SitesBLAST
Comparing WP_084235998.1 NCBI__GCF_001592305.1:WP_084235998.1 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)
62% identity, 98% coverage: 22:917/917 of query aligns to 342:1222/1227 of P13009
- E694 (= E375) binding methylcob(III)alamin
- GDVHD 756:760 (= GDVHD 444:448) binding methylcob(III)alamin
- D757 (= D445) mutation to E: Decreases activity by about 70%.; mutation to N: Decreases activity by about 45%.
- H759 (= H447) binding axial binding residue; mutation to G: Loss of catalytic activity.
- S804 (= S492) binding methylcob(III)alamin
- T808 (= T496) binding methylcob(III)alamin
- S810 (= S498) mutation to A: Decreases activity by about 40%.
- A860 (= A552) binding methylcob(III)alamin
- D946 (= D637) binding S-adenosyl-L-methionine
- R1134 (= R830) binding S-adenosyl-L-methionine
- YY 1189:1190 (≠ YF 884:885) 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)
53% identity, 99% coverage: 11:917/917 of query aligns to 346:1260/1265 of Q99707
- GSR 382:384 (≠ GSK 47:49) binding (6S)-5,6,7,8-tetrahydrofolate
- D449 (= D114) binding (6S)-5,6,7,8-tetrahydrofolate
- N470 (= N135) binding (6S)-5,6,7,8-tetrahydrofolate
- D537 (= D202) binding (6S)-5,6,7,8-tetrahydrofolate
- N579 (= N244) binding (6S)-5,6,7,8-tetrahydrofolate
- R585 (= R250) binding (6S)-5,6,7,8-tetrahydrofolate
- R591 (= R256) binding (6S)-5,6,7,8-tetrahydrofolate
- D919 (≠ Q584) to G: in dbSNP:rs1805087
- D963 (≠ N626) mutation to E: Decreases binding to MTRR; when associated with N-1071.
- K1071 (= K727) 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)
55% identity, 64% coverage: 330:917/917 of query aligns to 3:572/576 of 3ivaA
- active site: D107 (= D445), H109 (= H447), S160 (= S498)
- binding cobalamin: H109 (= H447), G112 (= G450), V116 (= V454), G152 (= G490), L153 (= L491), S154 (= S492), L156 (= L494), I157 (= I495), T158 (= T496), G183 (= G525), G184 (= G526), Q208 (≠ P550), N209 (≠ D551), T303 (= T644), D443 (= D789), A486 (= A832), G488 (= G834), Y489 (= Y835), H495 (= H841), A520 (= A865), M521 (= M866), G524 (≠ A869), V527 (= V872), S528 (= S873)
- binding s-adenosyl-l-homocysteine: E447 (= E793), R484 (= R830), P485 (= P831), Y489 (= Y835), A491 (= A837), Y539 (= Y884)
3bulA E. Coli i690c/g743c meth c-terminal fragment (649-1227) (see paper)
55% identity, 64% coverage: 330:917/917 of query aligns to 3:572/577 of 3bulA
- active site: D107 (= D445), H109 (= H447), S160 (= S498)
- binding cobalamin: H109 (= H447), V116 (= V454), G152 (= G490), L153 (= L491), S154 (= S492), L156 (= L494), I157 (= I495), T158 (= T496), G183 (= G525), G184 (= G526), Q208 (≠ P550), N209 (≠ D551), A210 (= A552), T213 (≠ S555), M302 (≠ Q643), D443 (= D789), A486 (= A832), P487 (= P833), G488 (= G834), Y489 (= Y835), H495 (= H841), K498 (= K844), M521 (= M866), G524 (≠ A869), V527 (= V872), S528 (= S873)
3k13C Structure of the pterin-binding domain metr of 5- methyltetrahydrofolate-homocysteine methyltransferase from bacteroides thetaiotaomicron
68% identity, 31% coverage: 36:319/917 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 (= E41), G15 (= G47), R17 (≠ K49), N103 (= N135), D170 (= D202), G209 (= G241), S211 (= S243), N212 (= N244), R218 (= R250), R224 (= R256), I244 (= I276)
4cczA Crystal structure of human 5-methyltetrahydrofolate-homocysteine methyltransferase, the homocysteine and folate binding domains
60% identity, 33% coverage: 11:316/917 of query aligns to 306:611/611 of 4cczA
- binding (6s)-5,6,7,8-tetrahydrofolate: E336 (= E41), G342 (= G47), R344 (≠ K49), N430 (= N135), M458 (= M163), D497 (= D202), G536 (= G241), S538 (= S243), N539 (= N244), F542 (= F247), R545 (= R250), R551 (= R256)
6bdyA Crystal structure of the meth reactivation domain bound to sinefungin (see paper)
53% identity, 35% coverage: 596:917/917 of query aligns to 6:322/326 of 6bdyA
1mskA Methionine synthase (activation domain) (see paper)
53% identity, 35% coverage: 596:917/917 of query aligns to 6:322/327 of 1mskA
8g3hA Structure of cobalamin-dependent methionine synthase (meth) in a resting state (see paper)
36% identity, 61% coverage: 10:564/917 of query aligns to 306:834/841 of 8g3hA
- binding cobalamin: Q328 (≠ D32), T330 (≠ S34), S331 (≠ L35), F675 (= F389), V685 (= V399), K693 (= K407), G720 (= G444), V722 (= V446), H723 (= H447), D724 (= D448), I725 (= I449), G726 (= G450), V730 (= V454), M767 (≠ L491), S768 (= S492), L770 (= L494), V772 (≠ T496), I795 (≠ L523), L796 (≠ I524), G797 (= G525), G798 (= G526), A799 (= A527), Y818 (= Y548), A819 (≠ V549), E820 (≠ P550), D821 (= D551)
1bmtA How a protein binds b12: a 3.O angstrom x-ray structure of the b12- binding domains of methionine synthase (see paper)
60% identity, 28% coverage: 330:586/917 of query aligns to 3:245/246 of 1bmtA
- active site: D107 (= D445), H109 (= H447), S160 (= S498)
- binding co-methylcobalamin: E44 (= E375), M48 (= M379), M51 (= M382), G55 (= G386), L65 (= L396), V68 (= V399), D107 (= D445), V108 (= V446), H109 (= H447), D110 (= D448), I111 (= I449), I115 (= I453), G152 (= G490), L153 (= L491), S154 (= S492), L156 (= L494), I157 (= I495), T158 (= T496), G183 (= G525), G184 (= G526), A185 (= A527), V207 (= V549), N209 (≠ D551), A210 (= A552)
8sseA Methionine synthase, c-terminal fragment, cobalamin and reactivation domains from thermus thermophilus hb8 (see paper)
31% identity, 60% coverage: 335:887/917 of query aligns to 1:506/507 of 8sseA
- binding cobalamin: H97 (= H447), G100 (= G450), V104 (= V454), S142 (= S492), L145 (≠ I495), V146 (≠ T496), I169 (≠ L523), G171 (= G525), G172 (= G526), A173 (= A527), H405 (≠ K785), V409 (≠ D789), S451 (≠ A832), F452 (≠ P833), G453 (= G834), Y454 (= Y835), Q463 (≠ K844), L485 (≠ M866), E488 (≠ A869), A490 (≠ S871), S492 (= S873)
5vooA Methionine synthase folate-binding domain with methyltetrahydrofolate from thermus thermophilus hb8 (see paper)
37% identity, 30% coverage: 34:312/917 of query aligns to 1:273/282 of 5vooA
- binding 5-methyl-5,6,7,8-tetrahydrofolic acid: E7 (= E41), R8 (= R42), G13 (= G47), S14 (= S48), K15 (= K49), D77 (= D114), N98 (= N135), D165 (= D202), G204 (= G241), N207 (= N244), F210 (= F247), R217 (= R256), I237 (= I276)
7xcnP Crystal structure of the mttb-mttc complex at 2.7 a resolution (see paper)
32% identity, 21% coverage: 337:531/917 of query aligns to 3:188/215 of 7xcnP
- binding 5-hydroxybenzimidazolylcobamide: D104 (= D445), I105 (≠ V446), H106 (= H447), I108 (= I449), G109 (= G450), V113 (= V454), S150 (≠ L491), S151 (= S492), L153 (= L494), M154 (≠ I495), T155 (= T496), M180 (≠ L523), G182 (= G525), G183 (= G526)
Sites not aligning to the query:
2i2xB Crystal structure of methanol:cobalamin methyltransferase complex mtabc from methanosarcina barkeri (see paper)
28% identity, 27% coverage: 337:580/917 of query aligns to 36:257/258 of 2i2xB
- active site: D134 (= D445), H136 (= H447), T187 (≠ S498)
- binding 5-hydroxybenzimidazolylcob(iii)amide: G133 (= G444), D134 (= D445), V135 (= V446), H136 (= H447), D137 (= D448), I138 (= I449), G139 (= G450), V143 (= V454), T179 (≠ G490), T181 (≠ S492), L183 (= L494), M184 (≠ I495), T185 (= T496), A208 (≠ L523), G210 (= G525), G211 (= G526), G212 (≠ A527), G228 (≠ V549), E229 (≠ P550), E230 (≠ D551), A231 (= A552)
Q46EH4 Methanol--corrinoid protein; Methanol:corrinoid methyltransferase 1 subunit of 27 kDa; MT1 subunit 27 kDa from Methanosarcina barkeri (strain Fusaro / DSM 804) (see paper)
28% identity, 27% coverage: 337:580/917 of query aligns to 36:257/258 of Q46EH4
- H129 (≠ A440) mutation to K: Does not affect cobalamin-binding.
- H136 (= H447) mutation H->G,K: Abolishes cobalamin-binding.
Sites not aligning to the query:
- 256:258 HKH→KKK: Does not affect cobalamin-binding.
1q8jA Cobalamin-dependent methionine synthase (1-566) from thermotoga maritima (cd2+, hcy, methyltetrahydrofolate complex) (see paper)
28% identity, 26% coverage: 36:278/917 of query aligns to 315:538/559 of 1q8jA
- binding 5-methyl-5,6,7,8-tetrahydrofolic acid: E320 (= E41), D390 (= D114), N411 (= N135), D473 (= D202), G505 (= G241), N508 (= N244), F511 (= F247), R516 (= R256), I536 (= I276)
3bofA Cobalamin-dependent methionine synthase (1-566) from thermotoga maritima complexed with zn2+ and homocysteine (see paper)
28% identity, 26% coverage: 36:278/917 of query aligns to 315:538/560 of 3bofA
Sites not aligning to the query:
4jgiB 1.5 angstrom crystal structure of a novel cobalamin-binding protein from desulfitobacterium hafniense dcb-2 (see paper)
34% identity, 16% coverage: 381:526/917 of query aligns to 45:174/206 of 4jgiB
- active site: D95 (= D445), H97 (= H447), A148 (≠ S498)
- binding co-methylcobalamin: L63 (≠ V399), D95 (= D445), L96 (≠ V446), H97 (= H447), D98 (= D448), I99 (= I449), G100 (= G450), F104 (≠ V454), G140 (= G490), S142 (= S492), L145 (≠ I495), G173 (= G525), G174 (= G526)
Sites not aligning to the query:
3ezxA Structure of methanosarcina barkeri monomethylamine corrinoid protein
35% identity, 16% coverage: 356:499/917 of query aligns to 21:156/212 of 3ezxA
- active site: D100 (= D445), H102 (= H447), S155 (= S498)
- binding 5-hydroxybenzimidazolylcobamide: M47 (= M382), F54 (= F389), D100 (= D445), I101 (≠ V446), H102 (= H447), D103 (= D448), I104 (= I449), V109 (= V454), V147 (= V489), S149 (= S492), L151 (= L494), M152 (≠ I495), T153 (= T496)
Sites not aligning to the query:
2yckX Methyltransferase bound with tetrahydrofolate (see paper)
28% identity, 26% coverage: 35:277/917 of query aligns to 10:238/272 of 2yckX
- binding (6s)-5,6,7,8-tetrahydrofolate: M21 (≠ G47), F22 (≠ S48), D85 (= D114), N106 (= N135), D170 (= D202), G206 (= G241), N209 (= N244), Q212 (≠ F247), K213 (≠ S248), R217 (= R256), I237 (= I276)
Query Sequence
>WP_084235998.1 NCBI__GCF_001592305.1:WP_084235998.1
MSAVSDSAVSPSSSAAVPPMLLSGLEPLRIGDDSLFVNVGERTNVTGSKAFARMILNGEY
EQALAVARQQVENGAQVIDINMDEAMLDSKAAMVKFLNLIAGEPDIARVPVMVDSSKWEV
IEAGLRCVQGKGVVNSISMKEGVDEFKRQARLVKRYGAAAVVMAFDEKGQADTYERKVEI
CERAYRILVDEVGFPPEDIIFDPNIFAIATGIEEHNNYAVDFINATRWIKQHLPGAKVSG
GVSNVSFSFRGNDPVREAIHTVFLYHAIKAGMDMGIVNAGMVGVYDELEPELRERVEDVV
LNRRPDAGERLVEVAENAKGAAKDDSKKNEWRALPIRERLAHALVRGMNEFISEDTEEMW
REIEAEGGRPLNVIEGPLMDGMNVVGDLFGQGKMFLPQVVKSARVMKQAVAHLLPYIEAE
KLAQQAAGADVKPKGKIVIATVKGDVHDIGKNIVTVVLQCNNFEVVNMGVMVPCHEILAK
AKEEGADIVGLSGLITPSLEEMQYVAGEMQKDAHFREKGIPLLIGGATTSRVHTAVKISP
HYEGPVVYVPDASRSVSVAQSLIGDSRVKYIAELNADYHRVRTQHANKKQVPLWPLAQAR
ANKTPIDWAGFKPMKPKVIGKRQFKNFDLAEIAKYIDWGPFFQTWDLAGPYPAILTDEVV
GEQASKVFADGQAMLKKIIEGRWLQANGVIGLYPANTVNDDDIQLYTDESRSQVALTWHG
LRQQTEKQEVDGVLRPSRCLADFVAPKGVADDYVGLFAVTAGLGIDKKEQQFLDAHDDYN
AILFKSLADRLAEAFAECLHQRVRTDLWGYAADEQLANDELIKEKYQGIRPAPGYPACPD
HSVKRAMFALLQAEEIGMALTDSLAMTPAASVSGFYLGHPDSSYFNVGKIGEDQVEDLAE
RSGVAASELRRWLGPNL
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