SitesBLAST
Comparing WP_013257706.1 NCBI__GCF_000143965.1:WP_013257706.1 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)
50% identity, 97% coverage: 11:548/553 of query aligns to 17:557/562 of I3VE77
- YPTM 76:79 (≠ QPTM 69:72) binding (3S)-3-hydroxybutanoyl-CoA
- TMR 86:88 (= TMR 79:81) binding (3S)-3-hydroxybutanoyl-CoA
- I90 (≠ Y83) 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 (≠ A110) binding (3S)-3-hydroxybutanoyl-CoA; mutation to A: 2-fold increase in catalytic efficiency with 2-hydroxyisobutyryl-CoA as substrate. Small increase in catalytic efficiency with (S)-3-hydroxybuytryl-CoA as substrate. 1800-fold increase in catalytic efficiency with (R)-3-hydroxybutyryl-CoA as substrate.; mutation to V: 1.5-fold increase in catalytic efficiency with 2-hydroxyisobutyryl-CoA as substrate. 3-fold decrease in catalytic efficiency with (S)-3-hydroxybuytryl-CoA as substrate. 1300-fold increase in catalytic efficiency with (R)-3-hydroxybutyryl-CoA as substrate. 74-fold increase in catalytic efficiency with pivalyl-CoA as substrate.
- TVQ 196:198 (≠ TIQ 189:191) binding (3S)-3-hydroxybutanoyl-CoA
- R235 (≠ Q228) binding (3S)-3-hydroxybutanoyl-CoA
- N240 (≠ S233) binding (3S)-3-hydroxybutanoyl-CoA
- H245 (= H238) binding (3S)-3-hydroxybutanoyl-CoA
- R284 (= R277) binding (3S)-3-hydroxybutanoyl-CoA
4r3uA Crystal structure of 2-hydroxyisobutyryl-coa mutase (see paper)
50% identity, 97% coverage: 11:548/553 of query aligns to 16:556/557 of 4r3uA
- active site: I89 (≠ Y83), Y243 (= Y237), H244 (= H238)
- binding 3-hydroxybutanoyl-coenzyme a: Y75 (≠ Q69), T77 (= T71), M78 (= M72), R82 (≠ Q76), T85 (= T79), R87 (= R81), I89 (≠ Y83), D116 (≠ A110), S164 (= S158), T166 (= T160), T195 (= T189), Q197 (= Q191), R234 (≠ Q228), N236 (= N230), N239 (≠ S233), Y243 (= Y237), H244 (= H238), R283 (= R277), F287 (= F281), R327 (= R321), F328 (= F322), H329 (= H323), Q331 (= Q325), Q362 (= Q356)
- binding S-{(3R,5R,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5-dioxido-10,14-dioxo-2,4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl} 2-hydroxy-2-methylpropanethioate: Y75 (≠ Q69), T77 (= T71), M78 (= M72), R82 (≠ Q76), T85 (= T79), R87 (= R81), I89 (≠ Y83), D116 (≠ A110), S164 (= S158), T166 (= T160), T195 (= T189), Q197 (= Q191), R234 (≠ Q228), N236 (= N230), N239 (≠ S233), H244 (= H238), R283 (= R277), F287 (= F281), R327 (= R321), F328 (= F322), H329 (= H323), Q331 (= Q325), Q362 (= Q356)
- binding cobalamin: D116 (≠ A110), M119 (≠ L113), E139 (≠ V133), Q207 (≠ R201), E209 (≠ T203), E247 (= E241), A334 (≠ G328), E371 (= E365), A372 (= A366), A374 (≠ C368)
6oxdA Structure of mycobacterium tuberculosis methylmalonyl-coa mutase with adenosyl cobalamin (see paper)
52% identity, 89% coverage: 58:549/553 of query aligns to 75:567/736 of 6oxdA
- active site: Y100 (= Y83), Y254 (= Y237), H255 (= H238)
- binding cobalamin: Y100 (= Y83), L130 (= L113), H133 (≠ Q116), A150 (≠ V133), R218 (= R201), E258 (= E241), G344 (= G328), W345 (≠ C329), E381 (= E365), A382 (= A366), A384 (≠ C368), L385 (= L369)
- binding Itaconyl coenzyme A: Y86 (≠ Q69), T88 (= T71), M89 (= M72), Q93 (= Q76), T96 (= T79), R98 (= R81), Y100 (= Y83), S175 (= S158), T177 (= T160), T206 (= T189), R218 (= R201), H255 (= H238), R294 (= R277), S296 (= S279), F298 (= F281), R337 (= R321), T338 (≠ F322), H339 (= H323), Q341 (= Q325), Q372 (= Q356)
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
8dyjB Crystal structure of human methylmalonyl-coa mutase in complex with adp and cob(ii)alamin (see paper)
48% identity, 97% coverage: 12:549/553 of query aligns to 6:542/708 of 8dyjB
- binding adenosine-5'-diphosphate: Y74 (= Y83), T151 (= T160), R192 (= R201), Y228 (= Y237), H229 (= H238), F272 (= F281), Q316 (= Q325), N352 (= N361), E356 (= E365), L360 (= L369), P361 (= P370)
- binding cobalamin: F102 (= F111), L104 (= L113), H107 (≠ Q116), A124 (≠ V133), V191 (≠ S200), R192 (= R201), H229 (= H238), E232 (= E241), G319 (= G328), W320 (≠ C329), E356 (= E365), G359 (≠ C368), L360 (= L369)
Sites not aligning to the query:
- binding cobalamin: 590, 591, 592, 593, 594, 598, 636, 638, 640, 666, 667, 668, 686, 687, 690
2xiqA Crystal structure of human methylmalonyl-coa mutase in complex with adenosylcobalamin and malonyl-coa (see paper)
48% identity, 97% coverage: 12:549/553 of query aligns to 7:543/714 of 2xiqA
- active site: Y75 (= Y83), Y229 (= Y237), H230 (= H238)
- binding cobalamin: Y75 (= Y83), L105 (= L113), H108 (≠ Q116), A125 (≠ V133), R193 (= R201), E233 (= E241), G320 (= G328), W321 (≠ C329), E357 (= E365), G360 (≠ C368), L361 (= L369)
- binding malonyl-coenzyme a: Y61 (≠ Q69), T63 (= T71), M64 (= M72), R68 (≠ Q76), T71 (= T79), R73 (= R81), Y75 (= Y83), S150 (= S158), T152 (= T160), T181 (= T189), R193 (= R201), K220 (≠ Q228), H230 (= H238), R269 (= R277), S271 (= S279), F273 (= F281), R313 (= R321), A314 (≠ F322), H315 (= H323), Q317 (= Q325), Q348 (= Q356)
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
P22033 Methylmalonyl-CoA mutase, mitochondrial; MCM; Methylmalonyl-CoA isomerase; EC 5.4.99.2 from Homo sapiens (Human) (see 28 papers)
48% identity, 97% coverage: 12:549/553 of query aligns to 42:578/750 of P22033
- Q50 (≠ L20) binding malonyl-CoA
- I69 (= I39) to V: in MMAM; likely benign; dbSNP:rs115923556
- P86 (= P59) 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 (= G60) to E: in MMAM; mut0; dbSNP:rs1554160986
- R93 (= R66) to H: in MMAM; mut0; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918251
- G94 (= G67) to R: in MMAM; mut0; dbSNP:rs727504022; to V: in MMAM; mut- and mut0; dbSNP:rs535411418
- P95 (≠ V68) to R: in MMAM; mut0; dbSNP:rs190834116
- YPTM 96:99 (≠ QPTM 69:72) binding malonyl-CoA
- Y100 (= Y73) 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 (= W78) to R: in MMAM; mut0; dbSNP:rs121918249
- TIRQY 106:110 (≠ TMRQY 79:83) binding malonyl-CoA
- R108 (= R81) to C: in MMAM; mut0; dbSNP:rs121918257; to G: in MMAM; mut-; to H: in MMAM; mut0; dbSNP:rs483352778
- Q109 (= Q82) to R: in MMAM; mut0; dbSNP:rs1461110052
- G133 (= G106) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253828
- A137 (= A110) to V: in MMAM; mut0; dbSNP:rs941483851
- D139 (= D112) to N: in MMAM; uncertain significance; dbSNP:rs879253829
- L140 (= L113) to P: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- A141 (≠ P114) to T: in MMAM; decreased protein expression; dbSNP:rs1554160730
- H143 (≠ Q116) to Y: in MMAM; mut0
- G145 (= G118) to S: in MMAM; mut0
- S148 (≠ A121) to L: in MMAM; mut0; dbSNP:rs1300547552
- D156 (≠ E129) to N: in MMAM; mut-
- G158 (= G131) to V: in MMAM; mut0
- G161 (= G134) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; to V: in MMAM; decreased protein expression
- F174 (= F147) to S: in MMAM; mut0; dbSNP:rs864309733
- M186 (= M159) to V: in MMAM; mut-; dbSNP:rs148331800
- T187 (= T160) to S: in MMAM; mut0; dbSNP:rs879253830
- N189 (= N162) to I: in MMAM; mut-; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs200908035; to K: in MMAM; mut-; dbSNP:rs1561959114
- A191 (≠ P164) to E: in MMAM; mut- and mut0; affects proper folding; reduced protein level; decreased methylmalonyl-CoA mutase activity; dbSNP:rs760782399
- A197 (= A170) to E: in MMAM; mut0
- G203 (≠ A176) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs778702777
- E205 (≠ K178) natural variant: Missing (in MMAM; mut0; dbSNP:rs879253831)
- G215 (= G188) to C: in MMAM; mut- and mut0; dbSNP:rs121918258; to S: in MMAM; mut0; dbSNP:rs121918258
- TIQ 216:218 (= TIQ 189:191) binding malonyl-CoA
- Q218 (= Q191) to H: in MMAM; mut0 and mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability; dbSNP:rs1446389693
- N219 (= N192) to Y: in MMAM; mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; dbSNP:rs121918256
- R228 (= R201) binding malonyl-CoA; to Q: in MMAM; mut0; dbSNP:rs770810987
- T230 (= T203) to I: in MMAM; mut-; to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253833
- Y231 (= Y204) 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 (≠ Q228) binding malonyl-CoA
- S262 (= S235) to N: in MMAM; mut0
- H265 (= H238) binding malonyl-CoA; to Y: in MMAM; mut-
- E276 (= E249) to D: in MMAM; uncertain significance; mut-; dbSNP:rs12175488
- L281 (= L254) to S: in MMAM; mut0; dbSNP:rs796052007
- G284 (= G257) to E: in MMAM; mut0; dbSNP:rs879253835; to R: in MMAM; mut0; dbSNP:rs761477436
- S288 (≠ V261) to P: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1179778233
- G291 (≠ A264) to E: in MMAM; mut0
- Q293 (≠ D266) to P: in MMAM; mut0
- RLS 304:306 (= RLS 277:279) binding malonyl-CoA
- L305 (= L278) to S: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554160246
- S306 (= S279) to F: in MMAM; mut0; dbSNP:rs1085307929
- W309 (≠ F282) to G: in MMAM; decreased protein expression
- G312 (≠ H285) to V: in MMAM; mut0; dbSNP:rs864309734
- Y316 (≠ L289) 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 (= A297) to T: in MMAM; mut-; dbSNP:rs780387525
- R326 (= R299) to K: in MMAM; uncertain significance; dbSNP:rs758577372
- L328 (= L301) to F: in MMAM; mut0; affects proper folding; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; dbSNP:rs796052002; to P: in MMAM; mut0; dbSNP:rs965316043
- S344 (= S317) to F: in MMAM; mut-; affects proper folding; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin
- L346 (≠ M319) natural variant: Missing (in MMAM; mut0)
- L347 (≠ I320) to R: in MMAM; mut0; dbSNP:rs1026703654
- H350 (= H323) to Y: in MMAM; mut0; dbSNP:rs1407914109
- L358 (= L331) to P: in MMAM; mut0
- N366 (= N339) to S: in MMAM; mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability; dbSNP:rs864309737
- R369 (= R342) to C: in MMAM; mut0; dbSNP:rs772552898; to H: in MMAM; mut- and mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability; dbSNP:rs564069299
- T370 (≠ V343) to P: in MMAM; mut0; dbSNP:rs368790885
- A377 (= A350) to E: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918250
- Q383 (= Q356) to H: in MMAM; mut0; to P: in MMAM; mut0
- H386 (= H359) to N: in MMAM; mut0; dbSNP:rs1554159937; to R: in MMAM; mut0; dbSNP:rs866933356
- T387 (= T360) to I: in MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability
- N388 (= N361) to H: in MMAM; mut0; dbSNP:rs766010704; to K: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253840
- S389 (= S362) natural variant: Missing (in MMAM; mut0)
- I412 (= I385) natural variant: Missing (in MMAM; mut0)
- P424 (= P397) to L: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253842
- G426 (≠ A399) to E: in MMAM; mut-; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs533755473; to R: in MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; strong decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability; dbSNP:rs769922244
- G427 (= G400) to D: in MMAM; mut0; dbSNP:rs753288303
- G454 (= G427) to E: in MMAM; mut0
- A499 (≠ V472) to T: in dbSNP:rs2229385
- I505 (≠ V478) to T: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- Q514 (= Q486) to E: in MMAM; uncertain significance; to K: in MMAM; decreased protein expression
- L518 (= L490) to P: in MMAM; mut0; dbSNP:rs864309738
- R532 (≠ A504) to H: in dbSNP:rs1141321
- A535 (= A507) to P: in MMAM; mut0; dbSNP:rs760183775
- A552 (≠ I523) to V: in MMAM; uncertain significance; dbSNP:rs879253845
- C560 (≠ A531) to Y: in MMAM; mut0; dbSNP:rs1238333040
- T566 (≠ C537) to R: in MMAM; mut0
- F573 (= F544) 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-)
- 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
8gjuJ Crystal structure of human methylmalonyl-coa mutase (mmut) in complex with methylmalonic acidemia type a protein (mmaa), coenzyme a, and gdp (see paper)
47% identity, 97% coverage: 12:548/553 of query aligns to 7:542/689 of 8gjuJ
- binding coenzyme a: Y61 (≠ Q69), T63 (= T71), R68 (≠ Q76), T71 (= T79), R73 (= R81), S150 (= S158), T152 (= T160), T181 (= T189), Q183 (= Q191), N222 (= N230), R269 (= R277), S271 (= S279), R313 (= R321), A314 (≠ F322), H315 (= H323), Q348 (= Q356)
P11653 Methylmalonyl-CoA mutase large subunit; MCM-alpha; EC 5.4.99.2 from Propionibacterium freudenreichii subsp. shermanii (see 4 papers)
49% identity, 96% coverage: 21:549/553 of query aligns to 28:561/728 of P11653
- Y75 (≠ Q69) binding (R)-methylmalonyl-CoA
- M78 (= M72) binding (R)-methylmalonyl-CoA
- R82 (≠ Q76) binding (R)-methylmalonyl-CoA
- T85 (= T79) binding (R)-methylmalonyl-CoA
- R87 (= R81) binding (R)-methylmalonyl-CoA
- Y89 (= Y83) binding (R)-methylmalonyl-CoA; mutation to F: Does not significantly affect affinity for succiny-CoA, but kcat is lowered about 580-fold.
- S114 (= S108) binding (R)-methylmalonyl-CoA
- F117 (= F111) binding cob(II)alamin
- A139 (≠ V133) binding cob(II)alamin
- T195 (= T189) binding (R)-methylmalonyl-CoA
- Q197 (= Q191) binding (R)-methylmalonyl-CoA
- V206 (≠ S200) binding cob(II)alamin
- R207 (= R201) binding (R)-methylmalonyl-CoA; binding cob(II)alamin
- H244 (= H238) binding (R)-methylmalonyl-CoA
- R283 (= R277) binding (R)-methylmalonyl-CoA
- S285 (= S279) binding (R)-methylmalonyl-CoA
- G333 (= G328) binding cob(II)alamin
- E370 (= E365) binding cob(II)alamin
- A373 (≠ C368) 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
7reqA Methylmalonyl-coa mutase, 2-carboxypropyl-coa inhibitor complex (see paper)
49% identity, 96% coverage: 21:549/553 of query aligns to 25:558/725 of 7reqA
- active site: Y86 (= Y83), Y240 (= Y237), H241 (= H238)
- binding 2-carboxypropyl-coenzyme a: Y72 (≠ Q69), T74 (= T71), M75 (= M72), F78 (≠ G75), R79 (≠ Q76), T82 (= T79), R84 (= R81), Y86 (= Y83), S161 (= S158), T163 (= T160), T192 (= T189), R204 (= R201), H241 (= H238), R280 (= R277), S282 (= S279), F284 (= F281), H325 (= H323), Q358 (= Q356)
- binding cobalamin: Y86 (= Y83), L116 (= L113), A136 (≠ V133), R204 (= R201), E244 (= E241), G330 (= G328), W331 (≠ C329), E367 (= E365), A368 (= A366), A370 (≠ C368)
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)
49% identity, 96% coverage: 21:549/553 of query aligns to 25:558/725 of 3reqA
- active site: Y86 (= Y83), Y240 (= Y237), H241 (= H238)
- binding adenosine: Y86 (= Y83), Y240 (= Y237), E244 (= E241), G330 (= G328)
- binding cobalamin: L116 (= L113), V203 (≠ S200), R204 (= R201), E244 (= E241), G330 (= G328), W331 (≠ C329), A368 (= A366)
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)
49% identity, 96% coverage: 21:549/553 of query aligns to 25:558/725 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)
49% identity, 96% coverage: 21:549/553 of query aligns to 27:560/727 of 6reqA
- active site: Y88 (= Y83), Y242 (= Y237), H243 (= H238)
- binding 3-carboxypropyl-coenzyme a: Y74 (≠ Q69), T76 (= T71), M77 (= M72), F80 (≠ G75), R81 (≠ Q76), T84 (= T79), R86 (= R81), Y88 (= Y83), S113 (= S108), S163 (= S158), T165 (= T160), T194 (= T189), R206 (= R201), H243 (= H238), R282 (= R277), S284 (= S279), F286 (= F281), H327 (= H323), Q329 (= Q325), Q360 (= Q356)
- binding cobalamin: Y88 (= Y83), F116 (= F111), L118 (= L113), H121 (≠ Q116), A138 (≠ V133), R206 (= R201), E246 (= E241), G332 (= G328), W333 (≠ C329), E369 (= E365), A370 (= A366), A372 (≠ C368)
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)
49% identity, 96% coverage: 21:549/553 of query aligns to 26:559/726 of 4reqA
- active site: Y87 (= Y83), Y241 (= Y237), H242 (= H238)
- binding cobalamin: Y87 (= Y83), L117 (= L113), A137 (≠ V133), V204 (≠ S200), R205 (= R201), H242 (= H238), E245 (= E241), G331 (= G328), W332 (≠ C329), E368 (= E365), A369 (= A366), A371 (≠ C368), L372 (= L369)
- binding methylmalonyl-coenzyme a: Y73 (≠ Q69), M76 (= M72), F79 (≠ G75), R80 (≠ Q76), T83 (= T79), R85 (= R81), Y87 (= Y83), S112 (= S108), S162 (= S158), T164 (= T160), T193 (= T189), R205 (= R201), N234 (= N230), Y241 (= Y237), H242 (= H238), R281 (= R277), S283 (= S279), F285 (= F281), H326 (= H323), Q328 (= Q325), Q359 (= Q356), S360 (= S357)
- binding succinyl-coenzyme a: Y73 (≠ Q69), M76 (= M72), F79 (≠ G75), R80 (≠ Q76), T83 (= T79), R85 (= R81), Y87 (= Y83), S162 (= S158), T164 (= T160), T193 (= T189), Q195 (= Q191), R205 (= R201), N234 (= N230), Y241 (= Y237), H242 (= H238), R281 (= R277), S283 (= S279), F285 (= F281), R324 (= R321), H326 (= H323), Q359 (= Q356)
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
5reqA Methylmalonyl-coa mutase, y89f mutant, substrate complex (see paper)
49% identity, 96% coverage: 21:549/553 of query aligns to 25:558/725 of 5reqA
- active site: F86 (≠ Y83), Y240 (= Y237), H241 (= H238)
- binding cobalamin: L116 (= L113), A136 (≠ V133), R204 (= R201), H241 (= H238), E244 (= E241), G330 (= G328), W331 (≠ C329), E367 (= E365), A368 (= A366), A370 (≠ C368)
- binding methylmalonyl(carbadethia)-coenzyme a: Y72 (≠ Q69), T74 (= T71), M75 (= M72), R79 (≠ Q76), T82 (= T79), R84 (= R81), F86 (≠ Y83), S111 (= S108), S161 (= S158), T163 (= T160), T192 (= T189), Q194 (= Q191), R204 (= R201), N233 (= N230), H241 (= H238), R280 (= R277), S282 (= S279), F284 (= F281), T324 (≠ F322), H325 (= H323), Q358 (= Q356), S359 (= S357)
- binding succinyl(carbadethia)-coenzyme a: Y72 (≠ Q69), T74 (= T71), M75 (= M72), R79 (≠ Q76), T82 (= T79), R84 (= R81), F86 (≠ Y83), S161 (= S158), T163 (= T160), T192 (= T189), R204 (= R201), N233 (= N230), H241 (= H238), R280 (= R277), S282 (= S279), F284 (= F281), H325 (= H323), Q358 (= Q356)
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
1e1cA Methylmalonyl-coa mutase h244a mutant (see paper)
49% identity, 96% coverage: 21:549/553 of query aligns to 27:560/727 of 1e1cA
- active site: Y88 (= Y83), Y242 (= Y237), A243 (≠ H238)
- binding cobalamin: Y88 (= Y83), L118 (= L113), H121 (≠ Q116), A138 (≠ V133), V205 (≠ S200), R206 (= R201), E246 (= E241), G332 (= G328), W333 (≠ C329), E369 (= E365), A370 (= A366), A372 (≠ C368), L373 (= L369)
- binding desulfo-coenzyme a: Y74 (≠ Q69), M77 (= M72), F80 (≠ G75), R81 (≠ Q76), T84 (= T79), R86 (= R81), S113 (= S108), S163 (= S158), T165 (= T160), T194 (= T189), R282 (= R277), S284 (= S279), H327 (= H323), Q360 (= Q356)
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
5cjtA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isobutyryl-coenzyme a (see paper)
37% identity, 96% coverage: 19:551/553 of query aligns to 490:1062/1062 of 5cjtA
- active site: F569 (≠ Y83), Y750 (= Y237), H751 (= H238)
- binding cobalamin: F598 (= F111), L603 (≠ Q116), S621 (≠ V133), Q713 (≠ R201), H751 (= H238), E754 (= E241), A755 (= A242), G839 (= G328), R840 (≠ C329), E876 (= E365), A877 (= A366), T879 (≠ C368), H964 (≠ E453)
- binding isobutyryl-coenzyme a: F556 (≠ Q69), F558 (≠ T71), R560 (≠ Y73), R567 (= R81), F569 (≠ Y83), R593 (vs. gap), S648 (vs. gap), T650 (= T160), R699 (= R187), T701 (= T189), Q703 (= Q191), Y743 (≠ N230), Y750 (= Y237), H751 (= H238), S792 (= S279), F794 (= F281), R827 (= R316), K832 (≠ R321), H834 (= H323)
- binding guanosine-5'-diphosphate: E944 (= E433)
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
5cjwA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate pivalyl-coenzyme a (see paper)
37% identity, 96% coverage: 19:551/553 of query aligns to 491:1063/1063 of 5cjwA
- active site: F571 (≠ Y83), Y752 (= Y237), H753 (= H238)
- binding pivalyl-coenzyme A: F558 (≠ Q69), F560 (≠ T71), R562 (≠ Y73), R569 (= R81), F571 (≠ Y83), R595 (vs. gap), S650 (vs. gap), T652 (= T160), R701 (= R187), T703 (= T189), Q705 (= Q191), Y745 (≠ N230), Y752 (= Y237), H753 (= H238), S794 (= S279), F796 (= F281), R829 (= R316), K834 (≠ R321), H836 (= H323)
- binding cobalamin: F600 (= F111), L605 (≠ Q116), S623 (≠ V133), Q715 (≠ R201), H753 (= H238), E756 (= E241), A757 (= A242), G841 (= G328), R842 (≠ C329), E878 (= E365), A879 (= A366), T881 (≠ C368), H966 (≠ E453)
- binding guanosine-5'-diphosphate: N1062 (≠ P550)
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
5cjvA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isovaleryl-coenzyme a (see paper)
37% identity, 96% coverage: 19:551/553 of query aligns to 489:1061/1061 of 5cjvA
- active site: F569 (≠ Y83), Y750 (= Y237), H751 (= H238)
- binding cobalamin: F598 (= F111), L603 (≠ Q116), S621 (≠ V133), Q713 (≠ R201), E754 (= E241), A755 (= A242), G839 (= G328), R840 (≠ C329), E876 (= E365), A877 (= A366), T879 (≠ C368), H964 (≠ E453)
- binding guanosine-5'-diphosphate: E944 (= E433)
- binding Isovaleryl-coenzyme A: F556 (≠ Q69), F558 (≠ T71), R560 (≠ Y73), R567 (= R81), F569 (≠ Y83), R593 (vs. gap), S648 (vs. gap), T650 (= T160), R699 (= R187), T701 (= T189), Q703 (= Q191), Q713 (≠ R201), Y743 (≠ N230), H751 (= H238), S792 (= S279), F794 (= F281), K832 (≠ R321), H834 (= H323)
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
4xc7A Isobutyryl-coa mutase fused with bound butyryl-coa and without cobalamin or gdp (apo-icmf) (see paper)
37% identity, 96% coverage: 19:551/553 of query aligns to 485:1053/1053 of 4xc7A
- active site: F566 (≠ Y83), Y747 (= Y237), H748 (= H238)
- binding Butyryl Coenzyme A: F553 (≠ Q69), R557 (≠ Y73), R564 (= R81), F566 (≠ Y83), R590 (vs. gap), S645 (vs. gap), T647 (= T160), R696 (= R187), T698 (= T189), Y740 (≠ N230), S789 (= S279), F791 (= F281), R824 (= R316), K829 (≠ R321), H831 (= H323)
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)
36% identity, 94% coverage: 33:551/553 of query aligns to 536:1086/1086 of Q5KUG0
Sites not aligning to the query:
- 213 K→A: Loss of GTPase and ATPase activities. No effect on the mutase activity.
Query Sequence
>WP_013257706.1 NCBI__GCF_000143965.1:WP_013257706.1
MSGQNFDESLRKWQAGVDKLLAKRPERKAAFHTISGLPIDRLYLPAAPDDDYMEKLGLPG
EFPYTRGVQPTMYRGQLWTMRQYAGFATAAESNKRYRYLLGQGQTGLSVAFDLPTQIGYD
ADHALAHGEVGKVGVSISSLKDMETLFDQIPLDKVSTSMTINSPAAVLLAMYIAVAEKQG
VGPAQLRGTIQNDILKEYSSRGTYIFPPRPSMRIITDIFAYCASDVPQWNTISISGYHIR
EAGSTAVQEVAFTLANGMAYVQAAIDAGLDVDVFGPRLSFFFNAHSDFLEEVAKYRAARR
LWAKIMRERFGAKNPRSQMIRFHTQTAGCSLTAKQPKNNIMRVAFQAMSAVLGGTQSLHT
NSMDEALCLPTQESVTIALRTQQVIGYETGVTETIDPLAGSYYVEDLTDRIEAQAAEYIR
RIDEMGGSVSAIEQGFIQREIQEAAYKYQKDIESGERVVVGQNKFVTDEEFVGDRLKVDL
SVGQAQAQALAALRAGRDNAAVQARLAALQAAAKGSDNLMPLILDAVRVYATLGEICDTL
RGVFGEYQAPMTI
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