SitesBLAST
Comparing SMc04331 FitnessBrowser__Smeli:SMc04331 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)
36% identity, 90% coverage: 12:219/232 of query aligns to 2:211/215 of 7xcnP
- binding 5-hydroxybenzimidazolylcobamide: D104 (= D112), I105 (= I113), H106 (≠ D114), I108 (= I116), G109 (= G117), V113 (= V121), S150 (≠ M158), S151 (= S159), L153 (= L161), M154 (≠ L162), T155 (= T163), M180 (≠ L188), G182 (= G190), G183 (= G191), G200 (≠ C208), S202 (≠ D210), A203 (= A211)
1y80A Structure of a corrinoid (factor iiim)-binding protein from moorella thermoacetica
52% identity, 53% coverage: 99:222/232 of query aligns to 2:125/125 of 1y80A
- active site: D15 (= D112), H17 (≠ D114), T68 (= T165)
- binding co-5-methoxybenzimidazolylcobamide: D15 (= D112), L16 (≠ I113), H17 (≠ D114), D18 (= D115), I19 (= I116), G20 (= G117), V24 (= V121), G60 (= G157), M61 (= M158), S62 (= S159), L64 (= L161), L65 (= L162), T66 (= T163), I91 (≠ L188), G93 (= G190), G94 (= G191), A95 (= A192), P112 (≠ R209), D113 (= D210), A114 (= A211)
4jgiB 1.5 angstrom crystal structure of a novel cobalamin-binding protein from desulfitobacterium hafniense dcb-2 (see paper)
33% identity, 88% coverage: 19:222/232 of query aligns to 9:205/206 of 4jgiB
- active site: D95 (= D112), H97 (≠ D114), A148 (≠ T165)
- binding co-methylcobalamin: L63 (≠ V75), D95 (= D112), L96 (≠ I113), H97 (≠ D114), D98 (= D115), I99 (= I116), G100 (= G117), F104 (≠ V121), G140 (= G157), S142 (= S159), L145 (= L162), G173 (= G190), G174 (= G191), V175 (≠ A192), S191 (≠ C208), T192 (≠ R209), N193 (≠ D210), A194 (= A211)
2i2xB Crystal structure of methanol:cobalamin methyltransferase complex mtabc from methanosarcina barkeri (see paper)
34% identity, 88% coverage: 14:218/232 of query aligns to 37:238/258 of 2i2xB
- active site: D134 (= D112), H136 (≠ D114), T187 (= T165)
- binding 5-hydroxybenzimidazolylcob(iii)amide: G133 (= G111), D134 (= D112), V135 (≠ I113), H136 (≠ D114), D137 (= D115), I138 (= I116), G139 (= G117), V143 (= V121), T179 (≠ G157), T181 (≠ S159), L183 (= L161), M184 (≠ L162), T185 (= T163), A208 (≠ V186), G210 (= G190), G211 (= G191), G212 (≠ A192), G228 (≠ C208), E229 (≠ R209), E230 (≠ D210), A231 (= A211)
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)
34% identity, 88% coverage: 14:218/232 of query aligns to 37:238/258 of Q46EH4
- H129 (≠ G107) mutation to K: Does not affect cobalamin-binding.
- H136 (≠ D114) mutation H->G,K: Abolishes cobalamin-binding.
Sites not aligning to the query:
- 256:258 HKH→KKK: Does not affect cobalamin-binding.
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)
35% identity, 77% coverage: 15:192/232 of query aligns to 658:835/1227 of P13009
- E694 (≠ T51) binding
- GDVHD 756:760 (≠ GDIDD 111:115) binding
- D757 (= D112) mutation to E: Decreases activity by about 70%.; mutation to N: Decreases activity by about 45%.
- H759 (≠ D114) binding axial binding residue; mutation to G: Loss of catalytic activity.
- S804 (= S159) binding
- T808 (= T163) binding
- S810 (≠ T165) 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
8sseA Methionine synthase, c-terminal fragment, cobalamin and reactivation domains from thermus thermophilus hb8
36% identity, 79% coverage: 16:198/232 of query aligns to 2:179/507 of 8sseA
Sites not aligning to the query:
- binding cobalamin: 405, 409, 451, 452, 453, 454, 463, 485, 488, 490, 492
3bulA E. Coli i690c/g743c meth c-terminal fragment (649-1227) (see paper)
34% identity, 77% coverage: 15:192/232 of query aligns to 8:185/577 of 3bulA
- active site: D107 (= D112), H109 (≠ D114), S160 (≠ T165)
- binding cobalamin: H109 (≠ D114), V116 (= V121), G152 (= G157), L153 (≠ M158), S154 (= S159), L156 (= L161), I157 (≠ L162), T158 (= T163), G183 (= G190), G184 (= G191)
Sites not aligning to the query:
- binding cobalamin: 208, 209, 210, 213, 302, 443, 486, 487, 488, 489, 495, 498, 521, 524, 527, 528
3ivaA Structure of the b12-dependent methionine synthase (meth) c-teminal half with adohcy bound (see paper)
34% identity, 77% coverage: 15:192/232 of query aligns to 8:185/576 of 3ivaA
- active site: D107 (= D112), H109 (≠ D114), S160 (≠ T165)
- binding cobalamin: H109 (≠ D114), G112 (= G117), V116 (= V121), G152 (= G157), L153 (≠ M158), S154 (= S159), L156 (= L161), I157 (≠ L162), T158 (= T163), G183 (= G190), G184 (= G191)
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
1bmtA How a protein binds b12: a 3.O angstrom x-ray structure of the b12- binding domains of methionine synthase (see paper)
35% identity, 78% coverage: 15:196/232 of query aligns to 8:189/246 of 1bmtA
- active site: D107 (= D112), H109 (≠ D114), S160 (≠ T165)
- binding co-methylcobalamin: E44 (≠ T51), M48 (≠ V55), M51 (= M58), G55 (= G62), L65 (≠ V72), V68 (= V75), D107 (= D112), V108 (≠ I113), H109 (≠ D114), D110 (= D115), I111 (= I116), I115 (≠ L120), G152 (= G157), L153 (≠ M158), S154 (= S159), L156 (= L161), I157 (≠ L162), T158 (= T163), G183 (= G190), G184 (= G191), A185 (= A192)
Sites not aligning to the query:
3ezxA Structure of methanosarcina barkeri monomethylamine corrinoid protein
34% identity, 80% coverage: 18:203/232 of query aligns to 3:193/212 of 3ezxA
- active site: D100 (= D112), H102 (≠ D114), S155 (≠ T165)
- binding 5-hydroxybenzimidazolylcobamide: M47 (= M58), F54 (= F65), D100 (= D112), I101 (= I113), H102 (≠ D114), D103 (= D115), I104 (= I116), V109 (= V121), V147 (≠ G157), S149 (= S159), L151 (= L161), M152 (≠ L162), T153 (= T163), M178 (≠ L188), G180 (= G190), G181 (= G191)
Sites not aligning to the query:
8g3hA Structure of cobalamin-dependent methionine synthase (meth) in a resting state (see paper)
35% identity, 85% coverage: 1:198/232 of query aligns to 615:805/841 of 8g3hA
- binding cobalamin: F675 (= F65), V685 (= V75), K693 (= K83), G720 (= G111), V722 (≠ I113), H723 (≠ D114), D724 (= D115), I725 (= I116), G726 (= G117), V730 (= V121), M767 (= M158), S768 (= S159), L770 (= L161), V772 (≠ T163), I795 (≠ L188), L796 (≠ V189), G797 (= G190), G798 (= G191), A799 (= A192)
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)
35% identity, 73% coverage: 24:192/232 of query aligns to 679:861/1265 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.
Q59268 2-methyleneglutarate mutase; Alpha-methyleneglutarate mutase; EC 5.4.99.4 from Eubacterium barkeri (Clostridium barkeri) (see paper)
36% identity, 42% coverage: 94:191/232 of query aligns to 465:562/614 of Q59268
- D483 (= D112) mutation to N: Activity reduced 2000-fold.
- H485 (≠ D114) mutation to Q: Loss of activity.
Sites not aligning to the query:
- 464 H→Q: No effect on activity.
Query Sequence
>SMc04331 FitnessBrowser__Smeli:SMc04331
MADDEIILEDLSDEELVQQMHDDLYDGLKEEIEEGTRILLKRGWTPYDVLTQALVEGMRI
VGIDFRDGILFVPEVLLSANAMKAGMFILRPLLVETGAPKLGKMVIGTVKGDIDDIGKNL
VGMMMEGAGFDVVDLGINNPVENYLEALEREKPDILGMSALLTTTMPYMKVVIDTMKEKG
LRDEYVVLVGGAPLNEEFGKAVGADAYCRDAAVAVETAKDYMKRKHNQLAAG
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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