FOLC_ECOLI
ID FOLC_ECOLI Reviewed; 422 AA.
AC P08192; P78237;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Dihydrofolate synthase/folylpolyglutamate synthase {ECO:0000305};
DE Short=DHFS / FPGS {ECO:0000303|PubMed:15705579};
DE EC=6.3.2.12 {ECO:0000269|PubMed:18232714, ECO:0000269|PubMed:1989505, ECO:0000269|PubMed:2985605};
DE EC=6.3.2.17 {ECO:0000269|PubMed:18232714};
DE AltName: Full=Folylpoly-gamma-glutamate synthetase-dihydrofolate synthetase {ECO:0000303|PubMed:2985605};
DE AltName: Full=Folylpolyglutamate synthetase {ECO:0000303|PubMed:18232714};
DE AltName: Full=Tetrahydrofolylpolyglutamate synthase;
GN Name=folC {ECO:0000303|PubMed:2985605}; Synonyms=dedC;
GN OrderedLocusNames=b2315, JW2312;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3040739; DOI=10.1016/s0021-9258(18)45358-6;
RA Bognar A.L., Osborne C., Shane B.;
RT "Primary structure of the Escherichia coli folC gene and its
RT folylpolyglutamate synthetase-dihydrofolate synthetase product and
RT regulation of expression by an upstream gene.";
RL J. Biol. Chem. 262:12337-12343(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3040734; DOI=10.1016/s0021-9258(18)45338-0;
RA Nonet M.L., Marvel C.C., Tolan D.R.;
RT "The hisT-purF region of the Escherichia coli K-12 chromosome.
RT Identification of additional genes of the hisT and purF operons.";
RL J. Biol. Chem. 262:12209-12217(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [4]
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 [5]
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP PATHWAY.
RC STRAIN=K12;
RX PubMed=2985605; DOI=10.1016/s0021-9258(18)89069-x;
RA Bognar A.L., Osborne C., Shane B., Singer S.C., Ferone R.;
RT "Folylpoly-gamma-glutamate synthetase-dihydrofolate synthetase. Cloning and
RT high expression of the Escherichia coli folC gene and purification and
RT properties of the gene product.";
RL J. Biol. Chem. 260:5625-5630(1985).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS VIA PROGRESSIVE DELETION FROM N- AND C-TER.
RX PubMed=1989505; DOI=10.1016/0003-9861(91)90254-g;
RA Kimlova L.J., Pyne C., Keshavjee K., Huy J., Beebakhee G., Bognar A.L.;
RT "Mutagenesis of the folC gene encoding folylpolyglutamate synthetase-
RT dihydrofolate synthetase in Escherichia coli.";
RL Arch. Biochem. Biophys. 284:9-16(1991).
RN [8]
RP FUNCTION, MUTAGENESIS OF THR-122; ASP-154 AND ALA-155, CHIMERA PROTEINS,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND DOMAIN.
RX PubMed=18232714; DOI=10.1021/bi701670y;
RA Sheng Y., Khanam N., Tsaksis Y., Shi X.M., Lu Q.S., Bognar A.L.;
RT "Mutagenesis of folylpolyglutamate synthetase indicates that
RT dihydropteroate and tetrahydrofolate bind to the same site.";
RL Biochemistry 47:2388-2396(2008).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) IN COMPLEXES WITH MAGNESIUM; ADP AND
RP PHOSPHORYLATED DIHYDROPTEROATE, COFACTOR, CARBOXYLATION AT LYS-188, AND
RP REACTION MECHANISM.
RX PubMed=15705579; DOI=10.1074/jbc.m413799200;
RA Mathieu M., Debousker G., Vincent S., Viviani F., Bamas-Jacques N.,
RA Mikol V.;
RT "Escherichia coli FolC structure reveals an unexpected dihydrofolate
RT binding site providing an attractive target for anti-microbial therapy.";
RL J. Biol. Chem. 280:18916-18922(2005).
CC -!- FUNCTION: Functions in two distinct reactions of the de novo folate
CC biosynthetic pathway. Catalyzes the addition of a glutamate residue to
CC dihydropteroate (7,8-dihydropteroate or H2Pte) to form dihydrofolate
CC (7,8-dihydrofolate monoglutamate or H2Pte-Glu). Also catalyzes
CC successive additions of L-glutamate to tetrahydrofolate or 10-
CC formyltetrahydrofolate or 5,10-methylenetetrahydrofolate, leading to
CC folylpolyglutamate derivatives. {ECO:0000269|PubMed:18232714,
CC ECO:0000269|PubMed:1989505, ECO:0000269|PubMed:2985605}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7,8-dihydropteroate + ATP + L-glutamate = 7,8-dihydrofolate +
CC ADP + H(+) + phosphate; Xref=Rhea:RHEA:23584, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17839, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57451, ChEBI:CHEBI:456216;
CC EC=6.3.2.12; Evidence={ECO:0000269|PubMed:18232714,
CC ECO:0000269|PubMed:1989505, ECO:0000269|PubMed:2985605};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + ATP + L-
CC glutamate = (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n+1) + ADP +
CC H(+) + phosphate; Xref=Rhea:RHEA:10580, Rhea:RHEA-COMP:14738,
CC Rhea:RHEA-COMP:14740, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:141005,
CC ChEBI:CHEBI:456216; EC=6.3.2.17;
CC Evidence={ECO:0000269|PubMed:18232714};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=10-formyltetrahydrofolyl-(gamma-L-Glu)(n) + ATP + L-glutamate
CC = 10-formyltetrahydrofolyl-(gamma-L-Glu)(n+1) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:51904, Rhea:RHEA-COMP:13088, Rhea:RHEA-
CC COMP:14300, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:134413, ChEBI:CHEBI:456216;
CC EC=6.3.2.17; Evidence={ECO:0000269|PubMed:1989505,
CC ECO:0000269|PubMed:2985605};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-5,10-methylenetetrahydrofolyl-(gamma-L-Glu)(n) + ATP + L-
CC glutamate = (6R)-5,10-methylenetetrahydrofolyl-(gamma-L-Glu)(n+1) +
CC ADP + H(+) + phosphate; Xref=Rhea:RHEA:51912, Rhea:RHEA-COMP:13257,
CC Rhea:RHEA-COMP:13258, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:136572,
CC ChEBI:CHEBI:456216; EC=6.3.2.17;
CC Evidence={ECO:0000269|PubMed:18232714};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:15705579};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000269|PubMed:15705579};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.6 uM for 7,8-dihydropteroate {ECO:0000269|PubMed:2985605};
CC KM=6.9 uM for ATP (in the assay for DHFS activity)
CC {ECO:0000269|PubMed:2985605};
CC KM=3.9 mM for glutamate (in the assay for DHFS activity)
CC {ECO:0000269|PubMed:2985605};
CC KM=0.6 uM for (6RS)-10-formyl-tetrahydropteroyl-gamma-Glu
CC {ECO:0000269|PubMed:2985605};
CC KM=66.5 uM for ATP (in the assay for FPGS activity)
CC {ECO:0000269|PubMed:2985605};
CC KM=333 uM for glutamate (in the assay for FPGS activity)
CC {ECO:0000269|PubMed:2985605};
CC KM=0.9 uM for 7,8-dihydropteroate {ECO:0000269|PubMed:1989505};
CC KM=10 uM for ATP (in the assay for DHFS activity)
CC {ECO:0000269|PubMed:1989505};
CC KM=2.8 mM for glutamate (in the assay for DHFS activity)
CC {ECO:0000269|PubMed:1989505};
CC KM=17 uM for 10-formyl-tetrahydropteroyl-gamma-Glu
CC {ECO:0000269|PubMed:1989505};
CC KM=54 uM for ATP (in the assay for FPGS activity)
CC {ECO:0000269|PubMed:1989505};
CC KM=300 uM for glutamate (in the assay for FPGS activity)
CC {ECO:0000269|PubMed:1989505};
CC KM=6.3 uM for 7,8-dihydropteroate {ECO:0000269|PubMed:18232714};
CC KM=50 uM for 5,10-methylenetetrahydrofolate
CC {ECO:0000269|PubMed:18232714};
CC KM=50 uM for tetrahydrofolate {ECO:0000269|PubMed:18232714};
CC KM=1.4 uM for tetrahydrofolate diglutamate
CC {ECO:0000269|PubMed:18232714};
CC Vmax=1.1 umol/h/mg enzyme for DHFS activity
CC {ECO:0000269|PubMed:1989505};
CC Vmax=4.1 umol/h/mg enzyme for FPGS activity with 10-formyl-
CC tetrahydropteroyl-gamma-Glu as substrate
CC {ECO:0000269|PubMed:1989505};
CC Vmax=415 umol/h/mg enzyme for FPGS activity with tetrahydrofolate as
CC substrate {ECO:0000269|PubMed:18232714};
CC Vmax=380 umol/h/mg enzyme for FPGS activity with tetrahydrofolate
CC diglutamate as substrate {ECO:0000269|PubMed:18232714};
CC Vmax=13 umol/h/mg enzyme for DHFS activity
CC {ECO:0000269|PubMed:18232714};
CC Note=kcat is 25 min(-1) with 7,8-dihydropteroate as substrate (at 30
CC degrees Celsius). {ECO:0000269|PubMed:2985605};
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-
CC dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-
CC dihydropteridine diphosphate and 4-aminobenzoate: step 2/2.
CC {ECO:0000305|PubMed:2985605}.
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolylpolyglutamate
CC biosynthesis. {ECO:0000305|PubMed:2985605}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:2985605}.
CC -!- DOMAIN: The N-terminal domain alone (residues 1-287) is sufficient to
CC bind both tetrahydrofolate and dihydropteroate with the same affinity
CC as the intact enzyme, but is not able to bind ATP and has no enzymatic
CC activity. {ECO:0000269|PubMed:18232714}.
CC -!- MISCELLANEOUS: Mutant studies have shown that dihydrofolate synthase
CC and folylpolyglutamate synthetase activities are catalyzed by a single
CC catalytic site. {ECO:0000269|PubMed:18232714,
CC ECO:0000269|PubMed:1989505}.
CC -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
CC {ECO:0000305}.
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DR EMBL; M32445; AAA23808.1; -; Genomic_DNA.
DR EMBL; J02808; AAA23802.1; -; Genomic_DNA.
DR EMBL; M68934; AAA23966.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75375.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16164.1; -; Genomic_DNA.
DR PIR; A65004; SYECFG.
DR RefSeq; NP_416818.1; NC_000913.3.
DR RefSeq; WP_000584546.1; NZ_LN832404.1.
DR PDB; 1W78; X-ray; 1.82 A; A=1-422.
DR PDB; 1W7K; X-ray; 2.10 A; A=1-422.
DR PDBsum; 1W78; -.
DR PDBsum; 1W7K; -.
DR AlphaFoldDB; P08192; -.
DR SMR; P08192; -.
DR BioGRID; 4261362; 413.
DR DIP; DIP-9674N; -.
DR IntAct; P08192; 10.
DR STRING; 511145.b2315; -.
DR BindingDB; P08192; -.
DR ChEMBL; CHEMBL3309008; -.
DR DrugBank; DB02437; (5r)-5-Amino-6-Hydroxyhexylcarbamic Acid.
DR DrugBank; DB03830; Phosphorylated Dihydropteroate.
DR DrugCentral; P08192; -.
DR jPOST; P08192; -.
DR PaxDb; P08192; -.
DR PRIDE; P08192; -.
DR EnsemblBacteria; AAC75375; AAC75375; b2315.
DR EnsemblBacteria; BAA16164; BAA16164; BAA16164.
DR GeneID; 945451; -.
DR KEGG; ecj:JW2312; -.
DR KEGG; eco:b2315; -.
DR PATRIC; fig|511145.12.peg.2410; -.
DR EchoBASE; EB0323; -.
DR eggNOG; COG0285; Bacteria.
DR HOGENOM; CLU_015869_1_0_6; -.
DR InParanoid; P08192; -.
DR OMA; YFEMGTL; -.
DR PhylomeDB; P08192; -.
DR BioCyc; EcoCyc:FOLC-MON; -.
DR BioCyc; MetaCyc:FOLC-MON; -.
DR BRENDA; 6.3.2.17; 2026.
DR UniPathway; UPA00077; UER00157.
DR UniPathway; UPA00850; -.
DR EvolutionaryTrace; P08192; -.
DR PRO; PR:P08192; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008841; F:dihydrofolate synthase activity; IDA:EcoCyc.
DR GO; GO:0097216; F:guanosine tetraphosphate binding; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IDA:EcoCyc.
DR GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009396; P:folic acid-containing compound biosynthetic process; IBA:GO_Central.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.1190.10; -; 1.
DR Gene3D; 3.90.190.20; -; 1.
DR InterPro; IPR001645; Folylpolyglutamate_synth.
DR InterPro; IPR018109; Folylpolyglutamate_synth_CS.
DR InterPro; IPR036565; Mur-like_cat_sf.
DR InterPro; IPR004101; Mur_ligase_C.
DR InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR InterPro; IPR013221; Mur_ligase_cen.
DR PANTHER; PTHR11136; PTHR11136; 1.
DR Pfam; PF02875; Mur_ligase_C; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR PIRSF; PIRSF001563; Folylpolyglu_synth; 1.
DR SUPFAM; SSF53244; SSF53244; 1.
DR SUPFAM; SSF53623; SSF53623; 1.
DR TIGRFAMs; TIGR01499; folC; 1.
DR PROSITE; PS01011; FOLYLPOLYGLU_SYNT_1; 1.
DR PROSITE; PS01012; FOLYLPOLYGLU_SYNT_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Folate biosynthesis; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; One-carbon metabolism;
KW Reference proteome.
FT CHAIN 1..422
FT /note="Dihydrofolate synthase/folylpolyglutamate synthase"
FT /id="PRO_0000168303"
FT BINDING 29..31
FT /ligand="7,8-dihydropteroate"
FT /ligand_id="ChEBI:CHEBI:17839"
FT /evidence="ECO:0000305|PubMed:15705579,
FT ECO:0007744|PDB:1W78"
FT BINDING 59..62
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:15705579,
FT ECO:0007744|PDB:1W78, ECO:0007744|PDB:1W7K"
FT BINDING 83
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15705579"
FT BINDING 122..125
FT /ligand="7,8-dihydropteroate"
FT /ligand_id="ChEBI:CHEBI:17839"
FT /evidence="ECO:0000305|PubMed:15705579,
FT ECO:0007744|PDB:1W78"
FT BINDING 146
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15705579"
FT BINDING 153..155
FT /ligand="7,8-dihydropteroate"
FT /ligand_id="ChEBI:CHEBI:17839"
FT /evidence="ECO:0000305|PubMed:15705579,
FT ECO:0007744|PDB:1W78"
FT BINDING 173
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15705579"
FT BINDING 257
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:15705579,
FT ECO:0007744|PDB:1W78, ECO:0007744|PDB:1W7K"
FT BINDING 289
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:15705579,
FT ECO:0007744|PDB:1W78, ECO:0007744|PDB:1W7K"
FT BINDING 302
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:15705579,
FT ECO:0007744|PDB:1W78, ECO:0007744|PDB:1W7K"
FT MOD_RES 188
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000269|PubMed:15705579"
FT MUTAGEN 122
FT /note="T->H,W: Causes large decrease in affinity for both
FT THF and DHP."
FT /evidence="ECO:0000269|PubMed:18232714"
FT MUTAGEN 154
FT /note="D->A: Severely impairs activity with THF as
FT substrate, even more so than with DHP. Both substrates show
FT a reduced affinity, but the catalytic rate with THF is 23-
FT fold lower than wild-type, whereas that with DHP is 2.5-
FT fold lower. The catalytic rate with THF diglutamate is 10-
FT fold higher than with monoglutamate and close to that of
FT the wild-type enzyme."
FT /evidence="ECO:0000269|PubMed:18232714"
FT MUTAGEN 155
FT /note="A->H: Causes large decrease in affinity for both THF
FT and DHP."
FT /evidence="ECO:0000269|PubMed:18232714"
FT CONFLICT 326
FT /note="V -> M (in Ref. 1; AAA23808/AAA23802)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="A -> AA (in Ref. 2; AAA23966)"
FT /evidence="ECO:0000305"
FT CONFLICT 391..392
FT /note="DA -> EP (in Ref. 2; AAA23966)"
FT /evidence="ECO:0000305"
FT HELIX 13..20
FT /evidence="ECO:0007829|PDB:1W78"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:1W78"
FT HELIX 33..42
FT /evidence="ECO:0007829|PDB:1W78"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:1W78"
FT HELIX 60..73
FT /evidence="ECO:0007829|PDB:1W78"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:1W78"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:1W78"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:1W78"
FT HELIX 102..115
FT /evidence="ECO:0007829|PDB:1W78"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:1W78"
FT HELIX 123..138
FT /evidence="ECO:0007829|PDB:1W78"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:1W78"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:1W78"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:1W78"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:1W78"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:1W78"
FT HELIX 181..188
FT /evidence="ECO:0007829|PDB:1W78"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:1W78"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:1W78"
FT HELIX 207..216
FT /evidence="ECO:0007829|PDB:1W78"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:1W78"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:1W78"
FT STRAND 227..231
FT /evidence="ECO:0007829|PDB:1W78"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:1W78"
FT STRAND 243..248
FT /evidence="ECO:0007829|PDB:1W78"
FT HELIX 255..268
FT /evidence="ECO:0007829|PDB:1W78"
FT HELIX 274..283
FT /evidence="ECO:0007829|PDB:1W78"
FT STRAND 289..294
FT /evidence="ECO:0007829|PDB:1W78"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:1W78"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:1W78"
FT HELIX 307..319
FT /evidence="ECO:0007829|PDB:1W78"
FT STRAND 326..330
FT /evidence="ECO:0007829|PDB:1W78"
FT HELIX 338..346
FT /evidence="ECO:0007829|PDB:1W78"
FT STRAND 350..354
FT /evidence="ECO:0007829|PDB:1W78"
FT STRAND 359..362
FT /evidence="ECO:0007829|PDB:1W78"
FT HELIX 365..372
FT /evidence="ECO:0007829|PDB:1W78"
FT HELIX 381..391
FT /evidence="ECO:0007829|PDB:1W78"
FT STRAND 397..403
FT /evidence="ECO:0007829|PDB:1W78"
FT HELIX 404..417
FT /evidence="ECO:0007829|PDB:1W78"
SQ SEQUENCE 422 AA; 45406 MW; 0C0F33D3CFB77705 CRC64;
MIIKRTPQAA SPLASWLSYL ENLHSKTIDL GLERVSLVAA RLGVLKPAPF VFTVAGTNGK
GTTCRTLESI LMAAGYKVGV YSSPHLVRYT ERVRVQGQEL PESAHTASFA EIESARGDIS
LTYFEYGTLS ALWLFKQAQL DVVILEVGLG GRLDATNIVD ADVAVVTSIA LDHTDWLGPD
RESIGREKAG IFRSEKPAIV GEPEMPSTIA DVAQEKGALL QRRGVEWNYS VTDHDWAFSD
AHGTLENLPL PLVPQPNAAT ALAALRASGL EVSENAIRDG IASAILPGRF QIVSESPRVI
FDVAHNPHAA EYLTGRMKAL PKNGRVLAVI GMLHDKDIAG TLAWLKSVVD DWYCAPLEGP
RGATAEQLLE HLGNGKSFDS VAQAWDAAMA DAKAEDTVLV CGSFHTVAHV MEVIDARRSG
GK
