ID   ENO_ENTH1               Reviewed;         436 AA.
AC   P51555; A0A175JIN2; C4LXE8; S0AUS0;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   02-SEP-2026, entry version 124.
DE   RecName: Full=Enolase 1 {ECO:0000303|PubMed:7723780};
DE            Short=EhENO {ECO:0000303|PubMed:21697600};
DE            EC=4.2.1.11 {ECO:0000269|PubMed:15794763};
DE   AltName: Full=2-phospho-D-glycerate hydro-lyase;
DE   AltName: Full=2-phosphoglycerate dehydratase;
GN   Name=ENO {ECO:0000303|PubMed:21697600};
GN   Synonyms=ENL-1 {ECO:0000303|PubMed:7723780};
GN   ORFNames=EHI_130700 {ECO:0000312|EMBL:EAL43773.1};
OS   Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM).
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC   Entamoeba.
OX   NCBI_TaxID=294381 {ECO:0000312|EMBL:EAL43773.1};
RN   [1] {ECO:0000312|EMBL:AAA80166.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ATCC 30459 / HM-1:IMSS / ABRM {ECO:0000312|EMBL:AAA80166.1};
RX   PubMed=7723780; DOI=10.1016/0166-6851(94)00201-w;
RA   Beanan M.J., Bailey G.B.;
RT   "The primary structure of an Entamoeba histolytica enolase.";
RL   Mol. Biochem. Parasitol. 69:119-121(1995).
RN   [2] {ECO:0000312|EMBL:BAN38528.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ATCC 30459 / HM-1:IMSS / ABRM {ECO:0000312|EMBL:BAN38528.1};
RA   Hiranuka K., Kumagai M., Wakaguri H., Suzuki Y., Sugano S., Watanabe J.,
RA   Makioka A.;
RT   "Short 5' UTR of Entamoeba genes.";
RL   Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000312|EMBL:EAL43773.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 30459 / HM-1:IMSS / ABRM {ECO:0000312|EMBL:EAL43773.1};
RX   PubMed=15729342; DOI=10.1038/nature03291;
RA   Loftus B.J., Anderson I., Davies R., Alsmark U.C., Samuelson J., Amedeo P.,
RA   Roncaglia P., Berriman M., Hirt R.P., Mann B.J., Nozaki T., Suh B., Pop M.,
RA   Duchene M., Ackers J., Tannich E., Leippe M., Hofer M., Bruchhaus I.,
RA   Willhoeft U., Bhattacharya A., Chillingworth T., Churcher C.M., Hance Z.,
RA   Harris B., Harris D., Jagels K., Moule S., Mungall K.L., Ormond D.,
RA   Squares R., Whitehead S., Quail M.A., Rabbinowitsch E., Norbertczak H.,
RA   Price C., Wang Z., Guillen N., Gilchrist C., Stroup S.E., Bhattacharya S.,
RA   Lohia A., Foster P.G., Sicheritz-Ponten T., Weber C., Singh U.,
RA   Mukherjee C., El-Sayed N.M.A., Petri W.A., Clark C.G., Embley T.M.,
RA   Barrell B.G., Fraser C.M., Hall N.;
RT   "The genome of the protist parasite Entamoeba histolytica.";
RL   Nature 433:865-868(2005).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP   PATHWAY, AND SUBUNIT.
RX   PubMed=15794763; DOI=10.1111/j.1742-4658.2005.04610.x;
RA   Saavedra E., Encalada R., Pineda E., Jasso-Chavez R., Moreno-Sanchez R.;
RT   "Glycolysis in Entamoeba histolytica. Biochemical characterization of
RT   recombinant glycolytic enzymes and flux control analysis.";
RL   FEBS J. 272:1767-1783(2005).
RN   [5]
RP   FUNCTION, INTERACTION WITH METH, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP   STAGE.
RX   PubMed=20174608; DOI=10.1371/journal.ppat.1000775;
RA   Tovy A., Siman Tov R., Gaentzsch R., Helm M., Ankri S.;
RT   "A new nuclear function of the Entamoeba histolytica glycolytic enzyme
RT   enolase: the metabolic regulation of cytosine-5 methyltransferase 2 (Dnmt2)
RT   activity.";
RL   PLoS Pathog. 6:e1000775-e1000775(2010).
RN   [6] {ECO:0000312|PDB:3QTP}
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND
RP   PHOSPHOGLYCERATE, SUBUNIT, COFACTOR, AND DISULFIDE BOND.
RX   PubMed=21697600; DOI=10.1107/s0907444911016544;
RA   Schulz E.C., Tietzel M., Tovy A., Ankri S., Ficner R.;
RT   "Structure analysis of Entamoeba histolytica enolase.";
RL   Acta Crystallogr. D 67:619-627(2011).
CC   -!- FUNCTION: Glycolytic enzyme that catalyzes the conversion of 2-
CC       phosphoglycerate to phosphoenolpyruvate (PubMed:15794763). Inhibits
CC       tRNA methyltransferase METH catalytic activity in the absence of 2-
CC       phosphoglycerate (PubMed:20174608). {ECO:0000269|PubMed:15794763,
CC       ECO:0000269|PubMed:20174608}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-2-phosphoglycerate = phosphoenolpyruvate + H2O;
CC         Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289,
CC         ChEBI:CHEBI:58702; EC=4.2.1.11;
CC         Evidence={ECO:0000269|PubMed:15794763};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10165;
CC         Evidence={ECO:0000269|PubMed:15794763};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10166;
CC         Evidence={ECO:0000269|PubMed:15794763};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:15794763, ECO:0000305|PubMed:21697600};
CC       Note=Binds 2 Mg(2+) ions per subunit. Required for catalysis and for
CC       stabilizing the dimer. {ECO:0000250|UniProtKB:P06733};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=55 uM for 2-phosphoglycerate (at pH 7 and 37 degrees Celsius)
CC         {ECO:0000269|PubMed:15794763};
CC         KM=60 uM for 2-phosphoglycerate (at pH 6 and 37 degrees Celsius)
CC         {ECO:0000269|PubMed:15794763};
CC         KM=63 uM for phosphoenolpyruvate (at pH 7 and 37 degrees Celsius)
CC         {ECO:0000269|PubMed:15794763};
CC         KM=102 uM for phosphoenolpyruvate (at pH 6 and 37 degrees Celsius)
CC         {ECO:0000269|PubMed:15794763};
CC         Vmax=103 umol/min/mg enzyme with 2-phosphoglycerate as substrate (at
CC         pH 7 and 37 degrees Celsius) {ECO:0000269|PubMed:15794763};
CC         Vmax=89 umol/min/mg enzyme with 2-phosphoglycerate as substrate (at
CC         pH 6 and 37 degrees Celsius) {ECO:0000269|PubMed:15794763};
CC         Vmax=26 umol/min/mg enzyme with phosphoenolpyruvate as substrate (at
CC         pH 7 and 37 degrees Celsius) {ECO:0000269|PubMed:15794763};
CC         Vmax=33 umol/min/mg enzyme with phosphoenolpyruvate as substrate (at
CC         pH 6 and 37 degrees Celsius) {ECO:0000269|PubMed:15794763};
CC         Note=kcat is 170 sec(-1) with 2-phosphoglycerate as substrate (at pH
CC         7 and 37 degrees Celsius) (PubMed:15794763). kcat is 147 sec(-1) with
CC         2-phosphoglycerate as substrate (at pH 6 and 37 degrees Celsius)
CC         (PubMed:15794763). kcat is 43 sec(-1) with phosphoenolpyruvate as
CC         substrate (at pH 7 and 37 degrees Celsius) (PubMed:15794763). kcat is
CC         55 sec(-1) with phosphoenolpyruvate as substrate (at pH 6 and 37
CC         degrees Celsius) (PubMed:15794763). {ECO:0000269|PubMed:15794763};
CC       pH dependence:
CC         Optimum pH is 6.5-7.7 for the conversion of 2-phosphoglycerate to
CC         phosphoenolpyruvate (PubMed:15794763). Optimum pH is 6.0 for the
CC         conversion of phosphoenolpyruvate to 2-phosphoglycerate
CC         (PubMed:15794763). {ECO:0000269|PubMed:15794763};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 4/5. {ECO:0000269|PubMed:15794763}.
CC   -!- SUBUNIT: Homodimer (Probable). Homotetramer (PubMed:15794763).
CC       Interacts with methyltransferase METH; the interaction inhibits METH
CC       catalytic activity; 2-phosphoglycerate binding to ENO prevents the
CC       interaction with METH (PubMed:20174608). {ECO:0000269|PubMed:15794763,
CC       ECO:0000269|PubMed:20174608, ECO:0000305|PubMed:21697600}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20174608}. Nucleus
CC       {ECO:0000269|PubMed:20174608}. Note=During glucose starvation,
CC       accumulates in the nucleus. {ECO:0000269|PubMed:20174608}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in trophozoites (at protein level).
CC       {ECO:0000269|PubMed:20174608}.
CC   -!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
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DR   EMBL; U09736; AAA80166.1; -; mRNA.
DR   EMBL; AK418805; BAN37550.1; -; mRNA.
DR   EMBL; AK418897; BAN37631.1; -; mRNA.
DR   EMBL; AK419306; BAN37996.1; -; mRNA.
DR   EMBL; AK419593; BAN38258.1; -; mRNA.
DR   EMBL; AK419617; BAN38282.1; -; mRNA.
DR   EMBL; AK419676; BAN38334.1; -; mRNA.
DR   EMBL; AK419790; BAN38438.1; -; mRNA.
DR   EMBL; AK419812; BAN38458.1; -; mRNA.
DR   EMBL; AK419816; BAN38462.1; -; mRNA.
DR   EMBL; AK419883; BAN38524.1; -; mRNA.
DR   EMBL; AK419887; BAN38528.1; -; mRNA.
DR   EMBL; AK419955; BAN38587.1; -; mRNA.
DR   EMBL; AK420022; BAN38653.1; -; mRNA.
DR   EMBL; AK420226; BAN38847.1; -; mRNA.
DR   EMBL; AK420333; BAN38948.1; -; mRNA.
DR   EMBL; AK420363; BAN38977.1; -; mRNA.
DR   EMBL; AK420379; BAN38992.1; -; mRNA.
DR   EMBL; AK420409; BAN39022.1; -; mRNA.
DR   EMBL; AK420534; BAN39141.1; -; mRNA.
DR   EMBL; AK420654; BAN39250.1; -; mRNA.
DR   EMBL; AK420726; BAN39317.1; -; mRNA.
DR   EMBL; AK420875; BAN39462.1; -; mRNA.
DR   EMBL; AK420910; BAN39494.1; -; mRNA.
DR   EMBL; AK421000; BAN39576.1; -; mRNA.
DR   EMBL; AK421082; BAN39654.1; -; mRNA.
DR   EMBL; AK421175; BAN39740.1; -; mRNA.
DR   EMBL; AK421207; BAN39770.1; -; mRNA.
DR   EMBL; AK421314; BAN39874.1; -; mRNA.
DR   EMBL; AK421366; BAN39922.1; -; mRNA.
DR   EMBL; AK421393; BAN39949.1; -; mRNA.
DR   EMBL; AK421613; BAN40145.1; -; mRNA.
DR   EMBL; DS571170; EAL43773.1; -; Genomic_DNA.
DR   RefSeq; XP_649161.1; XM_644069.2.
DR   PDB; 3QTP; X-ray; 1.90 A; A/B=1-436.
DR   AlphaFoldDB; P51555; -.
DR   SMR; P51555; -.
DR   STRING; 5759.C4LXE8; -.
DR   EnsemblProtists; GAT93425; GAT93425; CL6EHI_130700.
DR   EnsemblProtists; rna_EHI_130700-1; rna_EHI_130700-1; EHI_130700.
DR   GeneID; 3403451; -.
DR   KEGG; ehi:EHI_130700; -.
DR   VEuPathDB; AmoebaDB:EHI5A_036590; -.
DR   VEuPathDB; AmoebaDB:EHI7A_041120; -.
DR   VEuPathDB; AmoebaDB:EHI8A_039740; -.
DR   VEuPathDB; AmoebaDB:EHI_130700; -.
DR   VEuPathDB; AmoebaDB:KM1_070570; -.
DR   eggNOG; KOG2670; Eukaryota.
DR   HOGENOM; CLU_031223_0_0_1; -.
DR   OMA; RCMMSHR; -.
DR   OrthoDB; 1739814at2759; -.
DR   BRENDA; 4.2.1.11; 2080.
DR   SABIO-RK; P51555; -.
DR   UniPathway; UPA00109; UER00187.
DR   Proteomes; UP000001926; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; EXP:UniProtKB.
DR   GO; GO:0005634; C:nucleus; EXP:UniProtKB.
DR   GO; GO:0000015; C:phosphopyruvate hydratase complex; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004634; F:phosphopyruvate hydratase activity; EXP:UniProtKB.
DR   GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR   CDD; cd03313; enolase; 1.
DR   FunFam; 3.30.390.10:FF:000001; Enolase; 1.
DR   FunFam; 3.20.20.120:FF:000002; Enolase 1; 1.
DR   Gene3D; 3.20.20.120; Enolase-like C-terminal domain; 1.
DR   Gene3D; 3.30.390.10; Enolase-like, N-terminal domain; 1.
DR   HAMAP; MF_00318; Enolase; 1.
DR   InterPro; IPR000941; Enolase.
DR   InterPro; IPR036849; Enolase-like_C_sf.
DR   InterPro; IPR029017; Enolase-like_N.
DR   InterPro; IPR020810; Enolase_C.
DR   InterPro; IPR020809; Enolase_CS.
DR   InterPro; IPR020811; Enolase_N.
DR   NCBIfam; TIGR01060; eno; 1.
DR   PANTHER; PTHR11902; ENOLASE; 1.
DR   PANTHER; PTHR11902:SF1; ENOLASE; 1.
DR   Pfam; PF00113; Enolase_C; 1.
DR   Pfam; PF03952; Enolase_N; 1.
DR   PIRSF; PIRSF001400; Enolase; 1.
DR   PRINTS; PR00148; ENOLASE.
DR   SFLD; SFLDS00001; Enolase; 1.
DR   SFLD; SFLDF00002; enolase; 1.
DR   SFLD; SFLDG00178; enolase; 1.
DR   SMART; SM01192; Enolase_C; 1.
DR   SMART; SM01193; Enolase_N; 1.
DR   SUPFAM; SSF51604; Enolase C-terminal domain-like; 1.
DR   SUPFAM; SSF54826; Enolase N-terminal domain-like; 1.
DR   PROSITE; PS00164; ENOLASE; 1.
DR   PDBsum; 3QTP; -.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Disulfide bond; Glycolysis; Lyase; Magnesium;
KW   Metal-binding; Nucleus; Reference proteome.
FT   CHAIN           1..436
FT                   /note="Enolase 1"
FT                   /id="PRO_0000134080"
FT   ACT_SITE        208
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P00924"
FT   ACT_SITE        347
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P00924"
FT   BINDING         40
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P06733"
FT   BINDING         164
FT                   /ligand="(2R)-2-phosphoglycerate"
FT                   /ligand_id="ChEBI:CHEBI:58289"
FT                   /evidence="ECO:0000269|PubMed:21697600,
FT                   ECO:0007744|PDB:3QTP"
FT   BINDING         208
FT                   /ligand="(2R)-2-phosphoglycerate"
FT                   /ligand_id="ChEBI:CHEBI:58289"
FT                   /evidence="ECO:0000269|PubMed:21697600,
FT                   ECO:0007744|PDB:3QTP"
FT   BINDING         243
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:21697600,
FT                   ECO:0007744|PDB:3QTP"
FT   BINDING         296
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:21697600,
FT                   ECO:0007744|PDB:3QTP"
FT   BINDING         322
FT                   /ligand="(2R)-2-phosphoglycerate"
FT                   /ligand_id="ChEBI:CHEBI:58289"
FT                   /evidence="ECO:0000269|PubMed:21697600,
FT                   ECO:0007744|PDB:3QTP"
FT   BINDING         322
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:21697600,
FT                   ECO:0007744|PDB:3QTP"
FT   BINDING         376
FT                   /ligand="(2R)-2-phosphoglycerate"
FT                   /ligand_id="ChEBI:CHEBI:58289"
FT                   /evidence="ECO:0000269|PubMed:21697600,
FT                   ECO:0007744|PDB:3QTP"
FT   BINDING         377
FT                   /ligand="(2R)-2-phosphoglycerate"
FT                   /ligand_id="ChEBI:CHEBI:58289"
FT                   /evidence="ECO:0000269|PubMed:21697600,
FT                   ECO:0007744|PDB:3QTP"
FT   DISULFID        147..169
FT                   /evidence="ECO:0000269|PubMed:21697600,
FT                   ECO:0007744|PDB:3QTP"
FT   STRAND          5..12
FT                   /evidence="ECO:0007829|PDB:3QTP"
FT   STRAND          18..26
FT                   /evidence="ECO:0007829|PDB:3QTP"
FT   STRAND          29..34
FT                   /evidence="ECO:0007829|PDB:3QTP"
FT   HELIX           35..37
FT                   /evidence="ECO:0007829|PDB:3QTP"
FT   STRAND          43..45
FT                   /evidence="ECO:0007829|PDB:3QTP"
FT   HELIX           57..59
FT                   /evidence="ECO:0007829|PDB:3QTP"
FT   HELIX           63..68
FT                   /evidence="ECO:0007829|PDB:3QTP"
FT   HELIX           69..73
FT                   /evidence="ECO:0007829|PDB:3QTP"
FT   HELIX           74..77
FT                   /evidence="ECO:0007829|PDB:3QTP"
FT   HELIX           85..96
FT                   /evidence="ECO:0007829|PDB:3QTP"
FT   TURN            102..104
FT                   /evidence="ECO:0007829|PDB:3QTP"
FT   HELIX           106..123
FT                   /evidence="ECO:0007829|PDB:3QTP"
FT   HELIX           128..136
FT                   /evidence="ECO:0007829|PDB:3QTP"
FT   STRAND          145..152
FT                   /evidence="ECO:0007829|PDB:3QTP"
FT   HELIX           154..156
FT                   /evidence="ECO:0007829|PDB:3QTP"
FT   STRAND          158..160
FT                   /evidence="ECO:0007829|PDB:3QTP"
FT   STRAND          163..169
FT                   /evidence="ECO:0007829|PDB:3QTP"
FT   HELIX           176..198
FT                   /evidence="ECO:0007829|PDB:3QTP"
FT   HELIX           200..203
FT                   /evidence="ECO:0007829|PDB:3QTP"
FT   HELIX           218..232
FT                   /evidence="ECO:0007829|PDB:3QTP"
FT   TURN            235..237
FT                   /evidence="ECO:0007829|PDB:3QTP"
FT   STRAND          239..243
FT                   /evidence="ECO:0007829|PDB:3QTP"
FT   HELIX           246..249
FT                   /evidence="ECO:0007829|PDB:3QTP"
FT   TURN            252..255
FT                   /evidence="ECO:0007829|PDB:3QTP"
FT   STRAND          256..258
FT                   /evidence="ECO:0007829|PDB:3QTP"
FT   TURN            259..262
FT                   /evidence="ECO:0007829|PDB:3QTP"
FT   HELIX           265..267
FT                   /evidence="ECO:0007829|PDB:3QTP"
FT   HELIX           270..272
FT                   /evidence="ECO:0007829|PDB:3QTP"
FT   HELIX           276..289
FT                   /evidence="ECO:0007829|PDB:3QTP"
FT   STRAND          292..297
FT                   /evidence="ECO:0007829|PDB:3QTP"
FT   HELIX           304..313
FT                   /evidence="ECO:0007829|PDB:3QTP"
FT   TURN            314..316
FT                   /evidence="ECO:0007829|PDB:3QTP"
FT   STRAND          317..322
FT                   /evidence="ECO:0007829|PDB:3QTP"
FT   TURN            323..327
FT                   /evidence="ECO:0007829|PDB:3QTP"
FT   HELIX           329..338
FT                   /evidence="ECO:0007829|PDB:3QTP"
FT   STRAND          342..346
FT                   /evidence="ECO:0007829|PDB:3QTP"
FT   HELIX           348..350
FT                   /evidence="ECO:0007829|PDB:3QTP"
FT   HELIX           354..366
FT                   /evidence="ECO:0007829|PDB:3QTP"
FT   STRAND          370..374
FT                   /evidence="ECO:0007829|PDB:3QTP"
FT   HELIX           384..391
FT                   /evidence="ECO:0007829|PDB:3QTP"
FT   STRAND          395..398
FT                   /evidence="ECO:0007829|PDB:3QTP"
FT   HELIX           405..421
FT                   /evidence="ECO:0007829|PDB:3QTP"
SQ   SEQUENCE   436 AA;  47327 MW;  BFBA693A65B44289 CRC64;
     MSIQKVHARE ILDSRGNPTI EVEITTGKGM FRSCVPSGAS TGVHEAVELR DGDKKRYGGK
     GVLKAVENVN TIIGPALLGK NVLNQAELDE MMIKLDGTNN KGKLGANAIL GCSMSICRAA
     AAEKGLPLYK YLAELTGHKE MTMPVPCFNV INGGAHAGNA LAMQEFMICP TGATNFHEAL
     RMAAETYQCL KVVIKAKYGQ DATNVGDEGG FAPNVSGARE ALDLLVEAIA KAGYTGKIEI
     AMDCAASEFY NEETKKYDLG KKIPADKKDP SLVKDVDGLI AEYVDYGKHY PIASIEDPFA
     EDDWAAWNKF TVEHGNFQIV GDDLLVTNPA RVQMAMDKNA CNSVLIKVNQ IGTLTETFKT
     IKMAQEKGWG VMASHRSGET EDTFIADLVV GLNCKQIKTG APCRSERLCK YNQLMRIEEE
     LGNIPYAGKN WRNSTA
//