SitesBLAST
Comparing 2629598296 IMG__TrieryIMS101_FD:2629598296 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)
8g3hA Structure of cobalamin-dependent methionine synthase (meth) in a resting state (see paper)
49% identity, 71% coverage: 19:882/1224 of query aligns to 6:839/841 of 8g3hA
- binding cobalamin: Q328 (= Q358), T330 (≠ N360), S331 (= S361), F675 (= F711), V685 (= V721), K693 (= K729), G720 (= G761), V722 (= V763), H723 (= H764), D724 (= D765), I725 (= I766), G726 (= G767), V730 (= V771), M767 (= M808), S768 (= S809), L770 (= L811), V772 (= V813), I795 (= I836), L796 (= L837), G797 (= G838), G798 (= G839), A799 (= A840), Y818 (= Y861), A819 (≠ G862), E820 (≠ K863), D821 (= D864)
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)
31% identity, 99% coverage: 18:1223/1224 of query aligns to 9:1191/1227 of P13009
- C247 (= C238) binding Zn(2+)
- C310 (= C304) binding Zn(2+); mutation C->A,S: Loss of zinc binding. Loss of catalytic activity.
- C311 (= C305) binding Zn(2+); mutation C->A,S: Loss of zinc binding. Loss of catalytic activity.
- E694 (≠ N697) binding methylcob(III)alamin
- GDVHD 756:760 (= GDVHD 761:765) binding methylcob(III)alamin
- D757 (= D762) mutation to E: Decreases activity by about 70%.; mutation to N: Decreases activity by about 45%.
- H759 (= H764) binding axial binding residue; mutation to G: Loss of catalytic activity.
- S804 (= S809) binding methylcob(III)alamin
- T808 (≠ V813) binding methylcob(III)alamin
- S810 (= S815) mutation to A: Decreases activity by about 40%.
- A860 (= A865) binding methylcob(III)alamin
- D946 (= D976) binding S-adenosyl-L-methionine
- R1134 (= R1167) binding S-adenosyl-L-methionine
- YY 1189:1190 (≠ YF 1221:1222) 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)
31% identity, 98% coverage: 24:1223/1224 of query aligns to 28:1229/1265 of Q99707
- R61 (vs. gap) natural variant: R -> K
- C255 (≠ D232) to Y: in dbSNP:rs1140598
- GSR 382:384 (≠ GSK 373:375) 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 (≠ S572) binding (6S)-5,6,7,8-tetrahydrofolate
- R591 (= R576) binding (6S)-5,6,7,8-tetrahydrofolate
- D919 (≠ R900) to G: in dbSNP:rs1805087
- D963 (= D965) mutation to E: Decreases binding to MTRR; when associated with N-1071.
- K1071 (≠ R1073) mutation to N: Decreases binding to MTRR; when associated with E-963.
8sseA Methionine synthase, c-terminal fragment, cobalamin and reactivation domains from thermus thermophilus hb8 (see paper)
41% identity, 46% coverage: 661:1223/1224 of query aligns to 1:505/507 of 8sseA
- binding cobalamin: H97 (= H764), G100 (= G767), V104 (= V771), S142 (= S809), L145 (= L812), V146 (= V813), I169 (= I836), G171 (= G838), G172 (= G839), A173 (= A840), H405 (= H1123), V409 (= V1127), S451 (= S1169), F452 (= F1170), G453 (= G1171), Y454 (= Y1172), Q463 (= Q1181), L485 (= L1203), E488 (= E1206), A490 (≠ T1208), S492 (≠ T1210)
4cczA Crystal structure of human 5-methyltetrahydrofolate-homocysteine methyltransferase, the homocysteine and folate binding domains
34% identity, 49% coverage: 24:622/1224 of query aligns to 12:597/611 of 4cczA
- binding (6s)-5,6,7,8-tetrahydrofolate: E336 (= E367), G342 (= G373), R344 (≠ K375), N430 (= N458), M458 (≠ G486), D497 (= D524), G536 (= G563), S538 (= S565), N539 (= N566), F542 (= F569), R545 (≠ S572), R551 (= R576)
5vooA Methionine synthase folate-binding domain with methyltetrahydrofolate from thermus thermophilus hb8 (see paper)
49% identity, 23% coverage: 361:643/1224 of query aligns to 1:279/282 of 5vooA
- binding 5-methyl-5,6,7,8-tetrahydrofolic acid: E7 (= E367), R8 (= R368), G13 (= G373), S14 (= S374), K15 (= K375), D77 (= D437), N98 (= N458), D165 (= D524), G204 (= G563), N207 (= N566), F210 (= F569), R217 (= R576), I237 (= I596)
3ivaA Structure of the b12-dependent methionine synthase (meth) c-teminal half with adohcy bound (see paper)
29% identity, 46% coverage: 662:1223/1224 of query aligns to 9:541/576 of 3ivaA
- active site: D107 (= D762), H109 (= H764), S160 (= S815)
- binding cobalamin: H109 (= H764), G112 (= G767), V116 (= V771), G152 (≠ A807), L153 (≠ M808), S154 (= S809), L156 (= L811), I157 (≠ L812), T158 (≠ V813), G183 (= G838), G184 (= G839), Q208 (≠ K863), N209 (≠ D864), T303 (≠ Q984), D443 (≠ V1127), A486 (≠ S1169), G488 (= G1171), Y489 (= Y1172), H495 (≠ V1178), A520 (≠ Q1202), M521 (≠ L1203), G524 (≠ E1206), V527 (≠ T1209), S528 (≠ T1210)
- binding s-adenosyl-l-homocysteine: E447 (= E1131), R484 (= R1167), P485 (≠ Y1168), Y489 (= Y1172), A491 (= A1174), Y539 (= Y1221)
3bulA E. Coli i690c/g743c meth c-terminal fragment (649-1227) (see paper)
29% identity, 46% coverage: 662:1223/1224 of query aligns to 9:541/577 of 3bulA
- active site: D107 (= D762), H109 (= H764), S160 (= S815)
- binding cobalamin: H109 (= H764), V116 (= V771), G152 (≠ A807), L153 (≠ M808), S154 (= S809), L156 (= L811), I157 (≠ L812), T158 (≠ V813), G183 (= G838), G184 (= G839), Q208 (≠ K863), N209 (≠ D864), A210 (= A865), T213 (≠ D868), M302 (≠ A982), D443 (≠ V1127), A486 (≠ S1169), P487 (≠ F1170), G488 (= G1171), Y489 (= Y1172), H495 (≠ V1178), K498 (≠ Q1181), M521 (≠ L1203), G524 (≠ E1206), V527 (≠ T1209), S528 (≠ T1210)
1q8jA Cobalamin-dependent methionine synthase (1-566) from thermotoga maritima (cd2+, hcy, methyltetrahydrofolate complex) (see paper)
29% identity, 47% coverage: 26:598/1224 of query aligns to 15:538/559 of 1q8jA
- binding 5-methyl-5,6,7,8-tetrahydrofolic acid: E320 (= E367), D390 (= D437), N411 (= N458), D473 (= D524), G505 (= G563), N508 (= N566), F511 (= F569), R516 (= R576), I536 (= I596)
3bofA Cobalamin-dependent methionine synthase (1-566) from thermotoga maritima complexed with zn2+ and homocysteine (see paper)
29% identity, 47% coverage: 26:598/1224 of query aligns to 15:538/560 of 3bofA
3k13C Structure of the pterin-binding domain metr of 5- methyltetrahydrofolate-homocysteine methyltransferase from bacteroides thetaiotaomicron
39% identity, 20% coverage: 361:603/1224 of query aligns to 3:251/287 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 (= E367), G15 (= G373), R17 (≠ K375), N103 (= N458), D170 (= D524), G209 (= G563), S211 (= S565), N212 (= N566), R218 (vs. gap), R224 (= R576), I244 (= I596)
1bmtA How a protein binds b12: a 3.O angstrom x-ray structure of the b12- binding domains of methionine synthase (see paper)
34% identity, 18% coverage: 662:885/1224 of query aligns to 9:230/246 of 1bmtA
- active site: D107 (= D762), H109 (= H764), S160 (= S815)
- binding co-methylcobalamin: E44 (≠ N697), M48 (≠ L701), M51 (= M704), G55 (= G708), L65 (= L718), V68 (= V721), D107 (= D762), V108 (= V763), H109 (= H764), D110 (= D765), I111 (= I766), I115 (≠ L770), G152 (≠ A807), L153 (≠ M808), S154 (= S809), L156 (= L811), I157 (≠ L812), T158 (≠ V813), G183 (= G838), G184 (= G839), A185 (= A840), V207 (≠ G862), N209 (≠ D864), A210 (= A865)
2ycjA Methyltransferase bound with methyltetrahydrofolate (see paper)
31% identity, 21% coverage: 362:618/1224 of query aligns to 10:262/271 of 2ycjA
- binding 5-methyl-5,6,7,8-tetrahydrofolic acid: M20 (≠ S372), F21 (≠ G373), D84 (= D437), N105 (= N458), D169 (= D524), G205 (= G563), N208 (= N566), Q211 (≠ F569), R216 (= R576), I236 (= I596)
2yciX Methyltransferase native (see paper)
31% identity, 21% coverage: 362:618/1224 of query aligns to 10:262/271 of 2yciX
2yckX Methyltransferase bound with tetrahydrofolate (see paper)
31% identity, 21% coverage: 362:618/1224 of query aligns to 11:263/272 of 2yckX
- binding (6s)-5,6,7,8-tetrahydrofolate: M21 (≠ S372), F22 (≠ G373), D85 (= D437), N106 (= N458), D170 (= D524), G206 (= G563), N209 (= N566), Q212 (≠ F569), K213 (≠ G570), R217 (= R576), I237 (= I596)
4djfA Crystal structure of folate-bound corrinoid iron-sulfur protein (cfesp) in complex with its methyltransferase (metr), co-crystallized with folate and ti(iii) citrate reductant (see paper)
31% identity, 19% coverage: 362:599/1224 of query aligns to 1:230/262 of 4djfA
- binding 5-methyl-5,6,7,8-tetrahydrofolic acid: E6 (= E367), M11 (≠ S372), F12 (≠ G373), D75 (= D437), N96 (= N458), D160 (= D524), S198 (= S565), N199 (= N566), R207 (= R576)
- binding calcium ion: G222 (= G591), D224 (= D593)
- binding co-methylcobalamin: V168 (≠ T532), Q202 (≠ F569), N203 (≠ G570)
4djeA Crystal structure of folate-bound corrinoid iron-sulfur protein (cfesp) in complex with its methyltransferase (metr), co-crystallized with folate (see paper)
31% identity, 19% coverage: 362:599/1224 of query aligns to 1:230/262 of 4djeA
- binding cobalamin: V168 (≠ T532), N203 (≠ G570)
- binding 5-methyl-5,6,7,8-tetrahydrofolic acid: E6 (= E367), M11 (≠ S372), F12 (≠ G373), D75 (= D437), N96 (= N458), D160 (= D524), G196 (= G563), S198 (= S565), N199 (= N566), R207 (= R576)
- binding calcium ion: G222 (= G591), D224 (= D593)
4djdA Crystal structure of folate-free corrinoid iron-sulfur protein (cfesp) in complex with its methyltransferase (metr) (see paper)
31% identity, 19% coverage: 362:599/1224 of query aligns to 1:230/262 of 4djdA
2e7fA 5-methyltetrahydrofolate corrinoid/iron sulfur protein methyltransferase complexed with methyltetrahydrofolate to 2.2 angsrom resolution (see paper)
31% identity, 19% coverage: 362:599/1224 of query aligns to 1:230/262 of 2e7fA
- binding 5-methyl-5,6,7,8-tetrahydrofolic acid: E6 (= E367), M11 (≠ S372), F12 (≠ G373), D75 (= D437), N96 (= N458), D160 (= D524), G196 (= G563), S198 (= S565), N199 (= N566), Q202 (≠ F569), R207 (= R576), I227 (= I596)
- binding calcium ion: G222 (= G591), D224 (= D593)
Q46389 5-methyltetrahydrofolate:corrinoid/iron-sulfur protein co-methyltransferase; 5-methyltetrahydrofolate corrinoid/iron sulfur protein methyltransferase; MeTr; EC 2.1.1.258 from Moorella thermoacetica (Clostridium thermoaceticum) (see 2 papers)
31% identity, 19% coverage: 362:599/1224 of query aligns to 1:230/262 of Q46389
- N96 (= N458) binding (6S)-5-methyl-5,6,7,8-tetrahydrofolate
- D160 (= D524) binding (6S)-5-methyl-5,6,7,8-tetrahydrofolate
- K184 (≠ R549) binding Ca(2+)
- N199 (= N566) binding (6S)-5-methyl-5,6,7,8-tetrahydrofolate; mutation to A: 20-fold decreased affinity for methyltetrahydrofolate and nearly abolished catalytic activity.
- Q202 (≠ F569) binding (6S)-5-methyl-5,6,7,8-tetrahydrofolate
- R207 (= R576) binding (6S)-5-methyl-5,6,7,8-tetrahydrofolate
- G222 (= G591) binding Ca(2+); binding Ca(2+)
- D224 (= D593) binding Ca(2+); binding Ca(2+)
Query Sequence
>2629598296 IMG__TrieryIMS101_FD:2629598296
MLSVEIPKPQLKTSFLQRLQSPDRPVLIFDGAMGTNIQSQNLTAEDFGGAEYEGCNEYLV
VTKPEAVAKVHRDFLAAGADVVETDSFGSSPLVLAEYNLADRAYELSRKAAELARSCADE
FTSPEKPRFVAGSIGPGTKLPTLGHITYDELKASFMVQAEGLYDGGADLFIVETCQDVLQ
IKAALSAFEAVFAKKGSRLPLMVSVTMEIQGTMLVGTDISGVLAILEPFPIDILGLNCAT
GPNLMTSHIKYLSENSPFPISCIPNAGLPENIGGQAHYKMTPLEFKTSMSEFIGQYGVQI
VGGCCGTRPAHIQALADAVEETPLKERSVRKNAVGKVRTPLSYTPAAASIYSAQTYEQDN
SFLIVGERLNASGSKKVRKLLNEDDWDGLLAIAKSQVKEGAHMLDVNVDYVGRDGERDMR
ELVSRLVTNTTLPLMLDSTEWTKMEAGLKVAGGKCLLNSTNYEDGEERFFKVLELAKEYG
AGVVIGCIDEEGMARTAKKKFEIAQRAYKDALKFGIPPHEIFYDTLALPISTGIEEDREN
AKATIESIRLIRENLPGVHFMLGVSNISFGLSPATRITLNSIFLNEAMKAGMDGAIVSAA
KILPLSKIDEEHQQICCDLIYDNRKFEGDICTYDPLTKLTEIFAGVSAKDARSGPSLADL
PIDQRLKQHIIDGERIGLEDALKVALDAGHKALEIINTFLLDGMKVVGELFGSGQMQLPF
VLQSAETMKSAVAFLEPYMEKIEGEDEDRGKGKFLIATVKGDVHDIGKNLVDIILTNNGY
KVINLGIKQAIEAIVEAYEQHKPDCIAMSGLLVKSTAFMKENLAAFNAKGITVPVILGGA
ALTPKFVYGDCQDTYQGQVIYGKDAFADLTFMDRLMPAKDKDCWVDTEGFTGEFAQFNQR
GRKAIKDLERELNGDGEKSDGEVNGNGKKPNKPTVIDTKRSTDVAIDIERPAPPFWGTKI
LQSGDLKLEELFWYMDLQALFAGQWQFRKPKGQPREEYDWFLASKVYPILEEWKQKVRTE
QWLEPTLVYGYFPCAAIGNSVHVYDPSVIEQGLTPTTATPFVTWTFPRQKSMRRLCIADF
IRPLEHDQFDVLPMQAVTMGEIATQKAQELYQGNEYTNYLYFHGMAVQLAEALAEWSHAR
IRRELGYGDLEPDNIRDILAQRYQGSRYSFGYPACPVVIDQVPQLQLLGADRIGVSIDES
EQLYPEQTTTAFVIYHPVARYFSA
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