SitesBLAST
Comparing WP_020177190.1 NCBI__GCF_000385335.1:WP_020177190.1 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)
63% identity, 99% coverage: 4:1232/1242 of query aligns to 2:1225/1227 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 760:764) binding methylcob(III)alamin
- D757 (= D761) mutation to E: Decreases activity by about 70%.; mutation to N: Decreases activity by about 45%.
- H759 (= H763) binding axial binding residue; mutation to G: Loss of catalytic activity.
- S804 (= S808) binding methylcob(III)alamin
- T808 (= T812) binding methylcob(III)alamin
- S810 (= S814) mutation to A: Decreases activity by about 40%.
- A860 (= A865) binding methylcob(III)alamin
- D946 (= D952) 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, 98% coverage: 10:1232/1242 of query aligns to 22:1263/1265 of Q99707
- R61 (= R49) natural variant: R -> K
- C255 (≠ T243) 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 (= D523) binding (6S)-5,6,7,8-tetrahydrofolate
- N579 (= N565) binding (6S)-5,6,7,8-tetrahydrofolate
- R585 (= R571) binding (6S)-5,6,7,8-tetrahydrofolate
- R591 (= R577) binding (6S)-5,6,7,8-tetrahydrofolate
- D919 (≠ A898) to G: in dbSNP:rs1805087
- D963 (≠ T941) mutation to E: Decreases binding to MTRR; when associated with N-1071.
- K1071 (= K1041) mutation to N: Decreases binding to MTRR; when associated with E-963.
3bulA E. Coli i690c/g743c meth c-terminal fragment (649-1227) (see paper)
60% identity, 47% coverage: 653:1232/1242 of query aligns to 4:575/577 of 3bulA
- active site: D107 (= D761), H109 (= H763), S160 (= S814)
- binding cobalamin: H109 (= H763), V116 (= V770), G152 (= G806), L153 (= L807), S154 (= S808), L156 (= L810), I157 (= I811), T158 (= T812), G183 (= G837), G184 (= G838), Q208 (≠ T863), N209 (≠ D864), A210 (= A865), T213 (≠ A868), M302 (≠ Q958), D443 (= D1100), A486 (= A1143), P487 (= P1144), G488 (= G1145), Y489 (= Y1146), H495 (= H1152), K498 (= K1155), M521 (= M1178), G524 (= G1181), V527 (= V1184), S528 (= S1185)
3ivaA Structure of the b12-dependent methionine synthase (meth) c-teminal half with adohcy bound (see paper)
60% identity, 47% coverage: 653:1232/1242 of query aligns to 4:575/576 of 3ivaA
- active site: D107 (= D761), H109 (= H763), S160 (= S814)
- binding cobalamin: H109 (= H763), G112 (= G766), V116 (= V770), G152 (= G806), L153 (= L807), S154 (= S808), L156 (= L810), I157 (= I811), T158 (= T812), G183 (= G837), G184 (= G838), Q208 (≠ T863), N209 (≠ D864), T303 (= T959), D443 (= D1100), A486 (= A1143), G488 (= G1145), Y489 (= Y1146), H495 (= H1152), A520 (= A1177), M521 (= M1178), G524 (= G1181), V527 (= V1184), S528 (= S1185)
- binding s-adenosyl-l-homocysteine: E447 (= E1104), R484 (= R1141), P485 (= P1142), Y489 (= Y1146), A491 (= A1148), Y539 (= Y1196)
4cczA Crystal structure of human 5-methyltetrahydrofolate-homocysteine methyltransferase, the homocysteine and folate binding domains
54% identity, 51% coverage: 10:637/1242 of query aligns to 6:611/611 of 4cczA
- binding (6s)-5,6,7,8-tetrahydrofolate: E336 (= E362), G342 (= G368), R344 (≠ A370), N430 (= N456), M458 (= M484), D497 (= D523), G536 (= G562), S538 (= S564), N539 (= N565), F542 (= F568), R545 (= R571), R551 (= R577)
8g3hA Structure of cobalamin-dependent methionine synthase (meth) in a resting state (see paper)
37% identity, 70% coverage: 7:875/1242 of query aligns to 3:832/841 of 8g3hA
- binding cobalamin: Q328 (≠ K353), T330 (≠ I355), S331 (≠ R356), F675 (= F707), V685 (= V717), K693 (= K725), G720 (= G760), V722 (= V762), H723 (= H763), D724 (= D764), I725 (= I765), G726 (= G766), V730 (= V770), M767 (≠ L807), S768 (= S808), L770 (= L810), V772 (≠ T812), I795 (≠ L835), L796 (≠ I836), G797 (= G837), G798 (= G838), A799 (= A839), Y818 (= Y861), A819 (≠ V862), E820 (≠ T863), D821 (= D864)
3k13C Structure of the pterin-binding domain metr of 5- methyltetrahydrofolate-homocysteine methyltransferase from bacteroides thetaiotaomicron
66% identity, 23% coverage: 354:640/1242 of query aligns to 1:286/287 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 (= D523), G209 (= G562), S211 (= S564), N212 (= N565), R218 (= R571), R224 (= R577), I244 (= I597)
6bdyA Crystal structure of the meth reactivation domain bound to sinefungin (see paper)
55% identity, 26% coverage: 911:1232/1242 of query aligns to 6:325/326 of 6bdyA
1mskA Methionine synthase (activation domain) (see paper)
55% identity, 26% coverage: 911:1232/1242 of query aligns to 6:325/327 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)
67% identity, 20% coverage: 653:901/1242 of query aligns to 4:246/246 of 1bmtA
- active site: D107 (= D761), H109 (= H763), S160 (= S814)
- binding co-methylcobalamin: E44 (= E693), M48 (= M697), M51 (= M700), G55 (= G704), L65 (= L714), V68 (= V717), D107 (= D761), V108 (= V762), H109 (= H763), D110 (= D764), I111 (= I765), I115 (= I769), G152 (= G806), L153 (= L807), S154 (= S808), L156 (= L810), I157 (= I811), T158 (= T812), G183 (= G837), G184 (= G838), A185 (= A839), V207 (= V862), N209 (≠ D864), A210 (= A865)
8sseA Methionine synthase, c-terminal fragment, cobalamin and reactivation domains from thermus thermophilus hb8 (see paper)
34% identity, 44% coverage: 657:1199/1242 of query aligns to 1:506/507 of 8sseA
- binding cobalamin: H97 (= H763), G100 (= G766), V104 (= V770), S142 (= S808), L145 (≠ I811), V146 (≠ T812), I169 (≠ L835), G171 (= G837), G172 (= G838), A173 (= A839), H405 (≠ K1096), V409 (≠ D1100), S451 (≠ A1143), F452 (≠ P1144), G453 (= G1145), Y454 (= Y1146), Q463 (≠ K1155), L485 (≠ M1178), E488 (≠ G1181), A490 (≠ S1183), S492 (= S1185)
1q8jA Cobalamin-dependent methionine synthase (1-566) from thermotoga maritima (cd2+, hcy, methyltetrahydrofolate complex) (see paper)
29% identity, 47% coverage: 16:599/1242 of query aligns to 13:538/559 of 1q8jA
- binding 5-methyl-5,6,7,8-tetrahydrofolic acid: E320 (= E362), D390 (= D435), N411 (= N456), D473 (= D523), G505 (= G562), N508 (= N565), F511 (= F568), R516 (= R577), I536 (= I597)
3bofA Cobalamin-dependent methionine synthase (1-566) from thermotoga maritima complexed with zn2+ and homocysteine (see paper)
29% identity, 47% coverage: 16:599/1242 of query aligns to 13:538/560 of 3bofA
5vooA Methionine synthase folate-binding domain with methyltetrahydrofolate from thermus thermophilus hb8 (see paper)
35% identity, 23% coverage: 360:642/1242 of query aligns to 5:282/282 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 (= D523), G204 (= G562), N207 (= N565), F210 (= F568), R217 (= R577), I237 (= I597)
2i2xB Crystal structure of methanol:cobalamin methyltransferase complex mtabc from methanosarcina barkeri (see paper)
31% identity, 16% coverage: 645:843/1242 of query aligns to 27:216/258 of 2i2xB
- active site: D134 (= D761), H136 (= H763), T187 (≠ S814)
- binding 5-hydroxybenzimidazolylcob(iii)amide: G133 (= G760), D134 (= D761), V135 (= V762), H136 (= H763), D137 (= D764), I138 (= I765), G139 (= G766), V143 (= V770), T179 (≠ G806), T181 (≠ S808), L183 (= L810), M184 (≠ I811), T185 (= T812), A208 (≠ L835), G210 (= G837), G211 (= G838), G212 (≠ A839)
Sites not aligning to the query:
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, 16% coverage: 645:843/1242 of query aligns to 27:216/258 of Q46EH4
- H129 (≠ A756) mutation to K: Does not affect cobalamin-binding.
- H136 (= H763) mutation H->G,K: Abolishes cobalamin-binding.
Sites not aligning to the query:
- 256:258 HKH→KKK: Does not affect cobalamin-binding.
7xcnP Crystal structure of the mttb-mttc complex at 2.7 a resolution (see paper)
31% identity, 14% coverage: 670:843/1242 of query aligns to 14:188/215 of 7xcnP
- binding 5-hydroxybenzimidazolylcobamide: D104 (= D761), I105 (≠ V762), H106 (= H763), I108 (= I765), G109 (= G766), V113 (= V770), S150 (≠ L807), S151 (= S808), L153 (= L810), M154 (≠ I811), T155 (= T812), M180 (≠ L835), G182 (= G837), G183 (= G838)
Sites not aligning to the query:
3ezxA Structure of methanosarcina barkeri monomethylamine corrinoid protein
34% identity, 15% coverage: 661:842/1242 of query aligns to 8:185/212 of 3ezxA
- active site: D100 (= D761), H102 (= H763), S155 (= S814)
- binding 5-hydroxybenzimidazolylcobamide: M47 (= M700), F54 (= F707), D100 (= D761), I101 (≠ V762), H102 (= H763), D103 (= D764), I104 (= I765), V109 (= V770), V147 (≠ I805), S149 (= S808), L151 (= L810), M152 (≠ I811), T153 (= T812), M178 (≠ L835), G180 (= G837), G181 (= G838)
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)
30% identity, 16% coverage: 670:873/1242 of query aligns to 19:202/206 of 4jgiB
- active site: D95 (= D761), H97 (= H763), A148 (≠ S814)
- binding co-methylcobalamin: L63 (≠ V717), D95 (= D761), L96 (≠ V762), H97 (= H763), D98 (= D764), I99 (= I765), G100 (= G766), F104 (≠ V770), G140 (= G806), S142 (= S808), L145 (≠ I811), G173 (= G837), G174 (= G838), V175 (= V848), S191 (≠ V862), T192 (= T863), N193 (≠ D864), A194 (= A865)
4o1eA Structure of a methyltransferase component in complex with mthf involved in o-demethylation (see paper)
25% identity, 20% coverage: 357:599/1242 of query aligns to 5:232/271 of 4o1eA
- binding 5-methyl-5,6,7,8-tetrahydrofolic acid: E10 (= E362), K11 (≠ R363), I16 (≠ G368), N100 (= N456), D164 (= D523), K211 (≠ Q578), I230 (= I597), D232 (≠ N599)
Sites not aligning to the query:
Query Sequence
>WP_020177190.1 NCBI__GCF_000385335.1:WP_020177190.1
MKESDTFAALRAAAREKILVLDGAMGTMIQQHKFTEADFRAERFADWPRDLRGNNDLLVL
TQPHAIRAIHLAYCDAGADIIATNTFSSTRIAQADYGMERLVPELNFEAARLACEAAHES
EERHGRRHFVAGALGPTNRTASISPDVNNPGFRAVSFDELRDAYAEAARALIEGGVDILI
VETIFDTLNAKAALVGIDQVFDDMGKKLPVMISGTITDLSGRTLSGQTPTAFWNSLRHAK
PFTIGLNCALGAREMRAHLAEISRIADTYVCAYPNAGLPNEFGLYDESPEYMASLIGEFA
ESGLVNIVGGCCGTTPPHIHAIAKRVVGIAPRKIPEIVPLLRLSGLEPFALTKEIRFVNV
GERTNVTGSAKFRKLIKEGDFSAALDVARDQVVAGAQVIDINMDEGLLDSEKAMVDFLNL
VAAEPDIARVPVMVDSSKFQVIESGLKCIQGKPIVNSISMKEGEEKFVEVAKLVRRYGAA
VVVMAFDEQGQADTCARKIEICSRAYKILTETVGFPPEDIIFDPNIFAVATGIEEHNNYG
VDFIEATREVRKRFPLVHISGGVSNLSFSFRGNEMVRQAMHSVFLYHAISAGMDMGIVNA
GQLSVYEDIDPELRDACEDVVLNRRPDGTERLLALAERFKGQGTERAEKDLVWRSEPVEK
RLEHALVNGITEFIDADTEEARAKSTRPLDVIEGPLMAGMNVVGDLFGSGKMFLPQVVKS
ARVMKQAVAYLMPYMEEEKRKNGGAERKNAGKILMATVKGDVHDIGKNIVGVVLACNNYE
IIDLGVMVPCAKILDVARTEKVDAIGLSGLITPSLDEMCFVASEMEREGFSMPLLIGGAT
TSRVHTAVKINPNYTKGQTVYVTDASRAVGVVQNLFSPAARGPYIEAIKTEYENVAEAHM
RNEAEKNRQPLPRARANALKLDWAAYEPPHPTFLGTRIFRTYDVAELVPYIDWTPFFQTW
EMRGRYPDILSDPEKGAAAQQLFDDAQAMLARIVEEHWFDPKAVIGFWPANAIGDDIKLY
TGESRSEVLATFHTLRQQLSKRDGRPNIAMSDYIAPVESLKPDYLGGFVVTAGAREEKIA
DRFAKANDDYGSIMVKALADRIAEAFAERMHERVRKEFWAYAPDEALAPDELITEPYRGI
RPAPGYPAQPDHTEKATLFRLLEPERRIGVTLTESFAMWPGSSVSGLYLSHPDARYFGVA
KIERDQVEDYALRKGMDFAEMERWLAPILNYDPARHAKAAAE
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