SitesBLAST
Comparing WP_046009166.1 NCBI__GCF_000967895.1:WP_046009166.1 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)
66% identity, 100% coverage: 6:1231/1231 of query aligns to 4:1224/1227 of P13009
- C247 (= C248) binding
- C310 (= C311) binding ; mutation C->A,S: Loss of zinc binding. Loss of catalytic activity.
- C311 (= C312) 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 (= A861) binding
- D946 (= D947) binding
- R1134 (= R1141) binding
- YY 1189:1190 (≠ YF 1196:1197) 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)
53% identity, 99% coverage: 10:1231/1231 of query aligns to 22:1262/1265 of Q99707
- R61 (≠ Q49) natural variant: R -> K
- C255 (≠ S243) to Y: in dbSNP:rs1140598
- GSR 382:384 (≠ GSA 368:370) binding
- D449 (= D435) binding
- N470 (= N456) binding
- D537 (= D523) binding
- N579 (= N565) binding
- R585 (= R571) binding
- R591 (= R577) binding
- D919 (≠ R894) to G: in dbSNP:rs1805087
- D963 (≠ E936) mutation to E: Decreases binding to MTRR; when associated with N-1071.
- K1071 (= K1037) 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)
62% identity, 47% coverage: 652:1231/1231 of query aligns to 3:574/577 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 (≠ A859), N209 (≠ D860), A210 (= A861), T213 (≠ A864), M302 (≠ I953), D443 (= D1100), A486 (= A1143), P487 (= P1144), G488 (= G1145), Y489 (= Y1146), H495 (= H1152), K498 (= K1155), M521 (= M1178), G524 (≠ S1181), V527 (= V1184), S528 (= S1185)
3ivaA Structure of the b12-dependent methionine synthase (meth) c-teminal half with adohcy bound (see paper)
62% identity, 47% coverage: 652:1231/1231 of query aligns to 3:574/576 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 (≠ A859), N209 (≠ D860), T303 (≠ S954), D443 (= D1100), A486 (= A1143), G488 (= G1145), Y489 (= Y1146), H495 (= H1152), A520 (= A1177), M521 (= M1178), G524 (≠ S1181), V527 (= V1184), S528 (= S1185)
- binding s-adenosyl-l-homocysteine: E447 (= E1104), R484 (= R1141), P485 (= P1142), Y489 (= Y1146), A491 (= A1148), Y539 (= Y1196)
4cczA Crystal structure of human 5-methyltetrahydrofolate-homocysteine methyltransferase, the homocysteine and folate binding domains
55% identity, 51% coverage: 10:637/1231 of query aligns to 6:611/611 of 4cczA
- binding (6s)-5,6,7,8-tetrahydrofolate: E336 (= E362), G342 (= G368), R344 (≠ A370), N430 (= N456), M458 (= M484), D497 (= D523), G536 (= G562), S538 (= S564), N539 (= N565), F542 (= F568), R545 (= R571), R551 (= R577)
8g3hA Structure of cobalamin-dependent methionine synthase (meth) in a resting state (see paper)
36% identity, 70% coverage: 14:873/1231 of query aligns to 9:834/841 of 8g3hA
- binding cobalamin: Q328 (≠ S353), T330 (≠ S355), S331 (≠ L356), 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), Y818 (= Y857), A819 (≠ V858), E820 (≠ A859), D821 (= D860)
3k13C Structure of the pterin-binding domain metr of 5- methyltetrahydrofolate-homocysteine methyltransferase from bacteroides thetaiotaomicron
65% identity, 23% coverage: 357:640/1231 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 (= E362), G15 (= G368), R17 (≠ A370), N103 (= N456), D170 (= D523), G209 (= G562), S211 (= S564), N212 (= N565), R218 (= R571), R224 (= R577), I244 (= I597)
6bdyA Crystal structure of the meth reactivation domain bound to sinefungin (see paper)
58% identity, 27% coverage: 902:1231/1231 of query aligns to 2:324/326 of 6bdyA
1mskA Methionine synthase (activation domain) (see paper)
58% identity, 27% coverage: 902:1231/1231 of query aligns to 2:324/327 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)
69% identity, 20% coverage: 652:896/1231 of query aligns to 3:245/246 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 (= V858), N209 (≠ D860), A210 (= A861)
8sseA Methionine synthase, c-terminal fragment, cobalamin and reactivation domains from thermus thermophilus hb8 (see paper)
30% identity, 44% coverage: 657:1197/1231 of query aligns to 1:504/507 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 (≠ K1096), V409 (≠ D1100), S451 (≠ A1143), F452 (≠ P1144), G453 (= G1145), Y454 (= Y1146), Q463 (≠ K1155), L485 (≠ M1178), E488 (≠ S1181), A490 (= A1183), S492 (= S1185)
1q8jA Cobalamin-dependent methionine synthase (1-566) from thermotoga maritima (cd2+, hcy, methyltetrahydrofolate complex) (see paper)
28% identity, 50% coverage: 14:626/1231 of query aligns to 11:559/559 of 1q8jA
- binding 5-methyl-5,6,7,8-tetrahydrofolic acid: E320 (= E362), D390 (= D435), N411 (= N456), D473 (= D523), G505 (= G562), N508 (= N565), F511 (= F568), R516 (= R577), I536 (= I597)
3bofA Cobalamin-dependent methionine synthase (1-566) from thermotoga maritima complexed with zn2+ and homocysteine (see paper)
28% identity, 50% coverage: 14:626/1231 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: 355:639/1231 of query aligns to 1:279/282 of 5vooA
- binding 5-methyl-5,6,7,8-tetrahydrofolic acid: E7 (= E362), R8 (= R363), G13 (= G368), S14 (= S369), K15 (≠ A370), D77 (= D435), N98 (= N456), D165 (= D523), G204 (= G562), N207 (= N565), F210 (= F568), R217 (= R577), I237 (= I597)
2i2xB Crystal structure of methanol:cobalamin methyltransferase complex mtabc from methanosarcina barkeri (see paper)
31% identity, 14% coverage: 662:839/1231 of query aligns to 43:216/258 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)
31% identity, 14% coverage: 662:839/1231 of query aligns to 43:216/258 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.
7xcnP Crystal structure of the mttb-mttc complex at 2.7 a resolution (see paper)
28% identity, 14% coverage: 688:861/1231 of query aligns to 36:213/215 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 (≠ Q848), S202 (≠ Y850), A203 (≠ S851)
4jgiB 1.5 angstrom crystal structure of a novel cobalamin-binding protein from desulfitobacterium hafniense dcb-2 (see paper)
36% identity, 11% coverage: 699:834/1231 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
31% identity, 12% coverage: 689:838/1231 of query aligns to 36:185/212 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 (≠ S804), S149 (vs. gap), 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
31% identity, 10% coverage: 747:872/1231 of query aligns to 5:125/125 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), P112 (≠ A859), D113 (= D860), A114 (= A861)
Query Sequence
>WP_046009166.1 NCBI__GCF_000967895.1:WP_046009166.1
MDRQKRLEILHSTLKSRALILDGGMGTLIQAHQLEEADYRGDRFADLEQEIKGNNDLLVL
TQPDIIKGIHKAYLNAGADIIETNTFNSTRVSQADYDLEHLVPELNEMAAKIAREVCDEV
TAATGITRFVAGVLGPTSKTASISPDVNDPSFRNITFDALVNEYTEATHNLIKGGSDLIL
IETIFDTLNAKAAIYAVQGVFETLGYELPIMISGTITDASGRTLSGQTAEAFLNSVIHAR
PLSVGFNCALGADELRPHIEELSAKANCYVSAHPNAGLPNEFGEYDETPEQTAAIVGEFA
QSGFLNIIGGCCGTTPEHIAAIAEQVHKHPPRQIPEIEVACRLSGLEPFTINSDSLFVNV
GERANVTGSARFKRLIKDDKFEEALDVAREQVENGAQVIDINMDEGMLESQEAMVRYLNL
IACEPDISRVPIMVDSSKWEIIEAGLKCIQGKPIVNSISLKEGKEEFVARAKSCMRYGAA
VVVMAFDEKGQADTEQRKNEICAESYRILVDEVGFLPQDIIFDPNVFAVATGIEEHNNYA
VDFIESCKFITKNLPHALISGGVSNVSFSFRGNDPVREAIHSVFLYHAIKNGMTMGIVNA
GQLAVYDDLPAELKERVEDVILNKREDGTDRLLEIAEKFRGDGSVQEAETQEWRLLPVAA
RLSHALVKGINTFVVEDTEEARHLFDRPIEVIEGPLMDGMNVVGDLFSDGKMFLPQVVKS
ARVMKQAVAYLLPFIEEEKDGKSETQGKILMATVKGDVHDIGKNIVGVVLQCNNFEVLDL
GVMVSADKILKTAREENCDVIGLSGLITPSLDEMVHVAKEMQRLDFHLPLLIGGATTSKA
HTAVKIDQQYSNDVVAYVADASRAVGVAQKLVNPELKETFRLETLAEYEKVRARNANRKS
KPLLTYAAACERAPQITFADYTPPKPNKLGITVYDEFPLESLIKYIDWTPFFISWELAGK
YPRILEDEVVGEAATALFKDAQVMLKRIVDEKLFKARGVIGLWPANRKGTDDIEIYTDES
RTEVLETLHQLRQQTNKPAGQPNYSLADFIAPKVGDHPDGKDDYMGAFAVTSGIEAELLA
EEYKKDNDDYNNILMKALADRLAEGFAECMHAIVRNETWGYIDDKNLSNAELIKEKYQGI
RPAPGYPACPDHTEKAALFRLLNPEEHTGLTLTENFAMYPSAAVSGWYFSHPESKYFGLG
KIDKDQVEDISARKGEEVHVMERWLSPNLNY
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