SitesBLAST
Comparing H281DRAFT_02110 FitnessBrowser__Burk376:H281DRAFT_02110 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)
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)
69% identity, 100% coverage: 1:1132/1132 of query aligns to 1:1093/1093 of Q1LRY0
- H39 (= H33) binding axial binding residue
- 169:417 (vs. 194:448, 69% identical) GTPase chaperone MeaI
- GAGKSS 219:224 (= GAGKSS 246:251) binding
- S223 (= S250) binding
- I248 (= I275) binding
- D249 (= D276) binding
- D262 (= D289) binding ; binding
- R265 (= R292) binding
- E310 (= E341) binding ; binding
- T311 (= T342) binding
- NKFD 357:360 (≠ NRFD 388:391) binding
- 418:579 (vs. 449:618, 52% identical) Linker
- F587 (= F626) binding
- F598 (= F637) 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 (= R661) binding
- R728 (= R767) binding
- Y772 (= Y811) binding
- S821 (= S860) binding
- R856 (= R895) binding
- K861 (= K900) binding
- E973 (= E1012) binding
- N1092 (= N1131) binding
4xc6A Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, and mg (holo-icmf/gdp) (see paper)
70% identity, 98% coverage: 20:1132/1132 of query aligns to 6:1067/1067 of 4xc6A
- active site: K6 (≠ R20), F572 (= F637), Y753 (= Y818), H754 (= H819)
- binding cobalamin: G18 (= G32), H19 (= H33), D20 (= D34), A21 (= A35), S22 (= S36), M26 (= M40), Y66 (= Y80), Q67 (= Q81), G94 (= G108), G96 (= G110), V98 (= V112), Y116 (= Y130), S117 (= S131), P118 (= P132), M129 (= M143), F601 (= F666), L606 (= L671), S624 (= S689), Q716 (= Q781), H754 (= H819), E757 (= E822), A758 (= A823), G842 (= G907), R843 (= R908), E879 (= E944), A880 (= A945), T882 (= T947), H967 (= H1032)
- binding guanosine-5'-diphosphate: G199 (= G246), G201 (= G248), K202 (= K249), S203 (= S250), S204 (= S251), R245 (= R292), N337 (= N388), K338 (≠ R389), D340 (= D391), Q375 (≠ I426), S377 (= S428), E947 (= E1012)
- binding magnesium ion: S203 (= S250), D229 (= D276), D242 (= D289), D242 (= D289), E290 (= E341), E290 (= E341)
5cjwA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate pivalyl-coenzyme a (see paper)
70% identity, 98% coverage: 20:1132/1132 of query aligns to 6:1063/1063 of 5cjwA
- active site: K6 (≠ R20), F571 (= F637), Y752 (= Y818), H753 (= H819)
- binding pivalyl-coenzyme A: F558 (= F624), F560 (= F626), R562 (= R628), R569 (= R635), F571 (= F637), R595 (= R661), S650 (= S716), T652 (= T718), R701 (= R767), T703 (= T769), Q705 (= Q771), Y745 (= Y811), Y752 (= Y818), H753 (= H819), S794 (= S860), F796 (= F862), R829 (= R895), K834 (= K900), H836 (= H902)
- binding cobalamin: G18 (= G32), H19 (= H33), D20 (= D34), A21 (= A35), S22 (= S36), M26 (= M40), Y66 (= Y80), Q67 (= Q81), G94 (= G108), G96 (= G110), V98 (= V112), Y116 (= Y130), S117 (= S131), P118 (= P132), F600 (= F666), L605 (= L671), S623 (= S689), Q715 (= Q781), H753 (= H819), E756 (= E822), A757 (= A823), G841 (= G907), R842 (= R908), E878 (= E944), A879 (= A945), T881 (= T947), H966 (= H1032)
- binding guanosine-5'-diphosphate: G199 (= G246), G201 (= G248), K202 (= K249), S203 (= S250), S204 (= S251), R245 (= R292), N337 (= N388), K338 (≠ R389), D340 (= D391), Q375 (≠ I426), S377 (= S428), N1062 (= N1131)
- binding magnesium ion: S203 (= S250), D229 (= D276), D242 (= D289), D242 (= D289), E290 (= E341), E290 (= E341)
5cjtA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isobutyryl-coenzyme a (see paper)
70% identity, 98% coverage: 20:1132/1132 of query aligns to 6:1062/1062 of 5cjtA
- active site: K6 (≠ R20), F569 (= F637), Y750 (= Y818), H751 (= H819)
- binding cobalamin: G18 (= G32), H19 (= H33), D20 (= D34), A21 (= A35), S22 (= S36), M26 (= M40), Y66 (= Y80), Q67 (= Q81), G94 (= G108), G96 (= G110), V98 (= V112), Y116 (= Y130), S117 (= S131), F598 (= F666), L603 (= L671), S621 (= S689), Q713 (= Q781), H751 (= H819), E754 (= E822), A755 (= A823), G839 (= G907), R840 (= R908), E876 (= E944), A877 (= A945), T879 (= T947), H964 (= H1032)
- binding isobutyryl-coenzyme a: F556 (= F624), F558 (= F626), R560 (= R628), R567 (= R635), F569 (= F637), R593 (= R661), S648 (= S716), T650 (= T718), R699 (= R767), T701 (= T769), Q703 (= Q771), Y743 (= Y811), Y750 (= Y818), H751 (= H819), S792 (= S860), F794 (= F862), R827 (= R895), K832 (= K900), H834 (= H902)
- binding guanosine-5'-diphosphate: G199 (= G246), G201 (= G248), K202 (= K249), S203 (= S250), S204 (= S251), R245 (= R292), N336 (= N388), K337 (≠ R389), D339 (= D391), Q374 (≠ I426), S376 (= S428), E944 (= E1012)
- binding magnesium ion: S203 (= S250), D229 (= D276), D242 (= D289), D242 (= D289), E289 (= E341), E289 (= E341)
5cjvA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isovaleryl-coenzyme a (see paper)
70% identity, 98% coverage: 20:1132/1132 of query aligns to 6:1061/1061 of 5cjvA
- active site: K6 (≠ R20), F569 (= F637), Y750 (= Y818), H751 (= H819)
- binding cobalamin: G18 (= G32), H19 (= H33), D20 (= D34), A21 (= A35), S22 (= S36), M26 (= M40), Y66 (= Y80), Q67 (= Q81), G94 (= G108), G96 (= G110), V98 (= V112), Y116 (= Y130), S117 (= S131), M129 (= M143), F598 (= F666), L603 (= L671), S621 (= S689), Q713 (= Q781), E754 (= E822), A755 (= A823), G839 (= G907), R840 (= R908), E876 (= E944), A877 (= A945), T879 (= T947), H964 (= H1032)
- binding guanosine-5'-diphosphate: G199 (= G246), G201 (= G248), K202 (= K249), S203 (= S250), S204 (= S251), R245 (= R292), K336 (≠ R389), D338 (= D391), Q373 (≠ I426), S375 (= S428), E944 (= E1012)
- binding Isovaleryl-coenzyme A: F556 (= F624), F558 (= F626), R560 (= R628), R567 (= R635), F569 (= F637), R593 (= R661), S648 (= S716), T650 (= T718), R699 (= R767), T701 (= T769), Q703 (= Q771), Q713 (= Q781), Y743 (= Y811), H751 (= H819), S792 (= S860), F794 (= F862), K832 (= K900), H834 (= H902)
- binding magnesium ion: S203 (= S250), D229 (= D276), D242 (= D289), D242 (= D289), E288 (= E341), E288 (= E341)
4xc7A Isobutyryl-coa mutase fused with bound butyryl-coa and without cobalamin or gdp (apo-icmf) (see paper)
69% identity, 98% coverage: 20:1132/1132 of query aligns to 5:1053/1053 of 4xc7A
- active site: K5 (≠ R20), F566 (= F637), Y747 (= Y818), H748 (= H819)
- binding Butyryl Coenzyme A: F553 (= F624), R557 (= R628), R564 (= R635), F566 (= F637), R590 (= R661), S645 (= S716), T647 (= T718), R696 (= R767), T698 (= T769), Y740 (= Y811), S789 (= S860), F791 (= F862), R824 (= R895), K829 (= K900), H831 (= H902)
Q5KUG0 Fused isobutyryl-CoA mutase; EC 5.4.99.13; EC 3.6.5.- from Geobacillus kaustophilus (strain HTA426) (see paper)
60% identity, 98% coverage: 21:1132/1132 of query aligns to 11:1086/1086 of Q5KUG0
- K213 (= K249) mutation to A: Loss of GTPase and ATPase activities. No effect on the mutase activity.
I3VE77 2-hydroxyisobutanoyl-CoA mutase large subunit; 2-hydroxyisobutyryl-CoA mutase large subunit; HCM large subunit; EC 5.4.99.64 from Aquincola tertiaricarbonis (see 2 papers)
35% identity, 46% coverage: 613:1129/1132 of query aligns to 65:557/562 of I3VE77
- YPTM 76:79 (≠ FP-F 624:626) binding
- TMR 86:88 (≠ PTR 633:635) binding
- I90 (≠ F637) 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 (≠ A665) 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 (= TVQ 769:771) binding
- R235 (≠ N809) binding
- N240 (≠ S814) binding
- H245 (= H819) binding
- R284 (≠ N858) binding
4r3uA Crystal structure of 2-hydroxyisobutyryl-coa mutase (see paper)
35% identity, 46% coverage: 613:1129/1132 of query aligns to 64:556/557 of 4r3uA
- active site: I89 (≠ F637), Y243 (= Y818), H244 (= H819)
- binding 3-hydroxybutanoyl-coenzyme a: Y75 (≠ F624), T77 (vs. gap), M78 (≠ F626), R82 (≠ N630), T85 (≠ P633), R87 (= R635), I89 (≠ F637), D116 (≠ A665), S164 (= S716), T166 (= T718), T195 (= T769), Q197 (= Q771), R234 (≠ N809), N236 (≠ Y811), N239 (≠ S814), Y243 (= Y818), H244 (= H819), R283 (≠ N858), F287 (= F862), R327 (≠ K900), F328 (≠ Y901), H329 (= H902), Q331 (= Q904), Q362 (≠ N935)
- 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 (≠ F624), T77 (vs. gap), M78 (≠ F626), R82 (≠ N630), T85 (≠ P633), R87 (= R635), I89 (≠ F637), D116 (≠ A665), S164 (= S716), T166 (= T718), T195 (= T769), Q197 (= Q771), R234 (≠ N809), N236 (≠ Y811), N239 (≠ S814), H244 (= H819), R283 (≠ N858), F287 (= F862), R327 (≠ K900), F328 (≠ Y901), H329 (= H902), Q331 (= Q904), Q362 (≠ N935)
- binding cobalamin: D116 (≠ A665), M119 (≠ S668), E139 (≠ S689), Q207 (= Q781), E209 (≠ T783), E247 (= E822), A334 (≠ G907), E371 (= E944), A372 (= A945), A374 (≠ T947)
P22033 Methylmalonyl-CoA mutase, mitochondrial; MCM; Methylmalonyl-CoA isomerase; EC 5.4.99.2 from Homo sapiens (Human) (see 28 papers)
36% identity, 46% coverage: 611:1131/1132 of query aligns to 83:579/750 of P22033
- P86 (= P614) 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 (= G615) to E: in MMAM; mut0; dbSNP:rs1554160986
- R93 (≠ A621) to H: in MMAM; mut0; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918251
- G94 (= G622) to R: in MMAM; mut0; dbSNP:rs727504022; to V: in MMAM; mut- and mut0; dbSNP:rs535411418
- P95 (≠ V623) to R: in MMAM; mut0; dbSNP:rs190834116
- YPTM 96:99 (≠ FP-- 624:625) binding
- Y100 (vs. gap) 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 (≠ E629) to R: in MMAM; mut0; dbSNP:rs121918249
- T---IRQY 106:110 (≠ NEDPTRMF 630:637) binding
- R108 (= R635) to C: in MMAM; mut0; dbSNP:rs121918257; to G: in MMAM; mut-; to H: in MMAM; mut0; dbSNP:rs483352778
- Q109 (≠ M636) to R: in MMAM; mut0; dbSNP:rs1461110052
- G133 (vs. gap) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253828
- A137 (= A665) to V: in MMAM; mut0; dbSNP:rs941483851
- D139 (= D667) to N: in MMAM; uncertain significance; dbSNP:rs879253829
- L140 (≠ S668) to P: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- A141 (≠ V669) to T: in MMAM; decreased protein expression; dbSNP:rs1554160730
- H143 (≠ L671) to Y: in MMAM; mut0
- G145 (= G673) to S: in MMAM; mut0
- S148 (≠ P676) to L: in MMAM; mut0; dbSNP:rs1300547552
- D156 (≠ K685) to N: in MMAM; mut-
- G158 (= G687) to V: in MMAM; mut0
- G161 (= G690) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; to V: in MMAM; decreased protein expression
- F174 (≠ Y703) to S: in MMAM; mut0; dbSNP:rs864309733
- M186 (= M717) to V: in MMAM; mut-; dbSNP:rs148331800
- T187 (= T718) to S: in MMAM; mut0; dbSNP:rs879253830
- N189 (= N720) to I: in MMAM; mut-; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs200908035; to K: in MMAM; mut-; dbSNP:rs1561959114
- A191 (≠ P722) to E: in MMAM; mut- and mut0; affects proper folding; reduced protein level; decreased methylmalonyl-CoA mutase activity; dbSNP:rs760782399
- A197 (= A728) to E: in MMAM; mut0
- G203 (≠ A734) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs778702777
- E205 (≠ D736) natural variant: Missing (in MMAM; mut0; dbSNP:rs879253831)
- G215 (= G768) to C: in MMAM; mut- and mut0; dbSNP:rs121918258; to S: in MMAM; mut0; dbSNP:rs121918258
- TIQ 216:218 (≠ TVQ 769:771) binding
- Q218 (= Q771) to H: in MMAM; mut0 and mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability; dbSNP:rs1446389693
- N219 (≠ A772) to Y: in MMAM; mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; dbSNP:rs121918256
- R228 (≠ Q781) binding ; to Q: in MMAM; mut0; dbSNP:rs770810987
- T230 (= T783) to I: in MMAM; mut-; to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253833
- Y231 (≠ C784) 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 (≠ N809) binding
- S262 (= S816) to N: in MMAM; mut0
- H265 (= H819) binding ; to Y: in MMAM; mut-
- E276 (≠ Q830) to D: in MMAM; uncertain significance; mut-; dbSNP:rs12175488
- L281 (= L835) to S: in MMAM; mut0; dbSNP:rs796052007
- G284 (= G838) to E: in MMAM; mut0; dbSNP:rs879253835; to R: in MMAM; mut0; dbSNP:rs761477436
- S288 (≠ V842) to P: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1179778233
- G291 (≠ Y845) to E: in MMAM; mut0
- Q293 (≠ A847) to P: in MMAM; mut0
- RLS 304:306 (≠ NLS 858:860) binding
- L305 (= L859) to S: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554160246
- S306 (= S860) to F: in MMAM; mut0; dbSNP:rs1085307929
- W309 (≠ F863) to G: in MMAM; decreased protein expression
- G312 (= G866) to V: in MMAM; mut0; dbSNP:rs864309734
- Y316 (≠ E870) 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 (≠ V877) to T: in MMAM; mut-; dbSNP:rs780387525
- R326 (= R879) to K: in MMAM; uncertain significance; dbSNP:rs758577372
- L328 (≠ V881) 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 (= S896) 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 (≠ K898) natural variant: Missing (in MMAM; mut0)
- L347 (= L899) to R: in MMAM; mut0; dbSNP:rs1026703654
- H350 (= H902) to Y: in MMAM; mut0; dbSNP:rs1407914109
- L358 (= L910) to P: in MMAM; mut0
- N366 (= N918) 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 (= R921) 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 (= T922) to P: in MMAM; mut0; dbSNP:rs368790885
- A377 (= A929) to E: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918250
- Q383 (≠ N935) to H: in MMAM; mut0; to P: in MMAM; mut0
- H386 (= H938) to N: in MMAM; mut0; dbSNP:rs1554159937; to R: in MMAM; mut0; dbSNP:rs866933356
- T387 (= T939) 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 (= N940) to H: in MMAM; mut0; dbSNP:rs766010704; to K: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253840
- S389 (≠ A941) natural variant: Missing (in MMAM; mut0)
- I412 (= I964) natural variant: Missing (in MMAM; mut0)
- P424 (= P976) to L: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253842
- G426 (≠ Q978) 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 (= G979) to D: in MMAM; mut0; dbSNP:rs753288303
- G454 (= G1006) to E: in MMAM; mut0
- A499 (= A1052) to T: in dbSNP:rs2229385
- I505 (≠ L1058) to T: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- Q514 (= Q1067) to E: in MMAM; uncertain significance; to K: in MMAM; decreased protein expression
- L518 (= L1070) to P: in MMAM; mut0; dbSNP:rs864309738
- R532 (≠ A1086) to H: in dbSNP:rs1141321
- A535 (≠ E1089) to P: in MMAM; mut0; dbSNP:rs760183775
- A552 (≠ L1105) to V: in MMAM; uncertain significance; dbSNP:rs879253845
- C560 (= C1112) to Y: in MMAM; mut0; dbSNP:rs1238333040
- T566 (= T1118) to R: in MMAM; mut0
- F573 (≠ G1125) 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
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
- 152:750 natural variant: Missing (in MMAM; mut0)
- 228:750 natural variant: Missing (in MMAM; mut0)
- 587 Y → C: in MMAM; mut-
- 597 I → R: in MMAM; no changed in protein expression; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554158951
- 615 P → L: in MMAM; mut0; affects proper folding; reduced strongly protein level; P → R: in MMAM; mut0; dbSNP:rs1554158777; P → T: in MMAM; mut0; affects proper folding; reduced strongly protein level; loss of methylmalonyl-CoA mutase activity; dbSNP:rs1302409621
- 616 R → C: in MMAM; mut0; dbSNP:rs765284825
- 617 L → R: in MMAM; mut0; dbSNP:rs1554158775
- 621 K → N: in MMAM; mut0
- 623 G → R: in MMAM; mut0; dbSNP:rs121918254
- 624 Q → R: in MMAM; no effect on protein abundance; dbSNP:rs768521956
- 625 D → G: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253847; D → V: in MMAM; mut0; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity
- 626 G → C: in MMAM; mut-; dbSNP:rs982110849
- 627 binding axial binding residue; H → R: in MMAM; mut0; dbSNP:rs372486357
- 630 G → E: in MMAM; mut0; dbSNP:rs143023066
- 633 V → 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
- 637 G → E: in MMAM; mut-; G → R: in MMAM; mut0; dbSNP:rs781501004
- 638 F → I: in MMAM; mut0
- 640 D → Y: in MMAM; mut0; dbSNP:rs865815395
- 642 G → R: in MMAM; mut-; dbSNP:rs747897332
- 648 G → 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
- 669 V → E: in MMAM; mut0; dbSNP:rs1360470463
- 671 I → V: in dbSNP:rs8589
- 674 L → F: in MMAM; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1164271240
- 678 H → R: in MMAM; mut-; dbSNP:rs147094927
- 684 natural variant: E -> EL (in MMAM; mut-)
- 685 L → R: in MMAM; mut-; dbSNP:rs864309739
- 694 R → L: in MMAM; mut-; decreased protein abundance; loss of methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability; R → 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
- 700 M → 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
- 703 G → R: in MMAM; mut0; dbSNP:rs121918255
- 717 G → 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
- 723 G → D: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity; dbSNP:rs755077681
2xiqA Crystal structure of human methylmalonyl-coa mutase in complex with adenosylcobalamin and malonyl-coa (see paper)
36% identity, 46% coverage: 611:1131/1132 of query aligns to 48:544/714 of 2xiqA
- active site: Y75 (≠ F637), Y229 (= Y818), H230 (= H819)
- binding cobalamin: Y75 (≠ F637), L105 (≠ S668), H108 (≠ L671), A125 (≠ S689), R193 (≠ Q781), E233 (= E822), G320 (= G907), W321 (≠ R908), E357 (= E944), G360 (≠ T947), L361 (≠ T948)
- binding malonyl-coenzyme a: Y61 (≠ F624), T63 (vs. gap), M64 (vs. gap), R68 (= R627), T71 (≠ N630), R73 (= R635), Y75 (≠ F637), S150 (= S716), T152 (= T718), T181 (= T769), R193 (≠ Q781), K220 (≠ N809), H230 (= H819), R269 (≠ N858), S271 (= S860), F273 (= F862), R313 (≠ K900), A314 (≠ Y901), H315 (= H902), Q317 (= Q904), Q348 (≠ N935)
Sites not aligning to the query:
- active site: 586, 590, 592
- binding cobalamin: 591, 592, 593, 594, 595, 599, 635, 637, 639, 641, 667, 668, 687, 688, 691
8dyjB Crystal structure of human methylmalonyl-coa mutase in complex with adp and cob(ii)alamin (see paper)
36% identity, 46% coverage: 611:1131/1132 of query aligns to 47:543/708 of 8dyjB
- binding adenosine-5'-diphosphate: Y74 (≠ F637), T151 (= T718), R192 (≠ Q781), Y228 (= Y818), H229 (= H819), F272 (= F862), Q316 (= Q904), N352 (= N940), E356 (= E944), L360 (≠ T948), P361 (= P949)
- binding cobalamin: F102 (= F666), L104 (≠ S668), H107 (≠ L671), A124 (≠ S689), V191 (≠ G780), R192 (≠ Q781), H229 (= H819), E232 (= E822), G319 (= G907), W320 (≠ R908), E356 (= E944), G359 (≠ T947), L360 (≠ T948)
Sites not aligning to the query:
- binding cobalamin: 590, 591, 592, 593, 594, 598, 636, 638, 640, 666, 667, 668, 686, 687, 690
8gjuJ Crystal structure of human methylmalonyl-coa mutase (mmut) in complex with methylmalonic acidemia type a protein (mmaa), coenzyme a, and gdp (see paper)
36% identity, 46% coverage: 611:1129/1132 of query aligns to 48:542/689 of 8gjuJ
- binding coenzyme a: Y61 (≠ F624), T63 (vs. gap), R68 (= R627), T71 (≠ N630), R73 (= R635), S150 (= S716), T152 (= T718), T181 (= T769), Q183 (= Q771), N222 (≠ Y811), R269 (≠ N858), S271 (= S860), R313 (≠ K900), A314 (≠ Y901), H315 (= H902), Q348 (≠ N935)
6oxdA Structure of mycobacterium tuberculosis methylmalonyl-coa mutase with adenosyl cobalamin (see paper)
35% identity, 46% coverage: 610:1129/1132 of query aligns to 72:566/736 of 6oxdA
- active site: Y100 (≠ F637), Y254 (= Y818), H255 (= H819)
- binding cobalamin: Y100 (≠ F637), L130 (≠ S668), H133 (≠ L671), A150 (≠ S689), R218 (≠ Q781), E258 (= E822), G344 (= G907), W345 (≠ R908), E381 (= E944), A382 (= A945), A384 (≠ T947), L385 (≠ T948)
- binding Itaconyl coenzyme A: Y86 (≠ F624), T88 (≠ F626), M89 (≠ R627), Q93 (≠ E631), T96 (= T634), R98 (= R635), Y100 (≠ F637), S175 (= S716), T177 (= T718), T206 (= T769), R218 (≠ Q781), H255 (= H819), R294 (≠ N858), S296 (= S860), F298 (= F862), R337 (≠ K900), T338 (≠ Y901), H339 (= H902), Q341 (= Q904), Q372 (≠ N935)
Sites not aligning to the query:
- active site: 610, 614, 616
- binding cobalamin: 615, 616, 617, 618, 661, 663, 665, 691, 692, 711, 712, 715
5reqA Methylmalonyl-coa mutase, y89f mutant, substrate complex (see paper)
33% identity, 46% coverage: 610:1128/1132 of query aligns to 58:556/725 of 5reqA
- active site: F86 (= F637), Y240 (= Y818), H241 (= H819)
- binding cobalamin: L116 (≠ S668), A136 (≠ S689), R204 (≠ Q781), H241 (= H819), E244 (= E822), G330 (= G907), W331 (≠ R908), E367 (= E944), A368 (= A945), A370 (≠ T947)
- binding methylmalonyl(carbadethia)-coenzyme a: Y72 (vs. gap), T74 (vs. gap), M75 (≠ V623), R79 (= R627), T82 (≠ N630), R84 (= R635), F86 (= F637), S111 (= S663), S161 (= S716), T163 (= T718), T192 (= T769), Q194 (= Q771), R204 (≠ Q781), N233 (≠ Y811), H241 (= H819), R280 (≠ N858), S282 (= S860), F284 (= F862), T324 (≠ Y901), H325 (= H902), Q358 (≠ N935), S359 (= S936)
- binding succinyl(carbadethia)-coenzyme a: Y72 (vs. gap), T74 (vs. gap), M75 (≠ V623), R79 (= R627), T82 (≠ N630), R84 (= R635), F86 (= F637), S161 (= S716), T163 (= T718), T192 (= T769), R204 (≠ Q781), N233 (≠ Y811), H241 (= H819), R280 (≠ N858), S282 (= S860), F284 (= F862), H325 (= H902), Q358 (≠ N935)
Sites not aligning to the query:
- active site: 601, 605, 607
- binding cobalamin: 606, 607, 608, 609, 610, 614, 652, 654, 682, 683, 684, 702, 703, 706
P11653 Methylmalonyl-CoA mutase large subunit; MCM-alpha; EC 5.4.99.2 from Propionibacterium freudenreichii subsp. shermanii (see 4 papers)
33% identity, 46% coverage: 610:1128/1132 of query aligns to 61:559/728 of P11653
- Y75 (vs. gap) binding
- M78 (≠ V623) binding
- R82 (= R627) binding
- T85 (≠ N630) binding
- R87 (= R635) binding
- Y89 (≠ F637) binding ; mutation to F: Does not significantly affect affinity for succiny-CoA, but kcat is lowered about 580-fold.
- S114 (= S663) binding
- F117 (= F666) binding
- A139 (≠ S689) binding
- T195 (= T769) binding
- Q197 (= Q771) binding
- V206 (≠ G780) binding
- R207 (≠ Q781) binding ; binding
- H244 (= H819) binding
- R283 (≠ N858) binding
- S285 (= S860) binding
- G333 (= G907) binding
- E370 (= E944) binding
- A373 (≠ T947) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 609 binding
- 610 binding axial binding residue
- 611 binding
- 612 binding
- 655 binding
- 657 binding
- 686 binding
- 709 binding
4reqA Methylmalonyl-coa mutase substrate complex (see paper)
33% identity, 46% coverage: 610:1128/1132 of query aligns to 59:557/726 of 4reqA
- active site: Y87 (≠ F637), Y241 (= Y818), H242 (= H819)
- binding cobalamin: Y87 (≠ F637), L117 (≠ S668), A137 (≠ S689), V204 (≠ G780), R205 (≠ Q781), H242 (= H819), E245 (= E822), G331 (= G907), W332 (≠ R908), E368 (= E944), A369 (= A945), A371 (≠ T947), L372 (≠ T948)
- binding methylmalonyl-coenzyme a: Y73 (vs. gap), M76 (≠ V623), F79 (= F626), R80 (= R627), T83 (≠ N630), R85 (= R635), Y87 (≠ F637), S112 (= S663), S162 (= S716), T164 (= T718), T193 (= T769), R205 (≠ Q781), N234 (≠ Y811), Y241 (= Y818), H242 (= H819), R281 (≠ N858), S283 (= S860), F285 (= F862), H326 (= H902), Q328 (= Q904), Q359 (≠ N935), S360 (= S936)
- binding succinyl-coenzyme a: Y73 (vs. gap), M76 (≠ V623), F79 (= F626), R80 (= R627), T83 (≠ N630), R85 (= R635), Y87 (≠ F637), S162 (= S716), T164 (= T718), T193 (= T769), Q195 (= Q771), R205 (≠ Q781), N234 (≠ Y811), Y241 (= Y818), H242 (= H819), R281 (≠ N858), S283 (= S860), F285 (= F862), R324 (≠ K900), H326 (= H902), Q359 (≠ N935)
Sites not aligning to the query:
- active site: 602, 606, 608
- binding cobalamin: 607, 608, 609, 610, 611, 615, 653, 655, 683, 684, 685, 703, 704, 707
6reqA Methylmalonyl-coa mutase, 3-carboxypropyl-coa inhibitor complex (see paper)
33% identity, 46% coverage: 610:1128/1132 of query aligns to 60:558/727 of 6reqA
- active site: Y88 (≠ F637), Y242 (= Y818), H243 (= H819)
- binding 3-carboxypropyl-coenzyme a: Y74 (vs. gap), T76 (vs. gap), M77 (≠ V623), F80 (= F626), R81 (= R627), T84 (≠ N630), R86 (= R635), Y88 (≠ F637), S113 (= S663), S163 (= S716), T165 (= T718), T194 (= T769), R206 (≠ Q781), H243 (= H819), R282 (≠ N858), S284 (= S860), F286 (= F862), H327 (= H902), Q329 (= Q904), Q360 (≠ N935)
- binding cobalamin: Y88 (≠ F637), F116 (= F666), L118 (≠ S668), H121 (≠ L671), A138 (≠ S689), R206 (≠ Q781), E246 (= E822), G332 (= G907), W333 (≠ R908), E369 (= E944), A370 (= A945), A372 (≠ T947)
Sites not aligning to the query:
- active site: 603, 607, 609
- binding cobalamin: 608, 609, 610, 611, 612, 616, 620, 654, 656, 658, 684, 685, 704, 705, 708
7reqA Methylmalonyl-coa mutase, 2-carboxypropyl-coa inhibitor complex (see paper)
33% identity, 46% coverage: 610:1128/1132 of query aligns to 58:556/725 of 7reqA
- active site: Y86 (≠ F637), Y240 (= Y818), H241 (= H819)
- binding 2-carboxypropyl-coenzyme a: Y72 (vs. gap), T74 (vs. gap), M75 (≠ V623), F78 (= F626), R79 (= R627), T82 (≠ N630), R84 (= R635), Y86 (≠ F637), S161 (= S716), T163 (= T718), T192 (= T769), R204 (≠ Q781), H241 (= H819), R280 (≠ N858), S282 (= S860), F284 (= F862), H325 (= H902), Q358 (≠ N935)
- binding cobalamin: Y86 (≠ F637), L116 (≠ S668), A136 (≠ S689), R204 (≠ Q781), E244 (= E822), G330 (= G907), W331 (≠ R908), E367 (= E944), A368 (= A945), A370 (≠ T947)
Sites not aligning to the query:
- active site: 601, 605, 607
- binding cobalamin: 606, 607, 608, 609, 610, 614, 652, 654, 682, 683, 702, 703, 706
3reqA Methylmalonyl-coa mutase, substrate-free state (poor quality structure) (see paper)
33% identity, 46% coverage: 610:1128/1132 of query aligns to 58:556/725 of 3reqA
- active site: Y86 (≠ F637), Y240 (= Y818), H241 (= H819)
- binding adenosine: Y86 (≠ F637), Y240 (= Y818), E244 (= E822), G330 (= G907)
- binding cobalamin: L116 (≠ S668), V203 (≠ G780), R204 (≠ Q781), E244 (= E822), G330 (= G907), W331 (≠ R908), A368 (= A945)
Sites not aligning to the query:
- active site: 601, 605, 607
- binding cobalamin: 606, 607, 608, 609, 610, 614, 650, 652, 654, 682, 683, 702, 703, 704, 706
Query Sequence
>H281DRAFT_02110 FitnessBrowser__Burk376:H281DRAFT_02110
MTDLSTPQRAASHELPAGRRLRFVTAAALFDGHDASINIMRRILQASGVEVIHLGHNRSV
DEVATAALQEDADGVAVSSYQGGHNEYFRYLVDLLRARGGERIKVFGGGGGVIVSEEIVA
LENYGVEKIYSPHDGQRLGLQGMIDDMIARCSAAAREDATARTGAVGEWLASVTGQPLLH
LRSSAQVRGETSSADSLDASSLVFRRLAQLISAFETGGVASSKRAELSALTQAVQVPVLG
ITGTGGAGKSSLTDELIRRFRLDYGDTLTIAVLAIDPSRRKSGGALLGDRIRMNAIGDWG
GGARVYMRSMATREASSEISDALPDALMLCKAAGFDLIVVETSGIGQGDAAIVPFVDESL
YVMTPEFGAASQLEKIDMLDFADAVAINRFDRKGAPDALRDVAKQVQRNRADFAKSPEAM
PVFGTIASHFNDDGVTALYQYIAEALRKHGLRSGGGRLSIAADVRFSSGRHAIVPPARVR
YLAEIAQTIHAYRERVDQQAGVARERWQLVEARRMLGEASADAHDAQASLASLDALIEQR
TTALGEHERKLLDAWPQTVAAYSGDDHVVRIRDREIRTALTATTLSGTQLRKVALPKFVD
HGEILRWLMLDNLPGYFPFTAGVFPFRRENEDPTRMFAGEGDPSRTNRRFKLLSEGMPAK
RLSTAFDSVTLYGEEPDERPDIYGKVGNSGVSVATLDDMHALYDGFDLCAPQTSVSMTIN
GPAPTILAMFFNVAIDQQIARQAQQLGRALSEDELAETRRMALENVRGTVQADILKEDQG
QNTCIFSTEFSLKVMGDIQAYFVEHRVRNFYSVSISGYHIAEAGANPISQLAYTLANGFT
YVEAYLARGMSIDDFAPNLSFFFSNGMDPEYTVLGRVARRVWAIAMRERYGANERSQKLK
YHVQTSGRSLHAQEIDFNDIRTTLQALIAIYDNCNSLHTNAFDEAITTPTEESVRRAVAI
QLIINREWGLAKNQNPNQGSFVIDELTDLVEEAVLAEFDRLTERGGVLGAMETGYQRGRI
QDESMLYEHRKHDGSYPIVGVNTFVSAKPHEAPTPIALARSTEEEKQSQLKRLRDFQARH
RGAAPAALERLQRAVIDDENVFAVLMDVVRVCSLGQITHALFEVGGQYRRNM
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