SitesBLAST
Comparing Ga0059261_0990 FitnessBrowser__Korea:Ga0059261_0990 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)
63% identity, 99% coverage: 8:864/865 of query aligns to 356:1222/1227 of P13009
- E694 (= E343) binding methylcob(III)alamin
- GDVHD 756:760 (= GDVHD 406:410) binding methylcob(III)alamin
- D757 (= D407) mutation to E: Decreases activity by about 70%.; mutation to N: Decreases activity by about 45%.
- H759 (= H409) binding axial binding residue; mutation to G: Loss of catalytic activity.
- S804 (= S454) binding methylcob(III)alamin
- T808 (= T458) binding methylcob(III)alamin
- S810 (= S460) mutation to A: Decreases activity by about 40%.
- A860 (= A510) binding methylcob(III)alamin
- D946 (= D595) binding S-adenosyl-L-methionine
- R1134 (= R776) binding S-adenosyl-L-methionine
- YY 1189:1190 (≠ YF 831:832) 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)
54% identity, 99% coverage: 6:864/865 of query aligns to 369:1260/1265 of Q99707
- GSR 382:384 (≠ GSA 19:21) binding (6S)-5,6,7,8-tetrahydrofolate
- D449 (= D86) binding (6S)-5,6,7,8-tetrahydrofolate
- N470 (= N107) binding (6S)-5,6,7,8-tetrahydrofolate
- D537 (= D173) binding (6S)-5,6,7,8-tetrahydrofolate
- N579 (= N215) binding (6S)-5,6,7,8-tetrahydrofolate
- R585 (= R221) binding (6S)-5,6,7,8-tetrahydrofolate
- R591 (= R227) binding (6S)-5,6,7,8-tetrahydrofolate
- D919 (≠ A543) to G: in dbSNP:rs1805087
- D963 (= D584) mutation to E: Decreases binding to MTRR; when associated with N-1071.
- K1071 (= K681) 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
3ivaA Structure of the b12-dependent methionine synthase (meth) c-teminal half with adohcy bound (see paper)
59% identity, 65% coverage: 301:864/865 of query aligns to 2:572/576 of 3ivaA
- active site: D107 (= D407), H109 (= H409), S160 (= S460)
- binding cobalamin: H109 (= H409), G112 (= G412), V116 (= V416), G152 (= G452), L153 (= L453), S154 (= S454), L156 (= L456), I157 (= I457), T158 (= T458), G183 (= G483), G184 (= G484), Q208 (≠ L508), N209 (≠ D509), T303 (≠ A602), D443 (= D735), A486 (= A778), G488 (= G780), Y489 (= Y781), H495 (= H787), A520 (= A812), M521 (= M813), G524 (≠ T816), V527 (= V819), S528 (= S820)
- binding s-adenosyl-l-homocysteine: E447 (= E739), R484 (= R776), P485 (= P777), Y489 (= Y781), A491 (= A783), Y539 (= Y831)
3bulA E. Coli i690c/g743c meth c-terminal fragment (649-1227) (see paper)
59% identity, 65% coverage: 301:864/865 of query aligns to 2:572/577 of 3bulA
- active site: D107 (= D407), H109 (= H409), S160 (= S460)
- binding cobalamin: H109 (= H409), V116 (= V416), G152 (= G452), L153 (= L453), S154 (= S454), L156 (= L456), I157 (= I457), T158 (= T458), G183 (= G483), G184 (= G484), Q208 (≠ L508), N209 (≠ D509), A210 (= A510), T213 (≠ A513), M302 (≠ R601), D443 (= D735), A486 (= A778), P487 (= P779), G488 (= G780), Y489 (= Y781), H495 (= H787), K498 (= K790), M521 (= M813), G524 (≠ T816), V527 (= V819), S528 (= S820)
3k13C Structure of the pterin-binding domain metr of 5- methyltetrahydrofolate-homocysteine methyltransferase from bacteroides thetaiotaomicron
65% identity, 33% coverage: 8:290/865 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 (= E13), G15 (= G19), R17 (≠ A21), N103 (= N107), D170 (= D173), G209 (= G212), S211 (= S214), N212 (= N215), R218 (= R221), R224 (= R227), I244 (= I247)
4cczA Crystal structure of human 5-methyltetrahydrofolate-homocysteine methyltransferase, the homocysteine and folate binding domains
64% identity, 33% coverage: 6:287/865 of query aligns to 329:611/611 of 4cczA
- binding (6s)-5,6,7,8-tetrahydrofolate: E336 (= E13), G342 (= G19), R344 (≠ A21), N430 (= N107), M458 (= M135), D497 (= D173), G536 (= G212), S538 (= S214), N539 (= N215), F542 (= F218), R545 (= R221), R551 (= R227)
1bmtA How a protein binds b12: a 3.O angstrom x-ray structure of the b12- binding domains of methionine synthase (see paper)
73% identity, 28% coverage: 301:542/865 of query aligns to 2:242/246 of 1bmtA
- active site: D107 (= D407), H109 (= H409), S160 (= S460)
- binding co-methylcobalamin: E44 (= E343), M48 (= M347), M51 (= M350), G55 (= G354), L65 (= L364), V68 (= V367), D107 (= D407), V108 (= V408), H109 (= H409), D110 (= D410), I111 (= I411), I115 (= I415), G152 (= G452), L153 (= L453), S154 (= S454), L156 (= L456), I157 (= I457), T158 (= T458), G183 (= G483), G184 (= G484), A185 (= A485), V207 (= V507), N209 (≠ D509), A210 (= A510)
1mskA Methionine synthase (activation domain) (see paper)
51% identity, 36% coverage: 553:864/865 of query aligns to 4:322/327 of 1mskA
6bdyA Crystal structure of the meth reactivation domain bound to sinefungin (see paper)
51% identity, 36% coverage: 553:864/865 of query aligns to 4:322/326 of 6bdyA
8g3hA Structure of cobalamin-dependent methionine synthase (meth) in a resting state (see paper)
37% identity, 56% coverage: 4:491/865 of query aligns to 328:805/841 of 8g3hA