SitesBLAST
Comparing Echvi_4683 FitnessBrowser__Cola:Echvi_4683 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
2xiqA Crystal structure of human methylmalonyl-coa mutase in complex with adenosylcobalamin and malonyl-coa (see paper)
66% identity, 95% coverage: 31:679/685 of query aligns to 52:701/714 of 2xiqA
- active site: Y75 (= Y54), Y229 (= Y208), H230 (= H209), K586 (= K564), D590 (= D568), H592 (= H570)
- binding cobalamin: Y75 (= Y54), L105 (= L84), H108 (= H87), A125 (= A104), R193 (= R172), E233 (= E212), G320 (= G298), W321 (= W299), E357 (= E335), G360 (≠ A338), L361 (= L339), G591 (= G569), H592 (= H570), D593 (= D571), R594 (= R572), G595 (= G573), I599 (= I577), G635 (= G613), S637 (= S615), L639 (= L617), A641 (≠ G619), G667 (= G645), G668 (= G646), F687 (= F665), G688 (= G666), T691 (= T669)
- binding malonyl-coenzyme a: Y61 (= Y40), T63 (= T42), M64 (= M43), R68 (= R47), T71 (= T50), R73 (= R52), Y75 (= Y54), S150 (= S129), T152 (= T131), T181 (= T160), R193 (= R172), K220 (≠ A199), H230 (= H209), R269 (= R248), S271 (= S250), F273 (= F252), R313 (= R291), A314 (= A292), H315 (= H293), Q317 (= Q295), Q348 (= Q326)
P22033 Methylmalonyl-CoA mutase, mitochondrial; MCM; Methylmalonyl-CoA isomerase; EC 5.4.99.2 from Homo sapiens (Human) (see 28 papers)
66% identity, 95% coverage: 31:679/685 of query aligns to 87:736/750 of P22033
- G87 (= G31) to E: in MMAM; mut0; dbSNP:rs1554160986
- R93 (= R37) to H: in MMAM; mut0; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918251
- G94 (= G38) to R: in MMAM; mut0; dbSNP:rs727504022; to V: in MMAM; mut- and mut0; dbSNP:rs535411418
- P95 (= P39) to R: in MMAM; mut0; dbSNP:rs190834116
- YPTM 96:99 (≠ YSTM 40:43) binding
- Y100 (= Y44) 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 (= W49) to R: in MMAM; mut0; dbSNP:rs121918249
- TIRQY 106:110 (≠ TLRQY 50:54) binding
- R108 (= R52) to C: in MMAM; mut0; dbSNP:rs121918257; to G: in MMAM; mut-; to H: in MMAM; mut0; dbSNP:rs483352778
- Q109 (= Q53) to R: in MMAM; mut0; dbSNP:rs1461110052
- G133 (= G77) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253828
- A137 (= A81) to V: in MMAM; mut0; dbSNP:rs941483851
- D139 (= D83) to N: in MMAM; uncertain significance; dbSNP:rs879253829
- L140 (= L84) to P: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- A141 (= A85) to T: in MMAM; decreased protein expression; dbSNP:rs1554160730
- H143 (= H87) to Y: in MMAM; mut0
- G145 (= G89) to S: in MMAM; mut0
- S148 (= S92) to L: in MMAM; mut0; dbSNP:rs1300547552
- D156 (= D100) to N: in MMAM; mut-
- G158 (= G102) to V: in MMAM; mut0
- G161 (= G105) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; to V: in MMAM; decreased protein expression
- F174 (= F118) to S: in MMAM; mut0; dbSNP:rs864309733
- M186 (= M130) to V: in MMAM; mut-; dbSNP:rs148331800
- T187 (= T131) to S: in MMAM; mut0; dbSNP:rs879253830
- N189 (= N133) to I: in MMAM; mut-; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs200908035; to K: in MMAM; mut-; dbSNP:rs1561959114
- A191 (= A135) to E: in MMAM; mut- and mut0; affects proper folding; reduced protein level; decreased methylmalonyl-CoA mutase activity; dbSNP:rs760782399
- A197 (= A141) to E: in MMAM; mut0
- G203 (≠ A147) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs778702777
- E205 (= E149) natural variant: Missing (in MMAM; mut0; dbSNP:rs879253831)
- G215 (= G159) to C: in MMAM; mut- and mut0; dbSNP:rs121918258; to S: in MMAM; mut0; dbSNP:rs121918258
- TIQ 216:218 (= TIQ 160:162) binding
- Q218 (= Q162) to H: in MMAM; mut0 and mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability; dbSNP:rs1446389693
- N219 (= N163) to Y: in MMAM; mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; dbSNP:rs121918256
- R228 (= R172) binding ; to Q: in MMAM; mut0; dbSNP:rs770810987
- T230 (= T174) to I: in MMAM; mut-; to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253833
- Y231 (= Y175) 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 (≠ A199) binding
- S262 (= S206) to N: in MMAM; mut0
- H265 (= H209) binding ; to Y: in MMAM; mut-
- E276 (= E220) to D: in MMAM; uncertain significance; mut-; dbSNP:rs12175488
- L281 (= L225) to S: in MMAM; mut0; dbSNP:rs796052007
- G284 (= G228) to E: in MMAM; mut0; dbSNP:rs879253835; to R: in MMAM; mut0; dbSNP:rs761477436
- S288 (≠ V232) to P: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1179778233
- G291 (= G235) to E: in MMAM; mut0
- Q293 (≠ K237) to P: in MMAM; mut0
- RLS 304:306 (= RLS 248:250) binding
- L305 (= L249) to S: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554160246
- S306 (= S250) to F: in MMAM; mut0; dbSNP:rs1085307929
- W309 (= W253) to G: in MMAM; decreased protein expression
- G312 (= G256) to V: in MMAM; mut0; dbSNP:rs864309734
- Y316 (≠ F260) 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 (= A268) to T: in MMAM; mut-; dbSNP:rs780387525
- R326 (= R270) to K: in MMAM; uncertain significance; dbSNP:rs758577372
- L328 (= L272) 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 (= S287) 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 (≠ K289) natural variant: Missing (in MMAM; mut0)
- L347 (= L290) to R: in MMAM; mut0; dbSNP:rs1026703654
- H350 (= H293) to Y: in MMAM; mut0; dbSNP:rs1407914109
- L358 (= L301) to P: in MMAM; mut0
- N366 (= N309) 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 (= R312) 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 (= T313) to P: in MMAM; mut0; dbSNP:rs368790885
- A377 (= A320) to E: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918250
- Q383 (= Q326) to H: in MMAM; mut0; to P: in MMAM; mut0
- H386 (= H329) to N: in MMAM; mut0; dbSNP:rs1554159937; to R: in MMAM; mut0; dbSNP:rs866933356
- T387 (= T330) 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 (= N331) to H: in MMAM; mut0; dbSNP:rs766010704; to K: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253840
- S389 (≠ A332) natural variant: Missing (in MMAM; mut0)
- I412 (≠ L355) natural variant: Missing (in MMAM; mut0)
- P424 (= P367) to L: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253842
- G426 (= G369) 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 (= G370) to D: in MMAM; mut0; dbSNP:rs753288303
- G454 (= G397) to E: in MMAM; mut0
- A499 (≠ D442) to T: in dbSNP:rs2229385
- I505 (≠ V448) to T: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- Q514 (= Q457) to E: in MMAM; uncertain significance; to K: in MMAM; decreased protein expression
- L518 (= L461) to P: in MMAM; mut0; dbSNP:rs864309738
- R532 (= R475) to H: in dbSNP:rs1141321
- A535 (≠ E478) to P: in MMAM; mut0; dbSNP:rs760183775
- A552 (≠ S495) to V: in MMAM; uncertain significance; dbSNP:rs879253845
- C560 (≠ A503) to Y: in MMAM; mut0; dbSNP:rs1238333040
- T566 (≠ S509) to R: in MMAM; mut0
- F573 (≠ Y516) 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 (= Y530) to C: in MMAM; mut-
- I597 (≠ F540) to R: in MMAM; no changed in protein expression; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554158951
- P615 (= P558) 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 (= R559) to C: in MMAM; mut0; dbSNP:rs765284825
- L617 (≠ I560) to R: in MMAM; mut0; dbSNP:rs1554158775
- K621 (= K564) to N: in MMAM; mut0
- G623 (= G566) to R: in MMAM; mut0; dbSNP:rs121918254
- Q624 (= Q567) to R: in MMAM; no effect on protein abundance; dbSNP:rs768521956
- D625 (= D568) 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 (= G569) to C: in MMAM; mut-; dbSNP:rs982110849
- H627 (= H570) binding axial binding residue; to R: in MMAM; mut0; dbSNP:rs372486357
- G630 (= G573) to E: in MMAM; mut0; dbSNP:rs143023066
- V633 (= V576) 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 (= G580) to E: in MMAM; mut-; to R: in MMAM; mut0; dbSNP:rs781501004
- F638 (≠ M581) to I: in MMAM; mut0
- D640 (= D583) to Y: in MMAM; mut0; dbSNP:rs865815395
- G642 (= G585) to R: in MMAM; mut-; dbSNP:rs747897332
- G648 (= G591) 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 (= V612) to E: in MMAM; mut0; dbSNP:rs1360470463
- I671 (≠ A614) to V: in dbSNP:rs8589
- L674 (= L617) to F: in MMAM; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1164271240
- H678 (= H621) to R: in MMAM; mut-; dbSNP:rs147094927
- E684 (≠ Q627) natural variant: E -> EL (in MMAM; mut-)
- L685 (= L628) to R: in MMAM; mut-; dbSNP:rs864309739
- R694 (= R637) 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 (≠ V643) 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 (= G646) to R: in MMAM; mut0; dbSNP:rs121918255
- G717 (= G660) 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 (= G666) 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
- 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, 95% coverage: 31:679/685 of query aligns to 51:700/708 of 8dyjB
- binding adenosine-5'-diphosphate: Y74 (= Y54), T151 (= T131), R192 (= R172), Y228 (= Y208), H229 (= H209), F272 (= F252), Q316 (= Q295), N352 (= N331), E356 (= E335), L360 (= L339), P361 (= P340)
- binding cobalamin: F102 (= F82), L104 (= L84), H107 (= H87), A124 (= A104), V191 (= V171), R192 (= R172), H229 (= H209), E232 (= E212), G319 (= G298), W320 (= W299), E356 (= E335), G359 (≠ A338), L360 (= L339), G590 (= G569), H591 (= H570), D592 (= D571), R593 (= R572), G594 (= G573), I598 (= I577), S636 (= S615), L638 (= L617), A640 (≠ G619), G666 (= G645), G667 (= G646), V668 (= V647), F686 (= F665), G687 (= G666), T690 (= T669)
6reqA Methylmalonyl-coa mutase, 3-carboxypropyl-coa inhibitor complex (see paper)
63% identity, 96% coverage: 24:682/685 of query aligns to 58:721/727 of 6reqA
- active site: Y88 (= Y54), Y242 (= Y208), H243 (= H209), K603 (= K564), D607 (= D568), H609 (= H570)
- binding 3-carboxypropyl-coenzyme a: Y74 (= Y40), T76 (= T42), M77 (= M43), F80 (≠ T46), R81 (= R47), T84 (= T50), R86 (= R52), Y88 (= Y54), S113 (= S79), S163 (= S129), T165 (= T131), T194 (= T160), R206 (= R172), H243 (= H209), R282 (= R248), S284 (= S250), F286 (= F252), H327 (= H293), Q329 (= Q295), Q360 (= Q326)
- binding cobalamin: Y88 (= Y54), F116 (= F82), L118 (= L84), H121 (= H87), A138 (= A104), R206 (= R172), E246 (= E212), G332 (= G298), W333 (= W299), E369 (= E335), A370 (= A336), A372 (= A338), G608 (= G569), H609 (= H570), D610 (= D571), R611 (= R572), G612 (= G573), I616 (= I577), Y620 (≠ M581), S654 (= S615), L656 (= L617), G658 (= G619), G684 (= G645), G685 (= G646), Y704 (≠ F665), T705 (≠ G666), T708 (= T669)
P11653 Methylmalonyl-CoA mutase large subunit; MCM-alpha; EC 5.4.99.2 from Propionibacterium freudenreichii subsp. shermanii (see 4 papers)
63% identity, 96% coverage: 24:682/685 of query aligns to 59:722/728 of P11653
- Y75 (= Y40) binding
- M78 (= M43) binding
- R82 (= R47) binding
- T85 (= T50) binding
- R87 (= R52) binding
- Y89 (= Y54) binding ; mutation to F: Does not significantly affect affinity for succiny-CoA, but kcat is lowered about 580-fold.
- S114 (= S79) binding
- F117 (= F82) binding
- A139 (= A104) binding
- T195 (= T160) binding
- Q197 (= Q162) binding
- V206 (= V171) binding
- R207 (= R172) binding ; binding
- H244 (= H209) binding
- R283 (= R248) binding
- S285 (= S250) binding
- G333 (= G298) binding
- E370 (= E335) binding
- A373 (= A338) binding
- G609 (= G569) binding
- H610 (= H570) binding axial binding residue
- D611 (= D571) binding
- R612 (= R572) binding
- S655 (= S615) binding
- L657 (= L617) binding
- G686 (= G646) binding
- T709 (= T669) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
4reqA Methylmalonyl-coa mutase substrate complex (see paper)
63% identity, 96% coverage: 24:682/685 of query aligns to 57:720/726 of 4reqA
- active site: Y87 (= Y54), Y241 (= Y208), H242 (= H209), K602 (= K564), D606 (= D568), H608 (= H570)
- binding cobalamin: Y87 (= Y54), L117 (= L84), A137 (= A104), V204 (= V171), R205 (= R172), H242 (= H209), E245 (= E212), G331 (= G298), W332 (= W299), E368 (= E335), A369 (= A336), A371 (= A338), L372 (= L339), G607 (= G569), H608 (= H570), D609 (= D571), R610 (= R572), G611 (= G573), I615 (= I577), S653 (= S615), L655 (= L617), G683 (= G645), G684 (= G646), V685 (= V647), Y703 (≠ F665), T704 (≠ G666), T707 (= T669)
- binding methylmalonyl-coenzyme a: Y73 (= Y40), M76 (= M43), F79 (≠ T46), R80 (= R47), T83 (= T50), R85 (= R52), Y87 (= Y54), S112 (= S79), S162 (= S129), T164 (= T131), T193 (= T160), R205 (= R172), N234 (= N201), Y241 (= Y208), H242 (= H209), R281 (= R248), S283 (= S250), F285 (= F252), H326 (= H293), Q328 (= Q295), Q359 (= Q326), S360 (= S327)
- binding succinyl-coenzyme a: Y73 (= Y40), M76 (= M43), F79 (≠ T46), R80 (= R47), T83 (= T50), R85 (= R52), Y87 (= Y54), S162 (= S129), T164 (= T131), T193 (= T160), Q195 (= Q162), R205 (= R172), N234 (= N201), Y241 (= Y208), H242 (= H209), R281 (= R248), S283 (= S250), F285 (= F252), R324 (= R291), H326 (= H293), Q359 (= Q326)
7reqA Methylmalonyl-coa mutase, 2-carboxypropyl-coa inhibitor complex (see paper)
63% identity, 96% coverage: 24:682/685 of query aligns to 56:719/725 of 7reqA
- active site: Y86 (= Y54), Y240 (= Y208), H241 (= H209), K601 (= K564), D605 (= D568), H607 (= H570)
- binding 2-carboxypropyl-coenzyme a: Y72 (= Y40), T74 (= T42), M75 (= M43), F78 (≠ T46), R79 (= R47), T82 (= T50), R84 (= R52), Y86 (= Y54), S161 (= S129), T163 (= T131), T192 (= T160), R204 (= R172), H241 (= H209), R280 (= R248), S282 (= S250), F284 (= F252), H325 (= H293), Q358 (= Q326)
- binding cobalamin: Y86 (= Y54), L116 (= L84), A136 (= A104), R204 (= R172), E244 (= E212), G330 (= G298), W331 (= W299), E367 (= E335), A368 (= A336), A370 (= A338), G606 (= G569), H607 (= H570), D608 (= D571), R609 (= R572), G610 (= G573), I614 (= I577), S652 (= S615), L654 (= L617), G682 (= G645), G683 (= G646), Y702 (≠ F665), T703 (≠ G666), T706 (= T669)
3reqA Methylmalonyl-coa mutase, substrate-free state (poor quality structure) (see paper)
63% identity, 96% coverage: 24:682/685 of query aligns to 56:719/725 of 3reqA
- active site: Y86 (= Y54), Y240 (= Y208), H241 (= H209), K601 (= K564), D605 (= D568), H607 (= H570)
- binding adenosine: Y86 (= Y54), Y240 (= Y208), E244 (= E212), G330 (= G298)
- binding cobalamin: L116 (= L84), V203 (= V171), R204 (= R172), E244 (= E212), G330 (= G298), W331 (= W299), A368 (= A336), G606 (= G569), H607 (= H570), D608 (= D571), R609 (= R572), G610 (= G573), I614 (= I577), G650 (= G613), S652 (= S615), L654 (= L617), G682 (= G645), G683 (= G646), Y702 (≠ F665), T703 (≠ G666), P704 (= P667), T706 (= T669)
2reqA Methylmalonyl-coa mutase, non-productive coa complex, in open conformation representing substrate-free state (see paper)
63% identity, 96% coverage: 24:682/685 of query aligns to 56:719/725 of 2reqA
- active site: Y86 (= Y54), Y240 (= Y208), H241 (= H209), K601 (= K564), D605 (= D568), H607 (= H570)
- binding cobalamin: V203 (= V171), R204 (= R172), E244 (= E212), A245 (= A213), W331 (= W299), A368 (= A336), G606 (= G569), H607 (= H570), D608 (= D571), R609 (= R572), G610 (= G573), I614 (= I577), G650 (= G613), S652 (= S615), L654 (= L617), A655 (= A618), G682 (= G645), G683 (= G646), Y702 (≠ F665), T703 (≠ G666), T706 (= T669)
- binding coenzyme a: Y72 (= Y40), R79 (= R47), K318 (= K286)
5reqA Methylmalonyl-coa mutase, y89f mutant, substrate complex (see paper)
63% identity, 96% coverage: 24:682/685 of query aligns to 56:719/725 of 5reqA
- active site: F86 (≠ Y54), Y240 (= Y208), H241 (= H209), K601 (= K564), D605 (= D568), H607 (= H570)
- binding cobalamin: L116 (= L84), A136 (= A104), R204 (= R172), H241 (= H209), E244 (= E212), G330 (= G298), W331 (= W299), E367 (= E335), A368 (= A336), A370 (= A338), G606 (= G569), H607 (= H570), D608 (= D571), R609 (= R572), G610 (= G573), I614 (= I577), S652 (= S615), L654 (= L617), G682 (= G645), G683 (= G646), V684 (= V647), Y702 (≠ F665), T703 (≠ G666), T706 (= T669)
- binding methylmalonyl(carbadethia)-coenzyme a: Y72 (= Y40), T74 (= T42), M75 (= M43), R79 (= R47), T82 (= T50), R84 (= R52), F86 (≠ Y54), S111 (= S79), S161 (= S129), T163 (= T131), T192 (= T160), Q194 (= Q162), R204 (= R172), N233 (= N201), H241 (= H209), R280 (= R248), S282 (= S250), F284 (= F252), T324 (≠ A292), H325 (= H293), Q358 (= Q326), S359 (= S327)
- binding succinyl(carbadethia)-coenzyme a: Y72 (= Y40), T74 (= T42), M75 (= M43), R79 (= R47), T82 (= T50), R84 (= R52), F86 (≠ Y54), S161 (= S129), T163 (= T131), T192 (= T160), R204 (= R172), N233 (= N201), H241 (= H209), R280 (= R248), S282 (= S250), F284 (= F252), H325 (= H293), Q358 (= Q326)
1e1cA Methylmalonyl-coa mutase h244a mutant (see paper)
63% identity, 96% coverage: 24:682/685 of query aligns to 58:721/727 of 1e1cA
- active site: Y88 (= Y54), Y242 (= Y208), A243 (≠ H209), K603 (= K564), D607 (= D568), H609 (= H570)
- binding cobalamin: Y88 (= Y54), L118 (= L84), H121 (= H87), A138 (= A104), V205 (= V171), R206 (= R172), E246 (= E212), G332 (= G298), W333 (= W299), E369 (= E335), A370 (= A336), A372 (= A338), L373 (= L339), G608 (= G569), H609 (= H570), D610 (= D571), R611 (= R572), G612 (= G573), I616 (= I577), Y620 (≠ M581), S654 (= S615), L656 (= L617), G684 (= G645), G685 (= G646), V686 (= V647), Y704 (≠ F665), T705 (≠ G666), T708 (= T669), S713 (≠ A674)
- binding desulfo-coenzyme a: Y74 (= Y40), M77 (= M43), F80 (≠ T46), R81 (= R47), T84 (= T50), R86 (= R52), S113 (= S79), S163 (= S129), T165 (= T131), T194 (= T160), R282 (= R248), S284 (= S250), H327 (= H293), Q360 (= Q326)
6oxdA Structure of mycobacterium tuberculosis methylmalonyl-coa mutase with adenosyl cobalamin (see paper)
64% identity, 95% coverage: 31:684/685 of query aligns to 77:730/736 of 6oxdA
- active site: Y100 (= Y54), Y254 (= Y208), H255 (= H209), K610 (= K564), D614 (= D568), H616 (= H570)
- binding cobalamin: Y100 (= Y54), L130 (= L84), H133 (= H87), A150 (= A104), R218 (= R172), E258 (= E212), G344 (= G298), W345 (= W299), E381 (= E335), A382 (= A336), A384 (= A338), L385 (= L339), G615 (= G569), H616 (= H570), D617 (= D571), R618 (= R572), S661 (= S615), L663 (= L617), A665 (≠ G619), G691 (= G645), G692 (= G646), F711 (= F665), P712 (≠ G666), T715 (= T669)
- binding Itaconyl coenzyme A: Y86 (= Y40), T88 (= T42), M89 (= M43), Q93 (≠ R47), T96 (= T50), R98 (= R52), Y100 (= Y54), S175 (= S129), T177 (= T131), T206 (= T160), R218 (= R172), H255 (= H209), R294 (= R248), S296 (= S250), F298 (= F252), R337 (= R291), T338 (≠ A292), H339 (= H293), Q341 (= Q295), Q372 (= Q326)
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, 95% coverage: 31:679/685 of query aligns to 52:678/689 of 8gjuJ
- binding coenzyme a: Y61 (= Y40), T63 (= T42), R68 (= R47), T71 (= T50), R73 (= R52), S150 (= S129), T152 (= T131), T181 (= T160), Q183 (= Q162), N222 (= N201), R269 (= R248), S271 (= S250), R313 (= R291), A314 (= A292), H315 (= H293), Q348 (= Q326)
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)
44% identity, 72% coverage: 31:520/685 of query aligns to 67:557/562 of I3VE77
- YPTM 76:79 (≠ YSTM 40:43) binding
- TMR 86:88 (≠ TLR 50:52) binding
- I90 (≠ Y54) 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 (≠ A81) binding ; mutation to A: 2-fold increase in catalytic efficiency with 2-hydroxyisobutyryl-CoA as substrate. Small increase in catalytic efficiency with (S)-3-hydroxybuytryl-CoA as substrate. 1800-fold increase in catalytic efficiency with (R)-3-hydroxybutyryl-CoA as substrate.; mutation to V: 1.5-fold increase in catalytic efficiency with 2-hydroxyisobutyryl-CoA as substrate. 3-fold decrease in catalytic efficiency with (S)-3-hydroxybuytryl-CoA as substrate. 1300-fold increase in catalytic efficiency with (R)-3-hydroxybutyryl-CoA as substrate. 74-fold increase in catalytic efficiency with pivalyl-CoA as substrate.
- TVQ 196:198 (≠ TIQ 160:162) binding
- R235 (≠ A199) binding
- N240 (≠ S204) binding
- H245 (= H209) binding
- R284 (= R248) binding
4r3uA Crystal structure of 2-hydroxyisobutyryl-coa mutase (see paper)
44% identity, 72% coverage: 31:520/685 of query aligns to 66:556/557 of 4r3uA
- active site: I89 (≠ Y54), Y243 (= Y208), H244 (= H209)
- binding 3-hydroxybutanoyl-coenzyme a: Y75 (= Y40), T77 (= T42), M78 (= M43), R82 (= R47), T85 (= T50), R87 (= R52), I89 (≠ Y54), D116 (≠ A81), S164 (= S129), T166 (= T131), T195 (= T160), Q197 (= Q162), R234 (≠ A199), N236 (= N201), N239 (≠ S204), Y243 (= Y208), H244 (= H209), R283 (= R248), F287 (= F252), R327 (= R291), F328 (≠ A292), H329 (= H293), Q331 (= Q295), Q362 (= Q326)
- 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 (= Y40), T77 (= T42), M78 (= M43), R82 (= R47), T85 (= T50), R87 (= R52), I89 (≠ Y54), D116 (≠ A81), S164 (= S129), T166 (= T131), T195 (= T160), Q197 (= Q162), R234 (≠ A199), N236 (= N201), N239 (≠ S204), H244 (= H209), R283 (= R248), F287 (= F252), R327 (= R291), F328 (≠ A292), H329 (= H293), Q331 (= Q295), Q362 (= Q326)
- binding cobalamin: D116 (≠ A81), M119 (≠ L84), E139 (≠ A104), Q207 (≠ R172), E209 (≠ T174), E247 (= E212), A334 (≠ G298), E371 (= E335), A372 (= A336), A374 (= A338)
Q5KUG0 Fused isobutyryl-CoA mutase; EC 5.4.99.13; EC 3.6.5.- from Geobacillus kaustophilus (strain HTA426) (see paper)
36% identity, 73% coverage: 23:520/685 of query aligns to 566:1083/1086 of Q5KUG0
Sites not aligning to the query:
- 213 K→A: Loss of GTPase and ATPase activities. No effect on the mutase activity.
5cjwA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate pivalyl-coenzyme a (see paper)
36% identity, 73% coverage: 23:520/685 of query aligns to 548:1060/1063 of 5cjwA
- active site: F571 (≠ Y54), Y752 (= Y208), H753 (= H209)
- binding pivalyl-coenzyme A: F558 (≠ A33), F560 (= F35), R562 (= R37), R569 (= R52), F571 (≠ Y54), R595 (≠ G77), S650 (= S129), T652 (= T131), R701 (≠ K158), T703 (= T160), Q705 (= Q162), Y745 (≠ N201), Y752 (= Y208), H753 (= H209), S794 (= S250), F796 (= F252), R829 (≠ K286), K834 (≠ R291), H836 (= H293)
- binding cobalamin: F600 (= F82), L605 (≠ H87), S623 (≠ A104), Q715 (≠ R172), H753 (= H209), E756 (= E212), A757 (= A213), G841 (= G298), R842 (≠ W299), E878 (= E335), A879 (= A336), T881 (≠ A338), H966 (≠ D423)
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, 1062
- 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)
36% identity, 73% coverage: 23:520/685 of query aligns to 546:1058/1061 of 5cjvA
- active site: F569 (≠ Y54), Y750 (= Y208), H751 (= H209)
- binding cobalamin: F598 (= F82), L603 (≠ H87), S621 (≠ A104), Q713 (≠ R172), E754 (= E212), A755 (= A213), G839 (= G298), R840 (≠ W299), E876 (= E335), A877 (= A336), T879 (≠ A338), H964 (≠ D423)
- binding guanosine-5'-diphosphate: E944 (= E403)
- binding Isovaleryl-coenzyme A: F556 (≠ A33), F558 (= F35), R560 (= R37), R567 (= R52), F569 (≠ Y54), R593 (≠ G77), S648 (= S129), T650 (= T131), R699 (≠ K158), T701 (= T160), Q703 (= Q162), Q713 (≠ R172), Y743 (≠ N201), H751 (= H209), S792 (= S250), F794 (= F252), K832 (≠ R291), H834 (= H293)
Sites not aligning to the query:
- active site: 6
- binding cobalamin: 18, 19, 20, 21, 22, 26, 66, 67, 94, 96, 98, 116, 117, 129
- binding guanosine-5'-diphosphate: 199, 201, 202, 203, 204, 245, 336, 338, 373, 375
- binding magnesium ion: 203, 229, 242, 242, 288, 288
5cjtA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isobutyryl-coenzyme a (see paper)
37% identity, 73% coverage: 23:520/685 of query aligns to 546:1059/1062 of 5cjtA
- active site: F569 (≠ Y54), Y750 (= Y208), H751 (= H209)
- binding cobalamin: F598 (= F82), L603 (≠ H87), S621 (≠ A104), Q713 (≠ R172), H751 (= H209), E754 (= E212), A755 (= A213), G839 (= G298), R840 (≠ W299), E876 (= E335), A877 (= A336), T879 (≠ A338), H964 (≠ D423)
- binding isobutyryl-coenzyme a: F556 (≠ A33), F558 (= F35), R560 (= R37), R567 (= R52), F569 (≠ Y54), R593 (≠ G77), S648 (= S129), T650 (= T131), R699 (≠ K158), T701 (= T160), Q703 (= Q162), Y743 (≠ N201), Y750 (= Y208), H751 (= H209), S792 (= S250), F794 (= F252), R827 (≠ K286), K832 (≠ R291), H834 (= H293)
- binding guanosine-5'-diphosphate: E944 (= E403)
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
4xc7A Isobutyryl-coa mutase fused with bound butyryl-coa and without cobalamin or gdp (apo-icmf) (see paper)
36% identity, 73% coverage: 23:520/685 of query aligns to 543:1050/1053 of 4xc7A
- active site: F566 (≠ Y54), Y747 (= Y208), H748 (= H209)
- binding Butyryl Coenzyme A: F553 (≠ A33), R557 (= R37), R564 (= R52), F566 (≠ Y54), R590 (≠ G77), S645 (= S129), T647 (= T131), R696 (≠ K158), T698 (= T160), Y740 (≠ N201), S789 (= S250), F791 (= F252), R824 (≠ K286), K829 (≠ R291), H831 (= H293)
Sites not aligning to the query:
Query Sequence
>Echvi_4683 FitnessBrowser__Cola:Echvi_4683
MRPDLTKLSQAEPFMEAADRPRPDHVRYAAGIAPFLRGPYSTMYLTRPWTLRQYAGFSTA
EASNAFYKKNLEAGQKGLSVAFDLATHRGYDSDHPRVQGDVGKAGVAIDSVLGMKLLFDG
IPLDKMSVSMTMNGAVIPVMAFYIVAAEEQGVPLDQLKGTIQNDILKEFMVRNTYIYPPE
PSLRIIADIFAFTAKNMPAFNSISISGYHMLEAGATPELELAYTLADGLEYVRTGLKAGL
AIDDFAPRLSFFWGVGMDHFTEIAKLRAGRLLWAKLMKEFRPTHPKSLKLRAHCQTSGWS
LTEQDAFNNVARTTIEALAAVMGHTQSLHTNAFDEAFALPTDFSASIARNTQVILREEYG
LRKVVDPWGGSVLLEELTEDLVKKAWAHLQEVEKMGGMAKAIEAGLPKQMIEEAAARRQA
KVDQGKEIVVGVNRFLVDEEEDFDILEVDNEAVLKQQQARLSQLKNDRDAAAVARSLEAI
TQAAKSGEGNLLELSVEAARERATLGEISMAMEKVYGRHRAKNQVVSGVYSSEAGNDELF
KEALTLTARFEKLEGRRPRILIAKMGQDGHDRGAKVIASGMADMGFDVDIGPLFQTPEEV
AKQAVENDVHLVGASSLAGGHKVLIPQLIIALEEMGRPDILVVAGGVIPPHDYEFLKEKG
VLEVFGPGTVLTKAAIRIMSVLIEE
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