(data stored in SCRATCH zone)

SWISSPROT: PGMB_LACLA

ID   PGMB_LACLA              Reviewed;         221 AA.
AC   P71447;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   08-MAY-2019, entry version 138.
DE   RecName: Full=Beta-phosphoglucomutase;
DE            Short=Beta-PGM;
DE            EC=5.4.2.6;
GN   Name=pgmB; OrderedLocusNames=LL0429; ORFNames=L0001;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus
OS   lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-15, FUNCTION
RP   AS A PHOSPHOGLUCOMUTASE AND IN THE CARBOHYDRATE METABOLISM, INDUCTION,
RP   SUBSTRATE SPECIFICITY, AND NOMENCLATURE.
RC   STRAIN=ATCC 19435 / DSM 20481 / NCDO 604 / NCIB 6681 / NCTC 6681;
RX   PubMed=9084169; DOI=10.1099/00221287-143-3-855;
RA   Qian N., Stanley G.A., Bunte A., Raadstroem P.;
RT   "Product formation and phosphoglucomutase activities in Lactococcus
RT   lactis: cloning and characterization of a novel phosphoglucomutase
RT   gene.";
RL   Microbiology 143:855-865(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.GR-1697R;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K.,
RA   Weissenbach J., Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
RN   [3]
RP   INDUCTION, SUBSTRATE SPECIFICITY, COFACTOR, AND SUBUNIT.
RX   PubMed=8071206; DOI=10.1128/jb.176.17.5304-5311.1994;
RA   Qian N., Stanley G.A., Hahn-Hagerdal B., Radstrom P.;
RT   "Purification and characterization of two phosphoglucomutases from
RT   Lactococcus lactis subsp. lactis and their regulation in maltose- and
RT   glucose-utilizing cells.";
RL   J. Bacteriol. 176:5304-5311(1994).
RN   [4]
RP   FUNCTION AS A BETA-PHOSPHOGLUCOMUTASE, MUTAGENESIS OF LYS-45; GLY-46;
RP   ARG-49 AND SER-52, INDUCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC 19435 / DSM 20481 / NCDO 604 / NCIB 6681 / NCTC 6681;
RX   PubMed=15005616; DOI=10.1021/bi0356810;
RA   Lahiri S.D., Zhang G., Dai J., Dunaway-Mariano D., Allen K.N.;
RT   "Analysis of the substrate specificity loop of the HAD superfamily cap
RT   domain.";
RL   Biochemistry 43:2812-2820(2004).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS,
RP   REACTION MECHANISM, AND SUBUNIT.
RX   PubMed=12081483; DOI=10.1021/bi0202373;
RA   Lahiri S.D., Zhang G., Dunaway-Mariano D., Allen K.N.;
RT   "Caught in the act: the structure of phosphorylated beta-
RT   phosphoglucomutase from Lactococcus lactis.";
RL   Biochemistry 41:8351-8359(2002).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) IN COMPLEX WITH SUBSTRATE
RP   ANALOGS AND MAGNESIUM IONS.
RX   PubMed=12637673; DOI=10.1126/science.1082710;
RA   Lahiri S.D., Zhang G., Dunaway-Mariano D., Allen K.N.;
RT   "The pentacovalent phosphorus intermediate of a phosphoryl transfer
RT   reaction.";
RL   Science 299:2067-2071(2003).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS,
RP   PHOSPHORYLATION AT ASP-8, MUTAGENESIS OF ASP-8 AND ASP-170, COFACTOR,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND REACTION MECHANISM.
RX   PubMed=15996095; DOI=10.1021/bi050558p;
RA   Zhang G., Dai J., Wang L., Dunaway-Mariano D., Tremblay L.W.,
RA   Allen K.N.;
RT   "Catalytic cycling in beta-phosphoglucomutase: a kinetic and
RT   structural analysis.";
RL   Biochemistry 44:9404-9416(2005).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH SUBSTRATE
RP   ANALOGS AND MAGNESIUM IONS, ACTIVITY REGULATION, AND SUBUNIT.
RX   PubMed=15826149; DOI=10.1021/ja0509073;
RA   Tremblay L.W., Zhang G., Dai J., Dunaway-Mariano D., Allen K.N.;
RT   "Chemical confirmation of a pentavalent phosphorane in complex with
RT   beta-phosphoglucomutase.";
RL   J. Am. Chem. Soc. 127:5298-5299(2005).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS,
RP   MUTAGENESIS OF ASP-10; THR-16; HIS-20 AND LYS-76, AND REACTION
RP   MECHANISM.
RX   PubMed=19154134; DOI=10.1021/bi801653r;
RA   Dai J., Finci L., Zhang C., Lahiri S., Zhang G., Peisach E.,
RA   Allen K.N., Dunaway-Mariano D.;
RT   "Analysis of the structural determinants underlying discrimination
RT   between substrate and solvent in beta-phosphoglucomutase catalysis.";
RL   Biochemistry 48:1984-1995(2009).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) IN COMPLEX WITH SUBSTRATE
RP   ANALOGS AND MAGNESIUM IONS.
RA   Bowler M.W., Baxter N.J., Webster C.E., Pollard S., Alizadeh T.,
RA   Hounslow A.M., Cliff M.J., Bermel W., Williams N.H., Hollfelder F.,
RA   Blackburn G.M., Waltho J.P.;
RT   "The role of strain in enzyme catalysed phosphate transfer.";
RL   Submitted (APR-2009) to the PDB data bank.
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) IN COMPLEX WITH SUBSTRATE
RP   ANALOGS AND MAGNESIUM IONS.
RX   PubMed=20164409; DOI=10.1073/pnas.0910333106;
RA   Baxter N.J., Bowler M.W., Alizadeh T., Cliff M.J., Hounslow A.M.,
RA   Wu B., Berkowitz D.B., Williams N.H., Blackburn G.M., Waltho J.P.;
RT   "Atomic details of near-transition state conformers for enzyme
RT   phosphoryl transfer revealed by MgF-3 rather than by phosphoranes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:4555-4560(2010).
CC   -!- FUNCTION: Catalyzes the interconversion of D-glucose 1-phosphate
CC       (G1P) and D-glucose 6-phosphate (G6P), forming beta-D-glucose 1,6-
CC       (bis)phosphate (beta-G16P) as an intermediate. The beta-
CC       phosphoglucomutase (Beta-PGM) acts on the beta-C(1) anomer of G1P.
CC       Glucose or lactose are used in preference to maltose, which is
CC       only utilized after glucose or lactose has been exhausted. It
CC       plays a key role in the regulation of the flow of carbohydrate
CC       intermediates in glycolysis and the formation of the sugar
CC       nucleotide UDP-glucose. {ECO:0000269|PubMed:15005616,
CC       ECO:0000269|PubMed:9084169}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-glucose 1-phosphate = beta-D-glucose 6-phosphate;
CC         Xref=Rhea:RHEA:20113, ChEBI:CHEBI:57684, ChEBI:CHEBI:58247;
CC         EC=5.4.2.6;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:15996095,
CC         ECO:0000269|PubMed:8071206};
CC       Note=Binds 2 magnesium ions per subunit.
CC       {ECO:0000269|PubMed:15996095, ECO:0000269|PubMed:8071206};
CC   -!- ACTIVITY REGULATION: Competitively inhibited by alpha-D-galactose-
CC       1-phosphate. {ECO:0000269|PubMed:15826149}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=14.6 uM for beta-glucose 1-phosphate (at pH 7 and 25 degrees
CC         Celsius) {ECO:0000269|PubMed:15005616,
CC         ECO:0000269|PubMed:15996095};
CC         KM=20 uM for alpha-D-glucose 1,6-bisphosphate (at pH 7 and 25
CC         degrees Celsius) {ECO:0000269|PubMed:15005616,
CC         ECO:0000269|PubMed:15996095};
CC         KM=100 uM for alpha-D-fructose 1,6-bisphosphate (at pH 7 and 25
CC         degrees Celsius) {ECO:0000269|PubMed:15005616,
CC         ECO:0000269|PubMed:15996095};
CC         KM=270 uM for magnesium (at pH 7 and 25 degrees Celsius)
CC         {ECO:0000269|PubMed:15005616, ECO:0000269|PubMed:15996095};
CC         KM=800 uM for acetyl-phosphate (at pH 7 and 25 degrees Celsius)
CC         {ECO:0000269|PubMed:15005616, ECO:0000269|PubMed:15996095};
CC       pH dependence:
CC         Optimum pH is around 7. Relatively stable in solution within the
CC         pH range of 5-9.5. {ECO:0000269|PubMed:15005616,
CC         ECO:0000269|PubMed:15996095};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12081483,
CC       ECO:0000269|PubMed:12637673, ECO:0000269|PubMed:15826149,
CC       ECO:0000269|PubMed:15996095, ECO:0000269|PubMed:19154134,
CC       ECO:0000269|PubMed:20164409, ECO:0000269|PubMed:8071206,
CC       ECO:0000269|Ref.10}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- INDUCTION: By maltose, trehalose and sucrose and repressed by
CC       glucose and lactose. {ECO:0000269|PubMed:15005616,
CC       ECO:0000269|PubMed:8071206, ECO:0000269|PubMed:9084169}.
CC   -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:15996095}.
CC   -!- MISCELLANEOUS: The catalysis proceeds via a phosphoenzyme formed
CC       by reaction of an active-site nucleophile with the cofactor
CC       glucose 1,6-diphosphate (G1,6-diP). The phosphorylated mutase
CC       binds either G1P or G6P and transfers the phosphoryl group to the
CC       C(6)OH or C(1)OH, respectively.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC       CbbY/CbbZ/Gph/YieH family. {ECO:0000305}.
DR   EMBL; Z70730; CAA94734.1; -; Genomic_DNA.
DR   EMBL; AE005176; AAK04527.1; -; Genomic_DNA.
DR   PIR; E86678; E86678.
DR   RefSeq; NP_266585.1; NC_002662.1.
DR   RefSeq; WP_010905331.1; NC_002662.1.
DR   PDB; 1LVH; X-ray; 2.30 A; A/B=1-221.
DR   PDB; 1O03; X-ray; 1.40 A; A=1-221.
DR   PDB; 1O08; X-ray; 1.20 A; A=1-221.
DR   PDB; 1Z4N; X-ray; 1.97 A; A/B=1-221.
DR   PDB; 1Z4O; X-ray; 1.90 A; A/B=1-221.
DR   PDB; 1ZOL; X-ray; 1.90 A; A=1-221.
DR   PDB; 2WF5; X-ray; 1.30 A; A=1-221.
DR   PDB; 2WF6; X-ray; 1.40 A; A=1-221.
DR   PDB; 2WF7; X-ray; 1.05 A; A=1-221.
DR   PDB; 2WF8; X-ray; 1.20 A; A=1-221.
DR   PDB; 2WF9; X-ray; 1.40 A; A=1-221.
DR   PDB; 2WFA; X-ray; 1.65 A; A=1-221.
DR   PDB; 2WHE; X-ray; 1.55 A; A=1-221.
DR   PDB; 3FM9; X-ray; 2.70 A; A=1-221.
DR   PDB; 3ZI4; X-ray; 1.33 A; A=1-221.
DR   PDB; 4C4R; X-ray; 1.10 A; A=1-221.
DR   PDB; 4C4S; X-ray; 1.50 A; A=1-221.
DR   PDB; 4C4T; X-ray; 1.50 A; A=1-221.
DR   PDB; 5O6P; X-ray; 2.20 A; A=1-221.
DR   PDB; 5O6R; X-ray; 1.36 A; A=1-221.
DR   PDB; 5OJZ; X-ray; 1.30 A; A=1-220.
DR   PDB; 5OK0; X-ray; 2.15 A; A=1-218.
DR   PDB; 5OK1; X-ray; 1.86 A; A=1-218.
DR   PDB; 5OK2; X-ray; 1.10 A; A=1-218.
DR   PDB; 5OLW; X-ray; 2.28 A; A/B=1-221.
DR   PDB; 5OLX; X-ray; 1.38 A; A=1-221.
DR   PDB; 5OLY; X-ray; 2.00 A; A/G=1-221.
DR   PDBsum; 1LVH; -.
DR   PDBsum; 1O03; -.
DR   PDBsum; 1O08; -.
DR   PDBsum; 1Z4N; -.
DR   PDBsum; 1Z4O; -.
DR   PDBsum; 1ZOL; -.
DR   PDBsum; 2WF5; -.
DR   PDBsum; 2WF6; -.
DR   PDBsum; 2WF7; -.
DR   PDBsum; 2WF8; -.
DR   PDBsum; 2WF9; -.
DR   PDBsum; 2WFA; -.
DR   PDBsum; 2WHE; -.
DR   PDBsum; 3FM9; -.
DR   PDBsum; 3ZI4; -.
DR   PDBsum; 4C4R; -.
DR   PDBsum; 4C4S; -.
DR   PDBsum; 4C4T; -.
DR   PDBsum; 5O6P; -.
DR   PDBsum; 5O6R; -.
DR   PDBsum; 5OJZ; -.
DR   PDBsum; 5OK0; -.
DR   PDBsum; 5OK1; -.
DR   PDBsum; 5OK2; -.
DR   PDBsum; 5OLW; -.
DR   PDBsum; 5OLX; -.
DR   PDBsum; 5OLY; -.
DR   SMR; P71447; -.
DR   STRING; 272623.L0001; -.
DR   DrugBank; DB02317; Alpha-D-Galactose-1-Phosphate.
DR   DrugBank; DB01857; Phosphoaspartate.
DR   PaxDb; P71447; -.
DR   EnsemblBacteria; AAK04527; AAK04527; L0001.
DR   GeneID; 1114041; -.
DR   KEGG; lla:L0001; -.
DR   PATRIC; fig|272623.7.peg.467; -.
DR   eggNOG; ENOG4107URF; Bacteria.
DR   eggNOG; COG0637; LUCA.
DR   KO; K01838; -.
DR   OMA; AAWKEMF; -.
DR   BioCyc; LLAC272623:L0001-MONOMER; -.
DR   BioCyc; MetaCyc:MONOMER-5821; -.
DR   BRENDA; 5.4.2.6; 2903.
DR   SABIO-RK; P71447; -.
DR   EvolutionaryTrace; P71447; -.
DR   Proteomes; UP000002196; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008801; F:beta-phosphoglucomutase activity; IDA:UniProtKB.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IDA:UniProtKB.
DR   Gene3D; 1.10.150.240; -; 1.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR010976; B-phosphoglucomutase_hydrolase.
DR   InterPro; IPR010972; Beta-phosphoglucomutase.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006439; HAD-SF_hydro_IA.
DR   InterPro; IPR041492; HAD_2.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR023198; PGP-like_dom2.
DR   Pfam; PF13419; HAD_2; 1.
DR   PRINTS; PR00413; HADHALOGNASE.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01990; bPGM; 1.
DR   TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
DR   TIGRFAMs; TIGR02009; PGMB-YQAB-SF; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P71447.
DR   SWISS-2DPAGE; P71447.
KW   3D-structure; Carbohydrate metabolism; Complete proteome; Cytoplasm;
KW   Direct protein sequencing; Isomerase; Magnesium; Metal-binding;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN         1    221       Beta-phosphoglucomutase.
FT                                /FTId=PRO_0000108053.
FT   REGION        8     10       Substrate binding.
FT   REGION       44     49       Substrate binding.
FT   REGION      114    118       Substrate binding.
FT   ACT_SITE      8      8       Nucleophile.
FT   ACT_SITE     10     10       Proton donor.
FT   METAL         8      8       Magnesium 1.
FT   METAL         8      8       Magnesium 2.
FT   METAL        10     10       Magnesium 1.
FT   METAL        10     10       Magnesium 2; via carbonyl oxygen.
FT   METAL       169    169       Magnesium 1.
FT   METAL       170    170       Magnesium 1.
FT   METAL       170    170       Magnesium 2.
FT   BINDING      24     24       Substrate.
FT   BINDING      52     52       Substrate.
FT   BINDING      76     76       Substrate.
FT   BINDING     145    145       Substrate.
FT   SITE        114    114       Important for catalytic activity and
FT                                assists the phosphoryl transfer reaction
FT                                to Asp8 by balancing charge and orienting
FT                                the reacting groups.
FT   SITE        145    145       Important for catalytic activity and
FT                                assists the phosphoryl transfer reaction
FT                                to Asp8 by balancing charge and orienting
FT                                the reacting groups.
FT   MOD_RES       8      8       4-aspartylphosphate.
FT                                {ECO:0000269|PubMed:15996095}.
FT   MUTAGEN       8      8       D->A: Inactive.
FT                                {ECO:0000269|PubMed:15996095}.
FT   MUTAGEN       8      8       D->E: Inactive.
FT                                {ECO:0000269|PubMed:15996095}.
FT   MUTAGEN      10     10       D->A: Inactive.
FT                                {ECO:0000269|PubMed:19154134}.
FT   MUTAGEN      10     10       D->E: Inactive.
FT                                {ECO:0000269|PubMed:19154134}.
FT   MUTAGEN      10     10       D->N: Inactive.
FT                                {ECO:0000269|PubMed:19154134}.
FT   MUTAGEN      10     10       D->S: Inactive.
FT                                {ECO:0000269|PubMed:19154134}.
FT   MUTAGEN      16     16       T->P: 500-fold reduction in the rate
FT                                constant for Asp-8 phosphorylation by
FT                                beta-G1,6bisP. 6,700-fold reduction in
FT                                the apparent rate constant for cycling of
FT                                the phosphorylated enzyme to convert
FT                                beta-G1P to G6P. 13-fold increase in the
FT                                estimated rate constant for phosphoryl
FT                                transfer from the phospho-Asp8 to water.
FT                                {ECO:0000269|PubMed:19154134}.
FT   MUTAGEN      20     20       H->A: Impairs Asp-8 phosphorylation by
FT                                beta-G1,6bisP and phosphoryl transfer
FT                                from the phospho-Asp8 to the substrate
FT                                beta-G1P. {ECO:0000269|PubMed:19154134}.
FT   MUTAGEN      20     20       H->N: 300-fold reduction in the
FT                                conversion of beta-G1P to G6P in the
FT                                presence of beta-G1,6bisP.
FT                                {ECO:0000269|PubMed:19154134}.
FT   MUTAGEN      20     20       H->Q: 8-fold reduction in the conversion
FT                                of beta-G1P to G6P in the presence of
FT                                beta-G1,6bisP.
FT                                {ECO:0000269|PubMed:19154134}.
FT   MUTAGEN      45     45       K->A: 20'000-fold decrease in Kcat/KM.
FT                                {ECO:0000269|PubMed:15005616}.
FT   MUTAGEN      46     46       G->A: 1'000'000-fold decrease in Kcat/KM.
FT                                {ECO:0000269|PubMed:15005616}.
FT   MUTAGEN      46     46       G->P: 100'000-fold decrease in Kcat/KM.
FT                                {ECO:0000269|PubMed:15005616}.
FT   MUTAGEN      46     46       G->V: 10'000-fold decrease in Kcat/KM.
FT                                {ECO:0000269|PubMed:15005616}.
FT   MUTAGEN      49     49       R->K: 1'000'000-fold decrease in Kcat/KM.
FT                                {ECO:0000269|PubMed:15005616}.
FT   MUTAGEN      52     52       S->A: Wild-type activity.
FT                                {ECO:0000269|PubMed:15005616}.
FT   MUTAGEN      76     76       K->A: 100-fold reduction in the
FT                                conversion of beta-G1P to G6P in the
FT                                presence of beta-G1,6bisP.
FT                                {ECO:0000269|PubMed:19154134}.
FT   MUTAGEN     170    170       D->A: Impaired, but active with an
FT                                increase in the affinity for G1P.
FT                                {ECO:0000269|PubMed:15996095}.
FT   CONFLICT    125    125       K -> R (in Ref. 1; CAA94734).
FT                                {ECO:0000305}.
FT   CONFLICT    206    206       Y -> H (in Ref. 1; CAA94734).
FT                                {ECO:0000305}.
FT   STRAND        4      7       {ECO:0000244|PDB:2WF7}.
FT   TURN         10     12       {ECO:0000244|PDB:2WF7}.
FT   STRAND       13     15       {ECO:0000244|PDB:2WF7}.
FT   HELIX        16     30       {ECO:0000244|PDB:2WF7}.
FT   HELIX        38     41       {ECO:0000244|PDB:2WF7}.
FT   TURN         42     46       {ECO:0000244|PDB:2WF7}.
FT   HELIX        49     59       {ECO:0000244|PDB:2WF7}.
FT   STRAND       60     62       {ECO:0000244|PDB:1O08}.
FT   HELIX        66     83       {ECO:0000244|PDB:2WF7}.
FT   HELIX        84     86       {ECO:0000244|PDB:2WF7}.
FT   HELIX        89     91       {ECO:0000244|PDB:2WF7}.
FT   HELIX        96    105       {ECO:0000244|PDB:2WF7}.
FT   STRAND      109    112       {ECO:0000244|PDB:2WF7}.
FT   HELIX       119    125       {ECO:0000244|PDB:2WF7}.
FT   HELIX       129    131       {ECO:0000244|PDB:2WF7}.
FT   STRAND      133    135       {ECO:0000244|PDB:2WF7}.
FT   TURN        138    140       {ECO:0000244|PDB:2WF7}.
FT   STRAND      141    143       {ECO:0000244|PDB:2WF7}.
FT   HELIX       149    157       {ECO:0000244|PDB:2WF7}.
FT   HELIX       162    164       {ECO:0000244|PDB:2WF7}.
FT   STRAND      165    171       {ECO:0000244|PDB:2WF7}.
FT   HELIX       172    181       {ECO:0000244|PDB:2WF7}.
FT   STRAND      184    189       {ECO:0000244|PDB:2WF7}.
FT   HELIX       191    194       {ECO:0000244|PDB:2WF7}.
FT   STRAND      196    203       {ECO:0000244|PDB:2WF7}.
FT   HELIX       204    206       {ECO:0000244|PDB:2WF7}.
FT   HELIX       209    217       {ECO:0000244|PDB:2WF7}.
FT   HELIX       218    221       {ECO:0000244|PDB:5OLW}.
SQ   SEQUENCE   221 AA;  24209 MW;  53AC0BF0FA249EFC CRC64;
     MFKAVLFDLD GVITDTAEYH FRAWKALAEE IGINGVDRQF NEQLKGVSRE DSLQKILDLA
     DKKVSAEEFK ELAKRKNDNY VKMIQDVSPA DVYPGILQLL KDLRSNKIKI ALASASKNGP
     FLLEKMNLTG YFDAIADPAE VAASKPAPDI FIAAAHAVGV APSESIGLED SQAGIQAIKD
     SGALPIGVGR PEDLGDDIVI VPDTSYYTLE FLKEVWLQKQ K
//

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