SitesBLAST
Comparing WP_084517158.1 NCBI__GCF_000422285.1:WP_084517158.1 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, 99% coverage: 5:561/561 of query aligns to 4:562/562 of I3VE77
- YPTM 76:79 (≠ QPSM 77:80) binding (3S)-3-hydroxybutanoyl-CoA
- TMR 86:88 (= TMR 87:89) binding (3S)-3-hydroxybutanoyl-CoA
- I90 (≠ F91) 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 (≠ A118) 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 197:199) binding (3S)-3-hydroxybutanoyl-CoA
- R235 (= R236) binding (3S)-3-hydroxybutanoyl-CoA
- N240 (≠ S241) binding (3S)-3-hydroxybutanoyl-CoA
- H245 (= H246) binding (3S)-3-hydroxybutanoyl-CoA
- R284 (= R285) binding (3S)-3-hydroxybutanoyl-CoA
4r3uA Crystal structure of 2-hydroxyisobutyryl-coa mutase (see paper)
50% identity, 99% coverage: 5:557/561 of query aligns to 3:557/557 of 4r3uA
- active site: I89 (≠ F91), Y243 (= Y245), H244 (= H246)
- binding 3-hydroxybutanoyl-coenzyme a: Y75 (≠ Q77), T77 (≠ S79), M78 (= M80), R82 (= R84), T85 (= T87), R87 (= R89), I89 (≠ F91), D116 (≠ A118), S164 (= S166), T166 (= T168), T195 (= T197), Q197 (= Q199), R234 (= R236), N236 (= N238), N239 (≠ S241), Y243 (= Y245), H244 (= H246), R283 (= R285), F287 (= F289), R327 (= R329), F328 (= F330), H329 (= H331), Q331 (= Q333), Q362 (= Q364)
- 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 (≠ Q77), T77 (≠ S79), M78 (= M80), R82 (= R84), T85 (= T87), R87 (= R89), I89 (≠ F91), D116 (≠ A118), S164 (= S166), T166 (= T168), T195 (= T197), Q197 (= Q199), R234 (= R236), N236 (= N238), N239 (≠ S241), H244 (= H246), R283 (= R285), F287 (= F289), R327 (= R329), F328 (= F330), H329 (= H331), Q331 (= Q333), Q362 (= Q364)
- binding cobalamin: D116 (≠ A118), M119 (= M121), E139 (≠ C141), Q207 (= Q209), E209 (≠ T211), E247 (= E249), A334 (≠ G336), E371 (= E373), A372 (≠ V374), A374 (= A376)
P22033 Methylmalonyl-CoA mutase, mitochondrial; MCM; Methylmalonyl-CoA isomerase; EC 5.4.99.2 from Homo sapiens (Human) (see 28 papers)
45% identity, 93% coverage: 38:556/561 of query aligns to 61:577/750 of P22033
- I69 (= I46) to V: in MMAM; likely benign; dbSNP:rs115923556
- P86 (= P67) 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 (= G68) to E: in MMAM; mut0; dbSNP:rs1554160986
- R93 (= R74) to H: in MMAM; mut0; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918251
- G94 (= G75) to R: in MMAM; mut0; dbSNP:rs727504022; to V: in MMAM; mut- and mut0; dbSNP:rs535411418
- P95 (≠ V76) to R: in MMAM; mut0; dbSNP:rs190834116
- YPTM 96:99 (≠ QPSM 77:80) binding malonyl-CoA
- Y100 (= Y81) 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 (= W86) to R: in MMAM; mut0; dbSNP:rs121918249
- TIRQY 106:110 (≠ TMRMF 87:91) binding malonyl-CoA
- R108 (= R89) to C: in MMAM; mut0; dbSNP:rs121918257; to G: in MMAM; mut-; to H: in MMAM; mut0; dbSNP:rs483352778
- Q109 (≠ M90) to R: in MMAM; mut0; dbSNP:rs1461110052
- G133 (= G114) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253828
- A137 (= A118) to V: in MMAM; mut0; dbSNP:rs941483851
- D139 (= D120) to N: in MMAM; uncertain significance; dbSNP:rs879253829
- L140 (≠ M121) to P: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- A141 (≠ P122) to T: in MMAM; decreased protein expression; dbSNP:rs1554160730
- H143 (≠ L124) to Y: in MMAM; mut0
- G145 (= G126) to S: in MMAM; mut0
- S148 (= S129) to L: in MMAM; mut0; dbSNP:rs1300547552
- D156 (≠ E137) to N: in MMAM; mut-
- G158 (= G139) to V: in MMAM; mut0
- G161 (= G142) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; to V: in MMAM; decreased protein expression
- F174 (= F155) to S: in MMAM; mut0; dbSNP:rs864309733
- M186 (= M167) to V: in MMAM; mut-; dbSNP:rs148331800
- T187 (= T168) to S: in MMAM; mut0; dbSNP:rs879253830
- N189 (= N170) to I: in MMAM; mut-; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs200908035; to K: in MMAM; mut-; dbSNP:rs1561959114
- A191 (≠ P172) to E: in MMAM; mut- and mut0; affects proper folding; reduced protein level; decreased methylmalonyl-CoA mutase activity; dbSNP:rs760782399
- A197 (= A178) to E: in MMAM; mut0
- G203 (≠ A184) to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs778702777
- E205 (≠ N186) natural variant: Missing (in MMAM; mut0; dbSNP:rs879253831)
- G215 (= G196) to C: in MMAM; mut- and mut0; dbSNP:rs121918258; to S: in MMAM; mut0; dbSNP:rs121918258
- TIQ 216:218 (= TIQ 197:199) binding malonyl-CoA
- Q218 (= Q199) to H: in MMAM; mut0 and mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability; dbSNP:rs1446389693
- N219 (= N200) to Y: in MMAM; mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; dbSNP:rs121918256
- R228 (≠ Q209) binding malonyl-CoA; to Q: in MMAM; mut0; dbSNP:rs770810987
- T230 (= T211) to I: in MMAM; mut-; to R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253833
- Y231 (≠ F212) 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 (≠ R236) binding malonyl-CoA
- S262 (= S243) to N: in MMAM; mut0
- H265 (= H246) binding malonyl-CoA; to Y: in MMAM; mut-
- E276 (= E257) to D: in MMAM; uncertain significance; mut-; dbSNP:rs12175488
- L281 (= L262) to S: in MMAM; mut0; dbSNP:rs796052007
- G284 (= G265) to E: in MMAM; mut0; dbSNP:rs879253835; to R: in MMAM; mut0; dbSNP:rs761477436
- S288 (≠ T269) to P: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1179778233
- G291 (≠ A272) to E: in MMAM; mut0
- Q293 (≠ K274) to P: in MMAM; mut0
- RLS 304:306 (≠ RFS 285:287) binding malonyl-CoA
- L305 (≠ F286) to S: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554160246
- S306 (= S287) to F: in MMAM; mut0; dbSNP:rs1085307929
- W309 (≠ F290) to G: in MMAM; decreased protein expression
- G312 (≠ H293) to V: in MMAM; mut0; dbSNP:rs864309734
- Y316 (≠ F297) 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 (= A305) to T: in MMAM; mut-; dbSNP:rs780387525
- R326 (= R307) to K: in MMAM; uncertain significance; dbSNP:rs758577372
- L328 (≠ M309) 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 (= S325) 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 (≠ W327) natural variant: Missing (in MMAM; mut0)
- L347 (= L328) to R: in MMAM; mut0; dbSNP:rs1026703654
- H350 (= H331) to Y: in MMAM; mut0; dbSNP:rs1407914109
- L358 (= L339) to P: in MMAM; mut0
- N366 (= N347) 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 (= R350) 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 (= T351) to P: in MMAM; mut0; dbSNP:rs368790885
- A377 (= A358) to E: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918250
- Q383 (= Q364) to H: in MMAM; mut0; to P: in MMAM; mut0
- H386 (= H367) to N: in MMAM; mut0; dbSNP:rs1554159937; to R: in MMAM; mut0; dbSNP:rs866933356
- T387 (= T368) 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 (= N369) to H: in MMAM; mut0; dbSNP:rs766010704; to K: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253840
- S389 (= S370) natural variant: Missing (in MMAM; mut0)
- I412 (= I393) natural variant: Missing (in MMAM; mut0)
- P424 (= P405) to L: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253842
- G426 (= G407) 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 (= G408) to D: in MMAM; mut0; dbSNP:rs753288303
- G454 (= G435) to E: in MMAM; mut0
- A499 (≠ P480) to T: in dbSNP:rs2229385
- I505 (= I486) to T: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- Q514 (= Q494) to E: in MMAM; uncertain significance; to K: in MMAM; decreased protein expression
- L518 (= L498) to P: in MMAM; mut0; dbSNP:rs864309738
- R532 (≠ E512) to H: in dbSNP:rs1141321
- A535 (≠ E515) to P: in MMAM; mut0; dbSNP:rs760183775
- A552 (≠ V531) to V: in MMAM; uncertain significance; dbSNP:rs879253845
- C560 (≠ A539) to Y: in MMAM; mut0; dbSNP:rs1238333040
- T566 (≠ C545) to R: in MMAM; mut0
- F573 (= F552) 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
8gjuJ Crystal structure of human methylmalonyl-coa mutase (mmut) in complex with methylmalonic acidemia type a protein (mmaa), coenzyme a, and gdp (see paper)
45% identity, 93% coverage: 38:557/561 of query aligns to 26:543/689 of 8gjuJ
- binding coenzyme a: Y61 (≠ Q77), T63 (≠ S79), R68 (= R84), T71 (= T87), R73 (= R89), S150 (= S166), T152 (= T168), T181 (= T197), Q183 (= Q199), N222 (= N238), R269 (= R285), S271 (= S287), R313 (= R329), A314 (≠ F330), H315 (= H331), Q348 (= Q364)
2xiqA Crystal structure of human methylmalonyl-coa mutase in complex with adenosylcobalamin and malonyl-coa (see paper)
45% identity, 93% coverage: 38:556/561 of query aligns to 26:542/714 of 2xiqA
- active site: Y75 (≠ F91), Y229 (= Y245), H230 (= H246)
- binding cobalamin: Y75 (≠ F91), L105 (≠ M121), H108 (≠ L124), A125 (≠ C141), R193 (≠ Q209), E233 (= E249), G320 (= G336), W321 (≠ C337), E357 (= E373), G360 (≠ A376), L361 (≠ I377)
- binding malonyl-coenzyme a: Y61 (≠ Q77), T63 (≠ S79), M64 (= M80), R68 (= R84), T71 (= T87), R73 (= R89), Y75 (≠ F91), S150 (= S166), T152 (= T168), T181 (= T197), R193 (≠ Q209), K220 (≠ R236), H230 (= H246), R269 (= R285), S271 (= S287), F273 (= F289), R313 (= R329), A314 (≠ F330), H315 (= H331), Q317 (= Q333), Q348 (= Q364)
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)
45% identity, 93% coverage: 38:556/561 of query aligns to 25:541/708 of 8dyjB
- binding adenosine-5'-diphosphate: Y74 (≠ F91), T151 (= T168), R192 (≠ Q209), Y228 (= Y245), H229 (= H246), F272 (= F289), Q316 (= Q333), N352 (= N369), E356 (= E373), L360 (≠ I377), P361 (= P378)
- binding cobalamin: F102 (= F119), L104 (≠ M121), H107 (≠ L124), A124 (≠ C141), V191 (≠ A208), R192 (≠ Q209), H229 (= H246), E232 (= E249), G319 (= G336), W320 (≠ C337), E356 (= E373), G359 (≠ A376), L360 (≠ I377)
Sites not aligning to the query:
- binding cobalamin: 590, 591, 592, 593, 594, 598, 636, 638, 640, 666, 667, 668, 686, 687, 690
5reqA Methylmalonyl-coa mutase, y89f mutant, substrate complex (see paper)
43% identity, 95% coverage: 22:555/561 of query aligns to 20:556/725 of 5reqA
- active site: F86 (= F91), Y240 (= Y245), H241 (= H246)
- binding cobalamin: L116 (≠ M121), A136 (≠ C141), R204 (≠ Q209), H241 (= H246), E244 (= E249), G330 (= G336), W331 (≠ C337), E367 (= E373), A368 (≠ V374), A370 (= A376)
- binding methylmalonyl(carbadethia)-coenzyme a: Y72 (≠ Q77), T74 (≠ S79), M75 (= M80), R79 (= R84), T82 (= T87), R84 (= R89), F86 (= F91), S111 (= S116), S161 (= S166), T163 (= T168), T192 (= T197), Q194 (= Q199), R204 (≠ Q209), N233 (= N238), H241 (= H246), R280 (= R285), S282 (= S287), F284 (= F289), T324 (≠ F330), H325 (= H331), Q358 (= Q364), S359 (= S365)
- binding succinyl(carbadethia)-coenzyme a: Y72 (≠ Q77), T74 (≠ S79), M75 (= M80), R79 (= R84), T82 (= T87), R84 (= R89), F86 (= F91), S161 (= S166), T163 (= T168), T192 (= T197), R204 (≠ Q209), N233 (= N238), H241 (= H246), R280 (= R285), S282 (= S287), F284 (= F289), H325 (= H331), Q358 (= Q364)
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
4reqA Methylmalonyl-coa mutase substrate complex (see paper)
43% identity, 95% coverage: 22:555/561 of query aligns to 21:557/726 of 4reqA
- active site: Y87 (≠ F91), Y241 (= Y245), H242 (= H246)
- binding cobalamin: Y87 (≠ F91), L117 (≠ M121), A137 (≠ C141), V204 (≠ A208), R205 (≠ Q209), H242 (= H246), E245 (= E249), G331 (= G336), W332 (≠ C337), E368 (= E373), A369 (≠ V374), A371 (= A376), L372 (≠ I377)
- binding methylmalonyl-coenzyme a: Y73 (≠ Q77), M76 (= M80), F79 (≠ G83), R80 (= R84), T83 (= T87), R85 (= R89), Y87 (≠ F91), S112 (= S116), S162 (= S166), T164 (= T168), T193 (= T197), R205 (≠ Q209), N234 (= N238), Y241 (= Y245), H242 (= H246), R281 (= R285), S283 (= S287), F285 (= F289), H326 (= H331), Q328 (= Q333), Q359 (= Q364), S360 (= S365)
- binding succinyl-coenzyme a: Y73 (≠ Q77), M76 (= M80), F79 (≠ G83), R80 (= R84), T83 (= T87), R85 (= R89), Y87 (≠ F91), S162 (= S166), T164 (= T168), T193 (= T197), Q195 (= Q199), R205 (≠ Q209), N234 (= N238), Y241 (= Y245), H242 (= H246), R281 (= R285), S283 (= S287), F285 (= F289), R324 (= R329), H326 (= H331), Q359 (= Q364)
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
7reqA Methylmalonyl-coa mutase, 2-carboxypropyl-coa inhibitor complex (see paper)
43% identity, 95% coverage: 22:555/561 of query aligns to 20:556/725 of 7reqA
- active site: Y86 (≠ F91), Y240 (= Y245), H241 (= H246)
- binding 2-carboxypropyl-coenzyme a: Y72 (≠ Q77), T74 (≠ S79), M75 (= M80), F78 (≠ G83), R79 (= R84), T82 (= T87), R84 (= R89), Y86 (≠ F91), S161 (= S166), T163 (= T168), T192 (= T197), R204 (≠ Q209), H241 (= H246), R280 (= R285), S282 (= S287), F284 (= F289), H325 (= H331), Q358 (= Q364)
- binding cobalamin: Y86 (≠ F91), L116 (≠ M121), A136 (≠ C141), R204 (≠ Q209), E244 (= E249), G330 (= G336), W331 (≠ C337), E367 (= E373), A368 (≠ V374), A370 (= A376)
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)
43% identity, 95% coverage: 22:555/561 of query aligns to 20:556/725 of 3reqA
- active site: Y86 (≠ F91), Y240 (= Y245), H241 (= H246)
- binding adenosine: Y86 (≠ F91), Y240 (= Y245), E244 (= E249), G330 (= G336)
- binding cobalamin: L116 (≠ M121), V203 (≠ A208), R204 (≠ Q209), E244 (= E249), G330 (= G336), W331 (≠ C337), A368 (≠ V374)
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)
43% identity, 95% coverage: 22:555/561 of query aligns to 20:556/725 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
6reqA Methylmalonyl-coa mutase, 3-carboxypropyl-coa inhibitor complex (see paper)
43% identity, 95% coverage: 22:555/561 of query aligns to 22:558/727 of 6reqA
- active site: Y88 (≠ F91), Y242 (= Y245), H243 (= H246)
- binding 3-carboxypropyl-coenzyme a: Y74 (≠ Q77), T76 (≠ S79), M77 (= M80), F80 (≠ G83), R81 (= R84), T84 (= T87), R86 (= R89), Y88 (≠ F91), S113 (= S116), S163 (= S166), T165 (= T168), T194 (= T197), R206 (≠ Q209), H243 (= H246), R282 (= R285), S284 (= S287), F286 (= F289), H327 (= H331), Q329 (= Q333), Q360 (= Q364)
- binding cobalamin: Y88 (≠ F91), F116 (= F119), L118 (≠ M121), H121 (≠ L124), A138 (≠ C141), R206 (≠ Q209), E246 (= E249), G332 (= G336), W333 (≠ C337), E369 (= E373), A370 (≠ V374), A372 (= A376)
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)
43% identity, 95% coverage: 22:555/561 of query aligns to 23:559/728 of P11653
- Y75 (≠ Q77) binding (R)-methylmalonyl-CoA
- M78 (= M80) binding (R)-methylmalonyl-CoA
- R82 (= R84) binding (R)-methylmalonyl-CoA
- T85 (= T87) binding (R)-methylmalonyl-CoA
- R87 (= R89) binding (R)-methylmalonyl-CoA
- Y89 (≠ F91) binding (R)-methylmalonyl-CoA; mutation to F: Does not significantly affect affinity for succiny-CoA, but kcat is lowered about 580-fold.
- S114 (= S116) binding (R)-methylmalonyl-CoA
- F117 (= F119) binding cob(II)alamin
- A139 (≠ C141) binding cob(II)alamin
- T195 (= T197) binding (R)-methylmalonyl-CoA
- Q197 (= Q199) binding (R)-methylmalonyl-CoA
- V206 (≠ A208) binding cob(II)alamin
- R207 (≠ Q209) binding (R)-methylmalonyl-CoA; binding cob(II)alamin
- H244 (= H246) binding (R)-methylmalonyl-CoA
- R283 (= R285) binding (R)-methylmalonyl-CoA
- S285 (= S287) binding (R)-methylmalonyl-CoA
- G333 (= G336) binding cob(II)alamin
- E370 (= E373) binding cob(II)alamin
- A373 (= A376) 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
6oxdA Structure of mycobacterium tuberculosis methylmalonyl-coa mutase with adenosyl cobalamin (see paper)
45% identity, 88% coverage: 66:556/561 of query aligns to 75:566/736 of 6oxdA
- active site: Y100 (≠ F91), Y254 (= Y245), H255 (= H246)
- binding cobalamin: Y100 (≠ F91), L130 (≠ M121), H133 (≠ L124), A150 (≠ C141), R218 (≠ Q209), E258 (= E249), G344 (= G336), W345 (≠ C337), E381 (= E373), A382 (≠ V374), A384 (= A376), L385 (≠ I377)
- binding Itaconyl coenzyme A: Y86 (≠ Q77), T88 (≠ S79), M89 (= M80), Q93 (≠ R84), T96 (= T87), R98 (= R89), Y100 (≠ F91), S175 (= S166), T177 (= T168), T206 (= T197), R218 (≠ Q209), H255 (= H246), R294 (= R285), S296 (= S287), F298 (= F289), R337 (= R329), T338 (≠ F330), H339 (= H331), Q341 (= Q333), Q372 (= Q364)
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
1e1cA Methylmalonyl-coa mutase h244a mutant (see paper)
43% identity, 95% coverage: 22:555/561 of query aligns to 22:558/727 of 1e1cA
- active site: Y88 (≠ F91), Y242 (= Y245), A243 (≠ H246)
- binding cobalamin: Y88 (≠ F91), L118 (≠ M121), H121 (≠ L124), A138 (≠ C141), V205 (≠ A208), R206 (≠ Q209), E246 (= E249), G332 (= G336), W333 (≠ C337), E369 (= E373), A370 (≠ V374), A372 (= A376), L373 (≠ I377)
- binding desulfo-coenzyme a: Y74 (≠ Q77), M77 (= M80), F80 (≠ G83), R81 (= R84), T84 (= T87), R86 (= R89), S113 (= S116), S163 (= S166), T165 (= T168), T194 (= T197), R282 (= R285), S284 (= S287), H327 (= H331), Q360 (= Q364)
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)
36% identity, 89% coverage: 59:556/561 of query aligns to 558:1083/1086 of Q5KUG0
Sites not aligning to the query:
- 213 K→A: Loss of GTPase and ATPase activities. No effect on the mutase activity.
5cjtA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isobutyryl-coenzyme a (see paper)
37% identity, 87% coverage: 67:556/561 of query aligns to 546:1059/1062 of 5cjtA
- active site: F569 (= F91), Y750 (= Y245), H751 (= H246)
- binding cobalamin: F598 (= F119), L603 (= L124), S621 (≠ C141), Q713 (= Q209), H751 (= H246), E754 (= E249), A755 (= A250), G839 (= G336), R840 (≠ C337), E876 (= E373), A877 (≠ V374), T879 (≠ A376), H964 (≠ D461)
- binding isobutyryl-coenzyme a: F556 (≠ Q77), F558 (≠ S79), R560 (≠ Y81), R567 (= R89), F569 (= F91), R593 (vs. gap), S648 (vs. gap), T650 (= T168), R699 (≠ G195), T701 (= T197), Q703 (= Q199), Y743 (≠ N238), Y750 (= Y245), H751 (= H246), S792 (= S287), F794 (= F289), R827 (= R324), K832 (≠ R329), H834 (= H331)
- binding guanosine-5'-diphosphate: E944 (= E441)
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)
36% identity, 87% coverage: 67:556/561 of query aligns to 546:1058/1061 of 5cjvA
- active site: F569 (= F91), Y750 (= Y245), H751 (= H246)
- binding cobalamin: F598 (= F119), L603 (= L124), S621 (≠ C141), Q713 (= Q209), E754 (= E249), A755 (= A250), G839 (= G336), R840 (≠ C337), E876 (= E373), A877 (≠ V374), T879 (≠ A376), H964 (≠ D461)
- binding guanosine-5'-diphosphate: E944 (= E441)
- binding Isovaleryl-coenzyme A: F556 (≠ Q77), F558 (≠ S79), R560 (≠ Y81), R567 (= R89), F569 (= F91), R593 (vs. gap), S648 (vs. gap), T650 (= T168), R699 (≠ G195), T701 (= T197), Q703 (= Q199), Q713 (= Q209), Y743 (≠ N238), H751 (= H246), S792 (= S287), F794 (= F289), K832 (≠ R329), H834 (= H331)
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
8sslA Isobutyryl-coa mutase fused q341a in the presence of gtp (see paper)
36% identity, 87% coverage: 67:556/561 of query aligns to 554:1069/1072 of 8sslA
Sites not aligning to the query:
- binding guanosine-5'-diphosphate: 200, 201, 202, 241, 244, 337, 339, 374, 375, 376, 1071
- binding magnesium ion: 201, 241
5cjwA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate pivalyl-coenzyme a (see paper)
36% identity, 87% coverage: 67:556/561 of query aligns to 548:1060/1063 of 5cjwA
- active site: F571 (= F91), Y752 (= Y245), H753 (= H246)
- binding pivalyl-coenzyme A: F558 (≠ Q77), F560 (≠ S79), R562 (≠ Y81), R569 (= R89), F571 (= F91), R595 (vs. gap), S650 (vs. gap), T652 (= T168), R701 (≠ G195), T703 (= T197), Q705 (= Q199), Y745 (≠ N238), Y752 (= Y245), H753 (= H246), S794 (= S287), F796 (= F289), R829 (= R324), K834 (≠ R329), H836 (= H331)
- binding cobalamin: F600 (= F119), L605 (= L124), S623 (≠ C141), Q715 (= Q209), H753 (= H246), E756 (= E249), A757 (= A250), G841 (= G336), R842 (≠ C337), E878 (= E373), A879 (≠ V374), T881 (≠ A376), H966 (≠ D461)
Sites not aligning to the query:
- active site: 6
- binding cobalamin: 18, 19, 20, 21, 22, 26, 66, 67, 94, 96, 98, 116, 117, 118
- binding guanosine-5'-diphosphate: 199, 201, 202, 203, 204, 245, 337, 338, 340, 375, 377, 1062
- binding magnesium ion: 203, 229, 242, 242, 290, 290
Query Sequence
>WP_084517158.1 NCBI__GCF_000422285.1:WP_084517158.1
MSMTFNPKVFGDIEKAEERWRKELEEIFRQHGERLERFSTVSDVEIGRLYTPLDVRDQRY
MDALGFPGEYPFTRGVQPSMYRGRLWTMRMFAGLGTAKDTNRRFHVLVNAGQTGLSTAFD
MPTLMGYDSDASKARGECGRCGVAIDTLKDMEDLFDGLPIDQITTSMTINPPASVVWAMY
IAMAENRGIPRNVIGGTIQNDMLKEFIAQKTFMCPPRPSVRLVTDTVEFGTREVPRWNTI
SISGYHIREAGSTAVQELAFTLADGIAYTEEALKRGLPVDSFAPRFSFFFNSHLDFFEEI
AKFRAARRMWGKIMRERFKAQNPRSWWLRFHTQTAGCSLTAQQPYNNVVRTALEALAAVL
GGTQSLHTNSLDEVLAIPTEEAATIALRTQQIIAEESGVANTIDPLGGSYFVEGLTDKME
RDAFEIIRKIDDMGGMLAAIERNYPQQEIADAAYHYQRQIDAGEKTVVGVNKYVTEEDVP
VEILEIDEELERLQIEKLNRVKSLRDQTRVAECLERVGEACAADTNVMEPVIAAVKAQAT
LQEVCDVYRSVFGIYRDPGIY
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