SitesBLAST
Comparing WP_076477891.1 NCBI__GCF_900156495.1:WP_076477891.1 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)
6oxdA Structure of mycobacterium tuberculosis methylmalonyl-coa mutase with adenosyl cobalamin (see paper)
81% identity, 97% coverage: 6:741/759 of query aligns to 1:734/736 of 6oxdA
- active site: Y100 (= Y103), Y254 (= Y257), H255 (= H258), K610 (= K617), D614 (= D621), H616 (= H623)
- binding cobalamin: Y100 (= Y103), L130 (= L133), H133 (= H136), A150 (= A153), R218 (= R221), E258 (= E261), G344 (= G347), W345 (= W348), E381 (= E384), A382 (= A385), A384 (= A387), L385 (= L388), G615 (= G622), H616 (= H623), D617 (= D624), R618 (= R625), S661 (= S668), L663 (= L670), A665 (= A672), G691 (= G698), G692 (= G699), F711 (= F718), P712 (= P719), T715 (= T722)
- binding Itaconyl coenzyme A: Y86 (= Y89), T88 (= T91), M89 (= M92), Q93 (= Q96), T96 (= T99), R98 (= R101), Y100 (= Y103), S175 (= S178), T177 (= T180), T206 (= T209), R218 (= R221), H255 (= H258), R294 (= R297), S296 (= S299), F298 (= F301), R337 (= R340), T338 (= T341), H339 (= H342), Q341 (= Q344), Q372 (= Q375)
6reqA Methylmalonyl-coa mutase, 3-carboxypropyl-coa inhibitor complex (see paper)
70% identity, 94% coverage: 23:739/759 of query aligns to 15:725/727 of 6reqA
- active site: Y88 (= Y103), Y242 (= Y257), H243 (= H258), K603 (= K617), D607 (= D621), H609 (= H623)
- binding 3-carboxypropyl-coenzyme a: Y74 (= Y89), T76 (= T91), M77 (= M92), F80 (≠ N95), R81 (≠ Q96), T84 (= T99), R86 (= R101), Y88 (= Y103), S113 (= S128), S163 (= S178), T165 (= T180), T194 (= T209), R206 (= R221), H243 (= H258), R282 (= R297), S284 (= S299), F286 (= F301), H327 (= H342), Q329 (= Q344), Q360 (= Q375)
- binding cobalamin: Y88 (= Y103), F116 (= F131), L118 (= L133), H121 (= H136), A138 (= A153), R206 (= R221), E246 (= E261), G332 (= G347), W333 (= W348), E369 (= E384), A370 (= A385), A372 (= A387), G608 (= G622), H609 (= H623), D610 (= D624), R611 (= R625), G612 (= G626), I616 (= I630), Y620 (≠ F634), S654 (= S668), L656 (= L670), G658 (≠ A672), G684 (= G698), G685 (= G699), Y704 (≠ F718), T705 (≠ P719), T708 (= T722)
P11653 Methylmalonyl-CoA mutase large subunit; MCM-alpha; EC 5.4.99.2 from Propionibacterium freudenreichii subsp. shermanii (see 4 papers)
70% identity, 94% coverage: 23:739/759 of query aligns to 16:726/728 of P11653
- Y75 (= Y89) binding (R)-methylmalonyl-CoA
- M78 (= M92) binding (R)-methylmalonyl-CoA
- R82 (≠ Q96) binding (R)-methylmalonyl-CoA
- T85 (= T99) binding (R)-methylmalonyl-CoA
- R87 (= R101) binding (R)-methylmalonyl-CoA
- Y89 (= Y103) binding (R)-methylmalonyl-CoA; mutation to F: Does not significantly affect affinity for succiny-CoA, but kcat is lowered about 580-fold.
- S114 (= S128) binding (R)-methylmalonyl-CoA
- F117 (= F131) binding cob(II)alamin
- A139 (= A153) binding cob(II)alamin
- T195 (= T209) binding (R)-methylmalonyl-CoA
- Q197 (= Q211) binding (R)-methylmalonyl-CoA
- V206 (= V220) binding cob(II)alamin
- R207 (= R221) binding (R)-methylmalonyl-CoA; binding cob(II)alamin
- H244 (= H258) binding (R)-methylmalonyl-CoA
- R283 (= R297) binding (R)-methylmalonyl-CoA
- S285 (= S299) binding (R)-methylmalonyl-CoA
- G333 (= G347) binding cob(II)alamin
- E370 (= E384) binding cob(II)alamin
- A373 (= A387) binding cob(II)alamin
- G609 (= G622) binding cob(II)alamin
- H610 (= H623) binding axial binding residue
- D611 (= D624) binding cob(II)alamin
- R612 (= R625) binding cob(II)alamin
- S655 (= S668) binding cob(II)alamin
- L657 (= L670) binding cob(II)alamin
- G686 (= G699) binding cob(II)alamin
- T709 (= T722) binding cob(II)alamin
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
4reqA Methylmalonyl-coa mutase substrate complex (see paper)
70% identity, 94% coverage: 23:739/759 of query aligns to 14:724/726 of 4reqA
- active site: Y87 (= Y103), Y241 (= Y257), H242 (= H258), K602 (= K617), D606 (= D621), H608 (= H623)
- binding cobalamin: Y87 (= Y103), L117 (= L133), A137 (= A153), V204 (= V220), R205 (= R221), H242 (= H258), E245 (= E261), G331 (= G347), W332 (= W348), E368 (= E384), A369 (= A385), A371 (= A387), L372 (= L388), G607 (= G622), H608 (= H623), D609 (= D624), R610 (= R625), G611 (= G626), I615 (= I630), S653 (= S668), L655 (= L670), G683 (= G698), G684 (= G699), V685 (= V700), Y703 (≠ F718), T704 (≠ P719), T707 (= T722)
- binding methylmalonyl-coenzyme a: Y73 (= Y89), M76 (= M92), F79 (≠ N95), R80 (≠ Q96), T83 (= T99), R85 (= R101), Y87 (= Y103), S112 (= S128), S162 (= S178), T164 (= T180), T193 (= T209), R205 (= R221), N234 (= N250), Y241 (= Y257), H242 (= H258), R281 (= R297), S283 (= S299), F285 (= F301), H326 (= H342), Q328 (= Q344), Q359 (= Q375), S360 (= S376)
- binding succinyl-coenzyme a: Y73 (= Y89), M76 (= M92), F79 (≠ N95), R80 (≠ Q96), T83 (= T99), R85 (= R101), Y87 (= Y103), S162 (= S178), T164 (= T180), T193 (= T209), Q195 (= Q211), R205 (= R221), N234 (= N250), Y241 (= Y257), H242 (= H258), R281 (= R297), S283 (= S299), F285 (= F301), R324 (= R340), H326 (= H342), Q359 (= Q375)
7reqA Methylmalonyl-coa mutase, 2-carboxypropyl-coa inhibitor complex (see paper)
70% identity, 94% coverage: 23:739/759 of query aligns to 13:723/725 of 7reqA
- active site: Y86 (= Y103), Y240 (= Y257), H241 (= H258), K601 (= K617), D605 (= D621), H607 (= H623)
- binding 2-carboxypropyl-coenzyme a: Y72 (= Y89), T74 (= T91), M75 (= M92), F78 (≠ N95), R79 (≠ Q96), T82 (= T99), R84 (= R101), Y86 (= Y103), S161 (= S178), T163 (= T180), T192 (= T209), R204 (= R221), H241 (= H258), R280 (= R297), S282 (= S299), F284 (= F301), H325 (= H342), Q358 (= Q375)
- binding cobalamin: Y86 (= Y103), L116 (= L133), A136 (= A153), R204 (= R221), E244 (= E261), G330 (= G347), W331 (= W348), E367 (= E384), A368 (= A385), A370 (= A387), G606 (= G622), H607 (= H623), D608 (= D624), R609 (= R625), G610 (= G626), I614 (= I630), S652 (= S668), L654 (= L670), G682 (= G698), G683 (= G699), Y702 (≠ F718), T703 (≠ P719), T706 (= T722)
3reqA Methylmalonyl-coa mutase, substrate-free state (poor quality structure) (see paper)
70% identity, 94% coverage: 23:739/759 of query aligns to 13:723/725 of 3reqA