METH_ECOLI
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 03-AUG-2022, entry version 206.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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 (3.0 ANGSTROMS) OF 651-896 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 (1.8 ANGSTROMS) OF 897-1227 IN COMPLEX WITH
RP 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 (3.0 ANGSTROMS) OF 651-1227 OF WILD-TYPE AND MUTANT
RP GLY-759 IN COMPLEX WITH 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}.
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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_SSZK01000049.1.
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 PDBsum; 1BMT; -.
DR PDBsum; 1K7Y; -.
DR PDBsum; 1K98; -.
DR PDBsum; 1MSK; -.
DR PDBsum; 3BUL; -.
DR PDBsum; 3IV9; -.
DR PDBsum; 3IVA; -.
DR PDBsum; 6BDY; -.
DR PDBsum; 6BM5; -.
DR PDBsum; 6BM6; -.
DR AlphaFoldDB; P13009; -.
DR SMR; P13009; -.
DR BioGRID; 4263452; 39.
DR IntAct; P13009; 13.
DR STRING; 511145.b4019; -.
DR SWISS-2DPAGE; P13009; -.
DR jPOST; P13009; -.
DR PaxDb; P13009; -.
DR PRIDE; P13009; -.
DR EnsemblBacteria; AAC76989; AAC76989; b4019.
DR EnsemblBacteria; BAE78021; BAE78021; BAE78021.
DR GeneID; 66672070; -.
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; ADCIAMS; -.
DR PhylomeDB; P13009; -.
DR BioCyc; EcoCyc:HOMOCYSMETB12-MON; -.
DR BioCyc; MetaCyc:HOMOCYSMETB12-MON; -.
DR BRENDA; 2.1.1.13; 2026.
DR UniPathway; UPA00051; UER00081.
DR EvolutionaryTrace; P13009; -.
DR PRO; PR:P13009; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
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:BHF-UCL.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
DR GO; GO:0050667; P:homocysteine metabolic process; IDA:BHF-UCL.
DR GO; GO:0009086; P:methionine biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0035999; P:tetrahydrofolate interconversion; IDA:BHF-UCL.
DR CDD; cd02069; methionine_synthase_B12_BD; 1.
DR Gene3D; 1.10.1240.10; -; 1.
DR Gene3D; 3.10.196.10; -; 1.
DR Gene3D; 3.20.20.20; -; 1.
DR Gene3D; 3.20.20.330; -; 1.
DR InterPro; IPR003759; Cbl-bd_cap.
DR InterPro; IPR006158; Cobalamin-bd.
DR InterPro; IPR036724; Cobalamin-bd_sf.
DR InterPro; IPR011005; Dihydropteroate_synth-like.
DR InterPro; IPR003726; HCY_dom.
DR InterPro; IPR036589; HCY_dom_sf.
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 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; SSF47644; SSF47644; 1.
DR SUPFAM; SSF51717; SSF51717; 1.
DR SUPFAM; SSF52242; SSF52242; 1.
DR SUPFAM; SSF56507; SSF56507; 1.
DR SUPFAM; SSF82282; SSF82282; 1.
DR TIGRFAMs; TIGR02082; metH; 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 691..694
FT /evidence="ECO:0007829|PDB:3BUL"
FT HELIX 696..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 839..845
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 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..1109
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
