SitesBLAST
Comparing CCNA_02221 FitnessBrowser__Caulo:CCNA_02221 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: 8:889/899 of query aligns to 355:1225/1227 of P13009
- E694 (= E350) binding
- GDVHD 756:760 (= GDVHD 414:418) binding
- D757 (= D415) mutation to E: Decreases activity by about 70%.; mutation to N: Decreases activity by about 45%.
- H759 (= H417) binding axial binding residue; mutation to G: Loss of catalytic activity.
- S804 (= S462) binding
- T808 (= T466) binding
- S810 (= S468) mutation to A: Decreases activity by about 40%.
- A860 (= A519) binding
- D946 (= D605) binding
- R1134 (= R798) binding
- YY 1189:1190 (≠ YF 853:854) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 247 binding
- 310 binding ; mutation C->A,S: Loss of zinc binding. Loss of catalytic activity.
- 311 binding ; 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, 98% coverage: 9:889/899 of query aligns to 371:1263/1265 of Q99707
- GSR 382:384 (≠ GSA 20:22) binding
- D449 (= D87) binding
- N470 (= N108) binding
- D537 (= D175) binding
- N579 (= N217) binding
- R585 (= R223) binding
- R591 (= R229) binding
- D919 (≠ Q552) to G: in dbSNP:rs1805087
- D963 (≠ P595) mutation to E: Decreases binding to MTRR; when associated with N-1071.
- K1071 (= K694) 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: 309:889/899 of query aligns to 3:575/577 of 3bulA
- active site: D107 (= D415), H109 (= H417), S160 (= S468)
- binding cobalamin: V108 (= V416), H109 (= H417), G112 (= G420), V116 (= V424), G152 (= G460), L153 (= L461), S154 (= S462), L156 (= L464), I157 (= I465), T158 (= T466), L181 (= L489), G183 (= G491), G184 (= G492), A185 (= A493), T186 (= T494), V207 (= V516), Q208 (≠ V517), N209 (≠ D518), A210 (= A519), T213 (≠ A522), M302 (≠ A611), T303 (≠ S612), D443 (= D757), A486 (= A800), P487 (= P801), G488 (= G802), Y489 (= Y803), P490 (= P804), H495 (= H809), K498 (= K812), A520 (= A834), M521 (= M835), G524 (= G838), S526 (≠ A840), V527 (= V841), S528 (= S842)
3ivaA Structure of the b12-dependent methionine synthase (meth) c-teminal half with adohcy bound (see paper)
61% identity, 65% coverage: 309:889/899 of query aligns to 3:575/576 of 3ivaA
- active site: D107 (= D415), H109 (= H417), S160 (= S468)
- binding cobalamin: I101 (≠ M409), V108 (= V416), H109 (= H417), G112 (= G420), K113 (= K421), I115 (= I423), V116 (= V424), G152 (= G460), L153 (= L461), S154 (= S462), L156 (= L464), I157 (= I465), T158 (= T466), L181 (= L489), G183 (= G491), G184 (= G492), A185 (= A493), V207 (= V516), Q208 (≠ V517), N209 (≠ D518), A210 (= A519), T213 (≠ A522), T303 (≠ S612), D443 (= D757), R444 (= R758), A486 (= A800), P487 (= P801), G488 (= G802), Y489 (= Y803), P490 (= P804), H495 (= H809), K498 (= K812), A520 (= A834), M521 (= M835), G524 (= G838), S526 (≠ A840), V527 (= V841), S528 (= S842)
- binding s-adenosyl-l-homocysteine: D296 (= D605), P299 (= P608), R444 (= R758), E447 (= E761), E478 (= E792), R484 (= R798), P485 (= P799), A486 (= A800), Y489 (= Y803), P490 (= P804), A491 (= A805), Y539 (= Y853), Y540 (≠ F854)
3k13C Structure of the pterin-binding domain metr of 5- methyltetrahydrofolate-homocysteine methyltransferase from bacteroides thetaiotaomicron
69% identity, 32% coverage: 9:297/899 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 (= E14), N12 (= N17), G15 (= G20), S16 (= S21), R17 (≠ A22), D82 (= D87), N103 (= N108), M131 (= M136), D170 (= D175), G209 (= G214), S211 (= S216), N212 (= N217), R218 (= R223), R224 (= R229), I244 (= I249)
4cczA Crystal structure of human 5-methyltetrahydrofolate-homocysteine methyltransferase, the homocysteine and folate binding domains
64% identity, 32% coverage: 9:293/899 of query aligns to 331:610/611 of 4cczA
- binding (6s)-5,6,7,8-tetrahydrofolate: E336 (= E14), N339 (= N17), G342 (= G20), S343 (= S21), R344 (≠ A22), D409 (= D87), N430 (= N108), M458 (= M136), D497 (= D175), G536 (= G214), S538 (= S216), N539 (= N217), F542 (= F220), R545 (= R223), R551 (= R229), I571 (= I249)
1bmtA How a protein binds b12: a 3.O angstrom x-ray structure of the b12- binding domains of methionine synthase (see paper)
74% identity, 27% coverage: 309:555/899 of query aligns to 3:246/246 of 1bmtA
- active site: D107 (= D415), H109 (= H417), S160 (= S468)
- binding co-methylcobalamin: E44 (= E350), M48 (= M354), M51 (= M357), G55 (= G361), F58 (= F364), L65 (= L371), V68 (= V374), V69 (= V375), I101 (≠ M409), G106 (= G414), D107 (= D415), V108 (= V416), H109 (= H417), D110 (= D418), I111 (= I419), G112 (= G420), K113 (= K421), I115 (= I423), V116 (= V424), G152 (= G460), L153 (= L461), S154 (= S462), L156 (= L464), I157 (= I465), T158 (= T466), L181 (= L489), G183 (= G491), G184 (= G492), A185 (= A493), T186 (= T494), V207 (= V516), Q208 (≠ V517), N209 (≠ D518), A210 (= A519), T213 (≠ A522)
6bdyA Crystal structure of the meth reactivation domain bound to sinefungin (see paper)
53% identity, 36% coverage: 564:889/899 of query aligns to 5:325/326 of 6bdyA
- binding sinefungin: D46 (= D605), P49 (= P608), R194 (= R758), E197 (= E761), R234 (= R798), P235 (= P799), A236 (= A800), Y239 (= Y803), P240 (= P804), A241 (= A805), Y289 (= Y853), Y290 (≠ F854)
1mskA Methionine synthase (activation domain) (see paper)
53% identity, 36% coverage: 564:889/899 of query aligns to 5:325/327 of 1mskA