SitesBLAST
Comparing HSERO_RS21740 FitnessBrowser__HerbieS:HSERO_RS21740 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, 99% coverage: 13:1247/1247 of query aligns to 8:1222/1227 of P13009
- C247 (= C255) binding
- C310 (= C320) binding ; mutation C->A,S: Loss of zinc binding. Loss of catalytic activity.
- C311 (= C321) binding ; mutation C->A,S: Loss of zinc binding. Loss of catalytic activity.
- E694 (= E705) binding
- GDVHD 756:760 (= GDVHD 775:779) binding
- 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
- T808 (= T827) binding
- S810 (= S829) mutation to A: Decreases activity by about 40%.
- A860 (= A883) binding
- D946 (= D966) binding
- R1134 (= R1160) binding
- YY 1189:1190 (≠ YF 1214:1215) binding
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: 4:1247/1247 of query aligns to 6:1260/1265 of Q99707
- R61 (≠ V52) natural variant: R -> K
- C255 (≠ T250) to Y: in dbSNP:rs1140598
- GSR 382:384 (≠ GSK 377:379) binding
- D449 (= D444) binding
- N470 (= N465) binding
- D537 (= D532) binding
- N579 (= N574) binding
- R585 (= R580) binding
- R591 (= R586) binding
- D919 (≠ Q916) to G: in dbSNP:rs1805087
- D963 (≠ N955) mutation to E: Decreases binding to MTRR; when associated with N-1071.
- K1071 (= K1056) 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
56% identity, 51% coverage: 13:645/1247 of query aligns to 2:610/611 of 4cczA
- binding (6s)-5,6,7,8-tetrahydrofolate: E336 (= E371), G342 (= G377), R344 (≠ K379), N430 (= N465), M458 (= M493), D497 (= D532), G536 (= G571), S538 (= S573), N539 (= N574), F542 (= F577), R545 (= R580), R551 (= R586)
3ivaA Structure of the b12-dependent methionine synthase (meth) c-teminal half with adohcy bound (see paper)
59% identity, 47% coverage: 660:1247/1247 of query aligns to 3:572/576 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 (= G856), G184 (= G857), Q208 (≠ P881), N209 (≠ D882), T303 (= T973), D443 (= D1119), A486 (= A1162), G488 (= G1164), Y489 (= Y1165), H495 (= H1171), A520 (= A1195), M521 (= M1196), G524 (= G1199), V527 (= V1202), S528 (= S1203)
- binding s-adenosyl-l-homocysteine: E447 (= E1123), R484 (= R1160), P485 (= P1161), Y489 (= Y1165), A491 (= A1167), Y539 (= Y1214)
3bulA E. Coli i690c/g743c meth c-terminal fragment (649-1227) (see paper)
59% identity, 47% coverage: 660:1247/1247 of query aligns to 3:572/577 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 (= G856), G184 (= G857), Q208 (≠ P881), N209 (≠ D882), A210 (= A883), T213 (≠ A886), M302 (≠ Q972), D443 (= D1119), A486 (= A1162), P487 (= P1163), G488 (= G1164), Y489 (= Y1165), H495 (= H1171), K498 (= K1174), M521 (= M1196), G524 (= G1199), V527 (= V1202), S528 (= S1203)
8g3hA Structure of cobalamin-dependent methionine synthase (meth) in a resting state (see paper)
35% identity, 71% coverage: 17:899/1247 of query aligns to 9:838/841 of 8g3hA
- binding cobalamin: Q328 (≠ D362), T330 (≠ S364), S331 (≠ L365), F675 (= F719), V685 (= V729), K693 (= K737), G720 (= G775), V722 (= V777), H723 (= H778), D724 (= D779), I725 (= I780), G726 (= G781), V730 (= V785), M767 (≠ L822), S768 (= S823), L770 (= L825), V772 (≠ T827), I795 (≠ M854), L796 (≠ I855), G797 (= G856), G798 (= G857), A799 (= A858), Y818 (= Y879), A819 (≠ V880), E820 (≠ P881), D821 (= D882)
3k13C Structure of the pterin-binding domain metr of 5- methyltetrahydrofolate-homocysteine methyltransferase from bacteroides thetaiotaomicron
71% identity, 23% coverage: 366:649/1247 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 (= E371), G15 (= G377), R17 (≠ K379), N103 (= N465), D170 (= D532), G209 (= G571), S211 (= S573), N212 (= N574), R218 (= R580), R224 (= R586), I244 (= I606)
6bdyA Crystal structure of the meth reactivation domain bound to sinefungin (see paper)
56% identity, 26% coverage: 924:1247/1247 of query aligns to 2:322/326 of 6bdyA
1mskA Methionine synthase (activation domain) (see paper)
56% identity, 26% coverage: 924:1247/1247 of query aligns to 2:322/327 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)
65% identity, 21% coverage: 660:918/1247 of query aligns to 3:245/246 of 1bmtA
- active site: D107 (= D776), H109 (= H778), S160 (= S829)
- binding co-methylcobalamin: E44 (= E705), M48 (= M709), M51 (= M712), G55 (= G716), L65 (= L726), V68 (= V729), 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 (= G856), G184 (= G857), A185 (= A858), V207 (= V880), N209 (≠ D882), A210 (= A883)
8sseA Methionine synthase, c-terminal fragment, cobalamin and reactivation domains from thermus thermophilus hb8 (see paper)
30% identity, 44% coverage: 665:1217/1247 of query aligns to 1:506/507 of 8sseA
- binding cobalamin: H97 (= H778), G100 (= G781), V104 (= V785), S142 (= S823), L145 (≠ I826), V146 (≠ T827), I169 (≠ M854), G171 (= G856), G172 (= G857), A173 (= A858), H405 (≠ K1115), V409 (≠ D1119), S451 (≠ A1162), F452 (≠ P1163), G453 (= G1164), Y454 (= Y1165), Q463 (≠ K1174), L485 (≠ M1196), E488 (≠ G1199), A490 (≠ S1201), S492 (= S1203)
1q8jA Cobalamin-dependent methionine synthase (1-566) from thermotoga maritima (cd2+, hcy, methyltetrahydrofolate complex) (see paper)
27% identity, 48% coverage: 16:608/1247 of query aligns to 10:538/559 of 1q8jA
- binding 5-methyl-5,6,7,8-tetrahydrofolic acid: E320 (= E371), D390 (= D444), N411 (= N465), D473 (= D532), G505 (= G571), N508 (= N574), F511 (= F577), R516 (= R586), I536 (= I606)
3bofA Cobalamin-dependent methionine synthase (1-566) from thermotoga maritima complexed with zn2+ and homocysteine (see paper)
27% identity, 48% coverage: 16:608/1247 of query aligns to 10:538/560 of 3bofA
5vooA Methionine synthase folate-binding domain with methyltetrahydrofolate from thermus thermophilus hb8 (see paper)
34% identity, 23% coverage: 364:650/1247 of query aligns to 1:281/282 of 5vooA
- binding 5-methyl-5,6,7,8-tetrahydrofolic acid: E7 (= E371), R8 (= R372), G13 (= G377), S14 (= S378), K15 (= K379), D77 (= D444), N98 (= N465), D165 (= D532), G204 (= G571), N207 (= N574), F210 (= F577), R217 (= R586), I237 (= I606)
7xcnP Crystal structure of the mttb-mttc complex at 2.7 a resolution (see paper)
32% identity, 15% coverage: 676:862/1247 of query aligns to 12:188/215 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 (= M854), G182 (= G856), G183 (= G857)
Sites not aligning to the query:
2i2xB Crystal structure of methanol:cobalamin methyltransferase complex mtabc from methanosarcina barkeri (see paper)
32% identity, 19% coverage: 674:912/1247 of query aligns to 39:257/258 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 (≠ M854), G210 (= G856), G211 (= G857), G212 (≠ A858), G228 (≠ V880), E229 (≠ P881), E230 (≠ D882), A231 (= A883)
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, 19% coverage: 674:912/1247 of query aligns to 39:257/258 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.
4jgiB 1.5 angstrom crystal structure of a novel cobalamin-binding protein from desulfitobacterium hafniense dcb-2 (see paper)
33% identity, 12% coverage: 711:857/1247 of query aligns to 45:174/206 of 4jgiB
- active site: D95 (= D776), H97 (= H778), A148 (≠ S829)
- binding co-methylcobalamin: L63 (≠ V729), D95 (= D776), L96 (≠ V777), H97 (= H778), D98 (= D779), I99 (= I780), G100 (= G781), F104 (≠ V785), G140 (= G821), S142 (= S823), L145 (≠ I826), G173 (= G856), G174 (= G857)
Sites not aligning to the query:
3ezxA Structure of methanosarcina barkeri monomethylamine corrinoid protein
33% identity, 14% coverage: 683:861/1247 of query aligns to 18:185/212 of 3ezxA
- active site: D100 (= D776), H102 (= H778), S155 (= S829)
- binding 5-hydroxybenzimidazolylcobamide: M47 (= M712), F54 (= F719), D100 (= D776), I101 (≠ V777), H102 (= H778), D103 (= D779), I104 (= I780), V109 (= V785), V147 (≠ I820), S149 (= S823), L151 (= L825), M152 (≠ I826), T153 (= T827), M178 (= M854), G180 (= G856), G181 (= G857)
Sites not aligning to the query:
1y80A Structure of a corrinoid (factor iiim)-binding protein from moorella thermoacetica
34% identity, 10% coverage: 766:894/1247 of query aligns to 5:125/125 of 1y80A
- active site: D15 (= D776), H17 (= H778), T68 (≠ S829)
- binding co-5-methoxybenzimidazolylcobamide: D15 (= D776), L16 (≠ V777), H17 (= H778), D18 (= D779), I19 (= I780), G20 (= G781), V24 (= V785), G60 (= G821), M61 (≠ L822), S62 (= S823), L64 (= L825), L65 (≠ I826), T66 (= T827), I91 (≠ M854), G93 (= G856), G94 (= G857), A95 (= A858), P112 (= P881), D113 (= D882), A114 (= A883)
Query Sequence
>HSERO_RS21740 FitnessBrowser__HerbieS:HSERO_RS21740
MKPNELCQTELLLRDLMSQRILILDGAMGTMIQRYKLTEEDYRGQRFADFSVPGKDLFVK
GNNELLSLTQPHIIQEIHEQYLAAGADLIETNTFGATSVAQDDYHMAHLVYEMNVESARL
ARAACDKYATPDKPRFVAGALGPTPKTASISPDVNDPAARNVTFDQLVAAYLEQTRALVE
GGADVLLVETIFDTLNCKAALFAIDTFFEESGQRLPIMISGTVTDASGRILSGQTVTAFW
NSIRHARPLTVGLNCALGAALMRPYAEELSKIADTFVCIYPNAGLPNPMSDTGFDETPDV
TSALLKEFAESGFVNVAGGCCGTTPPHIKAIAETVAKIAPRKVPEPTHEMRLSGLEPFTI
NDDSLYVNVGERTNVTGSKAFARLILNEQYDEALAVARQQVENGAQIIDINMDEAMLDSV
AAMTRFLNLIASEPDIARVPIMIDSSKWEVIEAGLKCVQGKSIVNSISMKEGEEKFLREA
KLCRRYGAAVIVMAFDEVGQADTFARKIEICERAYRLLVDKLDFPPEDIIFDPNIFAVAT
GIEEHNNYAVDFIEATRWIHQNLPYAKISGGVSNVSFSFRGNDPAREAIHTVFLYHAIKA
GMTMGIVNAGMIGVYDDLPAELRERVEDVVLNRREDATERMIEYAATLKAGDKKEEATLE
WRNLPVAKRLSHALVHGITQWIVEDTEEVRQQIAADGGRPIHVIEGPLMDGMNVVGDLFG
QGKMFLPQVVKSARVMKQAVAHLIPFIEEEKRQLEIATGEVAKPKGKIVIATVKGDVHDI
GKNIVTVVLQCNNFEVVNMGVMVPCAEILAKAKEEKADIIGLSGLITPSLEEMAYVAKEM
QRDPYFAGLKMPLMIGGATTSRAHTAVKIAPNYEGPVVYVPDASRAVSVAQSLLADEQKT
QYVAELNADYERIREQHASKKAAPMLSLAAARANKTKLDFAPVKPKFIGRRLFKNVDLGL
LANYIDWGPFFQTWDLAGPYPAILTDEVVGEAATKVFQEAQAMLKKIIDGRWLTANGVIS
LLPANTVNDDDIEIYTDDSRSQVAFTYYGLRQQTEKPVVDGVARPNQCLSDFIAPKESGV
QDYIGMFAVTAGLGIEKYEKRFEDAHDDYSSIMLKALADRLAEAFAEYLHERVRKDLWGY
AADENLSSTDLIKEKYLGIRPAPGYPACPEHTVKADVFRTMQCDEIGMQLTESYAMFPGA
SVSGFYFAHPQSKYFVVGKIGEDQVVDMAERRHVPKEELERWLAPNL
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