SitesBLAST
Comparing WP_013841550.1 NCBI__GCF_000215085.1:WP_013841550.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 14 hits to proteins with known functional sites (download)
7xcnP Crystal structure of the mttb-mttc complex at 2.7 a resolution (see paper)
30% identity, 91% coverage: 14:213/220 of query aligns to 13:211/215 of 7xcnP
- binding 5-hydroxybenzimidazolylcobamide: D104 (= D107), I105 (≠ M108), H106 (= H109), I108 (≠ L111), G109 (= G112), V113 (= V116), S150 (≠ I153), S151 (= S154), L153 (= L156), M154 (≠ I157), T155 (= T158), M180 (≠ L182), G182 (= G184), G183 (= G185), G200 (≠ A202), S202 (≠ N204), A203 (≠ V205)
1y80A Structure of a corrinoid (factor iiim)-binding protein from moorella thermoacetica
42% identity, 48% coverage: 99:204/220 of query aligns to 7:113/125 of 1y80A
- active site: D15 (= D107), H17 (= H109), T68 (= T160)
- binding co-5-methoxybenzimidazolylcobamide: D15 (= D107), L16 (≠ M108), H17 (= H109), D18 (= D110), I19 (≠ L111), G20 (= G112), V24 (= V116), G60 (= G152), M61 (≠ I153), S62 (= S154), L64 (= L156), L65 (≠ I157), T66 (= T158), I91 (≠ L182), G93 (= G184), G94 (= G185), A95 (= A186), P112 (≠ Q203), D113 (≠ N204)
Sites not aligning to the query:
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)
32% identity, 69% coverage: 40:191/220 of query aligns to 692:840/1227 of P13009
- E694 (= E42) binding
- GDVHD 756:760 (≠ GDMHD 106:110) binding
- D757 (= D107) mutation to E: Decreases activity by about 70%.; mutation to N: Decreases activity by about 45%.
- H759 (= H109) binding axial binding residue; mutation to G: Loss of catalytic activity.
- S804 (= S154) binding
- T808 (= T158) binding
- S810 (≠ T160) mutation to A: Decreases activity by about 40%.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 247 binding
- 310 binding ; mutation C->A,S: Loss of zinc binding. Loss of catalytic activity.
- 311 binding ; mutation C->A,S: Loss of zinc binding. Loss of catalytic activity.
- 860 binding
- 946 binding
- 1134 binding
- 1189:1190 binding
1bmtA How a protein binds b12: a 3.O angstrom x-ray structure of the b12- binding domains of methionine synthase (see paper)
32% identity, 69% coverage: 40:191/220 of query aligns to 42:190/246 of 1bmtA
- active site: D107 (= D107), H109 (= H109), S160 (≠ T160)
- binding co-methylcobalamin: E44 (= E42), M48 (≠ T46), M51 (≠ L49), G55 (≠ S53), L65 (= L63), V68 (≠ I66), D107 (= D107), V108 (≠ M108), H109 (= H109), D110 (= D110), I111 (≠ L111), I115 (= I115), G152 (= G152), L153 (≠ I153), S154 (= S154), L156 (= L156), I157 (= I157), T158 (= T158), G183 (= G184), G184 (= G185), A185 (= A186)
Sites not aligning to the query:
3ivaA Structure of the b12-dependent methionine synthase (meth) c-teminal half with adohcy bound (see paper)
32% identity, 69% coverage: 40:191/220 of query aligns to 42:190/576 of 3ivaA
- active site: D107 (= D107), H109 (= H109), S160 (≠ T160)
- binding cobalamin: H109 (= H109), G112 (= G112), V116 (= V116), G152 (= G152), L153 (≠ I153), S154 (= S154), L156 (= L156), I157 (= I157), T158 (= T158), G183 (= G184), G184 (= G185)
Sites not aligning to the query:
- binding cobalamin: 208, 209, 303, 443, 486, 488, 489, 495, 520, 521, 524, 527, 528
- binding s-adenosyl-l-homocysteine: 447, 484, 485, 489, 491, 539
3bulA E. Coli i690c/g743c meth c-terminal fragment (649-1227) (see paper)
32% identity, 69% coverage: 40:191/220 of query aligns to 42:190/577 of 3bulA
- active site: D107 (= D107), H109 (= H109), S160 (≠ T160)
- binding cobalamin: H109 (= H109), V116 (= V116), G152 (= G152), L153 (≠ I153), S154 (= S154), L156 (= L156), I157 (= I157), T158 (= T158), G183 (= G184), G184 (= G185)
Sites not aligning to the query:
- binding cobalamin: 208, 209, 210, 213, 302, 443, 486, 487, 488, 489, 495, 498, 521, 524, 527, 528
2i2xB Crystal structure of methanol:cobalamin methyltransferase complex mtabc from methanosarcina barkeri (see paper)
30% identity, 72% coverage: 63:220/220 of query aligns to 95:236/258 of 2i2xB
- active site: D134 (= D107), H136 (= H109), T187 (= T160)
- binding 5-hydroxybenzimidazolylcob(iii)amide: G133 (= G106), D134 (= D107), V135 (≠ M108), H136 (= H109), D137 (= D110), I138 (≠ L111), G139 (= G112), V143 (= V116), T179 (≠ G152), T181 (≠ S154), L183 (= L156), M184 (≠ I157), T185 (= T158), A208 (≠ L182), G210 (= G184), G211 (= G185), G212 (≠ A186), G228 (≠ L212), E229 (≠ K213), E230 (= E214), A231 (≠ E215)
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)
30% identity, 72% coverage: 63:220/220 of query aligns to 95:236/258 of Q46EH4
- H129 (≠ G102) mutation to K: Does not affect cobalamin-binding.
- H136 (= H109) mutation H->G,K: Abolishes cobalamin-binding.
Sites not aligning to the query:
- 256:258 HKH→KKK: Does not affect cobalamin-binding.
8sseA Methionine synthase, c-terminal fragment, cobalamin and reactivation domains from thermus thermophilus hb8 (see paper)
32% identity, 59% coverage: 79:207/220 of query aligns to 66:192/507 of 8sseA
Sites not aligning to the query:
- binding cobalamin: 405, 409, 451, 452, 453, 454, 463, 485, 488, 490, 492
3ezxA Structure of methanosarcina barkeri monomethylamine corrinoid protein
28% identity, 78% coverage: 26:196/220 of query aligns to 24:192/212 of 3ezxA
- active site: D100 (= D107), H102 (= H109), S155 (≠ T160)
- binding 5-hydroxybenzimidazolylcobamide: M47 (≠ L49), F54 (≠ C56), D100 (= D107), I101 (≠ M108), H102 (= H109), D103 (= D110), I104 (≠ L111), V109 (= V116), V147 (≠ I151), S149 (= S154), L151 (= L156), M152 (≠ I157), T153 (= T158), M178 (≠ L182), G180 (= G184), G181 (= G185)
Sites not aligning to the query:
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)
40% identity, 41% coverage: 96:186/220 of query aligns to 772:861/1265 of Q99707
Sites not aligning to the query:
- 61 natural variant: R -> K
- 255 C → Y: in dbSNP:rs1140598
- 382:384 binding
- 449 binding
- 470 binding
- 537 binding
- 579 binding
- 585 binding
- 591 binding
- 919 D → G: in dbSNP:rs1805087
- 963 D→E: Decreases binding to MTRR; when associated with N-1071.
- 1071 K→N: Decreases binding to MTRR; when associated with E-963.
4jgiB 1.5 angstrom crystal structure of a novel cobalamin-binding protein from desulfitobacterium hafniense dcb-2 (see paper)
26% identity, 81% coverage: 26:204/220 of query aligns to 27:193/206 of 4jgiB
- active site: D95 (= D107), H97 (= H109), A148 (≠ T160)
- binding co-methylcobalamin: L63 (≠ I66), D95 (= D107), L96 (≠ M108), H97 (= H109), D98 (= D110), I99 (≠ L111), G100 (= G112), F104 (≠ V116), G140 (= G152), S142 (= S154), L145 (≠ I157), G173 (= G184), G174 (= G185), V175 (≠ A186), S191 (≠ A202), T192 (≠ Q203), N193 (= N204)
Sites not aligning to the query:
8g3hA Structure of cobalamin-dependent methionine synthase (meth) in a resting state (see paper)
27% identity, 80% coverage: 40:214/220 of query aligns to 659:831/841 of 8g3hA
- binding cobalamin: F675 (≠ C56), V685 (≠ I66), K693 (≠ E78), G720 (= G106), V722 (≠ M108), H723 (= H109), D724 (= D110), I725 (≠ L111), G726 (= G112), V730 (= V116), M767 (≠ I153), S768 (= S154), L770 (= L156), V772 (≠ T158), I795 (≠ L182), L796 (≠ A183), G797 (= G184), G798 (= G185), A799 (= A186), Y818 (≠ V201), A819 (= A202), E820 (≠ Q203), D821 (≠ N204)
Sites not aligning to the query:
8j2xA Saccharothrix syringae photocobilins protein, light state (see paper)
25% identity, 72% coverage: 10:167/220 of query aligns to 10:161/337 of 8j2xA
- binding cobalamin: A46 (≠ T46), Q49 (≠ L49), G53 (≠ S53), W56 (≠ C56), Q57 (≠ G57), W102 (≠ M108), H103 (= H109), A104 (≠ D110), L105 (= L111), P106 (≠ G112), V110 (= V116), A146 (≠ G152), L147 (≠ I153), S148 (= S154), L151 (≠ I157)
- binding biliverdine ix alpha: W56 (≠ C56)
Sites not aligning to the query:
- binding cobalamin: 173, 174, 175, 176, 195, 196, 197, 198, 287
- binding biliverdine ix alpha: 250, 253, 254, 257, 258, 261, 264, 287, 292, 295, 297, 301
Query Sequence
>WP_013841550.1 NCBI__GCF_000215085.1:WP_013841550.1
MTEKIPNTRELVVAITEGNNLEAVALARRLLDHGLDLETVVEEGLTKALESLSDKCGNDQ
FSLLEILLAGRAMMDVMEQVVSKHVCFSTLAMGKEQPVFVIGTIKGDMHDLGKNIVSMML
KVAGYRVIDLGKDVEPAKFIETAAAEQARYIGISSLITTTIPYVKEVKHLAVQEGMSDVK
VLAGGAALRQAEPEQLNVDFVAQNVFHLLGYLKEEDEAKR
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