SitesBLAST
Comparing GFF1835 FitnessBrowser__Marino:GFF1835 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: 5:1229/1232 of query aligns to 2:1225/1227 of P13009
- C247 (= C250) binding Zn(2+)
- C310 (= C313) binding Zn(2+); mutation C->A,S: Loss of zinc binding. Loss of catalytic activity.
- C311 (= C314) binding Zn(2+); mutation C->A,S: Loss of zinc binding. Loss of catalytic activity.
- E694 (= E694) binding methylcob(III)alamin
- GDVHD 756:760 (= GDVHD 757:761) binding methylcob(III)alamin
- D757 (= D758) mutation to E: Decreases activity by about 70%.; mutation to N: Decreases activity by about 45%.
- H759 (= H760) binding axial binding residue; mutation to G: Loss of catalytic activity.
- S804 (= S805) binding methylcob(III)alamin
- T808 (= T809) binding methylcob(III)alamin
- S810 (= S811) mutation to A: Decreases activity by about 40%.
- A860 (= A862) binding methylcob(III)alamin
- D946 (= D949) binding S-adenosyl-L-methionine
- R1134 (= R1138) binding S-adenosyl-L-methionine
- YY 1189:1190 (≠ YF 1193:1194) 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)
55% identity, 100% coverage: 4:1229/1232 of query aligns to 15:1263/1265 of Q99707
- R61 (= R50) natural variant: R -> K
- C255 (≠ S245) to Y: in dbSNP:rs1140598
- GSR 382:384 (≠ GSK 370:372) binding (6S)-5,6,7,8-tetrahydrofolate
- D449 (= D437) binding (6S)-5,6,7,8-tetrahydrofolate
- N470 (= N458) binding (6S)-5,6,7,8-tetrahydrofolate
- D537 (= D524) binding (6S)-5,6,7,8-tetrahydrofolate
- N579 (= N566) binding (6S)-5,6,7,8-tetrahydrofolate
- R585 (= R572) binding (6S)-5,6,7,8-tetrahydrofolate
- R591 (= R578) binding (6S)-5,6,7,8-tetrahydrofolate
- D919 (≠ R895) to G: in dbSNP:rs1805087
- D963 (≠ E938) mutation to E: Decreases binding to MTRR; when associated with N-1071.
- K1071 (= K1038) 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)
61% identity, 47% coverage: 654:1229/1232 of query aligns to 4:575/576 of 3ivaA
- active site: D107 (= D758), H109 (= H760), S160 (= S811)
- binding cobalamin: H109 (= H760), G112 (= G763), V116 (= V767), G152 (= G803), L153 (= L804), S154 (= S805), L156 (= L807), I157 (= I808), T158 (= T809), G183 (= G834), G184 (= G835), Q208 (≠ S860), N209 (≠ D861), T303 (≠ S956), D443 (= D1097), A486 (= A1140), G488 (= G1142), Y489 (= Y1143), H495 (= H1149), A520 (= A1174), M521 (= M1175), G524 (≠ T1178), V527 (= V1181), S528 (= S1182)
- binding s-adenosyl-l-homocysteine: E447 (= E1101), R484 (= R1138), P485 (= P1139), Y489 (= Y1143), A491 (= A1145), Y539 (= Y1193)
3bulA E. Coli i690c/g743c meth c-terminal fragment (649-1227) (see paper)
61% identity, 47% coverage: 654:1229/1232 of query aligns to 4:575/577 of 3bulA
- active site: D107 (= D758), H109 (= H760), S160 (= S811)
- binding cobalamin: H109 (= H760), V116 (= V767), G152 (= G803), L153 (= L804), S154 (= S805), L156 (= L807), I157 (= I808), T158 (= T809), G183 (= G834), G184 (= G835), Q208 (≠ S860), N209 (≠ D861), A210 (= A862), T213 (≠ C865), M302 (= M955), D443 (= D1097), A486 (= A1140), P487 (= P1141), G488 (= G1142), Y489 (= Y1143), H495 (= H1149), K498 (= K1152), M521 (= M1175), G524 (≠ T1178), V527 (= V1181), S528 (= S1182)
4cczA Crystal structure of human 5-methyltetrahydrofolate-homocysteine methyltransferase, the homocysteine and folate binding domains
54% identity, 51% coverage: 6:638/1232 of query aligns to 1:611/611 of 4cczA
- binding (6s)-5,6,7,8-tetrahydrofolate: E336 (= E364), G342 (= G370), R344 (≠ K372), N430 (= N458), M458 (= M486), D497 (= D524), G536 (= G563), S538 (= S565), N539 (= N566), F542 (= F569), R545 (= R572), R551 (= R578)
8g3hA Structure of cobalamin-dependent methionine synthase (meth) in a resting state (see paper)
36% identity, 67% coverage: 13:843/1232 of query aligns to 7:806/841 of 8g3hA
- binding cobalamin: Q328 (≠ G353), T330 (≠ D355), S331 (≠ N356), F675 (= F708), V685 (= V718), K693 (= K726), G720 (= G757), V722 (= V759), H723 (= H760), D724 (= D761), I725 (= I762), G726 (= G763), V730 (= V767), M767 (≠ L804), S768 (= S805), L770 (= L807), V772 (≠ T809), I795 (≠ M832), L796 (≠ I833), G797 (= G834), G798 (= G835), A799 (= A836)
Sites not aligning to the query:
3k13C Structure of the pterin-binding domain metr of 5- methyltetrahydrofolate-homocysteine methyltransferase from bacteroides thetaiotaomicron
66% identity, 23% coverage: 359:641/1232 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 (= E364), G15 (= G370), R17 (≠ K372), N103 (= N458), D170 (= D524), G209 (= G563), S211 (= S565), N212 (= N566), R218 (= R572), R224 (= R578), I244 (= I598)
6bdyA Crystal structure of the meth reactivation domain bound to sinefungin (see paper)
55% identity, 27% coverage: 903:1229/1232 of query aligns to 1:325/326 of 6bdyA
1mskA Methionine synthase (activation domain) (see paper)
55% identity, 27% coverage: 903:1229/1232 of query aligns to 1:325/327 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: 654:893/1232 of query aligns to 4:241/246 of 1bmtA
- active site: D107 (= D758), H109 (= H760), S160 (= S811)
- binding co-methylcobalamin: E44 (= E694), M48 (= M698), M51 (= M701), G55 (= G705), L65 (= L715), V68 (= V718), D107 (= D758), V108 (= V759), H109 (= H760), D110 (= D761), I111 (= I762), I115 (= I766), G152 (= G803), L153 (= L804), S154 (= S805), L156 (= L807), I157 (= I808), T158 (= T809), G183 (= G834), G184 (= G835), A185 (= A836), V207 (= V859), N209 (≠ D861), A210 (= A862)
8sseA Methionine synthase, c-terminal fragment, cobalamin and reactivation domains from thermus thermophilus hb8 (see paper)
30% identity, 44% coverage: 658:1196/1232 of query aligns to 1:506/507 of 8sseA
- binding cobalamin: H97 (= H760), G100 (= G763), V104 (= V767), S142 (= S805), L145 (≠ I808), V146 (≠ T809), I169 (≠ M832), G171 (= G834), G172 (= G835), A173 (= A836), H405 (≠ K1093), V409 (≠ D1097), S451 (≠ A1140), F452 (≠ P1141), G453 (= G1142), Y454 (= Y1143), Q463 (≠ K1152), L485 (≠ M1175), E488 (≠ T1178), A490 (= A1180), S492 (= S1182)
1q8jA Cobalamin-dependent methionine synthase (1-566) from thermotoga maritima (cd2+, hcy, methyltetrahydrofolate complex) (see paper)
27% identity, 48% coverage: 10:601/1232 of query aligns to 6:539/559 of 1q8jA
- binding 5-methyl-5,6,7,8-tetrahydrofolic acid: E320 (= E364), D390 (= D437), N411 (= N458), D473 (= D524), G505 (= G563), N508 (= N566), F511 (= F569), R516 (= R578), I536 (= I598)
3bofA Cobalamin-dependent methionine synthase (1-566) from thermotoga maritima complexed with zn2+ and homocysteine (see paper)
27% identity, 48% coverage: 10:601/1232 of query aligns to 6:539/560 of 3bofA
5vooA Methionine synthase folate-binding domain with methyltetrahydrofolate from thermus thermophilus hb8 (see paper)
36% identity, 22% coverage: 358:634/1232 of query aligns to 2:273/282 of 5vooA
- binding 5-methyl-5,6,7,8-tetrahydrofolic acid: E7 (= E364), R8 (= R365), G13 (= G370), S14 (= S371), K15 (= K372), D77 (= D437), N98 (= N458), D165 (= D524), G204 (= G563), N207 (= N566), F210 (= F569), R217 (= R578), I237 (= I598)
2i2xB Crystal structure of methanol:cobalamin methyltransferase complex mtabc from methanosarcina barkeri (see paper)
32% identity, 15% coverage: 657:840/1232 of query aligns to 41:216/258 of 2i2xB
- active site: D134 (= D758), H136 (= H760), T187 (≠ S811)
- binding 5-hydroxybenzimidazolylcob(iii)amide: G133 (= G757), D134 (= D758), V135 (= V759), H136 (= H760), D137 (= D761), I138 (= I762), G139 (= G763), V143 (= V767), T179 (≠ G803), T181 (≠ S805), L183 (= L807), M184 (≠ I808), T185 (= T809), A208 (≠ M832), G210 (= G834), G211 (= G835), G212 (≠ A836)
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)
32% identity, 15% coverage: 657:840/1232 of query aligns to 41:216/258 of Q46EH4
- H129 (≠ A753) mutation to K: Does not affect cobalamin-binding.
- H136 (= H760) 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, 12% coverage: 689:840/1232 of query aligns to 36:188/215 of 7xcnP
- binding 5-hydroxybenzimidazolylcobamide: D104 (= D758), I105 (≠ V759), H106 (= H760), I108 (= I762), G109 (= G763), V113 (= V767), S150 (≠ L804), S151 (= S805), L153 (= L807), M154 (≠ I808), T155 (= T809), M180 (= M832), G182 (= G834), G183 (= G835)
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)
35% identity, 11% coverage: 700:835/1232 of query aligns to 45:174/206 of 4jgiB
- active site: D95 (= D758), H97 (= H760), A148 (≠ S811)
- binding co-methylcobalamin: L63 (≠ V718), D95 (= D758), L96 (≠ V759), H97 (= H760), D98 (= D761), I99 (= I762), G100 (= G763), F104 (≠ V767), G140 (= G803), S142 (= S805), L145 (≠ I808), G173 (= G834), G174 (= G835)
Sites not aligning to the query:
3ezxA Structure of methanosarcina barkeri monomethylamine corrinoid protein
32% identity, 13% coverage: 680:839/1232 of query aligns to 23:185/212 of 3ezxA
- active site: D100 (= D758), H102 (= H760), S155 (= S811)
- binding 5-hydroxybenzimidazolylcobamide: M47 (= M701), F54 (= F708), D100 (= D758), I101 (≠ V759), H102 (= H760), D103 (= D761), I104 (= I762), V109 (= V767), V147 (≠ I802), S149 (= S805), L151 (= L807), M152 (≠ I808), T153 (= T809), M178 (= M832), G180 (= G834), G181 (= G835)
Sites not aligning to the query:
1y80A Structure of a corrinoid (factor iiim)-binding protein from moorella thermoacetica
32% identity, 10% coverage: 748:873/1232 of query aligns to 5:125/125 of 1y80A
- active site: D15 (= D758), H17 (= H760), T68 (≠ S811)
- binding co-5-methoxybenzimidazolylcobamide: D15 (= D758), L16 (≠ V759), H17 (= H760), D18 (= D761), I19 (= I762), G20 (= G763), V24 (= V767), G60 (= G803), M61 (≠ L804), S62 (= S805), L64 (= L807), L65 (≠ I808), T66 (= T809), I91 (≠ M832), G93 (= G834), G94 (= G835), A95 (= A836), P112 (≠ S860), D113 (= D861), A114 (= A862)
Query Sequence
>GFF1835 FitnessBrowser__Marino:GFF1835
MTDRTTRLDQLHKALQERIVILDGGMGTMIQNLKLDEKAFRGDRFADYEREVQGNNDLLN
LTQPALLRNIHADYLDAGADIIETNTFNSTQLSQADYGLEAIARELNVAAAELARQIADE
YTAKNPEKPRFVAGAVGPTSRTASISPDVNNPGYRNVDFQTLVDNYYEAVGGLVEGGCDL
ILIETIFDTLNAKAAIYATQQYFEDSGITLPIMISGTITDASGRTLSGQTTEAFWNSVAH
AKPISVGLNCALGADALRPYVEELSAKAETYVSAHPNAGLPNEFGEYDQTPEEMAEIIEG
FARDGFLNIIGGCCGSRPDHIEAIAQAVSKYPPRKIPERPKALRLSGLEPFTGDDNVLFI
NVGERTNVTGSKRFLRLIKEEQYEEALSVARDQVENGAQIIDINMDEGMLESKEVMVTFL
NLVASEPDISRVPIMIDSSKWDVIEAGLRCIQGKAVVNSISLKEGEEEFVKRARDCMRYG
AAVVVMAFDEQGQADTYERKTEICKRSYDVLTGIGFNPADIIFDPNIFAIATGIEEHNNY
AVDFINATRWIRENLPHASISGGVSNVSFSFRGNDVVREAIHSVFLYHAIKAGMNMGIVN
PGQLVIYDEIDPELKELVEDVVLNRRDDSTDRLLEIAERYKGKGGKTQEEDLAWREWPVE
KRLEHALVKGITTYIVDDTEACRQRATHPIEVIEGPLMDGMNVVGDLFGDGKMFLPQVVK
SARVMKQAVAHLIPYIEAEKTEDQKAKGKILMATVKGDVHDIGKNIVGVVLQCNNYEVID
LGVMVPCDKILAAAKEHDVDLIGLSGLITPSLDEMVHVAREMQRLDFNIPLMIGGATTSK
AHTAVKIEPQYKNDIALYVSDASRCVNVASQLLSKNAKPEFVEAARTEYDEIRERRKNRG
DRTKLVSLKEARDRAPDISFEGYQPPKPAFTGIRVFEEYDLNELVDYIDWTPFFMSWDIS
GKYPAIFDDPKRGEAARHLFDDAQKILHRMIDEKRVSARGVIGFWPANRRGDDVVLYTDE
SCTEELTTLHHLRQQDEKAPGKPMMALSDFVAPEGSGTVDYVGGFAVTTGIGAEEFSVEF
KDANDDYNAIMVKALADRLAEAFAERMHERVRQEFWGYAADEKLANDDLIKERYRGIRPA
PGYPACPDHTEKATLFSLLEATDTAGIELTEHFAMFPTAAVSGWYFAHPESKYFAVGKIG
ADQVEDYAERKGISKAEAERWLAPSLAYDPAE
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