SitesBLAST
Comparing BPHYT_RS02085 FitnessBrowser__BFirm:BPHYT_RS02085 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)
78% identity, 46% coverage: 699:1298/1298 of query aligns to 494:1093/1093 of Q1LRY0
- F587 (= F792) binding
- F598 (= F803) 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 (= R827) binding
- R728 (= R933) binding
- Y772 (= Y977) binding
- S821 (= S1026) binding
- R856 (= R1061) binding
- K861 (= K1066) binding
- E973 (= E1178) binding
- N1092 (= N1297) binding
Sites not aligning to the query:
- 39 binding axial binding residue
- 169:417 GTPase chaperone MeaI
- 219:224 binding
- 223 binding
- 248 binding
- 249 binding
- 262 binding ; binding
- 265 binding
- 310 binding ; binding
- 311 binding
- 357:360 binding
- 418:579 Linker
4xc6A Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, and mg (holo-icmf/gdp) (see paper)
78% identity, 46% coverage: 699:1298/1298 of query aligns to 474:1067/1067 of 4xc6A
- active site: F572 (= F803), Y753 (= Y984), H754 (= H985)
- binding cobalamin: F601 (= F832), L606 (= L837), S624 (= S855), Q716 (= Q947), H754 (= H985), E757 (= E988), A758 (= A989), G842 (= G1073), R843 (= R1074), E879 (= E1110), A880 (= A1111), T882 (= T1113), H967 (= H1198)
- binding guanosine-5'-diphosphate: E947 (= E1178)
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
5cjtA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isobutyryl-coenzyme a (see paper)
77% identity, 46% coverage: 699:1298/1298 of query aligns to 473:1062/1062 of 5cjtA
- active site: F569 (= F803), Y750 (= Y984), H751 (= H985)
- binding cobalamin: F598 (= F832), L603 (= L837), S621 (= S855), Q713 (= Q947), H751 (= H985), E754 (= E988), A755 (= A989), G839 (= G1073), R840 (= R1074), E876 (= E1110), A877 (= A1111), T879 (= T1113), H964 (= H1198)
- binding isobutyryl-coenzyme a: F556 (= F790), F558 (= F792), R560 (= R794), R567 (= R801), F569 (= F803), R593 (= R827), S648 (= S882), T650 (= T884), R699 (= R933), T701 (= T935), Q703 (= Q937), Y743 (= Y977), Y750 (= Y984), H751 (= H985), S792 (= S1026), F794 (= F1028), R827 (= R1061), K832 (= K1066), H834 (= H1068)
- binding guanosine-5'-diphosphate: E944 (= E1178)
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
5cjvA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isovaleryl-coenzyme a (see paper)
77% identity, 46% coverage: 699:1298/1298 of query aligns to 472:1061/1061 of 5cjvA
- active site: F569 (= F803), Y750 (= Y984), H751 (= H985)
- binding cobalamin: F598 (= F832), L603 (= L837), S621 (= S855), Q713 (= Q947), E754 (= E988), A755 (= A989), G839 (= G1073), R840 (= R1074), E876 (= E1110), A877 (= A1111), T879 (= T1113), H964 (= H1198)
- binding guanosine-5'-diphosphate: E944 (= E1178)
- binding Isovaleryl-coenzyme A: F556 (= F790), F558 (= F792), R560 (= R794), R567 (= R801), F569 (= F803), R593 (= R827), S648 (= S882), T650 (= T884), R699 (= R933), T701 (= T935), Q703 (= Q937), Q713 (= Q947), Y743 (= Y977), H751 (= H985), S792 (= S1026), F794 (= F1028), K832 (= K1066), H834 (= H1068)
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
5cjwA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate pivalyl-coenzyme a (see paper)
77% identity, 46% coverage: 699:1298/1298 of query aligns to 474:1063/1063 of 5cjwA
- active site: F571 (= F803), Y752 (= Y984), H753 (= H985)
- binding pivalyl-coenzyme A: F558 (= F790), F560 (= F792), R562 (= R794), R569 (= R801), F571 (= F803), R595 (= R827), S650 (= S882), T652 (= T884), R701 (= R933), T703 (= T935), Q705 (= Q937), Y745 (= Y977), Y752 (= Y984), H753 (= H985), S794 (= S1026), F796 (= F1028), R829 (= R1061), K834 (= K1066), H836 (= H1068)
- binding cobalamin: F600 (= F832), L605 (= L837), S623 (= S855), Q715 (= Q947), H753 (= H985), E756 (= E988), A757 (= A989), G841 (= G1073), R842 (= R1074), E878 (= E1110), A879 (= A1111), T881 (= T1113), H966 (= H1198)
- binding guanosine-5'-diphosphate: N1062 (= N1297)
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
4xc7A Isobutyryl-coa mutase fused with bound butyryl-coa and without cobalamin or gdp (apo-icmf) (see paper)
77% identity, 46% coverage: 699:1298/1298 of query aligns to 468:1053/1053 of 4xc7A
- active site: F566 (= F803), Y747 (= Y984), H748 (= H985)
- binding Butyryl Coenzyme A: F553 (= F790), R557 (= R794), R564 (= R801), F566 (= F803), R590 (= R827), S645 (= S882), T647 (= T884), R696 (= R933), T698 (= T935), Y740 (= Y977), S789 (= S1026), F791 (= F1028), R824 (= R1061), K829 (= K1066), H831 (= H1068)
Sites not aligning to the query:
Q5KUG0 Fused isobutyryl-CoA mutase; EC 5.4.99.13; EC 3.6.5.- from Geobacillus kaustophilus (strain HTA426) (see paper)
69% identity, 46% coverage: 696:1298/1298 of query aligns to 482:1086/1086 of Q5KUG0
Sites not aligning to the query:
- 213 K→A: Loss of GTPase and ATPase activities. No effect on the mutase activity.
P22033 Methylmalonyl-CoA mutase, mitochondrial; MCM; Methylmalonyl-CoA isomerase; EC 5.4.99.2 from Homo sapiens (Human) (see 28 papers)
36% identity, 40% coverage: 777:1297/1298 of query aligns to 83:579/750 of P22033
- P86 (= P780) 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 (= G781) to E: in MMAM; mut0; dbSNP:rs1554160986
- R93 (≠ A787) to H: in MMAM; mut0; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918251
- G94 (= G788) to R: in MMAM; mut0; dbSNP:rs727504022; to V: in MMAM; mut- and mut0; dbSNP:rs535411418
- P95 (≠ V789) to R: in MMAM; mut0; dbSNP:rs190834116
- YPTM 96:99 (≠ FP-- 790:791) 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 (≠ E795) to R: in MMAM; mut0; dbSNP:rs121918249
- T---IRQY 106:110 (≠ NEDPTRMF 796:803) binding
- R108 (= R801) to C: in MMAM; mut0; dbSNP:rs121918257; to G: in MMAM; mut-; to H: in MMAM; mut0; dbSNP:rs483352778
- Q109 (≠ M802) 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 (= A831) to V: in MMAM; mut0; dbSNP:rs941483851
- D139 (= D833) to N: in MMAM; uncertain significance; dbSNP:rs879253829
- L140 (≠ S834) to P: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- A141 (≠ V835) to T: in MMAM; decreased protein expression; dbSNP:rs1554160730
- H143 (≠ L837) to Y: in MMAM; mut0
- G145 (= G839) to S: in MMAM; mut0
- S148 (≠ P842) to L: in MMAM; mut0; dbSNP:rs1300547552
- D156 (≠ K851) to N: in MMAM; mut-
- G158 (= G853) to V: in MMAM; mut0
- G161 (= G856) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; to V: in MMAM; decreased protein expression
- F174 (≠ Y869) to S: in MMAM; mut0; dbSNP:rs864309733
- M186 (= M883) to V: in MMAM; mut-; dbSNP:rs148331800
- T187 (= T884) to S: in MMAM; mut0; dbSNP:rs879253830
- N189 (= N886) to I: in MMAM; mut-; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs200908035; to K: in MMAM; mut-; dbSNP:rs1561959114
- A191 (≠ P888) to E: in MMAM; mut- and mut0; affects proper folding; reduced protein level; decreased methylmalonyl-CoA mutase activity; dbSNP:rs760782399
- A197 (= A894) to E: in MMAM; mut0
- G203 (≠ A900) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs778702777
- E205 (≠ Q911) natural variant: Missing (in MMAM; mut0; dbSNP:rs879253831)
- G215 (= G934) to C: in MMAM; mut- and mut0; dbSNP:rs121918258; to S: in MMAM; mut0; dbSNP:rs121918258
- TIQ 216:218 (≠ TVQ 935:937) binding
- Q218 (= Q937) to H: in MMAM; mut0 and mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability; dbSNP:rs1446389693
- N219 (≠ A938) to Y: in MMAM; mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; dbSNP:rs121918256
- R228 (≠ Q947) binding ; to Q: in MMAM; mut0; dbSNP:rs770810987
- T230 (= T949) to I: in MMAM; mut-; to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253833
- Y231 (≠ C950) 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 (≠ N975) binding
- S262 (= S982) to N: in MMAM; mut0
- H265 (= H985) binding ; to Y: in MMAM; mut-
- E276 (≠ Q996) to D: in MMAM; uncertain significance; mut-; dbSNP:rs12175488
- L281 (= L1001) to S: in MMAM; mut0; dbSNP:rs796052007
- G284 (= G1004) to E: in MMAM; mut0; dbSNP:rs879253835; to R: in MMAM; mut0; dbSNP:rs761477436
- S288 (≠ V1008) to P: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1179778233
- G291 (≠ Y1011) to E: in MMAM; mut0
- Q293 (≠ A1013) to P: in MMAM; mut0
- RLS 304:306 (≠ NLS 1024:1026) binding
- L305 (= L1025) to S: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554160246
- S306 (= S1026) to F: in MMAM; mut0; dbSNP:rs1085307929
- W309 (≠ F1029) to G: in MMAM; decreased protein expression
- G312 (= G1032) to V: in MMAM; mut0; dbSNP:rs864309734
- Y316 (≠ E1036) 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 (≠ V1043) to T: in MMAM; mut-; dbSNP:rs780387525
- R326 (= R1045) to K: in MMAM; uncertain significance; dbSNP:rs758577372
- L328 (≠ I1047) 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 (= S1062) 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 (≠ K1064) natural variant: Missing (in MMAM; mut0)
- L347 (= L1065) to R: in MMAM; mut0; dbSNP:rs1026703654
- H350 (= H1068) to Y: in MMAM; mut0; dbSNP:rs1407914109
- L358 (= L1076) to P: in MMAM; mut0
- N366 (= N1084) 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 (= R1087) 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 (= T1088) to P: in MMAM; mut0; dbSNP:rs368790885
- A377 (= A1095) to E: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918250
- Q383 (≠ N1101) to H: in MMAM; mut0; to P: in MMAM; mut0
- H386 (= H1104) to N: in MMAM; mut0; dbSNP:rs1554159937; to R: in MMAM; mut0; dbSNP:rs866933356
- T387 (= T1105) 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 (= N1106) to H: in MMAM; mut0; dbSNP:rs766010704; to K: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253840
- S389 (≠ A1107) natural variant: Missing (in MMAM; mut0)
- I412 (= I1130) natural variant: Missing (in MMAM; mut0)
- P424 (= P1142) to L: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253842
- G426 (≠ Q1144) 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 (= G1145) to D: in MMAM; mut0; dbSNP:rs753288303
- G454 (= G1172) to E: in MMAM; mut0
- A499 (= A1218) to T: in dbSNP:rs2229385
- I505 (≠ L1224) to T: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- Q514 (= Q1235) to E: in MMAM; uncertain significance; to K: in MMAM; decreased protein expression
- L518 (= L1239) to P: in MMAM; mut0; dbSNP:rs864309738
- R532 (= R1256) to H: in dbSNP:rs1141321
- A535 (≠ R1259) to P: in MMAM; mut0; dbSNP:rs760183775
- A552 (≠ L1271) to V: in MMAM; uncertain significance; dbSNP:rs879253845
- C560 (= C1278) to Y: in MMAM; mut0; dbSNP:rs1238333040
- T566 (= T1284) to R: in MMAM; mut0
- F573 (≠ G1291) 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, 40% coverage: 777:1297/1298 of query aligns to 48:544/714 of 2xiqA
- active site: Y75 (≠ F803), Y229 (= Y984), H230 (= H985)
- binding cobalamin: Y75 (≠ F803), L105 (≠ S834), H108 (≠ L837), A125 (≠ S855), R193 (≠ Q947), E233 (= E988), G320 (= G1073), W321 (≠ R1074), E357 (= E1110), G360 (≠ T1113), L361 (≠ T1114)
- binding malonyl-coenzyme a: Y61 (≠ F790), T63 (vs. gap), M64 (vs. gap), R68 (= R793), T71 (≠ N796), R73 (= R801), Y75 (≠ F803), S150 (= S882), T152 (= T884), T181 (= T935), R193 (≠ Q947), K220 (≠ N975), H230 (= H985), R269 (≠ N1024), S271 (= S1026), F273 (= F1028), R313 (≠ K1066), A314 (≠ Y1067), H315 (= H1068), Q317 (= Q1070), Q348 (≠ N1101)
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
4r3uA Crystal structure of 2-hydroxyisobutyryl-coa mutase (see paper)
35% identity, 40% coverage: 779:1295/1298 of query aligns to 64:556/557 of 4r3uA
- active site: I89 (≠ F803), Y243 (= Y984), H244 (= H985)
- binding 3-hydroxybutanoyl-coenzyme a: Y75 (≠ F790), T77 (vs. gap), M78 (≠ F792), R82 (≠ N796), T85 (≠ P799), R87 (= R801), I89 (≠ F803), D116 (≠ A831), S164 (= S882), T166 (= T884), T195 (= T935), Q197 (= Q937), R234 (≠ N975), N236 (≠ Y977), N239 (≠ S980), Y243 (= Y984), H244 (= H985), R283 (≠ N1024), F287 (= F1028), R327 (≠ K1066), F328 (≠ Y1067), H329 (= H1068), Q331 (= Q1070), Q362 (≠ N1101)
- 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 (≠ F790), T77 (vs. gap), M78 (≠ F792), R82 (≠ N796), T85 (≠ P799), R87 (= R801), I89 (≠ F803), D116 (≠ A831), S164 (= S882), T166 (= T884), T195 (= T935), Q197 (= Q937), R234 (≠ N975), N236 (≠ Y977), N239 (≠ S980), H244 (= H985), R283 (≠ N1024), F287 (= F1028), R327 (≠ K1066), F328 (≠ Y1067), H329 (= H1068), Q331 (= Q1070), Q362 (≠ N1101)
- binding cobalamin: D116 (≠ A831), M119 (≠ S834), E139 (≠ S855), Q207 (= Q947), E209 (≠ T949), E247 (= E988), A334 (≠ G1073), E371 (= E1110), A372 (= A1111), A374 (≠ T1113)
8dyjB Crystal structure of human methylmalonyl-coa mutase in complex with adp and cob(ii)alamin (see paper)
36% identity, 40% coverage: 777:1297/1298 of query aligns to 47:543/708 of 8dyjB
- binding adenosine-5'-diphosphate: Y74 (≠ F803), T151 (= T884), R192 (≠ Q947), Y228 (= Y984), H229 (= H985), F272 (= F1028), Q316 (= Q1070), N352 (= N1106), E356 (= E1110), L360 (≠ T1114), P361 (= P1115)
- binding cobalamin: F102 (= F832), L104 (≠ S834), H107 (≠ L837), A124 (≠ S855), V191 (≠ G946), R192 (≠ Q947), H229 (= H985), E232 (= E988), G319 (= G1073), W320 (≠ R1074), E356 (= E1110), G359 (≠ T1113), L360 (≠ T1114)
Sites not aligning to the query:
- binding cobalamin: 590, 591, 592, 593, 594, 598, 636, 638, 640, 666, 667, 668, 686, 687, 690
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, 40% coverage: 779:1295/1298 of query aligns to 65:557/562 of I3VE77
- YPTM 76:79 (≠ FP-F 790:792) binding
- TMR 86:88 (≠ PTR 799:801) binding
- I90 (≠ F803) 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 (≠ A831) 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 935:937) binding
- R235 (≠ N975) binding
- N240 (≠ S980) binding
- H245 (= H985) binding
- R284 (≠ N1024) binding
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, 40% coverage: 777:1295/1298 of query aligns to 48:542/689 of 8gjuJ
- binding coenzyme a: Y61 (≠ F790), T63 (vs. gap), R68 (= R793), T71 (≠ N796), R73 (= R801), S150 (= S882), T152 (= T884), T181 (= T935), Q183 (= Q937), N222 (≠ Y977), R269 (≠ N1024), S271 (= S1026), R313 (≠ K1066), A314 (≠ Y1067), H315 (= H1068), Q348 (≠ N1101)
6oxdA Structure of mycobacterium tuberculosis methylmalonyl-coa mutase with adenosyl cobalamin (see paper)
36% identity, 40% coverage: 776:1295/1298 of query aligns to 72:566/736 of 6oxdA
- active site: Y100 (≠ F803), Y254 (= Y984), H255 (= H985)
- binding cobalamin: Y100 (≠ F803), L130 (≠ S834), H133 (≠ L837), A150 (≠ S855), R218 (≠ Q947), E258 (= E988), G344 (= G1073), W345 (≠ R1074), E381 (= E1110), A382 (= A1111), A384 (≠ T1113), L385 (≠ T1114)
- binding Itaconyl coenzyme A: Y86 (≠ F790), T88 (≠ F792), M89 (≠ R793), Q93 (≠ E797), T96 (= T800), R98 (= R801), Y100 (≠ F803), S175 (= S882), T177 (= T884), T206 (= T935), R218 (≠ Q947), H255 (= H985), R294 (≠ N1024), S296 (= S1026), F298 (= F1028), R337 (≠ K1066), T338 (≠ Y1067), H339 (= H1068), Q341 (= Q1070), Q372 (≠ N1101)
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, 40% coverage: 776:1294/1298 of query aligns to 58:556/725 of 5reqA
- active site: F86 (= F803), Y240 (= Y984), H241 (= H985)
- binding cobalamin: L116 (≠ S834), A136 (≠ S855), R204 (≠ Q947), H241 (= H985), E244 (= E988), G330 (= G1073), W331 (≠ R1074), E367 (= E1110), A368 (= A1111), A370 (≠ T1113)
- binding methylmalonyl(carbadethia)-coenzyme a: Y72 (vs. gap), T74 (vs. gap), M75 (≠ V789), R79 (= R793), T82 (≠ N796), R84 (= R801), F86 (= F803), S111 (= S829), S161 (= S882), T163 (= T884), T192 (= T935), Q194 (= Q937), R204 (≠ Q947), N233 (≠ Y977), H241 (= H985), R280 (≠ N1024), S282 (= S1026), F284 (= F1028), T324 (≠ Y1067), H325 (= H1068), Q358 (≠ N1101), S359 (= S1102)
- binding succinyl(carbadethia)-coenzyme a: Y72 (vs. gap), T74 (vs. gap), M75 (≠ V789), R79 (= R793), T82 (≠ N796), R84 (= R801), F86 (= F803), S161 (= S882), T163 (= T884), T192 (= T935), R204 (≠ Q947), N233 (≠ Y977), H241 (= H985), R280 (≠ N1024), S282 (= S1026), F284 (= F1028), H325 (= H1068), Q358 (≠ N1101)
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
6reqA Methylmalonyl-coa mutase, 3-carboxypropyl-coa inhibitor complex (see paper)
33% identity, 40% coverage: 776:1294/1298 of query aligns to 60:558/727 of 6reqA
- active site: Y88 (≠ F803), Y242 (= Y984), H243 (= H985)
- binding 3-carboxypropyl-coenzyme a: Y74 (vs. gap), T76 (vs. gap), M77 (≠ V789), F80 (= F792), R81 (= R793), T84 (≠ N796), R86 (= R801), Y88 (≠ F803), S113 (= S829), S163 (= S882), T165 (= T884), T194 (= T935), R206 (≠ Q947), H243 (= H985), R282 (≠ N1024), S284 (= S1026), F286 (= F1028), H327 (= H1068), Q329 (= Q1070), Q360 (≠ N1101)
- binding cobalamin: Y88 (≠ F803), F116 (= F832), L118 (≠ S834), H121 (≠ L837), A138 (≠ S855), R206 (≠ Q947), E246 (= E988), G332 (= G1073), W333 (≠ R1074), E369 (= E1110), A370 (= A1111), A372 (≠ T1113)
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
P11653 Methylmalonyl-CoA mutase large subunit; MCM-alpha; EC 5.4.99.2 from Propionibacterium freudenreichii subsp. shermanii (see 4 papers)
33% identity, 40% coverage: 776:1294/1298 of query aligns to 61:559/728 of P11653
- Y75 (vs. gap) binding
- M78 (≠ V789) binding
- R82 (= R793) binding
- T85 (≠ N796) binding
- R87 (= R801) binding
- Y89 (≠ F803) binding ; mutation to F: Does not significantly affect affinity for succiny-CoA, but kcat is lowered about 580-fold.
- S114 (= S829) binding
- F117 (= F832) binding
- A139 (≠ S855) binding
- T195 (= T935) binding
- Q197 (= Q937) binding
- V206 (≠ G946) binding
- R207 (≠ Q947) binding ; binding
- H244 (= H985) binding
- R283 (≠ N1024) binding
- S285 (= S1026) binding
- G333 (= G1073) binding
- E370 (= E1110) binding
- A373 (≠ T1113) 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
7reqA Methylmalonyl-coa mutase, 2-carboxypropyl-coa inhibitor complex (see paper)
33% identity, 40% coverage: 776:1294/1298 of query aligns to 58:556/725 of 7reqA
- active site: Y86 (≠ F803), Y240 (= Y984), H241 (= H985)
- binding 2-carboxypropyl-coenzyme a: Y72 (vs. gap), T74 (vs. gap), M75 (≠ V789), F78 (= F792), R79 (= R793), T82 (≠ N796), R84 (= R801), Y86 (≠ F803), S161 (= S882), T163 (= T884), T192 (= T935), R204 (≠ Q947), H241 (= H985), R280 (≠ N1024), S282 (= S1026), F284 (= F1028), H325 (= H1068), Q358 (≠ N1101)
- binding cobalamin: Y86 (≠ F803), L116 (≠ S834), A136 (≠ S855), R204 (≠ Q947), E244 (= E988), G330 (= G1073), W331 (≠ R1074), E367 (= E1110), A368 (= A1111), A370 (≠ T1113)
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, 40% coverage: 776:1294/1298 of query aligns to 58:556/725 of 3reqA
- active site: Y86 (≠ F803), Y240 (= Y984), H241 (= H985)
- binding adenosine: Y86 (≠ F803), Y240 (= Y984), E244 (= E988), G330 (= G1073)
- binding cobalamin: L116 (≠ S834), V203 (≠ G946), R204 (≠ Q947), E244 (= E988), G330 (= G1073), W331 (≠ R1074), A368 (= A1111)
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
2reqA Methylmalonyl-coa mutase, non-productive coa complex, in open conformation representing substrate-free state (see paper)
33% identity, 40% coverage: 776:1294/1298 of query aligns to 58:556/725 of 2reqA
Sites not aligning to the query:
- active site: 601, 605, 607
- binding cobalamin: 606, 607, 608, 609, 610, 614, 650, 652, 654, 655, 682, 683, 702, 703, 706
Query Sequence
>BPHYT_RS02085 FitnessBrowser__BFirm:BPHYT_RS02085
MTDLSTPQRAGSHKLPAGRRLRFVTAAALFDGHDASINIMRRILQASGVEVIHLGHNRSV
DEVATAALQEDADGVAVSSYQGGHNEYFRYLVDLLRARGGERIKVFGGGGGVIVPEEISE
LESYGVEKIYSPQDGQRLGLQGMIDDMIARCAEGARAAEAVGQSRVGEWVDEFSKRGLPR
FDSRGDAGGDEDAVRNPFSQASHVGCATSVGHVANAADTADAADTADTADAADTADAADT
ADTADTADTAIAANTANTANTANTANTANTANTANTSDPASSTFRRLAQLISAFEAGAVD
ASAREKLSAQAQAKATATPVLGITGTGGAGKSSLTDELIRRFRLDYGDALTIAVLAIDPS
RRKSGGALLGDRIRMNAIGDWGGGARVYMRSMATREASSEVSDSLPDALMLCKAAGFDLI
VVETSGIGQGNAAIVPFVDESLYVMTPEFGAASQLEKIDMLDFAGFVAINKFDRKGAPDA
LRDVAKQVQRNRADFAKPPEAMPVFGTIASRFNDDGVTALYRHVAEALRKHGLRSGGGRL
AAPEGLRFSSGRNAIVPPARVRYLADIAQTIHAYRERADAQARLARERWQLVEARRMLGE
AGTQAGAVTQSRASASGNSSGNPNANSDADSDADSDANANANANANANANANANANANAN
ANANANASANANSNPDPNSNKHAPANVTSADTPSPLQQLDTLIAQRTASLGERERALLDT
WPQTVAAYSGAEHIVRIRDREIRTALTVTTLSGSEVRKVSLPKFADHGEILRWLMLDNLP
GYFPFTAGVFPFRRENEDPTRMFAGEGDPQRTNRRFKLLSEGMPAKRLSTAFDSVTLYGE
EPDERPDIYGKVGNSGVSVATLDDMKTLYDGFDLCAPETSVSMTINGPAPTILAMFFNVA
IDQQIARMTQQQGRPLTHDELSATRRAALENVRGTVQADILKEDQGQNTCIFSTEFSLKV
MGDIQAYFVEHGVRNFYSVSISGYHIAEAGANPISQLAYTLANGFTYVEAYLARGMSIDD
FAPNLSFFFSNGMDPEYTVLGRVARRIWAVAMRERYGANERSQKLKYHVQTSGRSLHAQE
IDFNDIRTTLQALIAIYDNCNSLHTNAFDEAITTPTEDSVRRAVAIQLIINREWGLAKNQ
NPNQGSFVIEELTDLVEEAVLAEFDRLTERGGVLGAMETGYQRGRIQDESMLYEHRKHDG
SYPIVGVNTFLSAHPHEAPQPIALARSTDDEKQSQLQRLRAFQSQHRDAAPAALERLKRA
VIDDENVFAVLMDVVRVCSLGQITHALFEVGGQYRRNM
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