SitesBLAST
Comparing Ga0059261_0990 FitnessBrowser__Korea:Ga0059261_0990 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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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: 8:864/865 of query aligns to 356:1222/1227 of P13009
- E694 (= E343) binding
- GDVHD 756:760 (= GDVHD 406:410) binding
- D757 (= D407) mutation to E: Decreases activity by about 70%.; mutation to N: Decreases activity by about 45%.
- H759 (= H409) binding axial binding residue; mutation to G: Loss of catalytic activity.
- S804 (= S454) binding
- T808 (= T458) binding
- S810 (= S460) mutation to A: Decreases activity by about 40%.
- A860 (= A510) binding
- D946 (= D595) binding
- R1134 (= R776) binding
- YY 1189:1190 (≠ YF 831:832) binding
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.
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: 6:864/865 of query aligns to 369:1260/1265 of Q99707
- GSR 382:384 (≠ GSA 19:21) binding
- D449 (= D86) binding
- N470 (= N107) binding
- D537 (= D173) binding
- N579 (= N215) binding
- R585 (= R221) binding
- R591 (= R227) binding
- D919 (≠ A543) to G: in dbSNP:rs1805087
- D963 (= D584) mutation to E: Decreases binding to MTRR; when associated with N-1071.
- K1071 (= K681) 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)
59% identity, 65% coverage: 301:864/865 of query aligns to 2:572/576 of 3ivaA
- active site: D107 (= D407), H109 (= H409), S160 (= S460)
- binding cobalamin: H109 (= H409), G112 (= G412), V116 (= V416), G152 (= G452), L153 (= L453), S154 (= S454), L156 (= L456), I157 (= I457), T158 (= T458), G183 (= G483), G184 (= G484), Q208 (≠ L508), N209 (≠ D509), T303 (≠ A602), D443 (= D735), A486 (= A778), G488 (= G780), Y489 (= Y781), H495 (= H787), A520 (= A812), M521 (= M813), G524 (≠ T816), V527 (= V819), S528 (= S820)
- binding s-adenosyl-l-homocysteine: E447 (= E739), R484 (= R776), P485 (= P777), Y489 (= Y781), A491 (= A783), Y539 (= Y831)
3bulA E. Coli i690c/g743c meth c-terminal fragment (649-1227) (see paper)
59% identity, 65% coverage: 301:864/865 of query aligns to 2:572/577 of 3bulA
- active site: D107 (= D407), H109 (= H409), S160 (= S460)
- binding cobalamin: H109 (= H409), V116 (= V416), G152 (= G452), L153 (= L453), S154 (= S454), L156 (= L456), I157 (= I457), T158 (= T458), G183 (= G483), G184 (= G484), Q208 (≠ L508), N209 (≠ D509), A210 (= A510), T213 (≠ A513), M302 (≠ R601), D443 (= D735), A486 (= A778), P487 (= P779), G488 (= G780), Y489 (= Y781), H495 (= H787), K498 (= K790), M521 (= M813), G524 (≠ T816), V527 (= V819), S528 (= S820)
3k13C Structure of the pterin-binding domain metr of 5- methyltetrahydrofolate-homocysteine methyltransferase from bacteroides thetaiotaomicron
65% identity, 33% coverage: 8:290/865 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 (= E13), G15 (= G19), R17 (≠ A21), N103 (= N107), D170 (= D173), G209 (= G212), S211 (= S214), N212 (= N215), R218 (= R221), R224 (= R227), I244 (= I247)
4cczA Crystal structure of human 5-methyltetrahydrofolate-homocysteine methyltransferase, the homocysteine and folate binding domains
64% identity, 33% coverage: 6:287/865 of query aligns to 329:611/611 of 4cczA
- binding (6s)-5,6,7,8-tetrahydrofolate: E336 (= E13), G342 (= G19), R344 (≠ A21), N430 (= N107), M458 (= M135), D497 (= D173), G536 (= G212), S538 (= S214), N539 (= N215), F542 (= F218), R545 (= R221), R551 (= R227)
1bmtA How a protein binds b12: a 3.O angstrom x-ray structure of the b12- binding domains of methionine synthase (see paper)
73% identity, 28% coverage: 301:542/865 of query aligns to 2:242/246 of 1bmtA
- active site: D107 (= D407), H109 (= H409), S160 (= S460)
- binding co-methylcobalamin: E44 (= E343), M48 (= M347), M51 (= M350), G55 (= G354), L65 (= L364), V68 (= V367), D107 (= D407), V108 (= V408), H109 (= H409), D110 (= D410), I111 (= I411), I115 (= I415), G152 (= G452), L153 (= L453), S154 (= S454), L156 (= L456), I157 (= I457), T158 (= T458), G183 (= G483), G184 (= G484), A185 (= A485), V207 (= V507), N209 (≠ D509), A210 (= A510)
1mskA Methionine synthase (activation domain) (see paper)
51% identity, 36% coverage: 553:864/865 of query aligns to 4:322/327 of 1mskA
6bdyA Crystal structure of the meth reactivation domain bound to sinefungin (see paper)
51% identity, 36% coverage: 553:864/865 of query aligns to 4:322/326 of 6bdyA
8g3hA Structure of cobalamin-dependent methionine synthase (meth) in a resting state (see paper)
37% identity, 56% coverage: 4:491/865 of query aligns to 328:805/841 of 8g3hA
- binding cobalamin: Q328 (≠ S4), T330 (= T6), S331 (≠ A7), F675 (= F357), V685 (= V367), K693 (= K375), G720 (= G406), V722 (= V408), H723 (= H409), D724 (= D410), I725 (= I411), G726 (= G412), V730 (= V416), M767 (≠ L453), S768 (= S454), L770 (= L456), V772 (≠ T458), I795 (≠ L481), L796 (≠ I482), G797 (= G483), G798 (= G484), A799 (= A485)
Sites not aligning to the query:
8sseA Methionine synthase, c-terminal fragment, cobalamin and reactivation domains from thermus thermophilus hb8
31% identity, 61% coverage: 310:834/865 of query aligns to 4:506/507 of 8sseA
- binding cobalamin: H97 (= H409), G100 (= G412), V104 (= V416), S142 (= S454), L145 (≠ I457), V146 (≠ T458), I169 (≠ L481), G171 (= G483), G172 (= G484), A173 (= A485), H405 (≠ K731), V409 (≠ D735), S451 (≠ A778), F452 (≠ P779), G453 (= G780), Y454 (= Y781), Q463 (≠ K790), L485 (≠ M813), E488 (≠ T816), A490 (= A818), S492 (= S820)
5vooA Methionine synthase folate-binding domain with methyltetrahydrofolate from thermus thermophilus hb8 (see paper)
35% identity, 32% coverage: 11:289/865 of query aligns to 5:279/282 of 5vooA
- binding 5-methyl-5,6,7,8-tetrahydrofolic acid: E7 (= E13), R8 (= R14), G13 (= G19), S14 (= S20), K15 (≠ A21), D77 (= D86), N98 (= N107), D165 (= D173), G204 (= G212), N207 (= N215), F210 (= F218), R217 (= R227), I237 (= I247)
7xcnP Crystal structure of the mttb-mttc complex at 2.7 a resolution (see paper)
35% identity, 18% coverage: 338:489/865 of query aligns to 36:188/215 of 7xcnP
- binding 5-hydroxybenzimidazolylcobamide: D104 (= D407), I105 (≠ V408), H106 (= H409), I108 (= I411), G109 (= G412), V113 (= V416), S150 (≠ L453), S151 (= S454), L153 (= L456), M154 (≠ I457), T155 (= T458), M180 (≠ L481), G182 (= G483), G183 (= G484)
Sites not aligning to the query:
2i2xB Crystal structure of methanol:cobalamin methyltransferase complex mtabc from methanosarcina barkeri (see paper)
37% identity, 20% coverage: 315:489/865 of query aligns to 46:216/258 of 2i2xB
- active site: D134 (= D407), H136 (= H409), T187 (≠ S460)
- binding 5-hydroxybenzimidazolylcob(iii)amide: G133 (= G406), D134 (= D407), V135 (= V408), H136 (= H409), D137 (= D410), I138 (= I411), G139 (= G412), V143 (= V416), T179 (≠ G452), T181 (≠ S454), L183 (= L456), M184 (≠ I457), T185 (= T458), A208 (≠ L481), G210 (= G483), G211 (= G484), G212 (≠ A485)
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)
37% identity, 20% coverage: 315:489/865 of query aligns to 46:216/258 of Q46EH4
- H129 (≠ A402) mutation to K: Does not affect cobalamin-binding.
- H136 (= H409) 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, 18% coverage: 325:484/865 of query aligns to 22:174/206 of 4jgiB
- active site: D95 (= D407), H97 (= H409), A148 (≠ S460)
- binding co-methylcobalamin: L63 (≠ V367), D95 (= D407), L96 (≠ V408), H97 (= H409), D98 (= D410), I99 (= I411), G100 (= G412), F104 (≠ V416), G140 (= G452), S142 (= S454), L145 (≠ I457), G173 (= G483), G174 (= G484)
Sites not aligning to the query:
2yckX Methyltransferase bound with tetrahydrofolate (see paper)
32% identity, 28% coverage: 5:248/865 of query aligns to 8:238/272 of 2yckX
- binding (6s)-5,6,7,8-tetrahydrofolate: M21 (≠ R22), F22 (= F23), D85 (= D86), N106 (= N107), D170 (= D173), G206 (= G212), N209 (= N215), Q212 (≠ F218), K213 (≠ S219), R217 (= R227), I237 (= I247)
2ycjA Methyltransferase bound with methyltetrahydrofolate (see paper)
32% identity, 28% coverage: 5:248/865 of query aligns to 7:237/271 of 2ycjA
- binding 5-methyl-5,6,7,8-tetrahydrofolic acid: M20 (≠ R22), F21 (= F23), D84 (= D86), N105 (= N107), D169 (= D173), G205 (= G212), N208 (= N215), Q211 (≠ F218), R216 (= R227), I236 (= I247)
2yciX Methyltransferase native (see paper)
32% identity, 28% coverage: 5:248/865 of query aligns to 7:237/271 of 2yciX
3ezxA Structure of methanosarcina barkeri monomethylamine corrinoid protein
34% identity, 20% coverage: 320:488/865 of query aligns to 14:185/212 of 3ezxA
- active site: D100 (= D407), H102 (= H409), S155 (= S460)
- binding 5-hydroxybenzimidazolylcobamide: M47 (= M350), F54 (= F357), D100 (= D407), I101 (≠ V408), H102 (= H409), D103 (= D410), I104 (= I411), V109 (= V416), V147 (≠ S454), S149 (vs. gap), L151 (= L456), M152 (≠ I457), T153 (= T458), M178 (≠ L481), G180 (= G483), G181 (= G484)
Sites not aligning to the query:
Query Sequence
>Ga0059261_0990 FitnessBrowser__Korea:Ga0059261_0990
MTTSSTAFVNIGERTNVTGSARFKKLIMAGDYTAAIEVALQQVESGAQVLDVNMDEGLLD
AHEAMTTFLKLIQAEPDIARIPVMVDSSKWDVIEAGLKCVSGKPIVNSISMKEGVDQFLE
HARKCMAYGAAVVVMAFDEVGQADTKDRKVEICERAYKLLVGIGFPPEDIIFDPNVFAVA
TGIEEHNNYGVDFIEACREIKARCPHVHISGGLSNLSFSFRGNEPVRKAMHSVFLYHAIP
AGMDMAIVNAGQLDVYDQIEPELRTACEDVILNRDPEAGERLVALAEKFRGTDAVAEKQA
AEWRGWAVEKRLEHALVKGIDQYVVEDTEECRQKADRPIEVIEGPLMDGMNVVGDLFGSG
KMFLPQVVKSARVMKKAVAHLLPYIEAAKEPGAKGKGKVVMATVKGDVHDIGKNIVGVVL
QCNGFEVVDLGVMVPWSKILEAANENDADMIGLSGLITPSLDEMVTVAEEMKRARMTMPL
LIGGATTSKVHTALKIAPAYDGPVVHVLDASRAVGVATTLVSDTIRDDYVAKVAGEYEAV
RIARANKGQSELVPIAVARDNAFEADMSLKPGKPRMPGVHSFPDWDLADLRQYIDWTPFF
RAWELAGNYPAILTDKVVGESATSLFADAQKMLDKIVEEKWLTARGVAGLWPCRREGDDI
IVHVEDEKHVTLPMLRQQIQKREGRANMCLADFIDRQGDWIGGFAVGIHGIEPHLARFKN
AIDDYSDILLKALADRLAEAFAERLHHYVRTALWGYAEGEQLTNEALIKEEYRGIRPAPG
YPACPEHSLKPILFDMLDAHKRTGISLTESFAMLPTAAVSGFYFGHPQAEYFGVARVGRD
QLEEYATRRGVSIEQAERWLRPNLD
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