ID METH_ECOLI Reviewed; 1227 AA. AC P13009; Q2M6T5; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 5. DT 04-NOV-2026, entry version 223. DE RecName: Full=Methionine synthase; DE EC=2.1.1.13; DE AltName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase; DE AltName: Full=Methionine synthase, vitamin-B12-dependent; DE Short=MS; GN Name=metH; OrderedLocusNames=b4019, JW3979; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=K12; RX PubMed=2185137; DOI=10.1016/0378-1119(90)90490-i; RA Old I.G., Margarita D., Glass R.E., Saint-Girons I.; RT "Nucleotide sequence of the metH gene of Escherichia coli K-12 and RT comparison with that of Salmonella typhimurium LT2."; RL Gene 87:15-21(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. RC STRAIN=K12; RX PubMed=2668277; DOI=10.1016/s0021-9258(18)80083-7; RA Banerjee R.V., Johnston N.L., Sobeski J.K., Datta P., Matthews R.G.; RT "Cloning and sequence analysis of the Escherichia coli metH gene encoding RT cobalamin-dependent methionine synthase and isolation of a tryptic fragment RT containing the cobalamin-binding domain."; RL J. Biol. Chem. 264:13888-13895(1989). RN [3] RP SEQUENCE REVISION. RX PubMed=8369296; DOI=10.1021/bi00087a004; RA Drummond J.T., Loo R.R., Matthews R.G.; RT "Electrospray mass spectrometric analysis of the domains of a large enzyme: RT observation of the occupied cobalamin-binding domain and redefinition of RT the carboxyl terminus of methionine synthase."; RL Biochemistry 32:9282-9289(1993). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=8265357; DOI=10.1093/nar/21.23.5408; RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.; RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region RT from 89.2 to 92.8 minutes."; RL Nucleic Acids Res. 21:5408-5417(1993). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [7] RP PROTEIN SEQUENCE OF 2-7, FUNCTION, CATALYTIC ACTIVITY, DOMAIN, AND RP MUTAGENESIS OF CYS-310 AND CYS-311. RC STRAIN=K12; RX PubMed=9201956; DOI=10.1021/bi9705164; RA Goulding C.W., Postigo D., Matthews R.G.; RT "Cobalamin-dependent methionine synthase is a modular protein with distinct RT regions for binding homocysteine, methyltetrahydrofolate, cobalamin, and RT adenosylmethionine."; RL Biochemistry 36:8082-8091(1997). RN [8] RP CRYSTALLIZATION. RX PubMed=1593636; DOI=10.1016/0022-2836(92)90940-l; RA Luschinsky C.L., Drummond J.T., Matthews R.G., Ludwig M.L.; RT "Crystallization and preliminary X-ray diffraction studies of the RT cobalamin-binding domain of methionine synthase from Escherichia coli."; RL J. Mol. Biol. 225:557-560(1992). RN [9] RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-757; HIS-759 AND RP SER-810. RC STRAIN=K12; RX PubMed=8652590; DOI=10.1021/bi952389m; RA Jarrett J.T., Amaratunga M., Drennan C.L., Scholten J.D., Sands R.H., RA Ludwig M.L., Matthews R.G.; RT "Mutations in the B12-binding region of methionine synthase: how the RT protein controls methylcobalamin reactivity."; RL Biochemistry 35:2464-2475(1996). RN [10] RP ZINC BINDING SITES. RC STRAIN=K12; RX PubMed=9398304; DOI=10.1021/bi971988l; RA Goulding C.W., Matthews R.G.; RT "Cobalamin-dependent methionine synthase from Escherichia coli: involvement RT of zinc in homocysteine activation."; RL Biochemistry 36:15749-15757(1997). RN [11] RP IDENTIFICATION BY 2D-GEL. RX PubMed=9298644; DOI=10.1002/elps.1150180805; RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.; RT "Escherichia coli proteome analysis using the gene-protein database."; RL Electrophoresis 18:1243-1251(1997). RN [12] RP ZINC BINDING SITES, AND ROLE OF ZINC IN SUBSTRATE BINDING. RC STRAIN=K12; RX PubMed=11170420; DOI=10.1021/bi001711c; RA Peariso K., Zhou Z.S., Smith A.E., Matthews R.G., Penner-Hahn J.E.; RT "Characterization of the zinc sites in cobalamin-independent and cobalamin- RT dependent methionine synthase using zinc and selenium X-ray absorption RT spectroscopy."; RL Biochemistry 40:987-993(2001). RN [13] RP REVIEW. RX PubMed=11513576; DOI=10.1021/ar0000051; RA Matthews R.G.; RT "Cobalamin-dependent methyltransferases."; RL Acc. Chem. Res. 34:681-689(2001). RN [14] {ECO:0007744|PDB:1BMT} RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH COBALAMIN. RX PubMed=7992050; DOI=10.1126/science.7992050; RA Drennan C.L., Huang S., Drummond J.T., Matthews R.G., Ludwig M.L.; RT "How a protein binds B12: a 3.0 A X-ray structure of B12-binding domains of RT methionine synthase."; RL Science 266:1669-1674(1994). RN [15] {ECO:0007744|PDB:1MSK} RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH S-ADENOSYL-L-METHIONINE. RC STRAIN=K12; RX PubMed=8939751; DOI=10.1016/s0969-2126(96)00135-9; RA Dixon M.M., Huang S., Matthews R.G., Ludwig M.L.; RT "The structure of the C-terminal domain of methionine synthase: presenting RT S-adenosylmethionine for reductive methylation of B12."; RL Structure 4:1263-1275(1996). RN [16] {ECO:0007744|PDB:1K7Y, ECO:0007744|PDB:1K98} RP X-RAY CRYSTALLOGRAPHY OF WILD-TYPE AND MUTANT GLY-759 IN COMPLEX WITH RP COBALAMIN. RC STRAIN=K12; RX PubMed=11731805; DOI=10.1038/nsb738; RA Bandarian V., Pattridge K.A., Lennon B.W., Huddler D.P., Matthews R.G., RA Ludwig M.L.; RT "Domain alternation switches B(12)-dependent methionine synthase to the RT activation conformation."; RL Nat. Struct. Biol. 9:53-56(2002). CC -!- FUNCTION: Catalyzes the transfer of a methyl group from methyl- CC cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and CC methionine. Subsequently, remethylates the cofactor using CC methyltetrahydrofolate. {ECO:0000269|PubMed:8652590, CC ECO:0000269|PubMed:9201956}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(6S)-5-methyl-5,6,7,8-tetrahydrofolate + L-homocysteine = CC (6S)-5,6,7,8-tetrahydrofolate + L-methionine; Xref=Rhea:RHEA:11172, CC ChEBI:CHEBI:18608, ChEBI:CHEBI:57453, ChEBI:CHEBI:57844, CC ChEBI:CHEBI:58199; EC=2.1.1.13; Evidence={ECO:0000269|PubMed:8652590, CC ECO:0000269|PubMed:9201956}; CC -!- COFACTOR: CC Name=methylcob(III)alamin; Xref=ChEBI:CHEBI:28115; CC Evidence={ECO:0000269|PubMed:7992050}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000269|PubMed:9398304}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:9398304}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo CC pathway; L-methionine from L-homocysteine (MetH route): step 1/1. CC -!- DOMAIN: Modular enzyme with four functionally distinct domains. The CC isolated Hcy-binding domain catalyzes methyl transfer from free CC methylcobalamin to homocysteine. The Hcy-binding domain in association CC with the pterin-binding domain catalyzes the methylation of CC cob(I)alamin by methyltetrahydrofolate and the methylation of CC homocysteine. The B12-binding domain binds the cofactor. The AdoMet CC activation domain binds S-adenosyl-L-methionine. Under aerobic CC conditions cob(I)alamin can be converted to inactive cob(II)alamin. CC Reductive methylation by S-adenosyl-L-methionine and flavodoxin CC regenerates methylcobalamin. {ECO:0000269|PubMed:9201956}. CC -!- MISCELLANEOUS: L-homocysteine is bound via the zinc atom. CC -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine synthase CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X16584; CAA34601.1; -; Genomic_DNA. DR EMBL; J04975; AAA02995.1; -; Unassigned_DNA. DR EMBL; U00006; AAC43113.1; -; Genomic_DNA. DR EMBL; U00096; AAC76989.1; -; Genomic_DNA. DR EMBL; AP009048; BAE78021.1; -; Genomic_DNA. DR PIR; B65209; XYECMH. DR RefSeq; NP_418443.1; NC_000913.3. DR RefSeq; WP_000096011.1; NZ_CP009789.1. DR PDB; 1BMT; X-ray; 3.00 A; A/B=651-896. DR PDB; 1K7Y; X-ray; 3.00 A; A=651-1227. DR PDB; 1K98; X-ray; 3.75 A; A=651-1227. DR PDB; 1MSK; X-ray; 1.80 A; A=897-1227. DR PDB; 3BUL; X-ray; 2.30 A; A=649-1227. DR PDB; 3IV9; X-ray; 3.25 A; A=649-1227. DR PDB; 3IVA; X-ray; 2.70 A; A=649-1227. DR PDB; 6BDY; X-ray; 1.51 A; A=897-1227. DR PDB; 6BM5; X-ray; 1.50 A; A=897-1227. DR PDB; 6BM6; X-ray; 1.50 A; A=897-1227. DR AlphaFoldDB; P13009; -. DR MDposit; P13009; -. DR MDRepo; P13009; -. DR SMR; P13009; -. DR BioGRID; 4263452; 53. DR FunCoup; P13009; 709. DR IntAct; P13009; 13. DR STRING; 511145.b4019; -. DR jPOST; P13009; -. DR PaxDb; 511145-b4019; -. DR EnsemblBacteria; AAC76989; AAC76989; b4019. DR GeneID; 75204159; -. DR GeneID; 948522; -. DR KEGG; ecj:JW3979; -. DR KEGG; eco:b4019; -. DR PATRIC; fig|511145.12.peg.4132; -. DR EchoBASE; EB0582; -. DR eggNOG; COG0646; Bacteria. DR eggNOG; COG1410; Bacteria. DR HOGENOM; CLU_004914_2_0_6; -. DR InParanoid; P13009; -. DR OMA; AAAKHDC; -. DR OrthoDB; 9803687at2; -. DR PhylomeDB; P13009; -. DR BioCyc; EcoCyc:HOMOCYSMETB12-MONOMER; -. DR BioCyc; MetaCyc:HOMOCYSMETB12-MONOMER; -. DR BRENDA; 2.1.1.13; 2026. DR UniPathway; UPA00051; UER00081. DR EvolutionaryTrace; P13009; -. DR PRO; PR:P13009; -. DR Proteomes; UP000000625; Chromosome. DR AbasyAtlas; P13009; -. DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki. DR GO; GO:0005829; C:cytosol; IDA:EcoCyc. DR GO; GO:0031419; F:cobalamin binding; IDA:BHF-UCL. DR GO; GO:0008705; F:methionine synthase activity; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc. DR GO; GO:0071265; P:L-methionine biosynthetic process; IDA:UniProtKB. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IDA:BHF-UCL. DR GO; GO:0046653; P:tetrahydrofolate metabolic process; IBA:GO_Central. DR CDD; cd02069; methionine_synthase_B12_BD; 1. DR CDD; cd00740; MeTr; 1. DR FunFam; 1.10.1240.10:FF:000001; Methionine synthase; 1. DR FunFam; 3.20.20.20:FF:000002; Methionine synthase; 1. DR FunFam; 3.20.20.330:FF:000001; Methionine synthase; 1. DR FunFam; 3.40.50.280:FF:000001; Methionine synthase; 1. DR Gene3D; 3.40.50.280; Cobalamin-binding domain; 1. DR Gene3D; 1.10.288.10; Cobalamin-dependent Methionine Synthase, domain 2; 1. DR Gene3D; 3.20.20.20; Dihydropteroate synthase-like; 1. DR Gene3D; 3.20.20.330; Homocysteine-binding-like domain; 1. DR Gene3D; 1.10.1240.10; Methionine synthase domain; 1. DR Gene3D; 3.10.196.10; Vitamin B12-dependent methionine synthase, activation domain; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR036724; Cobalamin-bd_sf. DR InterPro; IPR011005; Dihydropteroate_synth-like_sf. DR InterPro; IPR003726; HCY_dom. DR InterPro; IPR036589; HCY_dom_sf. DR InterPro; IPR050554; Met_Synthase/Corrinoid. DR InterPro; IPR033706; Met_synthase_B12-bd. DR InterPro; IPR011822; MetH. DR InterPro; IPR036594; Meth_synthase_dom. DR InterPro; IPR000489; Pterin-binding_dom. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR InterPro; IPR037010; VitB12-dep_Met_synth_activ_sf. DR NCBIfam; NF007024; metH; 1. DR NCBIfam; TIGR02082; metH; 1. DR PANTHER; PTHR45833; METHIONINE SYNTHASE; 1. DR PANTHER; PTHR45833:SF1; METHIONINE SYNTHASE; 1. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF52242; Cobalamin (vitamin B12)-binding domain; 1. DR SUPFAM; SSF51717; Dihydropteroate synthetase-like; 1. DR SUPFAM; SSF82282; Homocysteine S-methyltransferase; 1. DR SUPFAM; SSF56507; Methionine synthase activation domain-like; 1. DR SUPFAM; SSF47644; Methionine synthase domain; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Cobalamin; Cobalt; KW Direct protein sequencing; Metal-binding; Methionine biosynthesis; KW Methyltransferase; Reference proteome; Repeat; S-adenosyl-L-methionine; KW Transferase; Zinc. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:9201956" FT CHAIN 2..1227 FT /note="Methionine synthase" FT /id="PRO_0000204532" FT DOMAIN 2..325 FT /note="Hcy-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00333" FT DOMAIN 356..617 FT /note="Pterin-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00334" FT DOMAIN 650..744 FT /note="B12-binding N-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00667" FT DOMAIN 746..881 FT /note="B12-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00666" FT DOMAIN 897..1227 FT /note="AdoMet activation" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00346" FT BINDING 247 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:9398304" FT BINDING 310 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:9398304" FT BINDING 311 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:9398304" FT BINDING 694 FT /ligand="methylcob(III)alamin" FT /ligand_id="ChEBI:CHEBI:28115" FT /evidence="ECO:0000269|PubMed:7992050, FT ECO:0007744|PDB:1BMT" FT BINDING 756..760 FT /ligand="methylcob(III)alamin" FT /ligand_id="ChEBI:CHEBI:28115" FT /evidence="ECO:0000269|PubMed:7992050, FT ECO:0007744|PDB:1BMT" FT BINDING 759 FT /ligand="methylcob(III)alamin" FT /ligand_id="ChEBI:CHEBI:28115" FT /ligand_part="Co" FT /ligand_part_id="ChEBI:CHEBI:27638" FT /note="axial binding residue" FT /evidence="ECO:0000269|PubMed:7992050, FT ECO:0007744|PDB:1BMT" FT BINDING 804 FT /ligand="methylcob(III)alamin" FT /ligand_id="ChEBI:CHEBI:28115" FT /evidence="ECO:0000269|PubMed:7992050, FT ECO:0007744|PDB:1BMT" FT BINDING 808 FT /ligand="methylcob(III)alamin" FT /ligand_id="ChEBI:CHEBI:28115" FT /evidence="ECO:0000269|PubMed:7992050, FT ECO:0007744|PDB:1BMT" FT BINDING 860 FT /ligand="methylcob(III)alamin" FT /ligand_id="ChEBI:CHEBI:28115" FT /evidence="ECO:0000269|PubMed:7992050, FT ECO:0007744|PDB:1BMT" FT BINDING 946 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000269|PubMed:8939751" FT BINDING 1134 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000269|PubMed:8939751" FT BINDING 1189..1190 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000269|PubMed:8939751" FT MUTAGEN 310 FT /note="C->A,S: Loss of zinc binding. Loss of catalytic FT activity." FT /evidence="ECO:0000269|PubMed:9201956" FT MUTAGEN 311 FT /note="C->A,S: Loss of zinc binding. Loss of catalytic FT activity." FT /evidence="ECO:0000269|PubMed:9201956" FT MUTAGEN 757 FT /note="D->E: Decreases activity by about 70%." FT /evidence="ECO:0000269|PubMed:8652590" FT MUTAGEN 757 FT /note="D->N: Decreases activity by about 45%." FT /evidence="ECO:0000269|PubMed:8652590" FT MUTAGEN 759 FT /note="H->G: Loss of catalytic activity." FT /evidence="ECO:0000269|PubMed:8652590" FT MUTAGEN 810 FT /note="S->A: Decreases activity by about 40%." FT /evidence="ECO:0000269|PubMed:8652590" FT CONFLICT 113 FT /note="A -> R (in Ref. 1 and 2)" FT /evidence="ECO:0000305" FT CONFLICT 641 FT /note="S -> T (in Ref. 1 and 2)" FT /evidence="ECO:0000305" FT CONFLICT 1079..1080 FT /note="QH -> HD (in Ref. 1; CAA34601)" FT /evidence="ECO:0000305" FT CONFLICT 1195..1227 FT /note="IQRDQVEDYARRKGMSVTEVERWLAPNLGYDAD -> TSARSG (in Ref. FT 1; CAA34601)" FT /evidence="ECO:0000305" FT HELIX 653..656 FT /evidence="ECO:0007829|PDB:3BUL" FT HELIX 659..669 FT /evidence="ECO:0007829|PDB:3BUL" FT HELIX 675..685 FT /evidence="ECO:0007829|PDB:3BUL" FT STRAND 686..688 FT /evidence="ECO:0007829|PDB:3BUL" FT HELIX 689..692 FT /evidence="ECO:0007829|PDB:1BMT" FT HELIX 693..697 FT /evidence="ECO:0007829|PDB:3BUL" FT HELIX 698..710 FT /evidence="ECO:0007829|PDB:3BUL" FT HELIX 715..737 FT /evidence="ECO:0007829|PDB:3BUL" FT STRAND 738..741 FT /evidence="ECO:0007829|PDB:1K7Y" FT STRAND 748..754 FT /evidence="ECO:0007829|PDB:3BUL" FT HELIX 761..771 FT /evidence="ECO:0007829|PDB:3BUL" FT TURN 772..774 FT /evidence="ECO:0007829|PDB:3BUL" FT STRAND 776..779 FT /evidence="ECO:0007829|PDB:3BUL" FT STRAND 782..784 FT /evidence="ECO:0007829|PDB:3BUL" FT HELIX 786..796 FT /evidence="ECO:0007829|PDB:3BUL" FT STRAND 799..804 FT /evidence="ECO:0007829|PDB:3BUL" FT HELIX 809..823 FT /evidence="ECO:0007829|PDB:3BUL" FT STRAND 830..834 FT /evidence="ECO:0007829|PDB:3BUL" FT STRAND 835..837 FT /evidence="ECO:0007829|PDB:3IV9" FT HELIX 842..846 FT /evidence="ECO:0007829|PDB:3BUL" FT HELIX 847..849 FT /evidence="ECO:0007829|PDB:3BUL" FT STRAND 854..856 FT /evidence="ECO:0007829|PDB:3BUL" FT HELIX 860..870 FT /evidence="ECO:0007829|PDB:3BUL" FT TURN 873..875 FT /evidence="ECO:0007829|PDB:3BUL" FT HELIX 876..893 FT /evidence="ECO:0007829|PDB:3BUL" FT HELIX 906..911 FT /evidence="ECO:0007829|PDB:6BM5" FT HELIX 918..920 FT /evidence="ECO:0007829|PDB:6BM5" FT HELIX 923..926 FT /evidence="ECO:0007829|PDB:6BM5" FT STRAND 930..935 FT /evidence="ECO:0007829|PDB:6BM5" FT HELIX 938..942 FT /evidence="ECO:0007829|PDB:6BM5" FT HELIX 948..953 FT /evidence="ECO:0007829|PDB:6BM5" FT HELIX 962..965 FT /evidence="ECO:0007829|PDB:6BM5" FT TURN 967..969 FT /evidence="ECO:0007829|PDB:6BM5" FT HELIX 970..990 FT /evidence="ECO:0007829|PDB:6BM5" FT STRAND 996..1007 FT /evidence="ECO:0007829|PDB:6BM5" FT STRAND 1010..1016 FT /evidence="ECO:0007829|PDB:6BM5" FT STRAND 1021..1027 FT /evidence="ECO:0007829|PDB:6BM5" FT STRAND 1036..1038 FT /evidence="ECO:0007829|PDB:6BM5" FT HELIX 1043..1046 FT /evidence="ECO:0007829|PDB:6BM5" FT HELIX 1050..1052 FT /evidence="ECO:0007829|PDB:6BM5" FT STRAND 1056..1065 FT /evidence="ECO:0007829|PDB:6BM5" FT HELIX 1069..1078 FT /evidence="ECO:0007829|PDB:6BM5" FT HELIX 1082..1106 FT /evidence="ECO:0007829|PDB:6BM5" FT HELIX 1107..1111 FT /evidence="ECO:0007829|PDB:6BM5" FT HELIX 1122..1126 FT /evidence="ECO:0007829|PDB:6BM5" FT STRAND 1130..1133 FT /evidence="ECO:0007829|PDB:6BM5" FT HELIX 1145..1147 FT /evidence="ECO:0007829|PDB:6BM5" FT HELIX 1148..1154 FT /evidence="ECO:0007829|PDB:6BM5" FT HELIX 1157..1161 FT /evidence="ECO:0007829|PDB:6BM5" FT STRAND 1167..1169 FT /evidence="ECO:0007829|PDB:3IV9" FT STRAND 1171..1182 FT /evidence="ECO:0007829|PDB:6BM5" FT HELIX 1197..1207 FT /evidence="ECO:0007829|PDB:6BM5" FT HELIX 1211..1217 FT /evidence="ECO:0007829|PDB:6BM5" FT HELIX 1219..1221 FT /evidence="ECO:0007829|PDB:6BM5" FT STRAND 1222..1224 FT /evidence="ECO:0007829|PDB:6BDY" SQ SEQUENCE 1227 AA; 135997 MW; 91F0CAA1E9127D9A CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDGLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAD //