SitesBLAST
Comparing 349708 FitnessBrowser__Btheta:349708 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)
57% identity, 100% coverage: 1:912/915 of query aligns to 1:914/1227 of P13009
- M1 (= M1) modified: Initiator methionine, Removed
- C247 (= C244) binding
- C310 (= C307) binding ; mutation C->A,S: Loss of zinc binding. Loss of catalytic activity.
- C311 (= C308) binding ; mutation C->A,S: Loss of zinc binding. Loss of catalytic activity.
- E694 (= E693) binding
- GDVHD 756:760 (= GDVHD 756:760) binding
- D757 (= D757) mutation to E: Decreases activity by about 70%.; mutation to N: Decreases activity by about 45%.
- H759 (= H759) binding axial binding residue; mutation to G: Loss of catalytic activity.
- S804 (= S804) binding
- T808 (= T808) binding
- S810 (= S810) mutation to A: Decreases activity by about 40%.
- A860 (= A860) binding
Sites not aligning to the query:
- 946 binding
- 1134 binding
- 1189:1190 binding
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, 100% coverage: 1:914/915 of query aligns to 18:942/1265 of Q99707
- R61 (≠ G44) natural variant: R -> K
- C255 (≠ S239) to Y: in dbSNP:rs1140598
- GSR 382:384 (= GSR 364:366) binding
- D449 (= D431) binding
- N470 (= N452) binding
- D537 (= D519) binding
- N579 (= N561) binding
- R585 (= R567) binding
- R591 (= R573) binding
- D919 (≠ K893) to G: in dbSNP:rs1805087
Sites not aligning to the query:
- 963 D→E: Decreases binding to MTRR; when associated with N-1071.
- 1071 K→N: Decreases binding to MTRR; when associated with E-963.
4cczA Crystal structure of human 5-methyltetrahydrofolate-homocysteine methyltransferase, the homocysteine and folate binding domains
54% identity, 69% coverage: 1:633/915 of query aligns to 2:611/611 of 4cczA
- binding (6s)-5,6,7,8-tetrahydrofolate: E336 (= E358), G342 (= G364), R344 (= R366), N430 (= N452), M458 (= M480), D497 (= D519), G536 (= G558), S538 (= S560), N539 (= N561), F542 (= F564), R545 (= R567), R551 (= R573)
3k13C Structure of the pterin-binding domain metr of 5- methyltetrahydrofolate-homocysteine methyltransferase from bacteroides thetaiotaomicron
100% identity, 31% coverage: 350:637/915 of query aligns to 1:287/287 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 (= E358), G15 (= G364), R17 (= R366), N103 (= N452), D170 (= D519), G209 (= G558), S211 (= S560), N212 (= N561), R218 (= R567), R224 (= R573), I244 (= I593)
8g3hA Structure of cobalamin-dependent methionine synthase (meth) in a resting state (see paper)
35% identity, 91% coverage: 9:841/915 of query aligns to 9:805/841 of 8g3hA
- binding cobalamin: Q328 (≠ P349), T330 (≠ I351), S331 (≠ N352), F675 (= F707), V685 (= V717), K693 (= K725), G720 (= G756), V722 (= V758), H723 (= H759), D724 (= D760), I725 (= I761), G726 (= G762), V730 (= V766), M767 (≠ L803), S768 (= S804), L770 (= L806), V772 (≠ T808), I795 (≠ L831), L796 (≠ I832), G797 (= G833), G798 (= G834), A799 (= A835)
Sites not aligning to the query:
3ivaA Structure of the b12-dependent methionine synthase (meth) c-teminal half with adohcy bound (see paper)
55% identity, 29% coverage: 650:912/915 of query aligns to 1:264/576 of 3ivaA
- active site: D107 (= D757), H109 (= H759), S160 (= S810)
- binding cobalamin: H109 (= H759), G112 (= G762), V116 (= V766), G152 (= G802), L153 (= L803), S154 (= S804), L156 (= L806), I157 (= I807), T158 (= T808), G183 (= G833), G184 (= G834), Q208 (≠ K858), N209 (≠ D859)
Sites not aligning to the query:
- binding cobalamin: 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)
55% identity, 29% coverage: 650:912/915 of query aligns to 1:264/577 of 3bulA
- active site: D107 (= D757), H109 (= H759), S160 (= S810)
- binding cobalamin: H109 (= H759), V116 (= V766), G152 (= G802), L153 (= L803), S154 (= S804), L156 (= L806), I157 (= I807), T158 (= T808), G183 (= G833), G184 (= G834), Q208 (≠ K858), N209 (≠ D859), A210 (= A860), T213 (≠ N863)
Sites not aligning to the query:
- binding cobalamin: 302, 443, 486, 487, 488, 489, 495, 498, 521, 524, 527, 528
1bmtA How a protein binds b12: a 3.O angstrom x-ray structure of the b12- binding domains of methionine synthase (see paper)
57% identity, 27% coverage: 650:895/915 of query aligns to 1:245/246 of 1bmtA
- active site: D107 (= D757), H109 (= H759), S160 (= S810)
- binding co-methylcobalamin: E44 (= E693), M48 (= M697), M51 (= M700), G55 (= G704), L65 (= L714), V68 (= V717), D107 (= D757), V108 (= V758), H109 (= H759), D110 (= D760), I111 (= I761), I115 (= I765), G152 (= G802), L153 (= L803), S154 (= S804), L156 (= L806), I157 (= I807), T158 (= T808), G183 (= G833), G184 (= G834), A185 (= A835), V207 (≠ L857), N209 (≠ D859), A210 (= A860)
3bofA Cobalamin-dependent methionine synthase (1-566) from thermotoga maritima complexed with zn2+ and homocysteine (see paper)
29% identity, 65% coverage: 2:596/915 of query aligns to 4:539/560 of 3bofA
1q8jA Cobalamin-dependent methionine synthase (1-566) from thermotoga maritima (cd2+, hcy, methyltetrahydrofolate complex) (see paper)
29% identity, 65% coverage: 2:596/915 of query aligns to 4:539/559 of 1q8jA
- binding 5-methyl-5,6,7,8-tetrahydrofolic acid: E320 (= E358), D390 (= D431), N411 (= N452), D473 (= D519), G505 (= G558), N508 (= N561), F511 (= F564), R516 (≠ N569), I536 (= I593)
5vooA Methionine synthase folate-binding domain with methyltetrahydrofolate from thermus thermophilus hb8 (see paper)
34% identity, 30% coverage: 356:629/915 of query aligns to 5:273/282 of 5vooA
- binding 5-methyl-5,6,7,8-tetrahydrofolic acid: E7 (= E358), R8 (= R359), G13 (= G364), S14 (= S365), K15 (≠ R366), D77 (= D431), N98 (= N452), D165 (= D519), G204 (= G558), N207 (= N561), F210 (= F564), R217 (= R573), I237 (= I593)
8sseA Methionine synthase, c-terminal fragment, cobalamin and reactivation domains from thermus thermophilus hb8
44% identity, 21% coverage: 660:852/915 of query aligns to 4:193/507 of 8sseA
Sites not aligning to the query:
- binding cobalamin: 405, 409, 451, 452, 453, 454, 463, 485, 488, 490, 492
7xcnP Crystal structure of the mttb-mttc complex at 2.7 a resolution (see paper)
35% identity, 18% coverage: 672:839/915 of query aligns to 19:188/215 of 7xcnP
- binding 5-hydroxybenzimidazolylcobamide: D104 (= D757), I105 (≠ V758), H106 (= H759), I108 (= I761), G109 (= G762), V113 (= V766), S150 (≠ L803), S151 (= S804), L153 (= L806), M154 (≠ I807), T155 (= T808), M180 (≠ L831), G182 (= G833), G183 (= G834)
Sites not aligning to the query:
2i2xB Crystal structure of methanol:cobalamin methyltransferase complex mtabc from methanosarcina barkeri (see paper)
33% identity, 21% coverage: 645:839/915 of query aligns to 22:216/258 of 2i2xB
- active site: D134 (= D757), H136 (= H759), T187 (≠ S810)
- binding 5-hydroxybenzimidazolylcob(iii)amide: G133 (= G756), D134 (= D757), V135 (= V758), H136 (= H759), D137 (= D760), I138 (= I761), G139 (= G762), V143 (= V766), T179 (≠ G802), T181 (≠ S804), L183 (= L806), M184 (≠ I807), T185 (= T808), A208 (≠ L831), G210 (= G833), G211 (= G834), G212 (≠ A835)
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)
33% identity, 21% coverage: 645:839/915 of query aligns to 22:216/258 of Q46EH4
- H129 (≠ A752) mutation to K: Does not affect cobalamin-binding.
- H136 (= H759) 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)
36% identity, 15% coverage: 699:834/915 of query aligns to 45:174/206 of 4jgiB
- active site: D95 (= D757), H97 (= H759), A148 (≠ S810)
- binding co-methylcobalamin: L63 (≠ V717), D95 (= D757), L96 (≠ V758), H97 (= H759), D98 (= D760), I99 (= I761), G100 (= G762), F104 (≠ V766), G140 (= G802), S142 (= S804), L145 (≠ I807), G173 (= G833), G174 (= G834)
Sites not aligning to the query:
3ezxA Structure of methanosarcina barkeri monomethylamine corrinoid protein
37% identity, 17% coverage: 680:838/915 of query aligns to 27:185/212 of 3ezxA
- active site: D100 (= D757), H102 (= H759), S155 (= S810)
- binding 5-hydroxybenzimidazolylcobamide: M47 (= M700), F54 (= F707), D100 (= D757), I101 (≠ V758), H102 (= H759), D103 (= D760), I104 (= I761), V109 (= V766), V147 (≠ I801), S149 (= S804), L151 (= L806), M152 (≠ I807), T153 (= T808), M178 (≠ L831), G180 (= G833), G181 (= G834)
Sites not aligning to the query:
1y80A Structure of a corrinoid (factor iiim)-binding protein from moorella thermoacetica
37% identity, 10% coverage: 745:839/915 of query aligns to 3:99/125 of 1y80A
- active site: D15 (= D757), H17 (= H759), T68 (≠ S810)
- binding co-5-methoxybenzimidazolylcobamide: D15 (= D757), L16 (≠ V758), H17 (= H759), D18 (= D760), I19 (= I761), G20 (= G762), V24 (= V766), G60 (= G802), M61 (≠ L803), S62 (= S804), L64 (= L806), L65 (≠ I807), T66 (= T808), I91 (≠ L831), G93 (= G833), G94 (= G834), A95 (= A835)
Sites not aligning to the query:
O09171 Betaine--homocysteine S-methyltransferase 1; EC 2.1.1.5 from Rattus norvegicus (Rat) (see 2 papers)
25% identity, 36% coverage: 58:382/915 of query aligns to 53:368/407 of O09171
- T73 (= T78) mutation to G: Decreases the catalytic efficiency.
- F74 (≠ N79) mutation to A: Decreases the catalytic efficiency. Decreases the affinity for glycine betaine.
- Y77 (≠ S82) mutation to A: Decreases the catalytic efficiency.
- A119 (= A127) mutation to G: Decreases the catalytic efficiency.
- E159 (≠ T179) mutation E->G,K: Loss of catalytic activity.
- T184 (≠ S209) mutation to G: Decreases the catalytic efficiency.
- C186 (≠ T211) mutation C->A,S: Decreases the catalytic efficiency. Increases the affinity for L-homocysteine.
Sites not aligning to the query:
- 7 K→A: Has no effect on tetramer assembly or catalytic efficiency.
- 8 K→A: Has no effect on tetramer assembly. Decreases the catalytic efficiency.
- 10 K→A: Has no effect on tetramer assembly. Decreases the catalytic efficiency. Alters nucleocytoplasmic distribution.
- 11 R→A: Has no effect on tetramer assembly.
- 21 mutation E->A,K: Decreases the catalytic efficiency. Increases the affinity for L-homocysteine.
- 26 mutation D->A,I: Decreases the catalytic efficiency. Decreases the affinity for glycine betaine.
2yckX Methyltransferase bound with tetrahydrofolate (see paper)
28% identity, 26% coverage: 353:594/915 of query aligns to 11:238/272 of 2yckX
- binding (6s)-5,6,7,8-tetrahydrofolate: M21 (≠ S365), F22 (≠ R366), D85 (= D431), N106 (= N452), D170 (= D519), G206 (= G558), N209 (= N561), Q212 (≠ F564), K213 (≠ S565), R217 (= R573), I237 (= I593)
Query Sequence
>349708 FitnessBrowser__Btheta:349708
MKKTISQIVSERILILDGAMGTMIQQYNLKEEDFRGERFAHIPGQLKGNNDLLCLTRPDV
IQDIHRKYLEAGADIIETNTFSSTTVSMADYHVEEYVREINLAATRLARELADEYTAKSP
DKPRFVAGSVGPTNKTCSMSPDVNNPAFRALSYDELAASYQQQMEAMLEGGVDAILIETI
FDTLNAKAAIFAAGQAMKVTGIEVPVMLSVTVSDIGGRTLSGQTLEAFLASVQHANIFSV
GLNCSFGARQLKPFLEQLASRAPYYISAYPNAGLPNSLGKYDQTPADMAHEVKEYIQEGL
VNIIGGCCGTTDAYIAEYQTLIAGAKPHVPAPKPDCMWLSGLELLEVKPEINFVNIGERC
NVAGSRKFLRLVNEKKYDEALSIARQQVEDGALVIDVNMDDGLLDARTEMTTFLNLIMSE
PEIARVPVMIDSSKWEVIEAGLKCLQGKSIVNSISLKEGEEVFLEHARIIKQYGAATVVM
AFDEKGQADTAARKIEVCERAYRLLVDKVGFNPHDIIFDPNVLAVATGIEEHNNYAVDFI
EATGWIRKNLPGAHVSGGVSNLSFSFRGNNYIREAMHAVFLYHAIQQGMDMGIVNPGTSV
LYSDIPADTLEKIEDVVLNRRPDAAERLIELAEALKETMGGTSGQAAVKQDAWREESVQE
RLKYALMKGIGDYLEQDLAEALPLYDKAVDVIEGPLMDGMNYVGELFGAGKMFLPQVVKT
ARTMKKAVAILQPIIESEKVEGSSSAGKVLLATVKGDVHDIGKNIVAVVMACNGYDIVDL
GVMVPAETIVQRAIEEKVDMIGLSGLITPSLEEMTHVAAELEKAGLDIPLLIGGATTSKM
HTALKIAPVYHAPVVHLKDASQNASVASRLLNSQMKAELINELDAEYQALREKSGLLRRE
TVSLEEAQKNKLNLF
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