-coenzyme a (see paper)
26% identity, 72% coverage: 21:498/665 of query aligns to 567:1059/1062 of 5cjtA
- active site: F569 (≠ Y23), Y750 (= Y177), H751 (= H178)
- binding cobalamin: F598 (= F51), L603 (≠ Q56), S621 (≠ V73), Q713 (≠ R141), H751 (= H178), E754 (= E181), A755 (= A182), G839 (≠ S270), R840 (≠ L271), E876 (= E310), A877 (= A311), T879 (≠ G313), H964 (≠ E398)
- binding isobutyryl-coenzyme a: R567 (= R21), F569 (≠ Y23), R593 (vs. gap), S648 (vs. gap), T650 (= T100), R699 (≠ N127), T701 (= T129), Q703 (= Q131), Y743 (≠ N170), Y750 (= Y177), H751 (= H178), S792 (= S221), F794 (= F223), R827 (≠ K258), K832 (≠ R263), H834 (≠ G265)
- binding guanosine-5'-diphosphate: E944 (= E378)
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
4xc6A Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, and mg (holo-icmf/gdp) (see paper)
26% identity, 72% coverage: 21:498/665 of query aligns to 570:1064/1067 of 4xc6A
- active site: F572 (≠ Y23), Y753 (= Y177), H754 (= H178)
- binding cobalamin: F601 (= F51), L606 (≠ Q56), S624 (≠ V73), Q716 (≠ R141), H754 (= H178), E757 (= E181), A758 (= A182), G842 (≠ S270), R843 (≠ L271), E879 (= E310), A880 (= A311), T882 (≠ G313), H967 (≠ E398)
- binding guanosine-5'-diphosphate: E947 (= E378)
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
5cjvA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isovaleryl-coenzyme a (see paper)
26% identity, 72% coverage: 21:498/665 of query aligns to 567:1058/1061 of 5cjvA
- active site: F569 (≠ Y23), Y750 (= Y177), H751 (= H178)
- binding cobalamin: F598 (= F51), L603 (≠ Q56), S621 (≠ V73), Q713 (≠ R141), E754 (= E181), A755 (= A182), G839 (≠ S270), R840 (≠ L271), E876 (= E310), A877 (= A311), T879 (≠ G313), H964 (≠ E398)
- binding guanosine-5'-diphosphate: E944 (= E378)
- binding Isovaleryl-coenzyme A: R567 (= R21), F569 (≠ Y23), R593 (vs. gap), S648 (vs. gap), T650 (= T100), R699 (≠ N127), T701 (= T129), Q703 (= Q131), Q713 (≠ R141), Y743 (≠ N170), H751 (= H178), S792 (= S221), F794 (= F223), K832 (≠ R263), H834 (≠ G265)
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 Isovaleryl-coenzyme A: 556, 558, 560
- binding magnesium ion: 203, 229, 242, 242, 288, 288
4xc7A Isobutyryl-coa mutase fused with bound butyryl-coa and without cobalamin or gdp (apo-icmf) (see paper)
25% identity, 72% coverage: 21:498/665 of query aligns to 564:1050/1053 of 4xc7A
- active site: F566 (≠ Y23), Y747 (= Y177), H748 (= H178)
- binding Butyryl Coenzyme A: R564 (= R21), F566 (≠ Y23), R590 (vs. gap), S645 (vs. gap), T647 (= T100), R696 (≠ N127), T698 (= T129), Y740 (≠ N170), S789 (= S221), F791 (= F223), R824 (≠ K258), K829 (≠ R263), H831 (≠ G265)
Sites not aligning to the query:
Query Sequence
>WP_011382757.1 AMB_RS01570 protein meaA
MTDKTAREAAAPSREKPWLFRTYSGHSSAAESNKLYRTNLTKGQTGLSIAFDLPTQTGYD
SDHVLAKGEVGKVGVPVCHLGDMMTLFEGIPLEKMNTSMTINAPAAWLLSLYIAAAERQG
ANRSVLNGTTQNDVIKEYLSRGTYIFAPQPSLKLTGDVIAFTYREVPKWNPMNVCSYHLQ
EAGATPEQELAYALATAVAVLDTVRPTVPAADFEQVVSRISFFVNAGIRFVTELCKMRAF
TELWDEICVGRYGVKDEKARRFRYGVQVNSLGLTEQQPENNVYRIVMEMLAVVLSKNARA
RAVQLPAWNEALGLPRPWDQQWSLRLQQIMAYETDLLEFGDIFDGSHEITRKVEALKEGA
REELARIDAMGGAVSAVESSYMKQKLVESNARRIGAIETGEQIVVGVNKWTETEPSPLTT
GEGSIMTVDPKAEAEQIERLKAFRAARDAKAVDKALAELRSAANEGRNVMEPSIAAAHAG
VTTGEWAQCLRDVFGEYRAPTGVARAAAEVKGEKMGAVRAKVEAVSAKLGRRVKILVGKP
GLDGHSNGAEQIAVRARDAGMEVVYEGIRLTPAQIVNAALEEGVHVVGLSILSGSHVPLV
TEVLERMKAAGLSDIPVVAGGIIPPEDEKVLLAAGCARIYTPKDYDITAIMGDIVALLDA
SPKAA
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