SitesBLAST
Comparing WP_049766682.1 NCBI__GCF_000016185.1:WP_049766682.1 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)
P13009 Methionine synthase; 5-methyltetrahydrofolate--homocysteine methyltransferase; Methionine synthase, vitamin-B12-dependent; MS; EC 2.1.1.13 from Escherichia coli (strain K12) (see 5 papers)
64% identity, 98% coverage: 11:891/903 of query aligns to 354:1227/1227 of P13009
- E694 (= E348) binding methylcob(III)alamin
- GDVHD 756:760 (= GDVHD 416:420) binding methylcob(III)alamin
- D757 (= D417) mutation to E: Decreases activity by about 70%.; mutation to N: Decreases activity by about 45%.
- H759 (= H419) binding axial binding residue; mutation to G: Loss of catalytic activity.
- S804 (= S464) binding methylcob(III)alamin
- T808 (= T468) binding methylcob(III)alamin
- S810 (= S470) mutation to A: Decreases activity by about 40%.
- A860 (= A520) binding methylcob(III)alamin
- D946 (= D607) binding S-adenosyl-L-methionine
- R1134 (= R798) binding S-adenosyl-L-methionine
- YY 1189:1190 (≠ YF 853:854) binding S-adenosyl-L-methionine
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 247 binding Zn(2+)
- 310 binding Zn(2+); mutation C->A,S: Loss of zinc binding. Loss of catalytic activity.
- 311 binding Zn(2+); mutation C->A,S: Loss of zinc binding. Loss of catalytic activity.
Q99707 Methionine synthase; MS; 5-methyltetrahydrofolate--homocysteine methyltransferase; Cobalamin-dependent methionine synthase; Vitamin-B12 dependent methionine synthase; EC 2.1.1.13 from Homo sapiens (Human) (see 6 papers)
56% identity, 97% coverage: 13:891/903 of query aligns to 371:1265/1265 of Q99707
- GSR 382:384 (≠ GSA 24:26) binding (6S)-5,6,7,8-tetrahydrofolate
- D449 (= D91) binding (6S)-5,6,7,8-tetrahydrofolate
- N470 (= N112) binding (6S)-5,6,7,8-tetrahydrofolate
- D537 (= D179) binding (6S)-5,6,7,8-tetrahydrofolate
- N579 (= N221) binding (6S)-5,6,7,8-tetrahydrofolate
- R585 (= R227) binding (6S)-5,6,7,8-tetrahydrofolate
- R591 (= R233) binding (6S)-5,6,7,8-tetrahydrofolate
- D919 (≠ A553) to G: in dbSNP:rs1805087
- D963 (= D596) mutation to E: Decreases binding to MTRR; when associated with N-1071.
- K1071 (≠ R696) mutation to N: Decreases binding to MTRR; when associated with E-963.
Sites not aligning to the query:
- 61 natural variant: R -> K
- 255 C → Y: in dbSNP:rs1140598
3bulA E. Coli i690c/g743c meth c-terminal fragment (649-1227) (see paper)
61% identity, 65% coverage: 308:891/903 of query aligns to 4:577/577 of 3bulA
- active site: D107 (= D417), H109 (= H419), S160 (= S470)
- binding cobalamin: H109 (= H419), V116 (= V426), G152 (= G462), L153 (= L463), S154 (= S464), L156 (= L466), I157 (= I467), T158 (= T468), G183 (= G493), G184 (= G494), Q208 (≠ L518), N209 (≠ D519), A210 (= A520), T213 (≠ A523), M302 (≠ E613), D443 (= D757), A486 (= A800), P487 (= P801), G488 (= G802), Y489 (= Y803), H495 (= H809), K498 (= K812), M521 (= M835), G524 (≠ T838), V527 (= V841), S528 (= S842)
3ivaA Structure of the b12-dependent methionine synthase (meth) c-teminal half with adohcy bound (see paper)
61% identity, 64% coverage: 308:889/903 of query aligns to 4:575/576 of 3ivaA
- active site: D107 (= D417), H109 (= H419), S160 (= S470)
- binding cobalamin: H109 (= H419), G112 (= G422), V116 (= V426), G152 (= G462), L153 (= L463), S154 (= S464), L156 (= L466), I157 (= I467), T158 (= T468), G183 (= G493), G184 (= G494), Q208 (≠ L518), N209 (≠ D519), T303 (≠ A614), D443 (= D757), A486 (= A800), G488 (= G802), Y489 (= Y803), H495 (= H809), A520 (= A834), M521 (= M835), G524 (≠ T838), V527 (= V841), S528 (= S842)
- binding s-adenosyl-l-homocysteine: E447 (= E761), R484 (= R798), P485 (= P799), Y489 (= Y803), A491 (= A805), Y539 (= Y853)
3k13C Structure of the pterin-binding domain metr of 5- methyltetrahydrofolate-homocysteine methyltransferase from bacteroides thetaiotaomicron
68% identity, 31% coverage: 13:296/903 of query aligns to 4:286/287 of 3k13C
- binding n-[4-({[(6s)-2-amino-4-hydroxy-5-methyl-5,6,7,8-tetrahydropteridin-6-yl]methyl}amino)benzoyl]-l-glutamic acid: E9 (= E18), G15 (= G24), R17 (≠ A26), N103 (= N112), D170 (= D179), G209 (= G218), S211 (= S220), N212 (= N221), R218 (= R227), R224 (= R233), I244 (= I253)
1mskA Methionine synthase (activation domain) (see paper)
59% identity, 36% coverage: 564:891/903 of query aligns to 4:327/327 of 1mskA
6bdyA Crystal structure of the meth reactivation domain bound to sinefungin (see paper)
59% identity, 36% coverage: 564:889/903 of query aligns to 4:325/326 of 6bdyA
4cczA Crystal structure of human 5-methyltetrahydrofolate-homocysteine methyltransferase, the homocysteine and folate binding domains
64% identity, 31% coverage: 13:292/903 of query aligns to 331:610/611 of 4cczA
- binding (6s)-5,6,7,8-tetrahydrofolate: E336 (= E18), G342 (= G24), R344 (≠ A26), N430 (= N112), M458 (= M140), D497 (= D179), G536 (= G218), S538 (= S220), N539 (= N221), F542 (= F224), R545 (= R227), R551 (= R233)
1bmtA How a protein binds b12: a 3.O angstrom x-ray structure of the b12- binding domains of methionine synthase (see paper)
65% identity, 28% coverage: 308:556/903 of query aligns to 4:246/246 of 1bmtA
- active site: D107 (= D417), H109 (= H419), S160 (= S470)
- binding co-methylcobalamin: E44 (= E348), M48 (= M352), M51 (= M355), G55 (= G359), L65 (= L369), V68 (= V372), D107 (= D417), V108 (= V418), H109 (= H419), D110 (= D420), I111 (= I421), I115 (= I425), G152 (= G462), L153 (= L463), S154 (= S464), L156 (= L466), I157 (= I467), T158 (= T468), G183 (= G493), G184 (= G494), A185 (= A495), V207 (= V517), N209 (≠ D519), A210 (= A520)
8g3hA Structure of cobalamin-dependent methionine synthase (meth) in a resting state (see paper)
37% identity, 55% coverage: 10:502/903 of query aligns to 330:806/841 of 8g3hA