SitesBLAST
Comparing WP_012709542.1 NCBI__GCF_000018545.1:WP_012709542.1 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)
62% identity, 97% coverage: 29:1246/1256 of query aligns to 14:1224/1227 of P13009
- C247 (= C261) binding Zn(2+)
- C310 (= C324) binding Zn(2+); mutation C->A,S: Loss of zinc binding. Loss of catalytic activity.
- C311 (= C325) binding Zn(2+); mutation C->A,S: Loss of zinc binding. Loss of catalytic activity.
- E694 (= E707) binding methylcob(III)alamin
- GDVHD 756:760 (= GDVHD 775:779) binding methylcob(III)alamin
- D757 (= D776) mutation to E: Decreases activity by about 70%.; mutation to N: Decreases activity by about 45%.
- H759 (= H778) binding axial binding residue; mutation to G: Loss of catalytic activity.
- S804 (= S823) binding methylcob(III)alamin
- T808 (= T827) binding methylcob(III)alamin
- S810 (= S829) mutation to A: Decreases activity by about 40%.
- A860 (= A880) binding methylcob(III)alamin
- D946 (= D967) binding S-adenosyl-L-methionine
- R1134 (= R1156) binding S-adenosyl-L-methionine
- YY 1189:1190 (≠ YF 1211:1212) 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)
56% identity, 97% coverage: 23:1246/1256 of query aligns to 22:1262/1265 of Q99707
- R61 (≠ C62) natural variant: R -> K
- C255 (≠ T256) to Y: in dbSNP:rs1140598
- GSR 382:384 (≠ GSA 381:383) binding (6S)-5,6,7,8-tetrahydrofolate
- D449 (= D448) binding (6S)-5,6,7,8-tetrahydrofolate
- N470 (= N469) binding (6S)-5,6,7,8-tetrahydrofolate
- D537 (= D536) binding (6S)-5,6,7,8-tetrahydrofolate
- N579 (= N578) binding (6S)-5,6,7,8-tetrahydrofolate
- R585 (= R584) binding (6S)-5,6,7,8-tetrahydrofolate
- R591 (= R590) binding (6S)-5,6,7,8-tetrahydrofolate
- D919 (≠ A913) to G: in dbSNP:rs1805087
- D963 (≠ S956) mutation to E: Decreases binding to MTRR; when associated with N-1071.
- K1071 (≠ R1057) mutation to 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
57% identity, 50% coverage: 23:650/1256 of query aligns to 6:611/611 of 4cczA
- binding (6s)-5,6,7,8-tetrahydrofolate: E336 (= E375), G342 (= G381), R344 (≠ A383), N430 (= N469), M458 (= M497), D497 (= D536), G536 (= G575), S538 (= S577), N539 (= N578), F542 (= F581), R545 (= R584), R551 (= R590)
3bulA E. Coli i690c/g743c meth c-terminal fragment (649-1227) (see paper)
60% identity, 46% coverage: 667:1246/1256 of query aligns to 4:574/577 of 3bulA
- active site: D107 (= D776), H109 (= H778), S160 (= S829)
- binding cobalamin: H109 (= H778), V116 (= V785), G152 (= G821), L153 (= L822), S154 (= S823), L156 (= L825), I157 (= I826), T158 (= T827), G183 (= G852), G184 (= G853), Q208 (≠ T878), N209 (≠ D879), A210 (= A880), T213 (≠ A883), M302 (≠ Q973), D443 (= D1115), A486 (= A1158), P487 (= P1159), G488 (= G1160), Y489 (= Y1161), H495 (= H1167), K498 (= K1170), M521 (= M1193), G524 (= G1196), V527 (= V1199), S528 (= S1200)
3ivaA Structure of the b12-dependent methionine synthase (meth) c-teminal half with adohcy bound (see paper)
60% identity, 46% coverage: 667:1246/1256 of query aligns to 4:574/576 of 3ivaA
- active site: D107 (= D776), H109 (= H778), S160 (= S829)
- binding cobalamin: H109 (= H778), G112 (= G781), V116 (= V785), G152 (= G821), L153 (= L822), S154 (= S823), L156 (= L825), I157 (= I826), T158 (= T827), G183 (= G852), G184 (= G853), Q208 (≠ T878), N209 (≠ D879), T303 (= T974), D443 (= D1115), A486 (= A1158), G488 (= G1160), Y489 (= Y1161), H495 (= H1167), A520 (= A1192), M521 (= M1193), G524 (= G1196), V527 (= V1199), S528 (= S1200)
- binding s-adenosyl-l-homocysteine: E447 (= E1119), R484 (= R1156), P485 (= P1157), Y489 (= Y1161), A491 (= A1163), Y539 (= Y1211)
8g3hA Structure of cobalamin-dependent methionine synthase (meth) in a resting state (see paper)
36% identity, 70% coverage: 20:897/1256 of query aligns to 6:839/841 of 8g3hA
- binding cobalamin: Q328 (≠ D366), T330 (≠ I368), S331 (≠ P369), F675 (= F721), V685 (= V731), K693 (= K739), G720 (= G775), V722 (= V777), H723 (= H778), D724 (= D779), I725 (= I780), G726 (= G781), V730 (= V785), M767 (≠ L822), S768 (= S823), L770 (= L825), V772 (≠ T827), I795 (≠ L850), L796 (≠ I851), G797 (= G852), G798 (= G853), A799 (= A854), Y818 (= Y876), A819 (≠ V877), E820 (≠ T878), D821 (= D879)
3k13C Structure of the pterin-binding domain metr of 5- methyltetrahydrofolate-homocysteine methyltransferase from bacteroides thetaiotaomicron
70% identity, 23% coverage: 367:650/1256 of query aligns to 1:283/287 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 (= E375), G15 (= G381), R17 (≠ A383), N103 (= N469), D170 (= D536), G209 (= G575), S211 (= S577), N212 (= N578), R218 (= R584), R224 (= R590), I244 (= I610)
1mskA Methionine synthase (activation domain) (see paper)
56% identity, 26% coverage: 926:1246/1256 of query aligns to 6:324/327 of 1mskA
6bdyA Crystal structure of the meth reactivation domain bound to sinefungin (see paper)
56% identity, 26% coverage: 926:1246/1256 of query aligns to 6:324/326 of 6bdyA
1bmtA How a protein binds b12: a 3.O angstrom x-ray structure of the b12- binding domains of methionine synthase (see paper)
68% identity, 20% coverage: 667:916/1256 of query aligns to 4:246/246 of 1bmtA
- active site: D107 (= D776), H109 (= H778), S160 (= S829)
- binding co-methylcobalamin: E44 (= E707), M48 (= M711), M51 (= M714), G55 (= G718), L65 (= L728), V68 (= V731), D107 (= D776), V108 (= V777), H109 (= H778), D110 (= D779), I111 (= I780), I115 (= I784), G152 (= G821), L153 (= L822), S154 (= S823), L156 (= L825), I157 (= I826), T158 (= T827), G183 (= G852), G184 (= G853), A185 (= A854), V207 (= V877), N209 (≠ D879), A210 (= A880)
8sseA Methionine synthase, c-terminal fragment, cobalamin and reactivation domains from thermus thermophilus hb8 (see paper)
34% identity, 43% coverage: 671:1214/1256 of query aligns to 1:506/507 of 8sseA
- binding cobalamin: H97 (= H778), G100 (= G781), V104 (= V785), S142 (= S823), L145 (≠ I826), V146 (≠ T827), I169 (≠ L850), G171 (= G852), G172 (= G853), A173 (= A854), H405 (≠ K1111), V409 (≠ D1115), S451 (≠ A1158), F452 (≠ P1159), G453 (= G1160), Y454 (= Y1161), Q463 (≠ K1170), L485 (≠ M1193), E488 (≠ G1196), A490 (≠ S1198), S492 (= S1200)
3bofA Cobalamin-dependent methionine synthase (1-566) from thermotoga maritima complexed with zn2+ and homocysteine (see paper)
28% identity, 47% coverage: 21:612/1256 of query aligns to 5:538/560 of 3bofA
1q8jA Cobalamin-dependent methionine synthase (1-566) from thermotoga maritima (cd2+, hcy, methyltetrahydrofolate complex) (see paper)
28% identity, 47% coverage: 21:612/1256 of query aligns to 5:538/559 of 1q8jA
- binding 5-methyl-5,6,7,8-tetrahydrofolic acid: E320 (= E375), D390 (= D448), N411 (= N469), D473 (= D536), G505 (= G575), N508 (= N578), F511 (= F581), R516 (= R590), I536 (= I610)
5vooA Methionine synthase folate-binding domain with methyltetrahydrofolate from thermus thermophilus hb8 (see paper)
36% identity, 22% coverage: 373:646/1256 of query aligns to 5:273/282 of 5vooA
- binding 5-methyl-5,6,7,8-tetrahydrofolic acid: E7 (= E375), R8 (= R376), G13 (= G381), S14 (= S382), K15 (≠ A383), D77 (= D448), N98 (= N469), D165 (= D536), G204 (= G575), N207 (= N578), F210 (= F581), R217 (= R590), I237 (= I610)
7xcnP Crystal structure of the mttb-mttc complex at 2.7 a resolution (see paper)
31% identity, 16% coverage: 686:892/1256 of query aligns to 20:215/215 of 7xcnP
- binding 5-hydroxybenzimidazolylcobamide: D104 (= D776), I105 (≠ V777), H106 (= H778), I108 (= I780), G109 (= G781), V113 (= V785), S150 (≠ L822), S151 (= S823), L153 (= L825), M154 (≠ I826), T155 (= T827), M180 (≠ L850), G182 (= G852), G183 (= G853), G200 (≠ V877), S202 (≠ D879), A203 (= A880)
2i2xB Crystal structure of methanol:cobalamin methyltransferase complex mtabc from methanosarcina barkeri (see paper)
29% identity, 18% coverage: 670:892/1256 of query aligns to 41:243/258 of 2i2xB
- active site: D134 (= D776), H136 (= H778), T187 (≠ S829)
- binding 5-hydroxybenzimidazolylcob(iii)amide: G133 (= G775), D134 (= D776), V135 (= V777), H136 (= H778), D137 (= D779), I138 (= I780), G139 (= G781), V143 (= V785), T179 (≠ G821), T181 (≠ S823), L183 (= L825), M184 (≠ I826), T185 (= T827), A208 (≠ L850), G210 (= G852), G211 (= G853), G212 (≠ A854), G228 (≠ V877), E229 (≠ T878), E230 (≠ D879), A231 (= A880)
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)
29% identity, 18% coverage: 670:892/1256 of query aligns to 41:243/258 of Q46EH4
- H129 (≠ A771) mutation to K: Does not affect cobalamin-binding.
- H136 (= H778) mutation H->G,K: Abolishes cobalamin-binding.
Sites not aligning to the query:
- 256:258 HKH→KKK: Does not affect cobalamin-binding.
3ezxA Structure of methanosarcina barkeri monomethylamine corrinoid protein
32% identity, 15% coverage: 675:857/1256 of query aligns to 8:185/212 of 3ezxA
- active site: D100 (= D776), H102 (= H778), S155 (= S829)
- binding 5-hydroxybenzimidazolylcobamide: M47 (= M714), F54 (= F721), D100 (= D776), I101 (≠ V777), H102 (= H778), D103 (= D779), I104 (= I780), V109 (= V785), V147 (vs. gap), S149 (= S823), L151 (= L825), M152 (≠ I826), T153 (= T827), M178 (≠ L850), G180 (= G852), G181 (= G853)
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)
34% identity, 11% coverage: 713:853/1256 of query aligns to 45:174/206 of 4jgiB
- active site: D95 (= D776), H97 (= H778), A148 (≠ S829)
- binding co-methylcobalamin: L63 (≠ V731), D95 (= D776), L96 (≠ V777), H97 (= H778), D98 (= D779), I99 (= I780), G100 (= G781), F104 (≠ V785), G140 (= G821), S142 (= S823), L145 (≠ I826), G173 (= G852), G174 (= G853)
Sites not aligning to the query:
2ycjA Methyltransferase bound with methyltetrahydrofolate (see paper)
28% identity, 19% coverage: 370:611/1256 of query aligns to 10:237/271 of 2ycjA
- binding 5-methyl-5,6,7,8-tetrahydrofolic acid: M20 (≠ S382), F21 (≠ A383), D84 (= D448), N105 (= N469), D169 (= D536), G205 (= G575), N208 (= N578), Q211 (≠ F581), R216 (= R590), I236 (= I610)
Query Sequence
>WP_012709542.1 NCBI__GCF_000018545.1:WP_012709542.1
MSAASLFGELSPKPDGSEIFRALNQAAAERILIMDGAMGTEIQQLGFVEDHFRGERFGGC
ACHQQGNNDLLTLTQPKAIEEIHYRYALAGADILETNTFSSTRIAQADYGMEDMVYDLNR
DGARLARRAAKRAEAEDGRRRFVAGALGPTNRTASISPDVNNPGYRAVSFDDLRLAYAEQ
VRGLIDGGADIILIETIFDTLNAKAAIFATQEVFAEKKIHLPVMVSGTITDLSGRTLSGQ
TPTAFWYSVRHAAPFTIGLNCALGADAMRAHIDELSTVADTLVCAYPNAGLPNEFGRYDE
SPETMAAQIEAFVRDGLVNIVGGCCGSTPAHIRAIAEAVQKYPPRQVPEIERRMRLSGLE
PFTLTDEIPFVNVGERTNVTGSAKFRKLITTGDYAAALDVARDQVANGAQIIDINMDEGL
IDSTRAMVEFLNLVASEPDIACVPVMIDSSKWEVIEAGLKCVQGKALVNSISLKEGEEAF
LHHARLVRAYGAAVVVMAFDEKGQADSRARKVEICRRAYRLLTEEVGFPPEDIIFDPNIF
AVATGIDEHNNYGVDFIEATHEIIATLPHVHVSGGVSNLSFSFRGNEPVREAMHAVFLYH
AIQAGMDMGIVNAGQLAVYDAIDPELREACEDVVLNRRPDATERLLEIAERYRGQGGAQG
KEKDLAWRQWPVAKRLEHALVNGITEFIEADTEEARLAAERPLHVIEGPLMAGMNVVGDL
FGAGKMFLPQVVKSARVMKQAVAVLLPYMEAEKLANGGEGTRASAGKILMATVKGDVHDI
GKNIVGVVLACNNYEIIDLGVMVPSAKILEVARQEKVDAIGLSGLITPSLDEMVHVASEL
EREGFDIPLLIGGATTSRVHTAVKINPRYGLGQTVYVTDASRAVGVVSSLLSPEARDGYK
ETVRAEYLKVADAHARNEAEKRRLPLSQARANASKLDWDAYRPKTPSFLGTRVFESWDLA
ELARYIDWTPFFQTWELKGVYPRILDDEHQGPAARQLFADAQAMLEKIIAEKWFAPKAVV
GFWPAGSAGDDIRLFTDERRERELATFFTLRQQLAKRDGRPNVALADFVAPVESGRRDYL
GGFVVTAGIEEVAIAERFERANDDYSSILVKALADRFAEAFAERMHEYVRKELWGYAPDE
SFTPQELIAEPYTGIRPAPGYPAQPDHTEKETLFRLLDAEAAIGVRLTENYAMWPGSSVS
GLYVGHPDAYYFGVAKIERDQVEDYATRKRMGVREVERWLSPILNYVPMRETQAAE
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