SitesBLAST
Comparing 18047 FitnessBrowser__Keio:18047 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)
100% identity, 100% coverage: 1:1227/1227 of query aligns to 1:1227/1227 of P13009
- M1 (= M1) modified: Initiator methionine, Removed
- C247 (= C247) binding Zn(2+)
- C310 (= C310) binding Zn(2+); mutation C->A,S: Loss of zinc binding. Loss of catalytic activity.
- C311 (= C311) 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 756:760) binding methylcob(III)alamin
- 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 methylcob(III)alamin
- T808 (= T808) binding methylcob(III)alamin
- S810 (= S810) mutation to A: Decreases activity by about 40%.
- A860 (= A860) binding methylcob(III)alamin
- D946 (= D946) binding S-adenosyl-L-methionine
- R1134 (= R1134) binding S-adenosyl-L-methionine
- YY 1189:1190 (= YY 1189:1190) binding S-adenosyl-L-methionine
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: 6:1227/1227 of query aligns to 20:1265/1265 of Q99707
- R61 (≠ C47) natural variant: R -> K
- C255 (≠ T242) to Y: in dbSNP:rs1140598
- GSR 382:384 (≠ GSA 367:369) binding (6S)-5,6,7,8-tetrahydrofolate
- D449 (= D434) binding (6S)-5,6,7,8-tetrahydrofolate
- N470 (= N455) binding (6S)-5,6,7,8-tetrahydrofolate
- D537 (= D522) binding (6S)-5,6,7,8-tetrahydrofolate
- N579 (= N564) binding (6S)-5,6,7,8-tetrahydrofolate
- R585 (= R570) binding (6S)-5,6,7,8-tetrahydrofolate
- R591 (= R576) binding (6S)-5,6,7,8-tetrahydrofolate
- D919 (≠ Q893) to G: in dbSNP:rs1805087
- D963 (vs. gap) mutation to E: Decreases binding to MTRR; when associated with N-1071.
- K1071 (= K1035) mutation to N: Decreases binding to MTRR; when associated with E-963.
3bulA E. Coli i690c/g743c meth c-terminal fragment (649-1227) (see paper)
100% identity, 47% coverage: 651:1227/1227 of query aligns to 1:577/577 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 (= Q858), N209 (= N859), A210 (= A860), T213 (= T863), M302 (= M952), D443 (= D1093), A486 (= A1136), P487 (= P1137), G488 (= G1138), Y489 (= Y1139), H495 (= H1145), K498 (= K1148), M521 (= M1171), G524 (= G1174), V527 (= V1177), S528 (= S1178)
3ivaA Structure of the b12-dependent methionine synthase (meth) c-teminal half with adohcy bound (see paper)
100% identity, 47% coverage: 651:1226/1227 of query aligns to 1:576/576 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 (= Q858), N209 (= N859), T303 (= T953), D443 (= D1093), A486 (= A1136), G488 (= G1138), Y489 (= Y1139), H495 (= H1145), A520 (= A1170), M521 (= M1171), G524 (= G1174), V527 (= V1177), S528 (= S1178)
- binding s-adenosyl-l-homocysteine: E447 (= E1097), R484 (= R1134), P485 (= P1135), Y489 (= Y1139), A491 (= A1141), Y539 (= Y1189)
1mskA Methionine synthase (activation domain) (see paper)
100% identity, 27% coverage: 901:1227/1227 of query aligns to 1:327/327 of 1mskA
6bdyA Crystal structure of the meth reactivation domain bound to sinefungin (see paper)
100% identity, 27% coverage: 901:1226/1227 of query aligns to 1:326/326 of 6bdyA
4cczA Crystal structure of human 5-methyltetrahydrofolate-homocysteine methyltransferase, the homocysteine and folate binding domains
54% identity, 51% coverage: 6:636/1227 of query aligns to 4:611/611 of 4cczA
- binding (6s)-5,6,7,8-tetrahydrofolate: E336 (= E361), G342 (= G367), R344 (≠ A369), N430 (= N455), M458 (= M483), D497 (= D522), G536 (= G561), S538 (= S563), N539 (= N564), F542 (= F567), R545 (= R570), R551 (= R576)
1bmtA How a protein binds b12: a 3.O angstrom x-ray structure of the b12- binding domains of methionine synthase (see paper)
100% identity, 20% coverage: 651:896/1227 of query aligns to 1:246/246 of 1bmtA
- active site: D107 (= D757), H109 (= H759), S160 (= S810)
- binding co-methylcobalamin: E44 (= E694), M48 (= M698), M51 (= M701), G55 (= G705), L65 (= L715), V68 (= V718), 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 (= V857), N209 (= N859), A210 (= A860)
8g3hA Structure of cobalamin-dependent methionine synthase (meth) in a resting state (see paper)
36% identity, 68% coverage: 8:842/1227 of query aligns to 6:806/841 of 8g3hA
- binding cobalamin: Q328 (≠ E352), T330 (≠ S354), S331 (≠ L355), F675 (= F708), V685 (= V718), K693 (= K726), 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:
3k13C Structure of the pterin-binding domain metr of 5- methyltetrahydrofolate-homocysteine methyltransferase from bacteroides thetaiotaomicron
67% identity, 23% coverage: 356:639/1227 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 (= E361), G15 (= G367), R17 (≠ A369), N103 (= N455), D170 (= D522), G209 (= G561), S211 (= S563), N212 (= N564), R218 (= R570), R224 (= R576), I244 (= I596)
8sseA Methionine synthase, c-terminal fragment, cobalamin and reactivation domains from thermus thermophilus hb8 (see paper)
31% identity, 43% coverage: 661:1192/1227 of query aligns to 4:506/507 of 8sseA
- binding cobalamin: H97 (= H759), G100 (= G762), V104 (= V766), S142 (= S804), L145 (≠ I807), V146 (≠ T808), I169 (≠ L831), G171 (= G833), G172 (= G834), A173 (= A835), H405 (≠ K1089), V409 (≠ D1093), S451 (≠ A1136), F452 (≠ P1137), G453 (= G1138), Y454 (= Y1139), Q463 (≠ K1148), L485 (≠ M1171), E488 (≠ G1174), A490 (≠ S1176), S492 (= S1178)
1q8jA Cobalamin-dependent methionine synthase (1-566) from thermotoga maritima (cd2+, hcy, methyltetrahydrofolate complex) (see paper)
28% identity, 50% coverage: 12:625/1227 of query aligns to 11:559/559 of 1q8jA
- binding 5-methyl-5,6,7,8-tetrahydrofolic acid: E320 (= E361), D390 (= D434), N411 (= N455), D473 (= D522), G505 (= G561), N508 (= N564), F511 (= F567), R516 (= R576), I536 (= I596)
3bofA Cobalamin-dependent methionine synthase (1-566) from thermotoga maritima complexed with zn2+ and homocysteine (see paper)
28% identity, 50% coverage: 12:625/1227 of query aligns to 11:559/560 of 3bofA
5vooA Methionine synthase folate-binding domain with methyltetrahydrofolate from thermus thermophilus hb8 (see paper)
36% identity, 23% coverage: 354:632/1227 of query aligns to 1:273/282 of 5vooA
- binding 5-methyl-5,6,7,8-tetrahydrofolic acid: E7 (= E361), R8 (= R362), G13 (= G367), S14 (= S368), K15 (≠ A369), D77 (= D434), N98 (= N455), D165 (= D522), G204 (= G561), N207 (= N564), F210 (= F567), R217 (= R576), I237 (= I596)
7xcnP Crystal structure of the mttb-mttc complex at 2.7 a resolution (see paper)
31% identity, 16% coverage: 673:872/1227 of query aligns to 20:215/215 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), G200 (≠ V857), S202 (≠ N859), A203 (= A860)
2i2xB Crystal structure of methanol:cobalamin methyltransferase complex mtabc from methanosarcina barkeri (see paper)
37% identity, 15% coverage: 662:839/1227 of query aligns to 38:216/258 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)
37% identity, 15% coverage: 662:839/1227 of query aligns to 38:216/258 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)
35% identity, 11% coverage: 700:834/1227 of query aligns to 45:174/206 of 4jgiB
- active site: D95 (= D757), H97 (= H759), A148 (≠ S810)
- binding co-methylcobalamin: L63 (≠ V718), 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
32% identity, 13% coverage: 680:838/1227 of query aligns to 26:185/212 of 3ezxA
- active site: D100 (= D757), H102 (= H759), S155 (= S810)
- binding 5-hydroxybenzimidazolylcobamide: M47 (= M701), F54 (= F708), D100 (= D757), I101 (≠ V758), H102 (= H759), D103 (= D760), I104 (= I761), V109 (= V766), V147 (≠ S804), S149 (vs. gap), L151 (= L806), M152 (≠ I807), T153 (= T808), M178 (≠ L831), G180 (= G833), G181 (= G834)
Sites not aligning to the query:
5dmmA Crystal structure of the homocysteine methyltransferase mmum from escherichia coli, metallated form (see paper)
24% identity, 26% coverage: 8:321/1227 of query aligns to 3:284/288 of 5dmmA
Query Sequence
>18047 FitnessBrowser__Keio:18047
MSSKVEQLRAQLNERILVLDGGMGTMIQSYRLNEADFRGERFADWPCDLKGNNDLLVLSK
PEVIAAIHNAYFEAGADIIETNTFNSTTIAMADYQMESLSAEINFAAAKLARACADEWTA
RTPEKPRYVAGVLGPTNRTASISPDVNDPAFRNITFDGLVAAYRESTKALVEGGADLILI
ETVFDTLNAKAAVFAVKTEFEALGVELPIMISGTITDASGRTLSGQTTEAFYNSLRHAEA
LTFGLNCALGPDELRQYVQELSRIAECYVTAHPNAGLPNAFGEYDLDADTMAKQIREWAQ
AGFLNIVGGCCGTTPQHIAAMSRAVEGLAPRKLPEIPVACRLSGLEPLNIGEDSLFVNVG
ERTNVTGSAKFKRLIKEEKYSEALDVARQQVENGAQIIDINMDEGMLDAEAAMVRFLNLI
AGEPDIARVPIMIDSSKWDVIEKGLKCIQGKGIVNSISMKEGVDAFIHHAKLLRRYGAAV
VVMAFDEQGQADTRARKIEICRRAYKILTEEVGFPPEDIIFDPNIFAVATGIEEHNNYAQ
DFIGACEDIKRELPHALISGGVSNVSFSFRGNDPVREAIHAVFLYYAIRNGMDMGIVNAG
QLAIYDDLPAELRDAVEDVILNRRDDGTERLLELAEKYRGSKTDDTANAQQAEWRSWEVN
KRLEYSLVKGITEFIEQDTEEARQQATRPIEVIEGPLMDGMNVVGDLFGEGKMFLPQVVK
SARVMKQAVAYLEPFIEASKEQGKTNGKMVIATVKGDVHDIGKNIVGVVLQCNNYEIVDL
GVMVPAEKILRTAKEVNADLIGLSGLITPSLDEMVNVAKEMERQGFTIPLLIGGATTSKA
HTAVKIEQNYSGPTVYVQNASRTVGVVAALLSDTQRDDFVARTRKEYETVRIQHGRKKPR
TPPVTLEAARDNDFAFDWQAYTPPVAHRLGVQEVEASIETLRNYIDWTPFFMTWSLAGKY
PRILEDEVVGVEAQRLFKDANDMLDKLSAEKTLNPRGVVGLFPANRVGDDIEIYRDETRT
HVINVSHHLRQQTEKTGFANYCLADFVAPKLSGKADYIGAFAVTGGLEEDALADAFEAQH
DDYNKIMVKALADRLAEAFAEYLHERVRKVYWGYAPNENLSNEELIRENYQGIRPAPGYP
ACPEHTEKATIWELLEVEKHTGMKLTESFAMWPGASVSGWYFSHPDSKYYAVAQIQRDQV
EDYARRKGMSVTEVERWLAPNLGYDAD
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