SitesBLAST
Comparing WP_029000812.1 NCBI__GCF_000430725.1:WP_029000812.1 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)
66% identity, 97% coverage: 14:712/717 of query aligns to 42:739/750 of P22033
- Q50 (≠ S22) binding malonyl-CoA
- I69 (≠ V41) to V: in MMAM; likely benign; dbSNP:rs115923556
- P86 (= P60) 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 (= G61) to E: in MMAM; mut0; dbSNP:rs1554160986
- R93 (= R67) to H: in MMAM; mut0; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918251
- G94 (= G68) to R: in MMAM; mut0; dbSNP:rs727504022; to V: in MMAM; mut- and mut0; dbSNP:rs535411418
- P95 (= P69) to R: in MMAM; mut0; dbSNP:rs190834116
- YPTM 96:99 (≠ QATM 70:73) binding malonyl-CoA
- Y100 (= Y74) 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 (= W79) to R: in MMAM; mut0; dbSNP:rs121918249
- TIRQY 106:110 (= TIRQY 80:84) binding malonyl-CoA
- R108 (= R82) to C: in MMAM; mut0; dbSNP:rs121918257; to G: in MMAM; mut-; to H: in MMAM; mut0; dbSNP:rs483352778
- Q109 (= Q83) to R: in MMAM; mut0; dbSNP:rs1461110052
- G133 (= G107) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253828
- A137 (= A111) to V: in MMAM; mut0; dbSNP:rs941483851
- D139 (= D113) to N: in MMAM; uncertain significance; dbSNP:rs879253829
- L140 (= L114) to P: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- A141 (= A115) to T: in MMAM; decreased protein expression; dbSNP:rs1554160730
- H143 (= H117) to Y: in MMAM; mut0
- G145 (= G119) to S: in MMAM; mut0
- S148 (= S122) to L: in MMAM; mut0; dbSNP:rs1300547552
- D156 (= D130) to N: in MMAM; mut-
- G158 (= G132) to V: in MMAM; mut0
- G161 (= G135) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; to V: in MMAM; decreased protein expression
- F174 (= F148) to S: in MMAM; mut0; dbSNP:rs864309733
- M186 (= M160) to V: in MMAM; mut-; dbSNP:rs148331800
- T187 (= T161) to S: in MMAM; mut0; dbSNP:rs879253830
- N189 (= N163) to I: in MMAM; mut-; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs200908035; to K: in MMAM; mut-; dbSNP:rs1561959114
- A191 (= A165) to E: in MMAM; mut- and mut0; affects proper folding; reduced protein level; decreased methylmalonyl-CoA mutase activity; dbSNP:rs760782399
- A197 (= A171) to E: in MMAM; mut0
- G203 (≠ A177) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs778702777
- E205 (= E179) natural variant: Missing (in MMAM; mut0; dbSNP:rs879253831)
- G215 (= G189) to C: in MMAM; mut- and mut0; dbSNP:rs121918258; to S: in MMAM; mut0; dbSNP:rs121918258
- TIQ 216:218 (= TIQ 190:192) binding malonyl-CoA
- Q218 (= Q192) to H: in MMAM; mut0 and mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability; dbSNP:rs1446389693
- N219 (= N193) to Y: in MMAM; mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; dbSNP:rs121918256
- R228 (= R202) binding malonyl-CoA; to Q: in MMAM; mut0; dbSNP:rs770810987
- T230 (= T204) to I: in MMAM; mut-; to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253833
- Y231 (= Y205) 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 (= K229) binding malonyl-CoA
- S262 (= S236) to N: in MMAM; mut0
- H265 (= H239) binding malonyl-CoA; to Y: in MMAM; mut-
- E276 (= E250) to D: in MMAM; uncertain significance; mut-; dbSNP:rs12175488
- L281 (= L255) to S: in MMAM; mut0; dbSNP:rs796052007
- G284 (= G258) to E: in MMAM; mut0; dbSNP:rs879253835; to R: in MMAM; mut0; dbSNP:rs761477436
- S288 (≠ V262) to P: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1179778233
- G291 (≠ A265) to E: in MMAM; mut0
- Q293 (≠ A267) to P: in MMAM; mut0
- RLS 304:306 (= RLS 278:280) binding malonyl-CoA
- L305 (= L279) to S: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554160246
- S306 (= S280) to F: in MMAM; mut0; dbSNP:rs1085307929
- W309 (= W283) to G: in MMAM; decreased protein expression
- G312 (= G286) to V: in MMAM; mut0; dbSNP:rs864309734
- Y316 (= Y290) 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 (= A298) to T: in MMAM; mut-; dbSNP:rs780387525
- R326 (= R300) to K: in MMAM; uncertain significance; dbSNP:rs758577372
- L328 (= L302) 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 (= S317) 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 (≠ M319) natural variant: Missing (in MMAM; mut0)
- L347 (= L320) to R: in MMAM; mut0; dbSNP:rs1026703654
- H350 (= H323) to Y: in MMAM; mut0; dbSNP:rs1407914109
- L358 (= L331) to P: in MMAM; mut0
- N366 (= N339) 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 (= R342) 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 (= T343) to P: in MMAM; mut0; dbSNP:rs368790885
- A377 (= A350) to E: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918250
- Q383 (= Q356) to H: in MMAM; mut0; to P: in MMAM; mut0
- H386 (= H359) to N: in MMAM; mut0; dbSNP:rs1554159937; to R: in MMAM; mut0; dbSNP:rs866933356
- T387 (= T360) 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 (= N361) to H: in MMAM; mut0; dbSNP:rs766010704; to K: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253840
- S389 (= S362) natural variant: Missing (in MMAM; mut0)
- I412 (= I385) natural variant: Missing (in MMAM; mut0)
- P424 (= P397) to L: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253842
- G426 (≠ A399) 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 (= G400) to D: in MMAM; mut0; dbSNP:rs753288303
- G454 (= G427) to E: in MMAM; mut0
- A499 (≠ P472) to T: in dbSNP:rs2229385
- I505 (≠ V478) to T: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- Q514 (= Q487) to E: in MMAM; uncertain significance; to K: in MMAM; decreased protein expression
- L518 (= L491) to P: in MMAM; mut0; dbSNP:rs864309738
- R532 (≠ A505) to H: in dbSNP:rs1141321
- A535 (≠ E508) to P: in MMAM; mut0; dbSNP:rs760183775
- A552 (= A525) to V: in MMAM; uncertain significance; dbSNP:rs879253845
- C560 (≠ A533) to Y: in MMAM; mut0; dbSNP:rs1238333040
- T566 (≠ S539) to R: in MMAM; mut0
- F573 (= F546) 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 (= Y560) to C: in MMAM; mut-
- I597 (≠ W570) to R: in MMAM; no changed in protein expression; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554158951
- P615 (= P588) 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 (= R589) to C: in MMAM; mut0; dbSNP:rs765284825
- L617 (≠ V590) to R: in MMAM; mut0; dbSNP:rs1554158775
- K621 (= K594) to N: in MMAM; mut0
- G623 (= G596) to R: in MMAM; mut0; dbSNP:rs121918254
- Q624 (= Q597) to R: in MMAM; no effect on protein abundance; dbSNP:rs768521956
- D625 (= D598) 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 (= G599) to C: in MMAM; mut-; dbSNP:rs982110849
- H627 (= H600) binding axial binding residue; to R: in MMAM; mut0; dbSNP:rs372486357
- G630 (= G603) to E: in MMAM; mut0; dbSNP:rs143023066
- V633 (= V606) 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 (≠ A610) to E: in MMAM; mut-; to R: in MMAM; mut0; dbSNP:rs781501004
- F638 (= F611) to I: in MMAM; mut0
- D640 (= D613) to Y: in MMAM; mut0; dbSNP:rs865815395
- G642 (= G615) to R: in MMAM; mut-; dbSNP:rs747897332
- G648 (= G621) 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 (= V642) to E: in MMAM; mut0; dbSNP:rs1360470463
- I671 (= I644) to V: in dbSNP:rs8589
- L674 (= L647) to F: in MMAM; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1164271240
- H678 (= H651) to R: in MMAM; mut-; dbSNP:rs147094927
- E684 (≠ A657) natural variant: E -> EL (in MMAM; mut-)
- L685 (≠ I658) to R: in MMAM; mut-; dbSNP:rs864309739
- R694 (≠ A667) 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 (≠ F673) 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 (= G676) to R: in MMAM; mut0; dbSNP:rs121918255
- G717 (= G690) 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 (= G696) 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)
8dyjB Crystal structure of human methylmalonyl-coa mutase in complex with adp and cob(ii)alamin (see paper)
66% identity, 97% coverage: 14:712/717 of query aligns to 6:703/708 of 8dyjB
- binding adenosine-5'-diphosphate: Y74 (= Y84), T151 (= T161), R192 (= R202), Y228 (= Y238), H229 (= H239), F272 (= F282), Q316 (= Q325), N352 (= N361), E356 (= E365), L360 (= L369), P361 (= P370)
- binding cobalamin: F102 (= F112), L104 (= L114), H107 (= H117), A124 (= A134), V191 (= V201), R192 (= R202), H229 (= H239), E232 (= E242), G319 (= G328), W320 (= W329), E356 (= E365), G359 (≠ A368), L360 (= L369), G590 (= G599), H591 (= H600), D592 (= D601), R593 (= R602), G594 (= G603), I598 (≠ V607), S636 (= S645), L638 (= L647), A640 (= A649), G666 (= G675), G667 (= G676), V668 (= V677), F686 (≠ Y695), G687 (= G696), T690 (= T699)
2xiqA Crystal structure of human methylmalonyl-coa mutase in complex with adenosylcobalamin and malonyl-coa (see paper)
66% identity, 97% coverage: 14:712/717 of query aligns to 7:704/714 of 2xiqA
- active site: Y75 (= Y84), Y229 (= Y238), H230 (= H239), K586 (= K594), D590 (= D598), H592 (= H600)
- binding cobalamin: Y75 (= Y84), L105 (= L114), H108 (= H117), A125 (= A134), R193 (= R202), E233 (= E242), G320 (= G328), W321 (= W329), E357 (= E365), G360 (≠ A368), L361 (= L369), G591 (= G599), H592 (= H600), D593 (= D601), R594 (= R602), G595 (= G603), I599 (≠ V607), G635 (= G643), S637 (= S645), L639 (= L647), A641 (= A649), G667 (= G675), G668 (= G676), F687 (≠ Y695), G688 (= G696), T691 (= T699)
- binding malonyl-coenzyme a: Y61 (≠ Q70), T63 (= T72), M64 (= M73), R68 (= R77), T71 (= T80), R73 (= R82), Y75 (= Y84), S150 (= S159), T152 (= T161), T181 (= T190), R193 (= R202), K220 (= K229), H230 (= H239), R269 (= R278), S271 (= S280), F273 (= F282), R313 (= R321), A314 (≠ T322), H315 (= H323), Q317 (= Q325), Q348 (= Q356)
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: 14:712/717 of query aligns to 7:681/689 of 8gjuJ
- binding coenzyme a: Y61 (≠ Q70), T63 (= T72), R68 (= R77), T71 (= T80), R73 (= R82), S150 (= S159), T152 (= T161), T181 (= T190), Q183 (= Q192), N222 (= N231), R269 (= R278), S271 (= S280), R313 (= R321), A314 (≠ T322), H315 (= H323), Q348 (= Q356)
P11653 Methylmalonyl-CoA mutase large subunit; MCM-alpha; EC 5.4.99.2 from Propionibacterium freudenreichii subsp. shermanii (see 4 papers)
60% identity, 100% coverage: 1:715/717 of query aligns to 1:725/728 of P11653
- M1 (= M1) modified: Initiator methionine, Removed
- Y75 (≠ Q70) binding (R)-methylmalonyl-CoA
- M78 (= M73) binding (R)-methylmalonyl-CoA
- R82 (= R77) binding (R)-methylmalonyl-CoA
- T85 (= T80) binding (R)-methylmalonyl-CoA
- R87 (= R82) binding (R)-methylmalonyl-CoA
- Y89 (= Y84) binding (R)-methylmalonyl-CoA; mutation to F: Does not significantly affect affinity for succiny-CoA, but kcat is lowered about 580-fold.
- S114 (= S109) binding (R)-methylmalonyl-CoA
- F117 (= F112) binding cob(II)alamin
- A139 (= A134) binding cob(II)alamin
- T195 (= T190) binding (R)-methylmalonyl-CoA
- Q197 (= Q192) binding (R)-methylmalonyl-CoA
- V206 (= V201) binding cob(II)alamin
- R207 (= R202) binding (R)-methylmalonyl-CoA; binding cob(II)alamin
- H244 (= H239) binding (R)-methylmalonyl-CoA
- R283 (= R278) binding (R)-methylmalonyl-CoA
- S285 (= S280) binding (R)-methylmalonyl-CoA
- G333 (= G328) binding cob(II)alamin
- E370 (= E365) binding cob(II)alamin
- A373 (= A368) binding cob(II)alamin
- G609 (= G599) binding cob(II)alamin
- H610 (= H600) binding axial binding residue
- D611 (= D601) binding cob(II)alamin
- R612 (= R602) binding cob(II)alamin
- S655 (= S645) binding cob(II)alamin
- L657 (= L647) binding cob(II)alamin
- G686 (= G676) binding cob(II)alamin
- T709 (= T699) binding cob(II)alamin
6reqA Methylmalonyl-coa mutase, 3-carboxypropyl-coa inhibitor complex (see paper)
62% identity, 95% coverage: 33:715/717 of query aligns to 37:724/727 of 6reqA
- active site: Y88 (= Y84), Y242 (= Y238), H243 (= H239), K603 (= K594), D607 (= D598), H609 (= H600)
- binding 3-carboxypropyl-coenzyme a: Y74 (≠ Q70), T76 (= T72), M77 (= M73), F80 (≠ V76), R81 (= R77), T84 (= T80), R86 (= R82), Y88 (= Y84), S113 (= S109), S163 (= S159), T165 (= T161), T194 (= T190), R206 (= R202), H243 (= H239), R282 (= R278), S284 (= S280), F286 (= F282), H327 (= H323), Q329 (= Q325), Q360 (= Q356)
- binding cobalamin: Y88 (= Y84), F116 (= F112), L118 (= L114), H121 (= H117), A138 (= A134), R206 (= R202), E246 (= E242), G332 (= G328), W333 (= W329), E369 (= E365), A370 (= A366), A372 (= A368), G608 (= G599), H609 (= H600), D610 (= D601), R611 (= R602), G612 (= G603), I616 (≠ V607), Y620 (≠ F611), S654 (= S645), L656 (= L647), G658 (≠ A649), G684 (= G675), G685 (= G676), Y704 (= Y695), T705 (≠ G696), T708 (= T699)
4reqA Methylmalonyl-coa mutase substrate complex (see paper)
62% identity, 95% coverage: 33:715/717 of query aligns to 36:723/726 of 4reqA
- active site: Y87 (= Y84), Y241 (= Y238), H242 (= H239), K602 (= K594), D606 (= D598), H608 (= H600)
- binding cobalamin: Y87 (= Y84), L117 (= L114), A137 (= A134), V204 (= V201), R205 (= R202), H242 (= H239), E245 (= E242), G331 (= G328), W332 (= W329), E368 (= E365), A369 (= A366), A371 (= A368), L372 (= L369), G607 (= G599), H608 (= H600), D609 (= D601), R610 (= R602), G611 (= G603), I615 (≠ V607), S653 (= S645), L655 (= L647), G683 (= G675), G684 (= G676), V685 (= V677), Y703 (= Y695), T704 (≠ G696), T707 (= T699)
- binding methylmalonyl-coenzyme a: Y73 (≠ Q70), M76 (= M73), F79 (≠ V76), R80 (= R77), T83 (= T80), R85 (= R82), Y87 (= Y84), S112 (= S109), S162 (= S159), T164 (= T161), T193 (= T190), R205 (= R202), N234 (= N231), Y241 (= Y238), H242 (= H239), R281 (= R278), S283 (= S280), F285 (= F282), H326 (= H323), Q328 (= Q325), Q359 (= Q356), S360 (= S357)
- binding succinyl-coenzyme a: Y73 (≠ Q70), M76 (= M73), F79 (≠ V76), R80 (= R77), T83 (= T80), R85 (= R82), Y87 (= Y84), S162 (= S159), T164 (= T161), T193 (= T190), Q195 (= Q192), R205 (= R202), N234 (= N231), Y241 (= Y238), H242 (= H239), R281 (= R278), S283 (= S280), F285 (= F282), R324 (= R321), H326 (= H323), Q359 (= Q356)
7reqA Methylmalonyl-coa mutase, 2-carboxypropyl-coa inhibitor complex (see paper)
62% identity, 95% coverage: 33:715/717 of query aligns to 35:722/725 of 7reqA
- active site: Y86 (= Y84), Y240 (= Y238), H241 (= H239), K601 (= K594), D605 (= D598), H607 (= H600)
- binding 2-carboxypropyl-coenzyme a: Y72 (≠ Q70), T74 (= T72), M75 (= M73), F78 (≠ V76), R79 (= R77), T82 (= T80), R84 (= R82), Y86 (= Y84), S161 (= S159), T163 (= T161), T192 (= T190), R204 (= R202), H241 (= H239), R280 (= R278), S282 (= S280), F284 (= F282), H325 (= H323), Q358 (= Q356)
- binding cobalamin: Y86 (= Y84), L116 (= L114), A136 (= A134), R204 (= R202), E244 (= E242), G330 (= G328), W331 (= W329), E367 (= E365), A368 (= A366), A370 (= A368), G606 (= G599), H607 (= H600), D608 (= D601), R609 (= R602), G610 (= G603), I614 (≠ V607), S652 (= S645), L654 (= L647), G682 (= G675), G683 (= G676), Y702 (= Y695), T703 (≠ G696), T706 (= T699)
3reqA Methylmalonyl-coa mutase, substrate-free state (poor quality structure) (see paper)
62% identity, 95% coverage: 33:715/717 of query aligns to 35:722/725 of 3reqA
- active site: Y86 (= Y84), Y240 (= Y238), H241 (= H239), K601 (= K594), D605 (= D598), H607 (= H600)
- binding adenosine: Y86 (= Y84), Y240 (= Y238), E244 (= E242), G330 (= G328)
- binding cobalamin: L116 (= L114), V203 (= V201), R204 (= R202), E244 (= E242), G330 (= G328), W331 (= W329), A368 (= A366), G606 (= G599), H607 (= H600), D608 (= D601), R609 (= R602), G610 (= G603), I614 (≠ V607), G650 (= G643), S652 (= S645), L654 (= L647), G682 (= G675), G683 (= G676), Y702 (= Y695), T703 (≠ G696), P704 (= P697), T706 (= T699)
2reqA Methylmalonyl-coa mutase, non-productive coa complex, in open conformation representing substrate-free state (see paper)
62% identity, 95% coverage: 33:715/717 of query aligns to 35:722/725 of 2reqA
- active site: Y86 (= Y84), Y240 (= Y238), H241 (= H239), K601 (= K594), D605 (= D598), H607 (= H600)
- binding cobalamin: V203 (= V201), R204 (= R202), E244 (= E242), A245 (= A243), W331 (= W329), A368 (= A366), G606 (= G599), H607 (= H600), D608 (= D601), R609 (= R602), G610 (= G603), I614 (≠ V607), G650 (= G643), S652 (= S645), L654 (= L647), A655 (= A648), G682 (= G675), G683 (= G676), Y702 (= Y695), T703 (≠ G696), T706 (= T699)
- binding coenzyme a: Y72 (≠ Q70), R79 (= R77), K318 (= K316)
5reqA Methylmalonyl-coa mutase, y89f mutant, substrate complex (see paper)
62% identity, 95% coverage: 33:715/717 of query aligns to 35:722/725 of 5reqA
- active site: F86 (≠ Y84), Y240 (= Y238), H241 (= H239), K601 (= K594), D605 (= D598), H607 (= H600)
- binding cobalamin: L116 (= L114), A136 (= A134), R204 (= R202), H241 (= H239), E244 (= E242), G330 (= G328), W331 (= W329), E367 (= E365), A368 (= A366), A370 (= A368), G606 (= G599), H607 (= H600), D608 (= D601), R609 (= R602), G610 (= G603), I614 (≠ V607), S652 (= S645), L654 (= L647), G682 (= G675), G683 (= G676), V684 (= V677), Y702 (= Y695), T703 (≠ G696), T706 (= T699)
- binding methylmalonyl(carbadethia)-coenzyme a: Y72 (≠ Q70), T74 (= T72), M75 (= M73), R79 (= R77), T82 (= T80), R84 (= R82), F86 (≠ Y84), S111 (= S109), S161 (= S159), T163 (= T161), T192 (= T190), Q194 (= Q192), R204 (= R202), N233 (= N231), H241 (= H239), R280 (= R278), S282 (= S280), F284 (= F282), T324 (= T322), H325 (= H323), Q358 (= Q356), S359 (= S357)
- binding succinyl(carbadethia)-coenzyme a: Y72 (≠ Q70), T74 (= T72), M75 (= M73), R79 (= R77), T82 (= T80), R84 (= R82), F86 (≠ Y84), S161 (= S159), T163 (= T161), T192 (= T190), R204 (= R202), N233 (= N231), H241 (= H239), R280 (= R278), S282 (= S280), F284 (= F282), H325 (= H323), Q358 (= Q356)
1e1cA Methylmalonyl-coa mutase h244a mutant (see paper)
62% identity, 95% coverage: 33:715/717 of query aligns to 37:724/727 of 1e1cA
- active site: Y88 (= Y84), Y242 (= Y238), A243 (≠ H239), K603 (= K594), D607 (= D598), H609 (= H600)
- binding cobalamin: Y88 (= Y84), L118 (= L114), H121 (= H117), A138 (= A134), V205 (= V201), R206 (= R202), E246 (= E242), G332 (= G328), W333 (= W329), E369 (= E365), A370 (= A366), A372 (= A368), L373 (= L369), G608 (= G599), H609 (= H600), D610 (= D601), R611 (= R602), G612 (= G603), I616 (≠ V607), Y620 (≠ F611), S654 (= S645), L656 (= L647), G684 (= G675), G685 (= G676), V686 (= V677), Y704 (= Y695), T705 (≠ G696), T708 (= T699), S713 (= S704)
- binding desulfo-coenzyme a: Y74 (≠ Q70), M77 (= M73), F80 (≠ V76), R81 (= R77), T84 (= T80), R86 (= R82), S113 (= S109), S163 (= S159), T165 (= T161), T194 (= T190), R282 (= R278), S284 (= S280), H327 (= H323), Q360 (= Q356)
6oxdA Structure of mycobacterium tuberculosis methylmalonyl-coa mutase with adenosyl cobalamin (see paper)
62% identity, 95% coverage: 31:712/717 of query aligns to 43:728/736 of 6oxdA
- active site: Y100 (= Y84), Y254 (= Y238), H255 (= H239), K610 (= K594), D614 (= D598), H616 (= H600)
- binding cobalamin: Y100 (= Y84), L130 (= L114), H133 (= H117), A150 (= A134), R218 (= R202), E258 (= E242), G344 (= G328), W345 (= W329), E381 (= E365), A382 (= A366), A384 (= A368), L385 (= L369), G615 (= G599), H616 (= H600), D617 (= D601), R618 (= R602), S661 (= S645), L663 (= L647), A665 (= A649), G691 (= G675), G692 (= G676), F711 (≠ Y695), P712 (≠ G696), T715 (= T699)
- binding Itaconyl coenzyme A: Y86 (≠ Q70), T88 (= T72), M89 (= M73), Q93 (≠ R77), T96 (= T80), R98 (= R82), Y100 (= Y84), S175 (= S159), T177 (= T161), T206 (= T190), R218 (= R202), H255 (= H239), R294 (= R278), S296 (= S280), F298 (= F282), R337 (= R321), T338 (= T322), H339 (= H323), Q341 (= Q325), Q372 (= Q356)
4r3uA Crystal structure of 2-hydroxyisobutyryl-coa mutase (see paper)
46% identity, 71% coverage: 41:550/717 of query aligns to 45:556/557 of 4r3uA
- active site: I89 (≠ Y84), Y243 (= Y238), H244 (= H239)
- binding 3-hydroxybutanoyl-coenzyme a: Y75 (≠ Q70), T77 (= T72), M78 (= M73), R82 (= R77), T85 (= T80), R87 (= R82), I89 (≠ Y84), D116 (≠ A111), S164 (= S159), T166 (= T161), T195 (= T190), Q197 (= Q192), R234 (≠ K229), N236 (= N231), N239 (≠ S234), Y243 (= Y238), H244 (= H239), R283 (= R278), F287 (= F282), R327 (= R321), F328 (≠ T322), H329 (= H323), Q331 (= Q325), Q362 (= Q356)
- 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 (≠ Q70), T77 (= T72), M78 (= M73), R82 (= R77), T85 (= T80), R87 (= R82), I89 (≠ Y84), D116 (≠ A111), S164 (= S159), T166 (= T161), T195 (= T190), Q197 (= Q192), R234 (≠ K229), N236 (= N231), N239 (≠ S234), H244 (= H239), R283 (= R278), F287 (= F282), R327 (= R321), F328 (≠ T322), H329 (= H323), Q331 (= Q325), Q362 (= Q356)
- binding cobalamin: D116 (≠ A111), M119 (≠ L114), E139 (≠ A134), Q207 (≠ R202), E209 (≠ T204), E247 (= E242), A334 (≠ G328), E371 (= E365), A372 (= A366), A374 (= A368)
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: 41:550/717 of query aligns to 46:557/562 of I3VE77
- YPTM 76:79 (≠ QATM 70:73) binding (3S)-3-hydroxybutanoyl-CoA
- TMR 86:88 (≠ TIR 80:82) binding (3S)-3-hydroxybutanoyl-CoA
- I90 (≠ Y84) 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 (≠ A111) 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 (≠ TIQ 190:192) binding (3S)-3-hydroxybutanoyl-CoA
- R235 (≠ K229) binding (3S)-3-hydroxybutanoyl-CoA
- N240 (≠ S234) binding (3S)-3-hydroxybutanoyl-CoA
- H245 (= H239) binding (3S)-3-hydroxybutanoyl-CoA
- R284 (= R278) binding (3S)-3-hydroxybutanoyl-CoA
5cjtA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isobutyryl-coenzyme a (see paper)
34% identity, 69% coverage: 57:553/717 of query aligns to 543:1062/1062 of 5cjtA
- active site: F569 (≠ Y84), Y750 (= Y238), H751 (= H239)
- binding cobalamin: F598 (= F112), L603 (≠ H117), S621 (≠ A134), Q713 (≠ R202), H751 (= H239), E754 (= E242), A755 (= A243), G839 (= G328), R840 (≠ W329), E876 (= E365), A877 (= A366), T879 (≠ A368), H964 (≠ D453)
- binding isobutyryl-coenzyme a: F556 (≠ Q70), F558 (≠ T72), R560 (≠ Y74), R567 (= R82), F569 (≠ Y84), R593 (≠ G107), S648 (= S159), T650 (= T161), R699 (≠ S188), T701 (= T190), Q703 (= Q192), Y743 (≠ N231), Y750 (= Y238), H751 (= H239), S792 (= S280), F794 (= F282), R827 (≠ K316), K832 (≠ R321), H834 (= H323)
- binding guanosine-5'-diphosphate: E944 (≠ D433)
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
4xc6A Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, and mg (holo-icmf/gdp) (see paper)
34% identity, 69% coverage: 57:553/717 of query aligns to 546:1067/1067 of 4xc6A
- active site: F572 (≠ Y84), Y753 (= Y238), H754 (= H239)
- binding cobalamin: F601 (= F112), L606 (≠ H117), S624 (≠ A134), Q716 (≠ R202), H754 (= H239), E757 (= E242), A758 (= A243), G842 (= G328), R843 (≠ W329), E879 (= E365), A880 (= A366), T882 (≠ A368), H967 (≠ D453)
- binding guanosine-5'-diphosphate: E947 (≠ D433)
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
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)
34% identity, 69% coverage: 57:553/717 of query aligns to 572:1093/1093 of Q1LRY0
- F587 (≠ T72) binding substrate
- F598 (≠ Y84) 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 (≠ G107) binding substrate
- R728 (≠ S188) binding substrate
- Y772 (≠ N231) binding substrate
- S821 (= S280) binding substrate
- R856 (≠ K316) binding substrate
- K861 (≠ R321) binding substrate
- E973 (≠ D433) binding GTP
- N1092 (≠ D552) 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
8sslA Isobutyryl-coa mutase fused q341a in the presence of gtp (see paper)
34% identity, 69% coverage: 57:553/717 of query aligns to 551:1072/1072 of 8sslA
Sites not aligning to the query:
- binding guanosine-5'-diphosphate: 200, 201, 202, 241, 244, 337, 339, 374, 375, 376
- binding magnesium ion: 201, 241
5cjwA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate pivalyl-coenzyme a (see paper)
34% identity, 69% coverage: 57:553/717 of query aligns to 545:1063/1063 of 5cjwA
- active site: F571 (≠ Y84), Y752 (= Y238), H753 (= H239)
- binding pivalyl-coenzyme A: F558 (≠ Q70), F560 (≠ T72), R562 (≠ Y74), R569 (= R82), F571 (≠ Y84), R595 (≠ G107), S650 (= S159), T652 (= T161), R701 (≠ S188), T703 (= T190), Q705 (= Q192), Y745 (≠ N231), Y752 (= Y238), H753 (= H239), S794 (= S280), F796 (= F282), R829 (≠ K316), K834 (≠ R321), H836 (= H323)
- binding cobalamin: F600 (= F112), L605 (≠ H117), S623 (≠ A134), Q715 (≠ R202), H753 (= H239), E756 (= E242), A757 (= A243), G841 (= G328), R842 (≠ W329), E878 (= E365), A879 (= A366), T881 (≠ A368), H966 (≠ D453)
- binding guanosine-5'-diphosphate: N1062 (≠ D552)
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
Query Sequence
>WP_029000812.1 NCBI__GCF_000430725.1:WP_029000812.1
MSSAPEFNRATLQQWAQAATKSAPGGDLNALTWTTPEGIAVKPLYTGADVEGLPFTDTLP
GFEPFIRGPQATMYAVRPWTIRQYAGFSTAEESNAFYRKALAAGGQGVSVAFDLATHRGY
DSDHPRVTGDVGKAGVAIDSVEDMKILFDGIPLDKVSVSMTMNGAVLPVLAGYVVAAEEQ
GVSQDKLSGTIQNDILKEFMVRNTYIYPPEPSMRIIGDIIEYTAKNMPKFNSISISGYHM
QEAGANQALELAFTLADGKEYVKTALAKGLDVDEFAGRLSFFWAIGMNFYLEIAKMRAAR
LLWCRIMKGFDAKKPKSLMLRTHCQTSGWSLTEQDPYNNVVRTTIEAMAAVFGGTQSLHT
NSLDEAIALPTEFSSRIARNTQLIIQEETHITSVVDPWAGSYMMEKLTQEMADKAWAIIE
EVEAMGGMTKAVDSGWAKLKIEASAAEKQARIDSGKDVIVGVNKYKLAKEDPVEILEVDN
VKVRDAQIARLQQIKATRDGQKVQAALEALTAAARESSGNLLGLAIDAIRARATVGEVSD
ALEVVFGRHRADIQKVTGVYAAAYDSAEGWDKLRGEIEAFAQEAGRRPRVMIAKLGQDGH
DRGAKVVATAFADLGFDVDMGPLFQTPEECARQAIENDVHAVGISTLAAGHKTLVPAIIA
ELRRQGADDIIVFVGGVIPQQDYGFLFDAGVKGVYGPGTPIPASAKDVLEQIRAAQR
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