SitesBLAST
Comparing WP_011189443.1 NCBI__GCF_000025945.1:WP_011189443.1 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)
8g3hA Structure of cobalamin-dependent methionine synthase (meth) in a resting state (see paper)
47% identity, 65% coverage: 10:532/807 of query aligns to 314:831/841 of 8g3hA
- binding cobalamin: Q328 (= Q24), T330 (≠ I26), S331 (≠ P27), F675 (= F373), V685 (= V383), K693 (≠ R391), G720 (= G419), V722 (= V421), H723 (= H422), D724 (= D423), I725 (= I424), G726 (= G425), V730 (= V429), M767 (≠ L466), S768 (= S467), L770 (= L469), V772 (= V471), I795 (≠ L494), L796 (= L495), G797 (= G496), G798 (= G497), A799 (= A498), Y818 (= Y519), A819 (≠ C520), E820 (≠ Q521), D821 (= D522)
8sseA Methionine synthase, c-terminal fragment, cobalamin and reactivation domains from thermus thermophilus hb8 (see paper)
40% identity, 60% coverage: 327:807/807 of query aligns to 4:506/507 of 8sseA
- binding cobalamin: H97 (= H422), G100 (= G425), V104 (= V429), S142 (= S467), L145 (= L470), V146 (= V471), I169 (≠ L494), G171 (= G496), G172 (= G497), A173 (= A498), H405 (= H720), V409 (= V724), S451 (= S752), F452 (= F753), G453 (= G754), Y454 (= Y755), Q463 (= Q764), L485 (≠ M786), E488 (= E789), A490 (≠ S791), S492 (= S793)
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)
30% identity, 96% coverage: 31:807/807 of query aligns to 359:1192/1227 of P13009
- E694 (≠ N359) binding methylcob(III)alamin
- GDVHD 756:760 (= GDVHD 419:423) binding methylcob(III)alamin
- D757 (= D420) mutation to E: Decreases activity by about 70%.; mutation to N: Decreases activity by about 45%.
- H759 (= H422) binding axial binding residue; mutation to G: Loss of catalytic activity.
- S804 (= S467) binding methylcob(III)alamin
- T808 (≠ V471) binding methylcob(III)alamin
- S810 (= S473) mutation to A: Decreases activity by about 40%.
- A860 (= A523) binding methylcob(III)alamin
- D946 (≠ K587) binding S-adenosyl-L-methionine
- R1134 (= R750) binding S-adenosyl-L-methionine
- YY 1189:1190 (≠ YF 804:805) 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)
31% identity, 96% coverage: 31:807/807 of query aligns to 374:1230/1265 of Q99707
- GSR 382:384 (≠ GSK 39:41) binding (6S)-5,6,7,8-tetrahydrofolate
- D449 (= D103) binding (6S)-5,6,7,8-tetrahydrofolate
- N470 (= N124) binding (6S)-5,6,7,8-tetrahydrofolate
- D537 (= D191) binding (6S)-5,6,7,8-tetrahydrofolate
- N579 (= N233) binding (6S)-5,6,7,8-tetrahydrofolate
- R585 (≠ P239) binding (6S)-5,6,7,8-tetrahydrofolate
- R591 (= R243) binding (6S)-5,6,7,8-tetrahydrofolate
- D919 (≠ R546) to G: in dbSNP:rs1805087
- D963 (vs. gap) mutation to E: Decreases binding to MTRR; when associated with N-1071.
- K1071 (vs. gap) 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
5vooA Methionine synthase folate-binding domain with methyltetrahydrofolate from thermus thermophilus hb8 (see paper)
45% identity, 34% coverage: 29:306/807 of query aligns to 3:279/282 of 5vooA
- binding 5-methyl-5,6,7,8-tetrahydrofolic acid: E7 (= E33), R8 (= R34), G13 (= G39), S14 (= S40), K15 (= K41), D77 (= D103), N98 (= N124), D165 (= D191), G204 (= G230), N207 (= N233), F210 (= F236), R217 (= R243), I237 (= I263)
3ivaA Structure of the b12-dependent methionine synthase (meth) c-teminal half with adohcy bound (see paper)
28% identity, 59% coverage: 332:807/807 of query aligns to 16:542/576 of 3ivaA
- active site: D107 (= D420), H109 (= H422), S160 (= S473)
- binding cobalamin: H109 (= H422), G112 (= G425), V116 (= V429), G152 (≠ C465), L153 (= L466), S154 (= S467), L156 (= L469), I157 (≠ L470), T158 (≠ V471), G183 (= G496), G184 (= G497), Q208 (= Q521), N209 (≠ D522), T303 (≠ R595), D443 (≠ V724), A486 (≠ S752), G488 (= G754), Y489 (= Y755), H495 (≠ L761), A520 (≠ Q785), M521 (= M786), G524 (≠ E789), V527 (= V792), S528 (= S793)
- binding s-adenosyl-l-homocysteine: E447 (= E728), R484 (= R750), P485 (≠ Y751), Y489 (= Y755), A491 (= A757), Y539 (= Y804)
3bulA E. Coli i690c/g743c meth c-terminal fragment (649-1227) (see paper)
28% identity, 59% coverage: 332:807/807 of query aligns to 16:542/577 of 3bulA
- active site: D107 (= D420), H109 (= H422), S160 (= S473)
- binding cobalamin: H109 (= H422), V116 (= V429), G152 (≠ C465), L153 (= L466), S154 (= S467), L156 (= L469), I157 (≠ L470), T158 (≠ V471), G183 (= G496), G184 (= G497), Q208 (= Q521), N209 (≠ D522), A210 (= A523), T213 (≠ G526), M302 (≠ R593), D443 (≠ V724), A486 (≠ S752), P487 (≠ F753), G488 (= G754), Y489 (= Y755), H495 (≠ L761), K498 (≠ Q764), M521 (= M786), G524 (≠ E789), V527 (= V792), S528 (= S793)
4cczA Crystal structure of human 5-methyltetrahydrofolate-homocysteine methyltransferase, the homocysteine and folate binding domains
37% identity, 34% coverage: 31:304/807 of query aligns to 334:611/611 of 4cczA
- binding (6s)-5,6,7,8-tetrahydrofolate: E336 (= E33), G342 (= G39), R344 (≠ K41), N430 (= N124), M458 (≠ L152), D497 (= D191), G536 (= G230), S538 (= S232), N539 (= N233), F542 (= F236), R545 (≠ P239), R551 (= R243)
3k13C Structure of the pterin-binding domain metr of 5- methyltetrahydrofolate-homocysteine methyltransferase from bacteroides thetaiotaomicron
33% identity, 31% coverage: 31:277/807 of query aligns to 7:262/287 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 (= E33), G15 (= G39), R17 (≠ K41), N103 (= N124), D170 (= D191), G209 (= G230), S211 (= S232), N212 (= N233), R218 (vs. gap), R224 (= R243), I244 (= I263)
1bmtA How a protein binds b12: a 3.O angstrom x-ray structure of the b12- binding domains of methionine synthase (see paper)
39% identity, 24% coverage: 332:523/807 of query aligns to 16:210/246 of 1bmtA
- active site: D107 (= D420), H109 (= H422), S160 (= S473)
- binding co-methylcobalamin: E44 (≠ N359), M48 (≠ V363), M51 (= M366), G55 (= G370), L65 (= L380), V68 (= V383), D107 (= D420), V108 (= V421), H109 (= H422), D110 (= D423), I111 (= I424), I115 (≠ L428), G152 (≠ C465), L153 (= L466), S154 (= S467), L156 (= L469), I157 (≠ L470), T158 (≠ V471), G183 (= G496), G184 (= G497), A185 (= A498), V207 (≠ C520), N209 (≠ D522), A210 (= A523)
4o1eA Structure of a methyltransferase component in complex with mthf involved in o-demethylation (see paper)
34% identity, 30% coverage: 29:268/807 of query aligns to 6:235/271 of 4o1eA
- binding 5-methyl-5,6,7,8-tetrahydrofolic acid: E10 (= E33), K11 (≠ R34), I16 (≠ S40), N100 (= N124), D164 (= D191), K211 (= K244), I230 (= I263), D232 (≠ N265), N235 (= N268)
2ycjA Methyltransferase bound with methyltetrahydrofolate (see paper)
32% identity, 29% coverage: 29:264/807 of query aligns to 11:237/271 of 2ycjA
- binding 5-methyl-5,6,7,8-tetrahydrofolic acid: M20 (≠ T38), F21 (≠ S40), D84 (= D103), N105 (= N124), D169 (= D191), G205 (= G230), N208 (= N233), Q211 (≠ F236), R216 (= R243), I236 (= I263)
2yciX Methyltransferase native (see paper)
32% identity, 29% coverage: 29:264/807 of query aligns to 11:237/271 of 2yciX
2yckX Methyltransferase bound with tetrahydrofolate (see paper)
32% identity, 29% coverage: 29:264/807 of query aligns to 12:238/272 of 2yckX
- binding (6s)-5,6,7,8-tetrahydrofolate: M21 (≠ T38), F22 (≠ S40), D85 (= D103), N106 (= N124), D170 (= D191), G206 (= G230), N209 (= N233), Q212 (≠ F236), K213 (≠ G237), R217 (= R243), I237 (= I263)
4o1fA Structure of a methyltransferase component in complex with thf involved in o-demethylation (see paper)
35% identity, 30% coverage: 29:268/807 of query aligns to 3:231/267 of 4o1fA
4djfA Crystal structure of folate-bound corrinoid iron-sulfur protein (cfesp) in complex with its methyltransferase (metr), co-crystallized with folate and ti(iii) citrate reductant (see paper)
32% identity, 29% coverage: 29:263/807 of query aligns to 2:227/262 of 4djfA
- binding 5-methyl-5,6,7,8-tetrahydrofolic acid: E6 (= E33), M11 (≠ T38), F12 (≠ G39), D75 (= D103), N96 (= N124), D160 (= D191), S198 (= S232), N199 (= N233), R207 (= R243)
- binding calcium ion: G222 (= G258), D224 (= D260)
- binding co-methylcobalamin: V168 (≠ S199), Q202 (≠ F236), N203 (≠ G237)
4djeA Crystal structure of folate-bound corrinoid iron-sulfur protein (cfesp) in complex with its methyltransferase (metr), co-crystallized with folate (see paper)
32% identity, 29% coverage: 29:263/807 of query aligns to 2:227/262 of 4djeA
- binding cobalamin: V168 (≠ S199), N203 (≠ G237)
- binding 5-methyl-5,6,7,8-tetrahydrofolic acid: E6 (= E33), M11 (≠ T38), F12 (≠ G39), D75 (= D103), N96 (= N124), D160 (= D191), G196 (= G230), S198 (= S232), N199 (= N233), R207 (= R243)
- binding calcium ion: G222 (= G258), D224 (= D260)
4djdA Crystal structure of folate-free corrinoid iron-sulfur protein (cfesp) in complex with its methyltransferase (metr) (see paper)
32% identity, 29% coverage: 29:263/807 of query aligns to 2:227/262 of 4djdA
2e7fA 5-methyltetrahydrofolate corrinoid/iron sulfur protein methyltransferase complexed with methyltetrahydrofolate to 2.2 angsrom resolution (see paper)
32% identity, 29% coverage: 29:263/807 of query aligns to 2:227/262 of 2e7fA
- binding 5-methyl-5,6,7,8-tetrahydrofolic acid: E6 (= E33), M11 (≠ T38), F12 (≠ G39), D75 (= D103), N96 (= N124), D160 (= D191), G196 (= G230), S198 (= S232), N199 (= N233), Q202 (≠ F236), R207 (= R243), I227 (= I263)
- binding calcium ion: G222 (= G258), D224 (= D260)
Q46389 5-methyltetrahydrofolate:corrinoid/iron-sulfur protein co-methyltransferase; 5-methyltetrahydrofolate corrinoid/iron sulfur protein methyltransferase; MeTr; EC 2.1.1.258 from Moorella thermoacetica (Clostridium thermoaceticum) (see 2 papers)
32% identity, 29% coverage: 29:263/807 of query aligns to 2:227/262 of Q46389
- N96 (= N124) binding (6S)-5-methyl-5,6,7,8-tetrahydrofolate
- D160 (= D191) binding (6S)-5-methyl-5,6,7,8-tetrahydrofolate
- K184 (= K219) binding Ca(2+)
- N199 (= N233) binding (6S)-5-methyl-5,6,7,8-tetrahydrofolate; mutation to A: 20-fold decreased affinity for methyltetrahydrofolate and nearly abolished catalytic activity.
- Q202 (≠ F236) binding (6S)-5-methyl-5,6,7,8-tetrahydrofolate
- R207 (= R243) binding (6S)-5-methyl-5,6,7,8-tetrahydrofolate
- G222 (= G258) binding Ca(2+); binding Ca(2+)
- D224 (= D260) binding Ca(2+); binding Ca(2+)
Query Sequence
>WP_011189443.1 NCBI__GCF_000025945.1:WP_011189443.1
MKVTEQNRVPAQVSSLFQAVDIHQQIPPLIVGERANPTGSKKFRELLLAEDFEGCLQVAK
DQEELGAHVLDVCAAWAGRDEVTDITRLIKDYSGTLKTPLMIDSTNPRAIKAALEVYPGR
PIINSINLEDGGKTLHEVLTLTKKYGATVIALTIDESGMALSCDEKISIAKRIHHIATTE
YGLDSSDLFFDPLTFTVGSGDKTLKDAAVQTMDAIKRIKVELPNCHTILGLSNISFGLPP
AARKVLNAVFLHEAVAIGLDAVIINPTNCIPLDSIDKRARELALDLLYNREVEGESEPLM
RYIEYFAENAAVGDQEGSPEELLSPEEGIRKAILKGSREGLEDTMQILLDQYTPLDIINQ
LLVPSMREVGELFGAGEMLLPFVLKSAEIMRASVDILEPYMEKAANSESTKILLATVQGD
VHDIGKNLVNIILSNNGYQVIDIGIKASIESIIEAAKRHEVDMICLSGLLVKSAIVMQES
MPIYREAGLTQPILLGGAALTKKFVAEACAPNYPSPVVYCQDAFSGLAAIQQHEAGTLET
TKWQARETQEVKEAKTITILPARDIPTPPLGRAELSVATSDFLDLVKTNTLFRGRWGYRQ
NKMSNDEYAQLISTEVMPQFENIRRRILEEELFQAKIRYGWFRCYRQGDSLTVLDGEREY
NFPLPRQKHGPHLCLADYFRDKNGGGDVVGFFVCTIGKKVAQALQQLYSTESYHDYFLLH
GLSVNAAEALAEHAHLWMRQQMGSQFGGKRYSFGYSACPDLDLQRPLFELLQAEKIGITL
SEELQMVPEQSVSAMVVHHDQASYFVV
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