ID   XAPA_ECOLI              Reviewed;         277 AA.
AC   P45563; P77325;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   02-SEP-2026, entry version 176.
DE   RecName: Full=Purine nucleoside phosphorylase 2;
DE            EC=2.4.2.1 {ECO:0000269|PubMed:10400599, ECO:0000269|PubMed:15808857, ECO:0000269|PubMed:17151449, ECO:0000269|PubMed:3042752, ECO:0000269|PubMed:7007809, ECO:0000269|PubMed:7559336};
DE   AltName: Full=Inosine-guanosine phosphorylase;
DE   AltName: Full=Purine nucleoside phosphorylase II;
DE            Short=PNP II;
DE   AltName: Full=Xanthosine phosphorylase;
GN   Name=xapA; Synonyms=pndA; OrderedLocusNames=b2407, JW2398;
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], CATALYTIC ACTIVITY, INDUCTION, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=K12;
RX   PubMed=7559336; DOI=10.1128/jb.177.19.5506-5516.1995;
RA   Seeger C., Poulsen C., Dandanell G.;
RT   "Identification and characterization of genes (xapA, xapB, and xapR)
RT   involved in xanthosine catabolism in Escherichia coli.";
RL   J. Bacteriol. 177:5506-5516(1995).
RN   [2]
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   [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   FUNCTION.
RC   STRAIN=K12;
RX   PubMed=7007808; DOI=10.1007/bf00425461;
RA   Buxton R.S., Hammer-Jespersen K., Valentin-Hansen P.;
RT   "A second purine nucleoside phosphorylase in Escherichia coli K-12. I.
RT   Xanthosine phosphorylase regulatory mutants isolated as secondary-site
RT   revertants of a deoD mutant.";
RL   Mol. Gen. Genet. 179:331-340(1980).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, SUBUNIT, AND
RP   INDUCTION.
RC   STRAIN=K12;
RX   PubMed=7007809; DOI=10.1007/bf00425462;
RA   Hammer-Jespersen K., Buxton R.S., Hansen T.D.;
RT   "A second purine nucleoside phosphorylase in Escherichia coli K-12. II.
RT   Properties of xanthosine phosphorylase and its induction by xanthosine.";
RL   Mol. Gen. Genet. 179:341-348(1980).
RN   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION,
RP   AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=K12;
RX   PubMed=3042752; DOI=10.1128/jb.170.8.3493-3498.1988;
RA   Koszalka G.W., Vanhooke J., Short S.A., Hall W.W.;
RT   "Purification and properties of inosine-guanosine phosphorylase from
RT   Escherichia coli K-12.";
RL   J. Bacteriol. 170:3493-3498(1988).
RN   [8]
RP   CATALYTIC ACTIVITY, AND INDUCTION.
RX   PubMed=10400599; DOI=10.1128/jb.181.14.4397-4403.1999;
RA   Jorgensen C., Dandanell G.;
RT   "Isolation and characterization of mutations in the Escherichia coli
RT   regulatory protein XapR.";
RL   J. Bacteriol. 181:4397-4403(1999).
RN   [9]
RP   CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=17151449; DOI=10.1271/bbb.60398;
RA   Shimaoka M., Takenaka Y., Mihara Y., Kurahashi O., Kawasaki H., Matsui H.;
RT   "Effects of xapA and guaA disruption on inosine accumulation in Escherichia
RT   coli.";
RL   Biosci. Biotechnol. Biochem. 70:3069-3072(2006).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH GUANINE, XANTHINE
RP   AND PHOSPHATE, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND MUTAGENESIS OF TYR-191 AND
RP   ASN-239.
RC   STRAIN=K12;
RX   PubMed=15808857; DOI=10.1016/j.jmb.2005.02.019;
RA   Dandanell G., Szczepanowski R.H., Kierdaszuk B., Shugar D., Bochtler M.;
RT   "Escherichia coli purine nucleoside phosphorylase II, the product of the
RT   xapA gene.";
RL   J. Mol. Biol. 348:113-125(2005).
CC   -!- FUNCTION: The purine nucleoside phosphorylases catalyze the
CC       phosphorolytic breakdown of the N-glycosidic bond in the beta-
CC       (deoxy)ribonucleoside molecules, with the formation of the
CC       corresponding free purine bases and pentose-1-phosphate. This protein
CC       can degrade all purine nucleosides including xanthosine, inosine and
CC       guanosine, but cannot cleave adenosine, deoxyadenosine or hypoxanthine
CC       arabinoside. Has a preference for the neutral over the monoanionic form
CC       of xanthosine. {ECO:0000269|PubMed:15808857,
CC       ECO:0000269|PubMed:3042752, ECO:0000269|PubMed:7007808,
CC       ECO:0000269|PubMed:7007809}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a purine D-ribonucleoside + phosphate = a purine nucleobase +
CC         alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:19805, ChEBI:CHEBI:26386,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57720, ChEBI:CHEBI:142355; EC=2.4.2.1;
CC         Evidence={ECO:0000269|PubMed:10400599, ECO:0000269|PubMed:15808857,
CC         ECO:0000269|PubMed:17151449, ECO:0000269|PubMed:3042752,
CC         ECO:0000269|PubMed:7007809, ECO:0000269|PubMed:7559336};
CC   -!- ACTIVITY REGULATION: Rapidly inactivated by p-
CC       chloromercuriphenylsulfonic acid (p-CMB). Dithiothreitol incubation
CC       restores the activity. {ECO:0000269|PubMed:3042752}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=51 uM for xanthosine (at pH 7.0) {ECO:0000269|PubMed:3042752};
CC         KM=72 uM for xanthosine (at 25 degrees Celsius and pH 7.1)
CC         {ECO:0000269|PubMed:15808857};
CC         KM=110 uM for guanosine (at pH 7.0) {ECO:0000269|PubMed:3042752};
CC         KM=155 uM for guanosine (at 25 degrees Celsius and pH 7.1)
CC         {ECO:0000269|PubMed:15808857};
CC         KM=963 uM for inosine (at 25 degrees Celsius and pH 7.1)
CC         {ECO:0000269|PubMed:15808857};
CC         KM=340 uM for inosine (at 25 degrees Celsius and pH 7.0)
CC         {ECO:0000269|PubMed:3042752};
CC         KM=62 uM for 2'-deoxyinosine (at 25 degrees Celsius and pH 7.0)
CC         {ECO:0000269|PubMed:3042752};
CC         KM=600 uM for 5'-deoxyinosine (at 25 degrees Celsius and pH 7.0)
CC         {ECO:0000269|PubMed:3042752};
CC         KM=2600 uM for 2',3'-dideoxyinosine (at 25 degrees Celsius and pH
CC         7.0) {ECO:0000269|PubMed:3042752};
CC         KM=44 uM for 2'-deoxyguanosine (at 25 degrees Celsius and pH 7.0)
CC         {ECO:0000269|PubMed:3042752};
CC         KM=3.3 uM for hypoxanthine (at 25 degrees Celsius and pH 7.0)
CC         {ECO:0000269|PubMed:3042752};
CC         KM=4.1 uM for guanine (at 25 degrees Celsius and pH 7.0)
CC         {ECO:0000269|PubMed:3042752};
CC         KM=760 uM for phosphate (at 25 degrees Celsius and pH 7.0)
CC         {ECO:0000269|PubMed:3042752};
CC         KM=59 uM for alpha-D-ribose 1-phosphate (at 25 degrees Celsius and pH
CC         7.0) {ECO:0000269|PubMed:3042752};
CC         KM=58 uM for alpha-D-2'-deoxyribose 1-phosphate (at 25 degrees
CC         Celsius and pH 7.0) {ECO:0000269|PubMed:3042752};
CC         Vmax=8.7 umol/min/mg enzyme with xanthosine as substrate (at 25
CC         degrees Celsius and pH 7.1) {ECO:0000269|PubMed:15808857};
CC         Vmax=14.2 umol/min/mg enzyme with guanosine as substrate (at 25
CC         degrees Celsius and pH 7.1) {ECO:0000269|PubMed:15808857};
CC         Vmax=11.9 umol/min/mg enzyme with inosine as substrate (at 25 degrees
CC         Celsius and pH 7.1) {ECO:0000269|PubMed:15808857};
CC       pH dependence:
CC         Optimum pH is 6.5-7.5 with guanosine as substrate. At pH higher than
CC         7.5, there is a marked reduction in reaction rate and a steep drop at
CC         pH higher than 9. Below pH 6.5, there is a dramatic decrease in
CC         activity reaching virtually zero at pH 6.0. With xanthosine as
CC         substrate, the pH optimum is 5.8-7.2. In the reverse reaction with
CC         guanine or xanthine as substrates, the pH optimum is 6.5-8.0. The pH
CC         dependence of inosine cleavage does not vary between pH 6 and 8.
CC         Maximal activity with inosine as substrate is observed at pH 6.6.
CC         {ECO:0000269|PubMed:15808857, ECO:0000269|PubMed:3042752};
CC       Temperature dependence:
CC         The half-life at 45 degrees Celsius between pH 5 and 8 is 5 to 9
CC         minutes. {ECO:0000269|PubMed:15808857, ECO:0000269|PubMed:3042752};
CC   -!- PATHWAY: Purine metabolism; xanthosine degradation.
CC   -!- PATHWAY: Purine metabolism; purine nucleoside salvage.
CC   -!- SUBUNIT: Hexamer. Dimer of trimers. {ECO:0000269|PubMed:15808857,
CC       ECO:0000269|PubMed:7007809}.
CC   -!- INDUCTION: By xanthosine and to a lesser extent by deoxyinosine. Full
CC       expression requires XapR-xanthosine DNA-binding transcriptional
CC       activator. {ECO:0000269|PubMed:10400599, ECO:0000269|PubMed:7007809,
CC       ECO:0000269|PubMed:7559336}.
CC   -!- DISRUPTION PHENOTYPE: Does not grow on xanthosine. Slightly increases
CC       inosine productivity compared to wild-type (5.6 g/l of inosine versus
CC       4.6 g/l, respectively, from 40 g/l of glucose).
CC       {ECO:0000269|PubMed:17151449, ECO:0000269|PubMed:7559336}.
CC   -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA52049.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X73828; CAA52049.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; U00096; AAC75460.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA16275.1; -; Genomic_DNA.
DR   PIR; F65014; F65014.
DR   RefSeq; NP_416902.1; NC_000913.3.
DR   RefSeq; WP_000084573.1; NZ_CP009789.1.
DR   PDB; 1YQQ; X-ray; 2.60 A; A/B/C=1-277.
DR   PDB; 1YQU; X-ray; 3.10 A; A/B/C=1-277.
DR   PDB; 1YR3; X-ray; 3.20 A; A/B/C/D/E/F=1-277.
DR   AlphaFoldDB; P45563; -.
DR   SMR; P45563; -.
DR   BioGRID; 4260565; 23.
DR   FunCoup; P45563; 942.
DR   IntAct; P45563; 4.
DR   STRING; 511145.b2407; -.
DR   DrugBank; DB02377; Guanine.
DR   DrugBank; DB02134; Xanthine.
DR   PaxDb; 511145-b2407; -.
DR   EnsemblBacteria; AAC75460; AAC75460; b2407.
DR   GeneID; 946878; -.
DR   KEGG; ecj:JW2398; -.
DR   KEGG; eco:b2407; -.
DR   KEGG; ecoc:C3026_13380; -.
DR   PATRIC; fig|1411691.4.peg.4325; -.
DR   EchoBASE; EB4152; -.
DR   eggNOG; COG0005; Bacteria.
DR   HOGENOM; CLU_054456_1_0_6; -.
DR   InParanoid; P45563; -.
DR   OMA; EGVYAQF; -.
DR   OrthoDB; 1523230at2; -.
DR   PhylomeDB; P45563; -.
DR   BioCyc; EcoCyc:XANTHOSINEPHOSPHORY-MONOMER; -.
DR   BioCyc; MetaCyc:XANTHOSINEPHOSPHORY-MONOMER; -.
DR   BRENDA; 2.4.2.1; 2026.
DR   UniPathway; UPA00119; -.
DR   UniPathway; UPA00606; -.
DR   EvolutionaryTrace; P45563; -.
DR   PRO; PR:P45563; -.
DR   Proteomes; UP000000625; Chromosome.
DR   AbasyAtlas; P45563; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0047975; F:guanosine phosphorylase activity; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR   GO; GO:0047724; F:inosine nucleosidase activity; IDA:UniProtKB.
DR   GO; GO:0004731; F:purine-nucleoside phosphorylase activity; IDA:UniProtKB.
DR   GO; GO:0006161; P:deoxyguanosine catabolic process; IDA:UniProtKB.
DR   GO; GO:0006149; P:deoxyinosine catabolic process; IDA:UniProtKB.
DR   GO; GO:0046115; P:guanosine catabolic process; IDA:UniProtKB.
DR   GO; GO:0006148; P:inosine catabolic process; IDA:UniProtKB.
DR   GO; GO:0034355; P:NAD+ biosynthetic process via the salvage pathway; EXP:EcoCyc.
DR   GO; GO:0015949; P:nucleobase-containing small molecule interconversion; IMP:EcoliWiki.
DR   GO; GO:0055086; P:nucleobase-containing small molecule metabolic process; IMP:EcoliWiki.
DR   GO; GO:0034214; P:protein hexamerization; IDA:UniProtKB.
DR   GO; GO:0006152; P:purine nucleoside catabolic process; IDA:UniProtKB.
DR   GO; GO:1903228; P:xanthosine catabolic process; IMP:EcoCyc.
DR   CDD; cd09009; PNP-EcPNPII_like; 1.
DR   FunFam; 3.40.50.1580:FF:000011; Purine nucleoside phosphorylase; 1.
DR   Gene3D; 3.40.50.1580; Nucleoside phosphorylase domain; 1.
DR   InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR   InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR   InterPro; IPR011268; Purine_phosphorylase.
DR   InterPro; IPR018099; Purine_phosphorylase-2_CS.
DR   InterPro; IPR010943; Xanthosine_phosphorylase.
DR   NCBIfam; TIGR01697; PNPH-PUNA-XAPA; 1.
DR   NCBIfam; NF006054; PRK08202.1; 1.
DR   NCBIfam; TIGR01699; XAPA; 1.
DR   PANTHER; PTHR11904; METHYLTHIOADENOSINE/PURINE NUCLEOSIDE PHOSPHORYLASE; 1.
DR   PANTHER; PTHR11904:SF9; PURINE NUCLEOSIDE PHOSPHORYLASE-RELATED; 1.
DR   Pfam; PF01048; PNP_UDP_1; 1.
DR   PIRSF; PIRSF000477; PurNPase; 1.
DR   SUPFAM; SSF53167; Purine and uridine phosphorylases; 1.
DR   PROSITE; PS01240; PNP_MTAP_2; 1.
DR   PDBsum; 1YQQ; -.
DR   PDBsum; 1YQU; -.
DR   PDBsum; 1YR3; -.
PE   1: Evidence at protein level;
KW   3D-structure; Glycosyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..277
FT                   /note="Purine nucleoside phosphorylase 2"
FT                   /id="PRO_0000184555"
FT   BINDING         65
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000269|PubMed:15808857,
FT                   ECO:0007744|PDB:1YQQ"
FT   BINDING         85..87
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000269|PubMed:15808857,
FT                   ECO:0007744|PDB:1YQQ, ECO:0007744|PDB:1YQU"
FT   BINDING         117
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000269|PubMed:15808857,
FT                   ECO:0007744|PDB:1YQQ, ECO:0007744|PDB:1YQU"
FT   BINDING         197
FT                   /ligand="a purine D-ribonucleoside"
FT                   /ligand_id="ChEBI:CHEBI:142355"
FT                   /evidence="ECO:0000269|PubMed:15808857"
FT   BINDING         216
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000269|PubMed:15808857,
FT                   ECO:0007744|PDB:1YQQ, ECO:0007744|PDB:1YQU"
FT   BINDING         239
FT                   /ligand="a purine D-ribonucleoside"
FT                   /ligand_id="ChEBI:CHEBI:142355"
FT                   /evidence="ECO:0000269|PubMed:15808857"
FT   MUTAGEN         191
FT                   /note="Y->L: No detectable activity with xanthosine as
FT                   substrate, but largely retains its activity against other
FT                   substrates, namely inosine and guanosine, although with
FT                   altered affinities, higher and lower respectively, and
FT                   clearly reduced maximal velocities for both."
FT                   /evidence="ECO:0000269|PubMed:15808857"
FT   MUTAGEN         239
FT                   /note="N->D: Catalyzes the phosphorolysis of adenosine with
FT                   moderate efficiency, and essentially has lost all activity
FT                   against the 6-oxo-purine substrates xanthosine, inosine and
FT                   guanosine."
FT                   /evidence="ECO:0000269|PubMed:15808857"
FT   CONFLICT        144
FT                   /note="P -> A (in Ref. 1; CAA52049)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        261
FT                   /note="S -> H (in Ref. 1; CAA52049)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        265
FT                   /note="F -> L (in Ref. 1; CAA52049)"
FT                   /evidence="ECO:0000305"
FT   HELIX           9..20
FT                   /evidence="ECO:0007829|PDB:1YQQ"
FT   STRAND          27..32
FT                   /evidence="ECO:0007829|PDB:1YQQ"
FT   HELIX           36..42
FT                   /evidence="ECO:0007829|PDB:1YQQ"
FT   STRAND          44..50
FT                   /evidence="ECO:0007829|PDB:1YQQ"
FT   HELIX           51..53
FT                   /evidence="ECO:0007829|PDB:1YQQ"
FT   STRAND          68..74
FT                   /evidence="ECO:0007829|PDB:1YQQ"
FT   STRAND          77..84
FT                   /evidence="ECO:0007829|PDB:1YQQ"
FT   HELIX           88..90
FT                   /evidence="ECO:0007829|PDB:1YQQ"
FT   TURN            94..97
FT                   /evidence="ECO:0007829|PDB:1YQQ"
FT   HELIX           98..107
FT                   /evidence="ECO:0007829|PDB:1YQQ"
FT   STRAND          110..121
FT                   /evidence="ECO:0007829|PDB:1YQQ"
FT   STRAND          130..137
FT                   /evidence="ECO:0007829|PDB:1YQQ"
FT   STRAND          140..142
FT                   /evidence="ECO:0007829|PDB:1YQQ"
FT   TURN            151..153
FT                   /evidence="ECO:0007829|PDB:1YQQ"
FT   STRAND          156..158
FT                   /evidence="ECO:0007829|PDB:1YQQ"
FT   HELIX           166..177
FT                   /evidence="ECO:0007829|PDB:1YQQ"
FT   TURN            178..180
FT                   /evidence="ECO:0007829|PDB:1YQQ"
FT   STRAND          183..190
FT                   /evidence="ECO:0007829|PDB:1YQQ"
FT   HELIX           196..198
FT                   /evidence="ECO:0007829|PDB:1YQQ"
FT   HELIX           199..207
FT                   /evidence="ECO:0007829|PDB:1YQQ"
FT   STRAND          211..217
FT                   /evidence="ECO:0007829|PDB:1YQQ"
FT   HELIX           218..226
FT                   /evidence="ECO:0007829|PDB:1YQQ"
FT   STRAND          230..240
FT                   /evidence="ECO:0007829|PDB:1YQQ"
FT   STRAND          244..246
FT                   /evidence="ECO:0007829|PDB:1YQQ"
FT   HELIX           247..249
FT                   /evidence="ECO:0007829|PDB:1YQQ"
FT   HELIX           251..256
FT                   /evidence="ECO:0007829|PDB:1YQQ"
FT   HELIX           257..259
FT                   /evidence="ECO:0007829|PDB:1YQQ"
FT   HELIX           262..276
FT                   /evidence="ECO:0007829|PDB:1YQQ"
SQ   SEQUENCE   277 AA;  29835 MW;  DD26545755C08F8B CRC64;
     MSQVQFSHNP LFCIDIIKTY KPDFTPRVAF ILGSGLGALA DQIENAVAIS YEKLPGFPVS
     TVHGHAGELV LGHLQGVPVV CMKGRGHFYE GRGMTIMTDA IRTFKLLGCE LLFCTNAAGS
     LRPEVGAGSL VALKDHINTM PGTPMVGLND DRFGERFFSL ANAYDAEYRA LLQKVAKEEG
     FPLTEGVFVS YPGPNFETAA EIRMMQIIGG DVVGMSVVPE VISARHCDLK VVAVSAITNM
     AEGLSDVKLS HAQTLAAAEL SKQNFINLIC GFLRKIA
//