SitesBLAST
Comparing YP_001313797.1 NCBI__GCF_000017145.1:YP_001313797.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
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)
59% identity, 98% coverage: 6:541/545 of query aligns to 24:558/562 of I3VE77
- YPTM 76:79 (= YPTM 58:61) binding (3S)-3-hydroxybutanoyl-CoA
- TMR 86:88 (≠ TIR 68:70) binding (3S)-3-hydroxybutanoyl-CoA
- I90 (≠ V72) 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 (= D99) binding (3S)-3-hydroxybutanoyl-CoA; mutation to A: 2-fold increase in catalytic efficiency with 2-hydroxyisobutyryl-CoA as substrate. Small increase in catalytic efficiency with (S)-3-hydroxybuytryl-CoA as substrate. 1800-fold increase in catalytic efficiency with (R)-3-hydroxybutyryl-CoA as substrate.; mutation to V: 1.5-fold increase in catalytic efficiency with 2-hydroxyisobutyryl-CoA as substrate. 3-fold decrease in catalytic efficiency with (S)-3-hydroxybuytryl-CoA as substrate. 1300-fold increase in catalytic efficiency with (R)-3-hydroxybutyryl-CoA as substrate. 74-fold increase in catalytic efficiency with pivalyl-CoA as substrate.
- TVQ 196:198 (≠ TLQ 178:180) binding (3S)-3-hydroxybutanoyl-CoA
- R235 (≠ K217) binding (3S)-3-hydroxybutanoyl-CoA
- N240 (≠ S222) binding (3S)-3-hydroxybutanoyl-CoA
- H245 (= H227) binding (3S)-3-hydroxybutanoyl-CoA
- R284 (= R266) binding (3S)-3-hydroxybutanoyl-CoA
4r3uA Crystal structure of 2-hydroxyisobutyryl-coa mutase (see paper)
59% identity, 98% coverage: 6:541/545 of query aligns to 23:557/557 of 4r3uA
- active site: I89 (≠ V72), Y243 (= Y226), H244 (= H227)
- binding 3-hydroxybutanoyl-coenzyme a: Y75 (= Y58), T77 (= T60), M78 (= M61), R82 (= R65), T85 (= T68), R87 (= R70), I89 (≠ V72), D116 (= D99), S164 (= S147), T166 (= T149), T195 (= T178), Q197 (= Q180), R234 (≠ K217), N236 (= N219), N239 (≠ S222), Y243 (= Y226), H244 (= H227), R283 (= R266), F287 (= F270), R327 (= R310), F328 (≠ V311), H329 (= H312), Q331 (= Q314), Q362 (= Q345)
- 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 (= Y58), T77 (= T60), M78 (= M61), R82 (= R65), T85 (= T68), R87 (= R70), I89 (≠ V72), D116 (= D99), S164 (= S147), T166 (= T149), T195 (= T178), Q197 (= Q180), R234 (≠ K217), N236 (= N219), N239 (≠ S222), H244 (= H227), R283 (= R266), F287 (= F270), R327 (= R310), F328 (≠ V311), H329 (= H312), Q331 (= Q314), Q362 (= Q345)
- binding cobalamin: D116 (= D99), M119 (≠ L102), E139 (≠ V122), Q207 (= Q190), E209 (= E192), E247 (≠ D230), A334 (= A317), E371 (= E354), A372 (= A355), A374 (= A357)
8gjuJ Crystal structure of human methylmalonyl-coa mutase (mmut) in complex with methylmalonic acidemia type a protein (mmaa), coenzyme a, and gdp (see paper)
43% identity, 98% coverage: 10:541/545 of query aligns to 16:543/689 of 8gjuJ
- binding coenzyme a: Y61 (= Y58), T63 (= T60), R68 (= R65), T71 (= T68), R73 (= R70), S150 (= S147), T152 (= T149), T181 (= T178), Q183 (= Q180), N222 (= N219), R269 (= R266), S271 (= S268), R313 (= R310), A314 (≠ V311), H315 (= H312), Q348 (= Q345)
2xiqA Crystal structure of human methylmalonyl-coa mutase in complex with adenosylcobalamin and malonyl-coa (see paper)
43% identity, 97% coverage: 10:539/545 of query aligns to 16:541/714 of 2xiqA
- active site: Y75 (≠ V72), Y229 (= Y226), H230 (= H227)
- binding cobalamin: Y75 (≠ V72), L105 (= L102), H108 (≠ L105), A125 (≠ V122), R193 (≠ Q190), E233 (≠ D230), G320 (≠ A317), W321 (≠ M318), E357 (= E354), G360 (≠ A357), L361 (≠ I358)
- binding malonyl-coenzyme a: Y61 (= Y58), T63 (= T60), M64 (= M61), R68 (= R65), T71 (= T68), R73 (= R70), Y75 (≠ V72), S150 (= S147), T152 (= T149), T181 (= T178), R193 (≠ Q190), K220 (= K217), H230 (= H227), R269 (= R266), S271 (= S268), F273 (= F270), R313 (= R310), A314 (≠ V311), H315 (= H312), Q317 (= Q314), Q348 (= Q345)
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)
43% identity, 97% coverage: 10:539/545 of query aligns to 15:540/708 of 8dyjB
- binding adenosine-5'-diphosphate: Y74 (≠ V72), T151 (= T149), R192 (≠ Q190), Y228 (= Y226), H229 (= H227), F272 (= F270), Q316 (= Q314), N352 (= N350), E356 (= E354), L360 (≠ I358), P361 (= P359)
- binding cobalamin: F102 (= F100), L104 (= L102), H107 (≠ L105), A124 (≠ V122), V191 (≠ A189), R192 (≠ Q190), H229 (= H227), E232 (≠ D230), G319 (≠ A317), W320 (≠ M318), E356 (= E354), G359 (≠ A357), L360 (≠ I358)
Sites not aligning to the query:
- binding cobalamin: 590, 591, 592, 593, 594, 598, 636, 638, 640, 666, 667, 668, 686, 687, 690
P22033 Methylmalonyl-CoA mutase, mitochondrial; MCM; Methylmalonyl-CoA isomerase; EC 5.4.99.2 from Homo sapiens (Human) (see 28 papers)
43% identity, 97% coverage: 10:539/545 of query aligns to 51:576/750 of P22033
- I69 (≠ L28) to V: in MMAM; likely benign; dbSNP:rs115923556
- P86 (= P48) 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 (= G49) to E: in MMAM; mut0; dbSNP:rs1554160986
- R93 (= R55) to H: in MMAM; mut0; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918251
- G94 (= G56) to R: in MMAM; mut0; dbSNP:rs727504022; to V: in MMAM; mut- and mut0; dbSNP:rs535411418
- P95 (≠ V57) to R: in MMAM; mut0; dbSNP:rs190834116
- YPTM 96:99 (= YPTM 58:61) binding malonyl-CoA
- Y100 (= Y62) 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 (= W67) to R: in MMAM; mut0; dbSNP:rs121918249
- TIRQY 106:110 (≠ TIRQV 68:72) binding malonyl-CoA
- R108 (= R70) to C: in MMAM; mut0; dbSNP:rs121918257; to G: in MMAM; mut-; to H: in MMAM; mut0; dbSNP:rs483352778
- Q109 (= Q71) to R: in MMAM; mut0; dbSNP:rs1461110052
- G133 (= G95) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253828
- A137 (≠ D99) to V: in MMAM; mut0; dbSNP:rs941483851
- D139 (= D101) to N: in MMAM; uncertain significance; dbSNP:rs879253829
- L140 (= L102) to P: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- A141 (≠ P103) to T: in MMAM; decreased protein expression; dbSNP:rs1554160730
- H143 (≠ L105) to Y: in MMAM; mut0
- G145 (= G107) to S: in MMAM; mut0
- S148 (= S110) to L: in MMAM; mut0; dbSNP:rs1300547552
- D156 (≠ E118) to N: in MMAM; mut-
- G158 (= G120) to V: in MMAM; mut0
- G161 (= G123) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; to V: in MMAM; decreased protein expression
- F174 (= F136) to S: in MMAM; mut0; dbSNP:rs864309733
- M186 (≠ L148) to V: in MMAM; mut-; dbSNP:rs148331800
- T187 (= T149) to S: in MMAM; mut0; dbSNP:rs879253830
- N189 (= N151) to I: in MMAM; mut-; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs200908035; to K: in MMAM; mut-; dbSNP:rs1561959114
- A191 (≠ S153) to E: in MMAM; mut- and mut0; affects proper folding; reduced protein level; decreased methylmalonyl-CoA mutase activity; dbSNP:rs760782399
- A197 (= A159) to E: in MMAM; mut0
- G203 (≠ A165) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs778702777
- E205 (= E167) natural variant: Missing (in MMAM; mut0; dbSNP:rs879253831)
- G215 (= G177) to C: in MMAM; mut- and mut0; dbSNP:rs121918258; to S: in MMAM; mut0; dbSNP:rs121918258
- TIQ 216:218 (≠ TLQ 178:180) binding malonyl-CoA
- Q218 (= Q180) to H: in MMAM; mut0 and mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability; dbSNP:rs1446389693
- N219 (≠ A181) to Y: in MMAM; mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; dbSNP:rs121918256
- R228 (≠ Q190) binding malonyl-CoA; to Q: in MMAM; mut0; dbSNP:rs770810987
- T230 (≠ E192) to I: in MMAM; mut-; to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253833
- Y231 (≠ W193) 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 (= K217) binding malonyl-CoA
- S262 (= S224) to N: in MMAM; mut0
- H265 (= H227) binding malonyl-CoA; to Y: in MMAM; mut-
- E276 (= E238) to D: in MMAM; uncertain significance; mut-; dbSNP:rs12175488
- L281 (≠ M243) to S: in MMAM; mut0; dbSNP:rs796052007
- G284 (≠ T246) to E: in MMAM; mut0; dbSNP:rs879253835; to R: in MMAM; mut0; dbSNP:rs761477436
- S288 (≠ C250) to P: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1179778233
- G291 (≠ V253) to E: in MMAM; mut0
- Q293 (≠ R255) to P: in MMAM; mut0
- RLS 304:306 (= RLS 266:268) binding malonyl-CoA
- L305 (= L267) to S: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554160246
- S306 (= S268) to F: in MMAM; mut0; dbSNP:rs1085307929
- W309 (≠ F271) to G: in MMAM; decreased protein expression
- G312 (≠ H274) to V: in MMAM; mut0; dbSNP:rs864309734
- Y316 (≠ F278) 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 (= A286) to T: in MMAM; mut-; dbSNP:rs780387525
- R326 (= R288) to K: in MMAM; uncertain significance; dbSNP:rs758577372
- L328 (≠ V290) 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 (= S306) 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 (≠ R308) natural variant: Missing (in MMAM; mut0)
- L347 (= L309) to R: in MMAM; mut0; dbSNP:rs1026703654
- H350 (= H312) to Y: in MMAM; mut0; dbSNP:rs1407914109
- L358 (= L320) to P: in MMAM; mut0
- N366 (= N328) 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 (= R331) 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 (= T332) to P: in MMAM; mut0; dbSNP:rs368790885
- A377 (= A339) to E: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918250
- Q383 (= Q345) to H: in MMAM; mut0; to P: in MMAM; mut0
- H386 (= H348) to N: in MMAM; mut0; dbSNP:rs1554159937; to R: in MMAM; mut0; dbSNP:rs866933356
- T387 (= T349) 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 (= N350) to H: in MMAM; mut0; dbSNP:rs766010704; to K: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253840
- S389 (≠ G351) natural variant: Missing (in MMAM; mut0)
- I412 (= I374) natural variant: Missing (in MMAM; mut0)
- P424 (= P386) to L: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253842
- G426 (= G388) 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 (= G389) to D: in MMAM; mut0; dbSNP:rs753288303
- G454 (= G416) to E: in MMAM; mut0
- A499 (≠ D463) to T: in dbSNP:rs2229385
- I505 (≠ Y469) to T: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- Q514 (= Q477) to E: in MMAM; uncertain significance; to K: in MMAM; decreased protein expression
- L518 (= L481) to P: in MMAM; mut0; dbSNP:rs864309738
- R532 (≠ S495) to H: in dbSNP:rs1141321
- A535 (≠ K498) to P: in MMAM; mut0; dbSNP:rs760183775
- A552 (≠ T515) to V: in MMAM; uncertain significance; dbSNP:rs879253845
- C560 (≠ A523) to Y: in MMAM; mut0; dbSNP:rs1238333040
- T566 (≠ C529) to R: in MMAM; mut0
- F573 (≠ W536) 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 malonyl-CoA
- 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
6oxdA Structure of mycobacterium tuberculosis methylmalonyl-coa mutase with adenosyl cobalamin (see paper)
40% identity, 90% coverage: 47:539/545 of query aligns to 75:565/736 of 6oxdA
- active site: Y100 (≠ V72), Y254 (= Y226), H255 (= H227)
- binding cobalamin: Y100 (≠ V72), L130 (= L102), H133 (≠ L105), A150 (≠ V122), R218 (≠ Q190), E258 (≠ D230), G344 (≠ A317), W345 (≠ M318), E381 (= E354), A382 (= A355), A384 (= A357), L385 (≠ I358)
- binding Itaconyl coenzyme A: Y86 (= Y58), T88 (= T60), M89 (= M61), Q93 (≠ R65), T96 (= T68), R98 (= R70), Y100 (≠ V72), S175 (= S147), T177 (= T149), T206 (= T178), R218 (≠ Q190), H255 (= H227), R294 (= R266), S296 (= S268), F298 (= F270), R337 (= R310), T338 (≠ V311), H339 (= H312), Q341 (= Q314), Q372 (= Q345)
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)
39% identity, 97% coverage: 10:540/545 of query aligns to 25:557/725 of 5reqA
- active site: F86 (≠ V72), Y240 (= Y226), H241 (= H227)
- binding cobalamin: L116 (= L102), A136 (≠ V122), R204 (≠ Q190), H241 (= H227), E244 (≠ D230), G330 (≠ A317), W331 (≠ M318), E367 (= E354), A368 (= A355), A370 (= A357)
- binding methylmalonyl(carbadethia)-coenzyme a: Y72 (= Y58), T74 (= T60), M75 (= M61), R79 (= R65), T82 (= T68), R84 (= R70), F86 (≠ V72), S111 (= S97), S161 (= S147), T163 (= T149), T192 (= T178), Q194 (= Q180), R204 (≠ Q190), N233 (= N219), H241 (= H227), R280 (= R266), S282 (= S268), F284 (= F270), T324 (≠ V311), H325 (= H312), Q358 (= Q345), S359 (= S346)
- binding succinyl(carbadethia)-coenzyme a: Y72 (= Y58), T74 (= T60), M75 (= M61), R79 (= R65), T82 (= T68), R84 (= R70), F86 (≠ V72), S161 (= S147), T163 (= T149), T192 (= T178), R204 (≠ Q190), N233 (= N219), H241 (= H227), R280 (= R266), S282 (= S268), F284 (= F270), H325 (= H312), Q358 (= Q345)
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
7reqA Methylmalonyl-coa mutase, 2-carboxypropyl-coa inhibitor complex (see paper)
39% identity, 97% coverage: 10:540/545 of query aligns to 25:557/725 of 7reqA
- active site: Y86 (≠ V72), Y240 (= Y226), H241 (= H227)
- binding 2-carboxypropyl-coenzyme a: Y72 (= Y58), T74 (= T60), M75 (= M61), F78 (≠ G64), R79 (= R65), T82 (= T68), R84 (= R70), Y86 (≠ V72), S161 (= S147), T163 (= T149), T192 (= T178), R204 (≠ Q190), H241 (= H227), R280 (= R266), S282 (= S268), F284 (= F270), H325 (= H312), Q358 (= Q345)
- binding cobalamin: Y86 (≠ V72), L116 (= L102), A136 (≠ V122), R204 (≠ Q190), E244 (≠ D230), G330 (≠ A317), W331 (≠ M318), E367 (= E354), A368 (= A355), A370 (= A357)
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)
39% identity, 97% coverage: 10:540/545 of query aligns to 25:557/725 of 3reqA
- active site: Y86 (≠ V72), Y240 (= Y226), H241 (= H227)
- binding adenosine: Y86 (≠ V72), Y240 (= Y226), E244 (≠ D230), G330 (≠ A317)
- binding cobalamin: L116 (= L102), V203 (≠ A189), R204 (≠ Q190), E244 (≠ D230), G330 (≠ A317), W331 (≠ M318), A368 (= A355)
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)
39% identity, 97% coverage: 10:540/545 of query aligns to 25:557/725 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
6reqA Methylmalonyl-coa mutase, 3-carboxypropyl-coa inhibitor complex (see paper)
39% identity, 97% coverage: 10:540/545 of query aligns to 27:559/727 of 6reqA
- active site: Y88 (≠ V72), Y242 (= Y226), H243 (= H227)
- binding 3-carboxypropyl-coenzyme a: Y74 (= Y58), T76 (= T60), M77 (= M61), F80 (≠ G64), R81 (= R65), T84 (= T68), R86 (= R70), Y88 (≠ V72), S113 (= S97), S163 (= S147), T165 (= T149), T194 (= T178), R206 (≠ Q190), H243 (= H227), R282 (= R266), S284 (= S268), F286 (= F270), H327 (= H312), Q329 (= Q314), Q360 (= Q345)
- binding cobalamin: Y88 (≠ V72), F116 (= F100), L118 (= L102), H121 (≠ L105), A138 (≠ V122), R206 (≠ Q190), E246 (≠ D230), G332 (≠ A317), W333 (≠ M318), E369 (= E354), A370 (= A355), A372 (= A357)
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
4reqA Methylmalonyl-coa mutase substrate complex (see paper)
39% identity, 97% coverage: 10:540/545 of query aligns to 26:558/726 of 4reqA
- active site: Y87 (≠ V72), Y241 (= Y226), H242 (= H227)
- binding cobalamin: Y87 (≠ V72), L117 (= L102), A137 (≠ V122), V204 (≠ A189), R205 (≠ Q190), H242 (= H227), E245 (≠ D230), G331 (≠ A317), W332 (≠ M318), E368 (= E354), A369 (= A355), A371 (= A357), L372 (≠ I358)
- binding methylmalonyl-coenzyme a: Y73 (= Y58), M76 (= M61), F79 (≠ G64), R80 (= R65), T83 (= T68), R85 (= R70), Y87 (≠ V72), S112 (= S97), S162 (= S147), T164 (= T149), T193 (= T178), R205 (≠ Q190), N234 (= N219), Y241 (= Y226), H242 (= H227), R281 (= R266), S283 (= S268), F285 (= F270), H326 (= H312), Q328 (= Q314), Q359 (= Q345), S360 (= S346)
- binding succinyl-coenzyme a: Y73 (= Y58), M76 (= M61), F79 (≠ G64), R80 (= R65), T83 (= T68), R85 (= R70), Y87 (≠ V72), S162 (= S147), T164 (= T149), T193 (= T178), Q195 (= Q180), R205 (≠ Q190), N234 (= N219), Y241 (= Y226), H242 (= H227), R281 (= R266), S283 (= S268), F285 (= F270), R324 (= R310), H326 (= H312), Q359 (= Q345)
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
P11653 Methylmalonyl-CoA mutase large subunit; MCM-alpha; EC 5.4.99.2 from Propionibacterium freudenreichii subsp. shermanii (see 4 papers)
39% identity, 97% coverage: 10:540/545 of query aligns to 28:560/728 of P11653
- Y75 (= Y58) binding (R)-methylmalonyl-CoA
- M78 (= M61) binding (R)-methylmalonyl-CoA
- R82 (= R65) binding (R)-methylmalonyl-CoA
- T85 (= T68) binding (R)-methylmalonyl-CoA
- R87 (= R70) binding (R)-methylmalonyl-CoA
- Y89 (≠ V72) binding (R)-methylmalonyl-CoA; mutation to F: Does not significantly affect affinity for succiny-CoA, but kcat is lowered about 580-fold.
- S114 (= S97) binding (R)-methylmalonyl-CoA
- F117 (= F100) binding cob(II)alamin
- A139 (≠ V122) binding cob(II)alamin
- T195 (= T178) binding (R)-methylmalonyl-CoA
- Q197 (= Q180) binding (R)-methylmalonyl-CoA
- V206 (≠ A189) binding cob(II)alamin
- R207 (≠ Q190) binding (R)-methylmalonyl-CoA; binding cob(II)alamin
- H244 (= H227) binding (R)-methylmalonyl-CoA
- R283 (= R266) binding (R)-methylmalonyl-CoA
- S285 (= S268) binding (R)-methylmalonyl-CoA
- G333 (≠ A317) binding cob(II)alamin
- E370 (= E354) binding cob(II)alamin
- A373 (= A357) binding cob(II)alamin
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 609 binding cob(II)alamin
- 610 binding axial binding residue
- 611 binding cob(II)alamin
- 612 binding cob(II)alamin
- 655 binding cob(II)alamin
- 657 binding cob(II)alamin
- 686 binding cob(II)alamin
- 709 binding cob(II)alamin
1e1cA Methylmalonyl-coa mutase h244a mutant (see paper)
38% identity, 97% coverage: 10:540/545 of query aligns to 27:559/727 of 1e1cA
- active site: Y88 (≠ V72), Y242 (= Y226), A243 (≠ H227)
- binding cobalamin: Y88 (≠ V72), L118 (= L102), H121 (≠ L105), A138 (≠ V122), V205 (≠ A189), R206 (≠ Q190), E246 (≠ D230), G332 (≠ A317), W333 (≠ M318), E369 (= E354), A370 (= A355), A372 (= A357), L373 (≠ I358)
- binding desulfo-coenzyme a: Y74 (= Y58), M77 (= M61), F80 (≠ G64), R81 (= R65), T84 (= T68), R86 (= R70), S113 (= S97), S163 (= S147), T165 (= T149), T194 (= T178), R282 (= R266), S284 (= S268), H327 (= H312), Q360 (= Q345)
Sites not aligning to the query:
- active site: 603, 607, 609
- binding cobalamin: 608, 609, 610, 611, 612, 616, 620, 654, 656, 684, 685, 686, 704, 705, 708, 713
Q5KUG0 Fused isobutyryl-CoA mutase; EC 5.4.99.13; EC 3.6.5.- from Geobacillus kaustophilus (strain HTA426) (see paper)
35% identity, 91% coverage: 48:543/545 of query aligns to 566:1086/1086 of Q5KUG0
Sites not aligning to the query:
- 213 K→A: Loss of GTPase and ATPase activities. No effect on the mutase activity.
5cjtA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isobutyryl-coenzyme a (see paper)
34% identity, 91% coverage: 48:543/545 of query aligns to 546:1062/1062 of 5cjtA
- active site: F569 (≠ V72), Y750 (= Y226), H751 (= H227)
- binding cobalamin: F598 (= F100), L603 (= L105), S621 (≠ V122), Q713 (= Q190), H751 (= H227), E754 (≠ D230), A755 (≠ V231), G839 (≠ A317), R840 (≠ M318), E876 (= E354), A877 (= A355), T879 (≠ A357), H964 (≠ G442)
- binding isobutyryl-coenzyme a: F556 (≠ Y58), F558 (≠ T60), R560 (≠ Y62), R567 (= R70), F569 (≠ V72), R593 (vs. gap), S648 (= S147), T650 (= T149), R699 (≠ T176), T701 (= T178), Q703 (= Q180), Y743 (≠ N219), Y750 (= Y226), H751 (= H227), S792 (= S268), F794 (= F270), R827 (≠ E305), K832 (≠ R310), H834 (= H312)
- binding guanosine-5'-diphosphate: E944 (= E422)
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)
34% identity, 91% coverage: 48:543/545 of query aligns to 543:1053/1053 of 4xc7A
- active site: F566 (≠ V72), Y747 (= Y226), H748 (= H227)
- binding Butyryl Coenzyme A: F553 (≠ Y58), R557 (≠ Y62), R564 (= R70), F566 (≠ V72), R590 (vs. gap), S645 (= S147), T647 (= T149), R696 (≠ T176), T698 (= T178), Y740 (≠ N219), S789 (= S268), F791 (= F270), R824 (≠ E305), K829 (≠ R310), H831 (= H312)
Sites not aligning to the query:
Q1LRY0 Fused isobutyryl-CoA mutase; EC 5.4.99.13; EC 3.6.5.- from Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34) (Ralstonia metallidurans) (see 2 papers)
34% identity, 91% coverage: 48:543/545 of query aligns to 575:1093/1093 of Q1LRY0
- F587 (≠ T60) binding substrate
- F598 (≠ V72) mutation to A: Switches the substrate specificity and enhances the catalytic efficiency of the isovaleryl-CoA mutase over the native isobutyryl-CoA mutase activity about 4000-fold. Is even more susceptible to inactivation than wild-type during turnover.
- R622 (vs. gap) binding substrate
- R728 (≠ T176) binding substrate
- Y772 (≠ N219) binding substrate
- S821 (= S268) binding substrate
- R856 (≠ E305) binding substrate
- K861 (≠ R310) binding substrate
- E973 (= E422) binding GTP
- N1092 (≠ P542) binding GTP
Sites not aligning to the query:
- 39 binding axial binding residue
- 169:417 GTPase chaperone MeaI
- 219:224 binding GTP
- 223 binding Mg(2+)
- 248 binding Mg(2+)
- 249 binding Mg(2+)
- 262 binding Mg(2+); binding Mg(2+)
- 265 binding GTP
- 310 binding Mg(2+); binding Mg(2+)
- 311 binding Mg(2+)
- 357:360 binding GTP
- 418:579 Linker
8sslA Isobutyryl-coa mutase fused q341a in the presence of gtp (see paper)
34% identity, 91% coverage: 48:543/545 of query aligns to 554:1072/1072 of 8sslA
Sites not aligning to the query:
- binding guanosine-5'-diphosphate: 200, 201, 202, 241, 244, 337, 339, 374, 375, 376
- binding magnesium ion: 201, 241
Query Sequence
>YP_001313797.1 NCBI__GCF_000017145.1:YP_001313797.1
MGGGALAATLKSRPEEKQTYETESGIPLKRIYTAADIADIPASELGFPGAYPFTRGVYPT
MYRGRPWTIRQVAGFGNPEATNQRYKYMIQTGQTGLSTDFDLPTLLGLDSDDPMAFGEVG
RVGVAIDTVDDVERLFDGIDLEKISVSLTINPSAWVIYAMFVTVAEERGCDLHKLTGTLQ
ADPLKEYVAQKEWIYPVRPAVRLLRDLIMYSARTTPKINPVSLSGYHLSDVGGNALQEIA
FTMAFTISYCEEVTRAGMDIDDFAPRLSFFFISHQDFFEQICKFRAARRVYAKIMSERFN
ARKPESMRLRVHVQTAAMSLTKVEHHNNLMRTAIQALGAVLGGCQSMHTNGLDEAFAIPT
EEAMKLAIRTQQIIREEINVTSVIDPLGGSYFIERLTKDMEDEVWKMLDEIQKRGGAIKL
VEEGWFQQKLADSAYATFKKIGSGEKISVGVNKYVDAASRSADVHIHPYDDHCTQLQIDR
LRAVRENRDDARIQSLLKELVEQARSDDINLLPKTIELVRAKATLGEICSALREVWGSYS
EPMIV
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