SitesBLAST
Comparing WP_036833956.1 NCBI__GCF_000775615.1:WP_036833956.1 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)
3oa4A Crystal structure of hypothetical protein bh1468 from bacillus halodurans c-125
57% identity, 49% coverage: 143:276/276 of query aligns to 4:137/138 of 3oa4A
I3VE74 2-hydroxyisobutanoyl-CoA mutase small subunit; 2-hydroxyisobutyryl-CoA mutase small subunit; HCM small subunit; EC 5.4.99.64 from Aquincola tertiaricarbonis (see paper)
52% identity, 43% coverage: 1:118/276 of query aligns to 1:118/136 of I3VE74
- H18 (= H18) binding axial binding residue
4r3uC Crystal structure of 2-hydroxyisobutyryl-coa mutase (see paper)
53% identity, 41% coverage: 6:118/276 of query aligns to 4:116/131 of 4r3uC
- active site: K10 (= K12), D14 (= D16), H16 (= H18)
- binding cobalamin: G15 (= G17), H16 (= H18), D17 (= D19), R18 (= R20), G19 (= G21), V23 (≠ I25), G59 (= G61), S61 (= S63), L63 (= L65), I89 (= I91), A90 (≠ G92), G91 (= G93), G92 (= G94), L111 (≠ F113), L112 (≠ T114), Q113 (≠ P115), T115 (= T117)
5reqA Methylmalonyl-coa mutase, y89f mutant, substrate complex (see paper)
43% identity, 47% coverage: 2:131/276 of query aligns to 591:720/725 of 5reqA
- active site: K601 (= K12), D605 (= D16), H607 (= H18)
- binding cobalamin: G606 (= G17), H607 (= H18), D608 (= D19), R609 (= R20), G610 (= G21), I614 (= I25), S652 (= S63), L654 (= L65), G682 (= G93), G683 (= G94), V684 (= V95), Y702 (≠ F113), T703 (= T114), T706 (= T117)
Sites not aligning to the query:
- active site: 86, 240, 241
- binding cobalamin: 116, 136, 204, 241, 244, 330, 331, 367, 368, 370
- binding methylmalonyl(carbadethia)-coenzyme a: 72, 74, 75, 79, 82, 84, 86, 111, 161, 163, 192, 194, 204, 233, 241, 280, 282, 284, 324, 325, 358, 359
- binding succinyl(carbadethia)-coenzyme a: 72, 74, 75, 79, 82, 84, 86, 161, 163, 192, 204, 233, 241, 280, 282, 284, 325, 358
4reqA Methylmalonyl-coa mutase substrate complex (see paper)
43% identity, 47% coverage: 2:131/276 of query aligns to 592:721/726 of 4reqA
- active site: K602 (= K12), D606 (= D16), H608 (= H18)
- binding cobalamin: G607 (= G17), H608 (= H18), D609 (= D19), R610 (= R20), G611 (= G21), I615 (= I25), S653 (= S63), L655 (= L65), G683 (= G93), G684 (= G94), V685 (= V95), Y703 (≠ F113), T704 (= T114), T707 (= T117)
Sites not aligning to the query:
- active site: 87, 241, 242
- binding cobalamin: 87, 117, 137, 204, 205, 242, 245, 331, 332, 368, 369, 371, 372
- binding methylmalonyl-coenzyme a: 73, 76, 79, 80, 83, 85, 87, 112, 162, 164, 193, 205, 234, 241, 242, 281, 283, 285, 326, 328, 359, 360
- binding succinyl-coenzyme a: 73, 76, 79, 80, 83, 85, 87, 162, 164, 193, 195, 205, 234, 241, 242, 281, 283, 285, 324, 326, 359
1e1cA Methylmalonyl-coa mutase h244a mutant (see paper)
43% identity, 47% coverage: 2:131/276 of query aligns to 593:722/727 of 1e1cA
- active site: K603 (= K12), D607 (= D16), H609 (= H18)
- binding cobalamin: G608 (= G17), H609 (= H18), D610 (= D19), R611 (= R20), G612 (= G21), I616 (= I25), Y620 (≠ L29), S654 (= S63), L656 (= L65), G684 (= G93), G685 (= G94), V686 (= V95), Y704 (≠ F113), T705 (= T114), T708 (= T117), S713 (≠ T122)
Sites not aligning to the query:
- active site: 88, 242, 243
- binding cobalamin: 88, 118, 121, 138, 205, 206, 246, 332, 333, 369, 370, 372, 373
- binding desulfo-coenzyme a: 74, 77, 80, 81, 84, 86, 113, 163, 165, 194, 282, 284, 327, 360
7reqA Methylmalonyl-coa mutase, 2-carboxypropyl-coa inhibitor complex (see paper)
43% identity, 47% coverage: 2:131/276 of query aligns to 591:720/725 of 7reqA
- active site: K601 (= K12), D605 (= D16), H607 (= H18)
- binding cobalamin: G606 (= G17), H607 (= H18), D608 (= D19), R609 (= R20), G610 (= G21), I614 (= I25), S652 (= S63), L654 (= L65), G682 (= G93), G683 (= G94), Y702 (≠ F113), T703 (= T114), T706 (= T117)
Sites not aligning to the query:
- active site: 86, 240, 241
- binding 2-carboxypropyl-coenzyme a: 72, 74, 75, 78, 79, 82, 84, 86, 161, 163, 192, 204, 241, 280, 282, 284, 325, 358
- binding cobalamin: 86, 116, 136, 204, 244, 330, 331, 367, 368, 370
6reqA Methylmalonyl-coa mutase, 3-carboxypropyl-coa inhibitor complex (see paper)
43% identity, 47% coverage: 2:131/276 of query aligns to 593:722/727 of 6reqA
- active site: K603 (= K12), D607 (= D16), H609 (= H18)
- binding cobalamin: G608 (= G17), H609 (= H18), D610 (= D19), R611 (= R20), G612 (= G21), I616 (= I25), Y620 (≠ L29), S654 (= S63), L656 (= L65), G658 (= G67), G684 (= G93), G685 (= G94), Y704 (≠ F113), T705 (= T114), T708 (= T117)
Sites not aligning to the query:
- active site: 88, 242, 243
- binding 3-carboxypropyl-coenzyme a: 74, 76, 77, 80, 81, 84, 86, 88, 113, 163, 165, 194, 206, 243, 282, 284, 286, 327, 329, 360
- binding cobalamin: 88, 116, 118, 121, 138, 206, 246, 332, 333, 369, 370, 372
3reqA Methylmalonyl-coa mutase, substrate-free state (poor quality structure) (see paper)
43% identity, 47% coverage: 2:131/276 of query aligns to 591:720/725 of 3reqA
- active site: K601 (= K12), D605 (= D16), H607 (= H18)
- binding cobalamin: G606 (= G17), H607 (= H18), D608 (= D19), R609 (= R20), G610 (= G21), I614 (= I25), G650 (= G61), S652 (= S63), L654 (= L65), G682 (= G93), G683 (= G94), Y702 (≠ F113), T703 (= T114), P704 (= P115), T706 (= T117)
Sites not aligning to the query:
- active site: 86, 240, 241
- binding adenosine: 86, 240, 244, 330
- binding cobalamin: 116, 203, 204, 244, 330, 331, 368
2reqA Methylmalonyl-coa mutase, non-productive coa complex, in open conformation representing substrate-free state (see paper)
43% identity, 47% coverage: 2:131/276 of query aligns to 591:720/725 of 2reqA
- active site: K601 (= K12), D605 (= D16), H607 (= H18)
- binding cobalamin: G606 (= G17), H607 (= H18), D608 (= D19), R609 (= R20), G610 (= G21), I614 (= I25), G650 (= G61), S652 (= S63), L654 (= L65), A655 (≠ S66), G682 (= G93), G683 (= G94), Y702 (≠ F113), T703 (= T114), T706 (= T117)
Sites not aligning to the query:
P11653 Methylmalonyl-CoA mutase large subunit; MCM-alpha; EC 5.4.99.2 from Propionibacterium freudenreichii subsp. shermanii (see 4 papers)
43% identity, 47% coverage: 2:131/276 of query aligns to 594:723/728 of P11653
- G609 (= G17) binding cob(II)alamin
- H610 (= H18) binding axial binding residue
- D611 (= D19) binding cob(II)alamin
- R612 (= R20) binding cob(II)alamin
- S655 (= S63) binding cob(II)alamin
- L657 (= L65) binding cob(II)alamin
- G686 (= G94) binding cob(II)alamin
- T709 (= T117) binding cob(II)alamin
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 75 binding (R)-methylmalonyl-CoA
- 78 binding (R)-methylmalonyl-CoA
- 82 binding (R)-methylmalonyl-CoA
- 85 binding (R)-methylmalonyl-CoA
- 87 binding (R)-methylmalonyl-CoA
- 89 binding (R)-methylmalonyl-CoA; Y→F: Does not significantly affect affinity for succiny-CoA, but kcat is lowered about 580-fold.
- 114 binding (R)-methylmalonyl-CoA
- 117 binding cob(II)alamin
- 139 binding cob(II)alamin
- 195 binding (R)-methylmalonyl-CoA
- 197 binding (R)-methylmalonyl-CoA
- 206 binding cob(II)alamin
- 207 binding (R)-methylmalonyl-CoA; binding cob(II)alamin
- 244 binding (R)-methylmalonyl-CoA
- 283 binding (R)-methylmalonyl-CoA
- 285 binding (R)-methylmalonyl-CoA
- 333 binding cob(II)alamin
- 370 binding cob(II)alamin
- 373 binding cob(II)alamin
Q96PE7 Methylmalonyl-CoA epimerase, mitochondrial; DL-methylmalonyl-CoA racemase; EC 5.1.99.1 from Homo sapiens (Human) (see paper)
41% identity, 49% coverage: 135:270/276 of query aligns to 39:175/176 of Q96PE7
- H50 (= H146) binding Co(2+)
- R104 (≠ D200) to L: in dbSNP:rs6748672
- H122 (= H217) binding Co(2+)
- E172 (= E267) binding Co(2+)
P22033 Methylmalonyl-CoA mutase, mitochondrial; MCM; Methylmalonyl-CoA isomerase; EC 5.4.99.2 from Homo sapiens (Human) (see 28 papers)
40% identity, 49% coverage: 2:136/276 of query aligns to 611:749/750 of P22033
- P615 (≠ I6) to L: in MMAM; mut0; affects proper folding; reduced strongly protein level; to R: in MMAM; mut0; dbSNP:rs1554158777; to T: in MMAM; mut0; affects proper folding; reduced strongly protein level; loss of methylmalonyl-CoA mutase activity; dbSNP:rs1302409621
- R616 (= R7) to C: in MMAM; mut0; dbSNP:rs765284825
- L617 (≠ V8) to R: in MMAM; mut0; dbSNP:rs1554158775
- K621 (= K12) to N: in MMAM; mut0
- G623 (= G14) to R: in MMAM; mut0; dbSNP:rs121918254
- Q624 (≠ L15) to R: in MMAM; no effect on protein abundance; dbSNP:rs768521956
- D625 (= D16) to G: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253847; to V: in MMAM; mut0; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity
- G626 (= G17) to C: in MMAM; mut-; dbSNP:rs982110849
- H627 (= H18) binding axial binding residue; to R: in MMAM; mut0; dbSNP:rs372486357
- G630 (= G21) to E: in MMAM; mut0; dbSNP:rs143023066
- V633 (= V24) to 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
- G637 (≠ A28) to E: in MMAM; mut-; to R: in MMAM; mut0; dbSNP:rs781501004
- F638 (≠ L29) to I: in MMAM; mut0
- D640 (= D31) to Y: in MMAM; mut0; dbSNP:rs865815395
- G642 (= G33) to R: in MMAM; mut-; dbSNP:rs747897332
- G648 (≠ T39) to 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
- V669 (≠ I60) to E: in MMAM; mut0; dbSNP:rs1360470463
- I671 (≠ L62) to V: in dbSNP:rs8589
- L674 (= L65) to F: in MMAM; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1164271240
- H678 (= H69) to R: in MMAM; mut-; dbSNP:rs147094927
- E684 (≠ K75) natural variant: E -> EL (in MMAM; mut-)
- L685 (≠ V76) to R: in MMAM; mut-; dbSNP:rs864309739
- R694 (≠ A85) to L: in MMAM; mut-; decreased protein abundance; loss of methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability; to 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
- M700 (≠ I91) to 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
- G703 (= G94) to R: in MMAM; mut0; dbSNP:rs121918255
- G717 (= G108) to 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
- G723 (≠ T114) to D: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity; dbSNP:rs755077681
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
- 7:750 natural variant: Missing (in MMAM; mut-)
- 50 binding malonyl-CoA
- 69 I → V: in MMAM; likely benign; dbSNP:rs115923556
- 86 P → 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
- 87 G → E: in MMAM; mut0; dbSNP:rs1554160986
- 93 R → H: in MMAM; mut0; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918251
- 94 G → R: in MMAM; mut0; dbSNP:rs727504022; G → V: in MMAM; mut- and mut0; dbSNP:rs535411418
- 95 P → R: in MMAM; mut0; dbSNP:rs190834116
- 96:99 binding malonyl-CoA
- 100 Y → 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
- 105 W → R: in MMAM; mut0; dbSNP:rs121918249
- 106:110 binding malonyl-CoA
- 108 R → C: in MMAM; mut0; dbSNP:rs121918257; R → G: in MMAM; mut-; R → H: in MMAM; mut0; dbSNP:rs483352778
- 109 Q → R: in MMAM; mut0; dbSNP:rs1461110052
- 133 G → R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253828
- 137 A → V: in MMAM; mut0; dbSNP:rs941483851
- 139 D → N: in MMAM; uncertain significance; dbSNP:rs879253829
- 140 L → P: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- 141 A → T: in MMAM; decreased protein expression; dbSNP:rs1554160730
- 143 H → Y: in MMAM; mut0
- 145 G → S: in MMAM; mut0
- 148 S → L: in MMAM; mut0; dbSNP:rs1300547552
- 152:750 natural variant: Missing (in MMAM; mut0)
- 156 D → N: in MMAM; mut-
- 158 G → V: in MMAM; mut0
- 161 G → R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; G → V: in MMAM; decreased protein expression
- 174 F → S: in MMAM; mut0; dbSNP:rs864309733
- 186 M → V: in MMAM; mut-; dbSNP:rs148331800
- 187 T → S: in MMAM; mut0; dbSNP:rs879253830
- 189 N → I: in MMAM; mut-; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs200908035; N → K: in MMAM; mut-; dbSNP:rs1561959114
- 191 A → E: in MMAM; mut- and mut0; affects proper folding; reduced protein level; decreased methylmalonyl-CoA mutase activity; dbSNP:rs760782399
- 197 A → E: in MMAM; mut0
- 203 G → R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs778702777
- 205 natural variant: Missing (in MMAM; mut0; dbSNP:rs879253831)
- 215 G → C: in MMAM; mut- and mut0; dbSNP:rs121918258; G → S: in MMAM; mut0; dbSNP:rs121918258
- 216:218 binding malonyl-CoA
- 218 Q → H: in MMAM; mut0 and mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability; dbSNP:rs1446389693
- 219 N → Y: in MMAM; mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; dbSNP:rs121918256
- 228 binding malonyl-CoA; R → Q: in MMAM; mut0; dbSNP:rs770810987
- 228:750 natural variant: Missing (in MMAM; mut0)
- 230 T → I: in MMAM; mut-; T → R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253833
- 231 Y → 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
- 255 binding malonyl-CoA
- 262 S → N: in MMAM; mut0
- 265 binding malonyl-CoA; H → Y: in MMAM; mut-
- 276 E → D: in MMAM; uncertain significance; mut-; dbSNP:rs12175488
- 281 L → S: in MMAM; mut0; dbSNP:rs796052007
- 284 G → E: in MMAM; mut0; dbSNP:rs879253835; G → R: in MMAM; mut0; dbSNP:rs761477436
- 288 S → P: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1179778233
- 291 G → E: in MMAM; mut0
- 293 Q → P: in MMAM; mut0
- 304:306 binding malonyl-CoA
- 305 L → S: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554160246
- 306 S → F: in MMAM; mut0; dbSNP:rs1085307929
- 309 W → G: in MMAM; decreased protein expression
- 312 G → V: in MMAM; mut0; dbSNP:rs864309734
- 316 Y → C: in MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; no decreased affinity for adenosylcob(III)alamin; dbSNP:rs781474200
- 324 A → T: in MMAM; mut-; dbSNP:rs780387525
- 326 R → K: in MMAM; uncertain significance; dbSNP:rs758577372
- 328 L → F: in MMAM; mut0; affects proper folding; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; dbSNP:rs796052002; L → P: in MMAM; mut0; dbSNP:rs965316043
- 344 S → F: in MMAM; mut-; affects proper folding; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin
- 346 natural variant: Missing (in MMAM; mut0)
- 347 L → R: in MMAM; mut0; dbSNP:rs1026703654
- 350 H → Y: in MMAM; mut0; dbSNP:rs1407914109
- 358 L → P: in MMAM; mut0
- 366 N → 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
- 369 R → C: in MMAM; mut0; dbSNP:rs772552898; R → H: in MMAM; mut- and mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability; dbSNP:rs564069299
- 370 T → P: in MMAM; mut0; dbSNP:rs368790885
- 377 A → E: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918250
- 383 Q → H: in MMAM; mut0; Q → P: in MMAM; mut0
- 386 H → N: in MMAM; mut0; dbSNP:rs1554159937; H → R: in MMAM; mut0; dbSNP:rs866933356
- 387 T → I: in MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability
- 388 N → H: in MMAM; mut0; dbSNP:rs766010704; N → K: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253840
- 389 natural variant: Missing (in MMAM; mut0)
- 412 natural variant: Missing (in MMAM; mut0)
- 424 P → L: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253842
- 426 G → E: in MMAM; mut-; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs533755473; G → 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
- 427 G → D: in MMAM; mut0; dbSNP:rs753288303
- 454 G → E: in MMAM; mut0
- 499 A → T: in dbSNP:rs2229385
- 505 I → T: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
- 514 Q → E: in MMAM; uncertain significance; Q → K: in MMAM; decreased protein expression
- 518 L → P: in MMAM; mut0; dbSNP:rs864309738
- 532 R → H: in dbSNP:rs1141321
- 535 A → P: in MMAM; mut0; dbSNP:rs760183775
- 552 A → V: in MMAM; uncertain significance; dbSNP:rs879253845
- 560 C → Y: in MMAM; mut0; dbSNP:rs1238333040
- 566 T → R: in MMAM; mut0
- 573 F → 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
- 587 Y → C: in MMAM; mut-
- 597 I → R: in MMAM; no changed in protein expression; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554158951
2xiqA Crystal structure of human methylmalonyl-coa mutase in complex with adenosylcobalamin and malonyl-coa (see paper)
40% identity, 49% coverage: 2:136/276 of query aligns to 576:714/714 of 2xiqA
- active site: K586 (= K12), D590 (= D16), H592 (= H18)
- binding cobalamin: G591 (= G17), H592 (= H18), D593 (= D19), R594 (= R20), G595 (= G21), I599 (= I25), G635 (= G61), S637 (= S63), L639 (= L65), A641 (≠ G67), G667 (= G93), G668 (= G94), F687 (= F113), G688 (≠ T114), T691 (= T117)
Sites not aligning to the query:
- active site: 75, 229, 230
- binding cobalamin: 75, 105, 108, 125, 193, 233, 320, 321, 357, 360, 361
- binding malonyl-coenzyme a: 61, 63, 64, 68, 71, 73, 75, 150, 152, 181, 193, 220, 230, 269, 271, 273, 313, 314, 315, 317, 348
8dyjB Crystal structure of human methylmalonyl-coa mutase in complex with adp and cob(ii)alamin (see paper)
41% identity, 45% coverage: 2:126/276 of query aligns to 575:699/708 of 8dyjB
- binding cobalamin: G590 (= G17), H591 (= H18), D592 (= D19), R593 (= R20), G594 (= G21), I598 (= I25), S636 (= S63), L638 (= L65), A640 (≠ G67), G666 (= G93), G667 (= G94), V668 (= V95), F686 (= F113), G687 (≠ T114), T690 (= T117)
Sites not aligning to the query:
- binding adenosine-5'-diphosphate: 74, 151, 192, 228, 229, 272, 316, 352, 356, 360, 361
- binding cobalamin: 102, 104, 107, 124, 191, 192, 229, 232, 319, 320, 356, 359, 360
6qh4C Crystal structure of human methylmalonyl-coa epimerase (mcee) p.Arg143cys variant
42% identity, 46% coverage: 143:268/276 of query aligns to 11:135/138 of 6qh4C
6wfhA Streptomyces coelicolor methylmalonyl-coa epimerase substrate complex (see paper)
34% identity, 46% coverage: 143:268/276 of query aligns to 4:135/139 of 6wfhA
- active site: H7 (= H146), E43 (≠ V182), Q60 (≠ E193), H84 (= H217), E134 (= E267)
- binding cobalt (ii) ion: H7 (= H146), Q60 (≠ E193), H84 (= H217), E134 (= E267)
- binding (3S,5R,9R,19E)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3,5,9,19-tetrahydroxy-8,8,20-trimethyl-10,14-dioxo-2,4,6-trioxa-18-thia-11,15-diaza-3,5-diphosphahenicos-19-en-21-oic acid 3,5-dioxide (non-preferred name): H7 (= H146), Q39 (≠ E178), Q60 (≠ E193), A70 (≠ P203), K73 (= K206), W74 (≠ F207), H83 (= H216), H84 (= H217), L107 (≠ I240), G114 (= G247), S115 (≠ A248), F122 (= F255), P125 (= P258), K126 (= K259), L132 (= L265), E134 (= E267)
6oxdA Structure of mycobacterium tuberculosis methylmalonyl-coa mutase with adenosyl cobalamin (see paper)
41% identity, 45% coverage: 2:124/276 of query aligns to 600:722/736 of 6oxdA
- active site: K610 (= K12), D614 (= D16), H616 (= H18)
- binding cobalamin: G615 (= G17), H616 (= H18), D617 (= D19), R618 (= R20), S661 (= S63), L663 (= L65), A665 (≠ G67), G691 (= G93), G692 (= G94), F711 (= F113), P712 (≠ T114), T715 (= T117)
Sites not aligning to the query:
- active site: 100, 254, 255
- binding cobalamin: 100, 130, 133, 150, 218, 258, 344, 345, 381, 382, 384, 385
- binding Itaconyl coenzyme A: 86, 88, 89, 93, 96, 98, 100, 175, 177, 206, 218, 255, 294, 296, 298, 337, 338, 339, 341, 372
6xbqA Streptomyces coelicolor methylmalonyl-coa epimerase in complex with carboxy-carba(dethia)-coa
34% identity, 46% coverage: 143:268/276 of query aligns to 4:135/144 of 6xbqA
- active site: H7 (= H146), E43 (≠ V182), Q60 (≠ E193), H84 (= H217), E134 (= E267)
- binding carboxymethyldethia coenzyme *a: Q39 (≠ E178), Q60 (≠ E193), A70 (≠ P203), K73 (= K206), W74 (≠ F207), H83 (= H216), H84 (= H217), L107 (≠ I240), F122 (= F255), P125 (= P258), K126 (= K259), L132 (= L265)
- binding cobalt (ii) ion: H7 (= H146), Q60 (≠ E193), H84 (= H217), E134 (= E267)
6wfiA Methylmalonyl-coa epimerase in complex with 2-nitronate-propionyl-coa (see paper)
34% identity, 46% coverage: 143:268/276 of query aligns to 4:135/144 of 6wfiA
- active site: H7 (= H146), E43 (≠ V182), Q60 (≠ E193), H84 (= H217), E134 (= E267)
- binding cobalt (ii) ion: H7 (= H146), Q60 (≠ E193), H84 (= H217), E134 (= E267)
- binding [1-[2-[3-[[(2~{R})-4-[[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-4-oxidanyl-3-phosphonooxy-oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxy-3,3-dimethyl-2-oxidanyl-butanoyl]amino]propanoylamino]ethylsulfanyl]-1-oxidanylidene-propan-2-ylidene]-bis(oxidanidyl)azanium: H7 (= H146), Q39 (≠ E178), Q60 (≠ E193), A70 (≠ P203), K73 (= K206), W74 (≠ F207), H83 (= H216), H84 (= H217), L107 (≠ I240), G114 (= G247), S115 (≠ A248), I120 (≠ V253), F122 (= F255), P125 (= P258), L132 (= L265), E134 (= E267)
Query Sequence
>WP_036833956.1 NCBI__GCF_000775615.1:WP_036833956.1
MEHKQIRVLIAKPGLDGHDRGALVIAQALRDHGMEVIYTGLRQSPQQIVQAAIQEDVDVI
GLSSLSGAHNSLFPKVIEELKKHNAEDIPVIGGGVIPYEDIPPLEKQGIHKIFTPGTPTE
ETALYIKRILQPEQTSSLTPPEKLAHIGIAVNSIEQALPFYTNALGLRLTGVEEVASEQV
KVAFVEIGETQIELLEPTDDNSPIAKFMEKRGEGIHHIAVEVTDIEERLRHYKEKGISLI
HDTPKLGAHQSQVAFLHPKATNGVLMELCQLEKEEE
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