SitesBLAST
Comparing WP_013834602.1 NCBI__GCF_000214825.1:WP_013834602.1 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)
65% identity, 99% coverage: 6:1232/1237 of query aligns to 4:1225/1227 of P13009
- C247 (= C248) binding Zn(2+)
- C310 (= C311) binding Zn(2+); mutation C->A,S: Loss of zinc binding. Loss of catalytic activity.
- C311 (= C312) binding Zn(2+); mutation C->A,S: Loss of zinc binding. Loss of catalytic activity.
- E694 (= E693) binding methylcob(III)alamin
- GDVHD 756:760 (= GDVHD 755:759) binding methylcob(III)alamin
- D757 (= D756) mutation to E: Decreases activity by about 70%.; mutation to N: Decreases activity by about 45%.
- H759 (= H758) binding axial binding residue; mutation to G: Loss of catalytic activity.
- S804 (= S803) binding methylcob(III)alamin
- T808 (= T807) binding methylcob(III)alamin
- S810 (= S809) mutation to A: Decreases activity by about 40%.
- A860 (= A859) binding methylcob(III)alamin
- D946 (= D946) binding S-adenosyl-L-methionine
- R1134 (= R1141) binding S-adenosyl-L-methionine
- YY 1189:1190 (≠ YF 1196:1197) binding S-adenosyl-L-methionine
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
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: 9:1232/1237 of query aligns to 21:1263/1265 of Q99707
- R61 (≠ M49) natural variant: R -> K
- C255 (≠ S243) to Y: in dbSNP:rs1140598
- GSR 382:384 (≠ GSA 368:370) binding (6S)-5,6,7,8-tetrahydrofolate
- D449 (= D435) binding (6S)-5,6,7,8-tetrahydrofolate
- N470 (= N456) binding (6S)-5,6,7,8-tetrahydrofolate
- D537 (= D522) binding (6S)-5,6,7,8-tetrahydrofolate
- N579 (= N564) binding (6S)-5,6,7,8-tetrahydrofolate
- R585 (= R570) binding (6S)-5,6,7,8-tetrahydrofolate
- R591 (= R576) binding (6S)-5,6,7,8-tetrahydrofolate
- D919 (≠ E892) to G: in dbSNP:rs1805087
- D963 (≠ N935) mutation to E: Decreases binding to MTRR; when associated with N-1071.
- K1071 (= K1035) mutation to N: Decreases binding to MTRR; when associated with E-963.
3ivaA Structure of the b12-dependent methionine synthase (meth) c-teminal half with adohcy bound (see paper)
62% identity, 47% coverage: 652:1232/1237 of query aligns to 3:575/576 of 3ivaA
- active site: D107 (= D756), H109 (= H758), S160 (= S809)
- binding cobalamin: H109 (= H758), G112 (= G761), V116 (= V765), G152 (= G801), L153 (= L802), S154 (= S803), L156 (= L805), I157 (= I806), T158 (= T807), G183 (= G832), G184 (= G833), Q208 (≠ K857), N209 (≠ D858), T303 (≠ S953), D443 (= D1100), A486 (= A1143), G488 (= G1145), Y489 (= Y1146), H495 (= H1152), A520 (= A1177), M521 (= M1178), G524 (≠ T1181), V527 (= V1184), S528 (= S1185)
- binding s-adenosyl-l-homocysteine: E447 (= E1104), R484 (= R1141), P485 (= P1142), Y489 (= Y1146), A491 (= A1148), Y539 (= Y1196)
3bulA E. Coli i690c/g743c meth c-terminal fragment (649-1227) (see paper)
62% identity, 47% coverage: 652:1232/1237 of query aligns to 3:575/577 of 3bulA
- active site: D107 (= D756), H109 (= H758), S160 (= S809)
- binding cobalamin: H109 (= H758), V116 (= V765), G152 (= G801), L153 (= L802), S154 (= S803), L156 (= L805), I157 (= I806), T158 (= T807), G183 (= G832), G184 (= G833), Q208 (≠ K857), N209 (≠ D858), A210 (= A859), T213 (≠ A862), M302 (≠ Q952), D443 (= D1100), A486 (= A1143), P487 (= P1144), G488 (= G1145), Y489 (= Y1146), H495 (= H1152), K498 (= K1155), M521 (= M1178), G524 (≠ T1181), V527 (= V1184), S528 (= S1185)
4cczA Crystal structure of human 5-methyltetrahydrofolate-homocysteine methyltransferase, the homocysteine and folate binding domains
53% identity, 51% coverage: 9:636/1237 of query aligns to 5:611/611 of 4cczA
- binding (6s)-5,6,7,8-tetrahydrofolate: E336 (= E362), G342 (= G368), R344 (≠ A370), N430 (= N456), M458 (= M484), D497 (= D522), G536 (= G561), S538 (= S563), N539 (= N564), F542 (= F567), R545 (= R570), R551 (= R576)
8g3hA Structure of cobalamin-dependent methionine synthase (meth) in a resting state (see paper)
35% identity, 70% coverage: 14:875/1237 of query aligns to 9:838/841 of 8g3hA
- binding cobalamin: Q328 (≠ D353), T330 (= T355), S331 (≠ L356), F675 (= F707), V685 (= V717), K693 (= K725), G720 (= G755), V722 (= V757), H723 (= H758), D724 (= D759), I725 (= I760), G726 (= G761), V730 (= V765), M767 (≠ L802), S768 (= S803), L770 (= L805), V772 (≠ T807), I795 (≠ L830), L796 (≠ I831), G797 (= G832), G798 (= G833), A799 (= A834), Y818 (= Y855), A819 (≠ V856), E820 (≠ K857), D821 (= D858)
3k13C Structure of the pterin-binding domain metr of 5- methyltetrahydrofolate-homocysteine methyltransferase from bacteroides thetaiotaomicron
67% identity, 23% coverage: 357:639/1237 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 (= E362), G15 (= G368), R17 (≠ A370), N103 (= N456), D170 (= D522), G209 (= G561), S211 (= S563), N212 (= N564), R218 (= R570), R224 (= R576), I244 (= I596)
6bdyA Crystal structure of the meth reactivation domain bound to sinefungin (see paper)
57% identity, 27% coverage: 903:1232/1237 of query aligns to 4:325/326 of 6bdyA
1mskA Methionine synthase (activation domain) (see paper)
57% identity, 27% coverage: 903:1232/1237 of query aligns to 4:325/327 of 1mskA
1bmtA How a protein binds b12: a 3.O angstrom x-ray structure of the b12- binding domains of methionine synthase (see paper)
71% identity, 19% coverage: 652:890/1237 of query aligns to 3:241/246 of 1bmtA
- active site: D107 (= D756), H109 (= H758), S160 (= S809)
- binding co-methylcobalamin: E44 (= E693), M48 (= M697), M51 (= M700), G55 (= G704), L65 (= L714), V68 (= V717), D107 (= D756), V108 (= V757), H109 (= H758), D110 (= D759), I111 (= I760), I115 (= I764), G152 (= G801), L153 (= L802), S154 (= S803), L156 (= L805), I157 (= I806), T158 (= T807), G183 (= G832), G184 (= G833), A185 (= A834), V207 (= V856), N209 (≠ D858), A210 (= A859)
8sseA Methionine synthase, c-terminal fragment, cobalamin and reactivation domains from thermus thermophilus hb8 (see paper)
31% identity, 44% coverage: 660:1199/1237 of query aligns to 4:506/507 of 8sseA
- binding cobalamin: H97 (= H758), G100 (= G761), V104 (= V765), S142 (= S803), L145 (≠ I806), V146 (≠ T807), I169 (≠ L830), G171 (= G832), G172 (= G833), A173 (= A834), H405 (≠ K1096), V409 (≠ D1100), S451 (≠ A1143), F452 (≠ P1144), G453 (= G1145), Y454 (= Y1146), Q463 (≠ K1155), L485 (≠ M1178), E488 (≠ T1181), A490 (= A1183), S492 (= S1185)
1q8jA Cobalamin-dependent methionine synthase (1-566) from thermotoga maritima (cd2+, hcy, methyltetrahydrofolate complex) (see paper)
28% identity, 48% coverage: 9:598/1237 of query aligns to 6:538/559 of 1q8jA
- binding 5-methyl-5,6,7,8-tetrahydrofolic acid: E320 (= E362), D390 (= D435), N411 (= N456), D473 (= D522), G505 (= G561), N508 (= N564), F511 (= F567), R516 (= R576), I536 (= I596)
3bofA Cobalamin-dependent methionine synthase (1-566) from thermotoga maritima complexed with zn2+ and homocysteine (see paper)
28% identity, 48% coverage: 9:598/1237 of query aligns to 6:538/560 of 3bofA
5vooA Methionine synthase folate-binding domain with methyltetrahydrofolate from thermus thermophilus hb8 (see paper)
34% identity, 23% coverage: 355:638/1237 of query aligns to 1:279/282 of 5vooA
- binding 5-methyl-5,6,7,8-tetrahydrofolic acid: E7 (= E362), R8 (= R363), G13 (= G368), S14 (= S369), K15 (≠ A370), D77 (= D435), N98 (= N456), D165 (= D522), G204 (= G561), N207 (= N564), F210 (= F567), R217 (= R576), I237 (= I596)
7xcnP Crystal structure of the mttb-mttc complex at 2.7 a resolution (see paper)
31% identity, 14% coverage: 670:838/1237 of query aligns to 14:188/215 of 7xcnP
- binding 5-hydroxybenzimidazolylcobamide: D104 (= D756), I105 (≠ V757), H106 (= H758), I108 (= I760), G109 (= G761), V113 (= V765), S150 (≠ L802), S151 (= S803), L153 (= L805), M154 (≠ I806), T155 (= T807), M180 (≠ L830), G182 (= G832), G183 (= G833)
Sites not aligning to the query:
2i2xB Crystal structure of methanol:cobalamin methyltransferase complex mtabc from methanosarcina barkeri (see paper)
31% identity, 18% coverage: 661:886/1237 of query aligns to 38:255/258 of 2i2xB
- active site: D134 (= D756), H136 (= H758), T187 (≠ S809)
- binding 5-hydroxybenzimidazolylcob(iii)amide: G133 (= G755), D134 (= D756), V135 (= V757), H136 (= H758), D137 (= D759), I138 (= I760), G139 (= G761), V143 (= V765), T179 (≠ G801), T181 (≠ S803), L183 (= L805), M184 (≠ I806), T185 (= T807), A208 (≠ L830), G210 (= G832), G211 (= G833), G212 (≠ A834), G228 (≠ V856), E229 (≠ K857), E230 (≠ D858), A231 (= A859)
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)
31% identity, 18% coverage: 661:886/1237 of query aligns to 38:255/258 of Q46EH4
- H129 (≠ A751) mutation to K: Does not affect cobalamin-binding.
- H136 (= H758) mutation H->G,K: Abolishes cobalamin-binding.
Sites not aligning to the query:
- 256:258 HKH→KKK: Does not affect cobalamin-binding.
4jgiB 1.5 angstrom crystal structure of a novel cobalamin-binding protein from desulfitobacterium hafniense dcb-2 (see paper)
35% identity, 11% coverage: 699:833/1237 of query aligns to 45:174/206 of 4jgiB
- active site: D95 (= D756), H97 (= H758), A148 (≠ S809)
- binding co-methylcobalamin: L63 (≠ V717), D95 (= D756), L96 (≠ V757), H97 (= H758), D98 (= D759), I99 (= I760), G100 (= G761), F104 (≠ V765), G140 (= G801), S142 (= S803), L145 (≠ I806), G173 (= G832), G174 (= G833)
Sites not aligning to the query:
3ezxA Structure of methanosarcina barkeri monomethylamine corrinoid protein
34% identity, 12% coverage: 686:837/1237 of query aligns to 32:185/212 of 3ezxA
- active site: D100 (= D756), H102 (= H758), S155 (= S809)
- binding 5-hydroxybenzimidazolylcobamide: M47 (= M700), F54 (= F707), D100 (= D756), I101 (≠ V757), H102 (= H758), D103 (= D759), I104 (= I760), V109 (= V765), V147 (≠ S803), S149 (vs. gap), L151 (= L805), M152 (≠ I806), T153 (= T807), M178 (≠ L830), G180 (= G832), G181 (= G833)
Sites not aligning to the query:
2yckX Methyltransferase bound with tetrahydrofolate (see paper)
27% identity, 20% coverage: 354:597/1237 of query aligns to 8:238/272 of 2yckX
- binding (6s)-5,6,7,8-tetrahydrofolate: M21 (≠ L371), F22 (= F372), D85 (= D435), N106 (= N456), D170 (= D522), G206 (= G561), N209 (= N564), Q212 (≠ G571), K213 (≠ N572), R217 (= R576), I237 (= I596)
Query Sequence
>WP_013834602.1 NCBI__GCF_000214825.1:WP_013834602.1
MTRVERIAQLKQLLTERVVVLDGAMGTMIQGLQLTEDDFRGELFADYHMDIKGNNDILVM
TKPEVIRDIHLGFLRQGVDILETNSFNATTIAQADYDMQDQVRAINICAAKVAREACDIA
AAEDGKPRFVAGVLGPTNRTASISPDVNDPGFRNTSFDELVGAYVQATEALLEGGADVIL
IETIFDTLNAKAAIFAVKQVEDALGEELPIMISGTITDASGRTLSGQTTEAFYNAIRHAK
PLSVGLNCALGPKELRPYVEELSRIAECYVSVHPNAGLPNEFGEYDETPEQMAAEVQTWA
QAGWLNIIGGCCGTTPDHVEAMAKAALAHPQRIIPTIKKACRLSGLEPMTIDDTTLFVNV
GERNNVTGSALFKRLIIEDNYEQAVEIAVKQVNDGAQIIDVNMDEGMLDAKACMSRFLNM
MAGEPDAARVPVMIDSSKWEAIEAGLKCIQGKGIVNSISLKEGEENFLAQAKLIQRYGAA
TIVMAFDEDGQADTFARKKEICQRSYDLLVANGFPPEDIIFDPNIFAVATGIEEHNNYAV
DFIEATGWIKQNLPYAMISGGVSNVSFSFRGNNPVREAIHSVFLYYAIQQGMDMGIVNAG
QMAIYDDLDPELKQAVEDVILNKDPEAADRLLEVAEKFRGDGSVQGKESDIKWREASVEK
RLEHALVKGITDFIEDDTEEARTTLGSPLQVIEGPLMDGMNVVGDLFGAGKMFLPQVVKS
ARVMKRAVAYLQPFLEAEKSSGQAKGKIVMATVKGDVHDIGKNIVGVVLQCNNFEVIDLG
VMVPAEKILDTALREGANVIGLSGLITPSLEEMVHVAKEMQRRGMSIPLLIGGATTSKAH
TAVKIEPQYEHPVVYVKDASRAVGVAQSLISNDLKVDFAIKIREEYVQLREERKARAQQV
KRVPLNKARDNAIPIDWSDYTPPKPKFLGKKVFDNIDLADLMPRIDWSPFFQSWDLHGLY
PRILDDKVVGEEAKKVFADAQAMLKQIIDEKWLTARAVIGFYPANAVGDDIELYTDDKRA
TLLTRLHNLRQQAEKKPGQYNQCLSDYIAPKDVKEQPGLVIPDYIGAFAVTAGIGIDEHI
ARFEAAHDDYNSIMVKALADRLAEALAEHMHELVRKEFWGYAADEALTNEELIKEKYQGI
RPAPGYPANPEHTEKGTLWELLQPDSEIGLELTSSYAMTPTAAVSGWYFAHPKSKYFGVG
SIGRDQAEDYAHRKGWSIAEAEKWLAPILGYDPEDFN
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