ASPG2_ECOLI
ID ASPG2_ECOLI Reviewed; 348 AA.
AC P00805; Q2M9N6;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=L-asparaginase 2;
DE EC=3.5.1.1;
DE AltName: Full=L-asparaginase II;
DE Short=L-ASNase II;
DE AltName: Full=L-asparagine amidohydrolase II;
DE AltName: INN=Colaspase;
DE Flags: Precursor;
GN Name=ansB; OrderedLocusNames=b2957, JW2924;
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=2407723; DOI=10.1128/jb.172.3.1491-1498.1990;
RA Jennings M.P., Beacham I.R.;
RT "Analysis of the Escherichia coli gene encoding L-asparaginase II, ansB,
RT and its regulation by cyclic AMP receptor and FNR proteins.";
RL J. Bacteriol. 172:1491-1498(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2144836; DOI=10.1016/0378-1119(90)90168-q;
RA Bonthron D.T.;
RT "L-asparaginase II of Escherichia coli K-12: cloning, mapping and
RT sequencing of the ansB gene.";
RL Gene 91:101-105(1990).
RN [3]
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 [4]
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 [5]
RP PROTEIN SEQUENCE OF 23-348.
RX PubMed=6766894; DOI=10.1515/bchm2.1980.361.1.105;
RA Maita T., Matsuda G.;
RT "The primary structure of L-asparaginase from Escherichia coli.";
RL Hoppe-Seyler's Z. Physiol. Chem. 361:105-117(1980).
RN [6]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=387570; DOI=10.1515/bchm2.1979.360.2.1483;
RA Maita T., Morokuma K., Matsuda G.;
RT "Amino acid sequences of the tryptic peptides from carboxymethylated L-
RT asparaginase from Escherichia coli.";
RL Hoppe-Seyler's Z. Physiol. Chem. 360:1483-1495(1979).
RN [7]
RP ACTIVE SITE.
RX PubMed=321449; DOI=10.1016/s0021-9258(18)71866-8;
RA Peterson R.G., Richards F.F., Handschumacher R.E.;
RT "Structure of peptide from active site region of Escherichia coli L-
RT asparaginase.";
RL J. Biol. Chem. 252:2072-2076(1977).
RN [8]
RP SUBUNIT.
RX PubMed=4561256; DOI=10.1016/0003-9861(72)90216-0;
RA Greenquist A.C., Wriston J.C. Jr.;
RT "Chemical evidence for identical subunits in L-asparaginase from
RT Escherichia coli B.";
RL Arch. Biochem. Biophys. 152:280-286(1972).
RN [9]
RP ACTIVE SITE THR-34, MUTAGENESIS OF THR-34, AND SUBUNIT.
RX PubMed=1906013; DOI=10.1016/0014-5793(91)80723-g;
RA Harms E., Wehner A., Aung H.P., Roehm K.H.;
RT "A catalytic role for threonine-12 of E. coli asparaginase II as
RT established by site-directed mutagenesis.";
RL FEBS Lett. 285:55-58(1991).
RN [10]
RP MUTAGENESIS OF HISTIDINE RESIDUES.
RX PubMed=1521538; DOI=10.1111/j.1432-1033.1992.tb17210.x;
RA Wehner A., Harms E., Jennings M.P., Beacham I.R., Derst C., Bast P.,
RA Roehm K.H.;
RT "Site-specific mutagenesis of Escherichia coli asparaginase II. None of the
RT three histidine residues is required for catalysis.";
RL Eur. J. Biochem. 208:475-480(1992).
RN [11]
RP MUTAGENESIS OF THREONINE AND SERINE RESIDUES.
RX PubMed=1287659; DOI=10.1093/protein/5.8.785;
RA Ders C., Henseling J., Roehm K.H.;
RT "Probing the role of threonine and serine residues of E. coli asparaginase
RT II by site-specific mutagenesis.";
RL Protein Eng. 5:785-789(1992).
RN [12] {ECO:0007744|PDB:3ECA}
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH ASPARTIC ACID,
RP DISULFIDE BOND, AND SUBUNIT.
RX PubMed=8434007; DOI=10.1073/pnas.90.4.1474;
RA Swain A.L., Jaskolski M., Housset D., Rao J.K.M., Wlodawer A.;
RT "Crystal structure of Escherichia coli L-asparaginase, an enzyme used in
RT cancer therapy.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:1474-1478(1993).
RN [13] {ECO:0007744|PDB:4ECA}
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT VAL-111, ACTIVE SITE,
RP MUTAGENESIS OF THR-111, CATALYTIC ACTIVITY, SUBUNIT, AND DISULFIDE BOND.
RX PubMed=8706862; DOI=10.1016/0014-5793(96)00660-6;
RA Palm G.J., Lubkowski J., Derst C., Schleper S., Roehm K.H., Wlodawer A.;
RT "A covalently bound catalytic intermediate in Escherichia coli
RT asparaginase: crystal structure of a Thr-89-Val mutant.";
RL FEBS Lett. 390:211-216(1996).
RN [14] {ECO:0007744|PDB:1NNS}
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 23-348 IN COMPLEXES WITH ASPARTIC
RP ACID, AND SUBUNIT.
RX PubMed=12595697; DOI=10.1107/s0907444902021200;
RA Sanches M., Barbosa J.A., de Oliveira R.T., Abrahao Neto J., Polikarpov I.;
RT "Structural comparison of Escherichia coli L-asparaginase in two monoclinic
RT space groups.";
RL Acta Crystallogr. D 59:416-422(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-asparagine = L-aspartate + NH4(+);
CC Xref=Rhea:RHEA:21016, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29991, ChEBI:CHEBI:58048; EC=3.5.1.1;
CC Evidence={ECO:0000269|PubMed:8706862};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.115 uM for L-asparagine;
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12595697,
CC ECO:0000269|PubMed:1906013, ECO:0000269|PubMed:4561256,
CC ECO:0000269|PubMed:8434007, ECO:0000269|PubMed:8706862}.
CC -!- INTERACTION:
CC P00805; P00805: ansB; NbExp=2; IntAct=EBI-907458, EBI-907458;
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- INDUCTION: By cAMP and anaerobiosis.
CC -!- PHARMACEUTICAL: Available under the names Crastinin (Bayer), Elspar
CC (Merck), Kidrolase (Rhone-Poulenc) and Leunase (Kyowa). Also available
CC as a PEG-conjugated form (Pegaspargase) under the name Oncaspar
CC (Enzon). Used as an antineoplastic in chemotherapy. Reduces the
CC quantity of asparagine available to cancer cells.
CC -!- MISCELLANEOUS: E.coli contains two L-asparaginase isoenzymes: L-
CC asparaginase I, a low-affinity enzyme located in the cytoplasm, and L-
CC asparaginase II, a high-affinity secreted enzyme.
CC -!- SIMILARITY: Belongs to the asparaginase 1 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC URL="https://www.worthington-biochem.com/ASPR/";
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; M34277; AAA24062.1; -; Genomic_DNA.
DR EMBL; M34234; AAA23445.1; -; Genomic_DNA.
DR EMBL; U28377; AAA69124.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75994.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77020.1; -; Genomic_DNA.
DR PIR; A35132; XDEC.
DR RefSeq; NP_417432.1; NC_000913.3.
DR RefSeq; WP_000394140.1; NZ_LN832404.1.
DR PDB; 1HO3; X-ray; 2.50 A; A/B=23-348.
DR PDB; 1IHD; X-ray; 2.65 A; A/C=23-348.
DR PDB; 1JAZ; X-ray; 2.27 A; A/B=23-348.
DR PDB; 1JJA; X-ray; 2.30 A; A/B/C/D/E/F=23-348.
DR PDB; 1NNS; X-ray; 1.95 A; A/B=23-348.
DR PDB; 3ECA; X-ray; 2.40 A; A/B/C/D=23-348.
DR PDB; 4ECA; X-ray; 2.20 A; A/B/C/D=23-348.
DR PDB; 5MQ5; X-ray; 1.60 A; A/B/C/D=23-348.
DR PDB; 6EOK; X-ray; 2.50 A; A/B/C/D=23-348.
DR PDB; 6NX6; X-ray; 2.15 A; A/B=23-348.
DR PDB; 6NX7; X-ray; 2.15 A; A/B=23-348.
DR PDB; 6NX8; X-ray; 1.85 A; A/B=23-348.
DR PDB; 6NX9; X-ray; 1.97 A; A/B/C/D=23-348.
DR PDB; 6NXA; X-ray; 1.93 A; A/B/C/D=23-348.
DR PDB; 6NXB; X-ray; 1.75 A; A/B/C/D=23-348.
DR PDB; 6PA2; X-ray; 1.90 A; A/B/C/D=23-348.
DR PDB; 6PA3; X-ray; 1.65 A; A/B/C/D=23-348.
DR PDB; 6PA4; X-ray; 1.85 A; A/B/C/D=23-348.
DR PDB; 6PA5; X-ray; 2.00 A; A/B/C/D/E/F/G/H=23-348.
DR PDB; 6PA6; X-ray; 2.12 A; A/B/C/D=23-348.
DR PDB; 6PA8; X-ray; 1.90 A; A/B/C/D=23-348.
DR PDB; 6PA9; X-ray; 1.88 A; A/B=23-348.
DR PDB; 6PAA; X-ray; 1.85 A; A/B/C/D=23-348.
DR PDB; 6PAB; X-ray; 1.73 A; A/B/C/D=23-348.
DR PDB; 6PAC; X-ray; 1.60 A; A/B/C/D=23-348.
DR PDB; 6UOD; X-ray; 2.40 A; A/B/C/D=23-348.
DR PDB; 6UOG; X-ray; 2.29 A; A/B/C/D/E/F/G/H=23-348.
DR PDB; 6UOH; X-ray; 2.10 A; A/B=23-348.
DR PDB; 6V23; X-ray; 1.75 A; A=23-348.
DR PDB; 6V24; X-ray; 1.90 A; A/B/C/D=23-348.
DR PDB; 6V25; X-ray; 1.78 A; A/B/C/D=23-348.
DR PDB; 6V26; X-ray; 1.80 A; A/B/C/D=23-348.
DR PDB; 6V27; X-ray; 2.30 A; A/B/C/D=23-348.
DR PDB; 6V28; X-ray; 1.95 A; A/B/C/D=23-348.
DR PDB; 6V29; X-ray; 2.00 A; A/B/C/D=23-348.
DR PDB; 6V2A; X-ray; 2.00 A; A/B/C/D=23-348.
DR PDB; 6V2B; X-ray; 2.05 A; A/B/C/D=23-348.
DR PDB; 6V2C; X-ray; 2.00 A; A/B/C/D=23-348.
DR PDB; 6V2G; X-ray; 1.90 A; A/B/C/D=23-348.
DR PDB; 6V5F; X-ray; 2.10 A; A/B/C/D=23-348.
DR PDB; 7A0U; X-ray; 2.26 A; A/B/C/D=23-348.
DR PDB; 7M11; X-ray; 1.83 A; A/B/C/D=23-348.
DR PDB; 7P9C; X-ray; 1.60 A; A/B/C/D=23-348.
DR PDBsum; 1HO3; -.
DR PDBsum; 1IHD; -.
DR PDBsum; 1JAZ; -.
DR PDBsum; 1JJA; -.
DR PDBsum; 1NNS; -.
DR PDBsum; 3ECA; -.
DR PDBsum; 4ECA; -.
DR PDBsum; 5MQ5; -.
DR PDBsum; 6EOK; -.
DR PDBsum; 6NX6; -.
DR PDBsum; 6NX7; -.
DR PDBsum; 6NX8; -.
DR PDBsum; 6NX9; -.
DR PDBsum; 6NXA; -.
DR PDBsum; 6NXB; -.
DR PDBsum; 6PA2; -.
DR PDBsum; 6PA3; -.
DR PDBsum; 6PA4; -.
DR PDBsum; 6PA5; -.
DR PDBsum; 6PA6; -.
DR PDBsum; 6PA8; -.
DR PDBsum; 6PA9; -.
DR PDBsum; 6PAA; -.
DR PDBsum; 6PAB; -.
DR PDBsum; 6PAC; -.
DR PDBsum; 6UOD; -.
DR PDBsum; 6UOG; -.
DR PDBsum; 6UOH; -.
DR PDBsum; 6V23; -.
DR PDBsum; 6V24; -.
DR PDBsum; 6V25; -.
DR PDBsum; 6V26; -.
DR PDBsum; 6V27; -.
DR PDBsum; 6V28; -.
DR PDBsum; 6V29; -.
DR PDBsum; 6V2A; -.
DR PDBsum; 6V2B; -.
DR PDBsum; 6V2C; -.
DR PDBsum; 6V2G; -.
DR PDBsum; 6V5F; -.
DR PDBsum; 7A0U; -.
DR PDBsum; 7M11; -.
DR PDBsum; 7P9C; -.
DR AlphaFoldDB; P00805; -.
DR SMR; P00805; -.
DR BioGRID; 4259243; 267.
DR BioGRID; 851774; 4.
DR DIP; DIP-9110N; -.
DR IntAct; P00805; 8.
DR MINT; P00805; -.
DR STRING; 511145.b2957; -.
DR DrugBank; DB01817; Threonine-Aspartic Ester.
DR Allergome; 8365; Esc c Asparaginase.
DR jPOST; P00805; -.
DR PaxDb; P00805; -.
DR PRIDE; P00805; -.
DR EnsemblBacteria; AAC75994; AAC75994; b2957.
DR EnsemblBacteria; BAE77020; BAE77020; BAE77020.
DR GeneID; 947454; -.
DR KEGG; ecj:JW2924; -.
DR KEGG; eco:b2957; -.
DR PATRIC; fig|1411691.4.peg.3775; -.
DR EchoBASE; EB0044; -.
DR eggNOG; COG0252; Bacteria.
DR HOGENOM; CLU_019134_1_2_6; -.
DR InParanoid; P00805; -.
DR OMA; RKNHTSR; -.
DR PhylomeDB; P00805; -.
DR BioCyc; EcoCyc:ANSB-MON; -.
DR BioCyc; MetaCyc:ANSB-MON; -.
DR BRENDA; 3.5.1.1; 2026.
DR SABIO-RK; P00805; -.
DR EvolutionaryTrace; P00805; -.
DR PRO; PR:P00805; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0042597; C:periplasmic space; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
DR GO; GO:0004067; F:asparaginase activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0006530; P:asparagine catabolic process; IBA:GO_Central.
DR GO; GO:0051289; P:protein homotetramerization; IDA:EcoCyc.
DR Gene3D; 3.40.50.1170; -; 1.
DR Gene3D; 3.40.50.40; -; 1.
DR InterPro; IPR004550; AsnASE_II.
DR InterPro; IPR036152; Asp/glu_Ase-like_sf.
DR InterPro; IPR006034; Asparaginase/glutaminase-like.
DR InterPro; IPR020827; Asparaginase/glutaminase_AS1.
DR InterPro; IPR027475; Asparaginase/glutaminase_AS2.
DR InterPro; IPR040919; Asparaginase_C.
DR InterPro; IPR027473; L-asparaginase_C.
DR InterPro; IPR027474; L-asparaginase_N.
DR InterPro; IPR037152; L-asparaginase_N_sf.
DR Pfam; PF00710; Asparaginase; 1.
DR Pfam; PF17763; Asparaginase_C; 1.
DR PIRSF; PIRSF001220; L-ASNase_gatD; 1.
DR PRINTS; PR00139; ASNGLNASE.
DR SMART; SM00870; Asparaginase; 1.
DR SUPFAM; SSF53774; SSF53774; 1.
DR TIGRFAMs; TIGR00520; asnASE_II; 1.
DR PROSITE; PS00144; ASN_GLN_ASE_1; 1.
DR PROSITE; PS00917; ASN_GLN_ASE_2; 1.
DR PROSITE; PS51732; ASN_GLN_ASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Periplasm; Pharmaceutical; Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:6766894"
FT CHAIN 23..348
FT /note="L-asparaginase 2"
FT /id="PRO_0000002356"
FT DOMAIN 24..348
FT /note="Asparaginase/glutaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01068"
FT ACT_SITE 34
FT /note="O-isoaspartyl threonine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10099,
FT ECO:0000255|PROSITE-ProRule:PRU10100,
FT ECO:0000269|PubMed:12595697, ECO:0000269|PubMed:1906013,
FT ECO:0000269|PubMed:8434007, ECO:0000269|PubMed:8706862"
FT BINDING 80..81
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12595697,
FT ECO:0000269|PubMed:8434007, ECO:0007744|PDB:1NNS,
FT ECO:0007744|PDB:3ECA"
FT BINDING 111..112
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12595697,
FT ECO:0000269|PubMed:8434007, ECO:0007744|PDB:1NNS,
FT ECO:0007744|PDB:3ECA"
FT DISULFID 99..127
FT /evidence="ECO:0000269|PubMed:8434007,
FT ECO:0000269|PubMed:8706862"
FT MUTAGEN 34
FT /note="T->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:1906013"
FT MUTAGEN 111
FT /note="T->S: Reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:8706862"
FT MUTAGEN 111
FT /note="T->V: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:8706862"
FT CONFLICT 49
FT /note="V -> A (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="N -> D (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="Missing (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="Missing (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="Missing (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="N -> D (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="N -> D (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="S -> T (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="T -> D (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="Missing (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="Missing (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 25..33
FT /evidence="ECO:0007829|PDB:5MQ5"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:5MQ5"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:5MQ5"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:6PAC"
FT HELIX 54..59
FT /evidence="ECO:0007829|PDB:5MQ5"
FT HELIX 62..66
FT /evidence="ECO:0007829|PDB:5MQ5"
FT STRAND 69..78
FT /evidence="ECO:0007829|PDB:5MQ5"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:5MQ5"
FT HELIX 85..98
FT /evidence="ECO:0007829|PDB:5MQ5"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:5MQ5"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:5MQ5"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:5MQ5"
FT HELIX 114..124
FT /evidence="ECO:0007829|PDB:5MQ5"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:5MQ5"
FT HELIX 147..159
FT /evidence="ECO:0007829|PDB:5MQ5"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:5MQ5"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:5MQ5"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:5MQ5"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:5MQ5"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:5MQ5"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:5MQ5"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:5MQ5"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:5MQ5"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:5MQ5"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:5MQ5"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:5MQ5"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:5MQ5"
FT HELIX 248..255
FT /evidence="ECO:0007829|PDB:5MQ5"
FT STRAND 259..266
FT /evidence="ECO:0007829|PDB:5MQ5"
FT TURN 267..269
FT /evidence="ECO:0007829|PDB:5MQ5"
FT HELIX 273..283
FT /evidence="ECO:0007829|PDB:5MQ5"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:5MQ5"
FT STRAND 288..298
FT /evidence="ECO:0007829|PDB:5MQ5"
FT STRAND 302..306
FT /evidence="ECO:0007829|PDB:5MQ5"
FT HELIX 308..311
FT /evidence="ECO:0007829|PDB:5MQ5"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:6PA3"
FT HELIX 321..331
FT /evidence="ECO:0007829|PDB:5MQ5"
FT TURN 332..334
FT /evidence="ECO:0007829|PDB:5MQ5"
FT HELIX 338..347
FT /evidence="ECO:0007829|PDB:5MQ5"
SQ SEQUENCE 348 AA; 36851 MW; 2076987C0E8B2F99 CRC64;
MEFFKKTALA ALVMGFSGAA LALPNITILA TGGTIAGGGD SATKSNYTVG KVGVENLVNA
VPQLKDIANV KGEQVVNIGS QDMNDNVWLT LAKKINTDCD KTDGFVITHG TDTMEETAYF
LDLTVKCDKP VVMVGAMRPS TSMSADGPFN LYNAVVTAAD KASANRGVLV VMNDTVLDGR
DVTKTNTTDV ATFKSVNYGP LGYIHNGKID YQRTPARKHT SDTPFDVSKL NELPKVGIVY
NYANASDLPA KALVDAGYDG IVSAGVGNGN LYKSVFDTLA TAAKTGTAVV RSSRVPTGAT
TQDAEVDDAK YGFVASGTLN PQKARVLLQL ALTQTKDPQQ IQQIFNQY
